RPP1_YEAST
ID RPP1_YEAST Reviewed; 293 AA.
AC P38786; D3DL11;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ribonuclease P/MRP protein subunit RPP1;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein RPP1;
DE AltName: Full=RNaseP/MRP 32.2 kDa subunit;
GN Name=RPP1; OrderedLocusNames=YHR062C;
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 [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=9308968; DOI=10.1101/gad.11.18.2414;
RA Stolc V., Altman S.;
RT "Rpp1, an essential protein subunit of nuclear RNase P required for
RT processing of precursor tRNA and 35S precursor rRNA in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 11:2414-2425(1997).
RN [2]
RP ERRATUM OF PUBMED:9308968.
RX PubMed=9353260; DOI=10.1101/gad.11.21.2926;
RA Stolc V., Altman S.;
RL Genes Dev. 11:2926-2937(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
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 [8]
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).
RN [9]
RP IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
RX PubMed=15637077; DOI=10.1074/jbc.m409568200;
RA Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.;
RT "Characterization and purification of Saccharomyces cerevisiae RNase MRP
RT reveals a new unique protein component.";
RL J. Biol. Chem. 280:11352-11360(2005).
CC -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. Also a component of
CC RNase MRP, which cleaves pre-rRNA sequences.
CC {ECO:0000269|PubMed:9308968, 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 -!- SUBUNIT: Component of nuclear RNase P and RNase MRP complexes. RNase P
CC consists of an RNA moiety and at least 9 protein subunits including
CC POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP
CC complex consists of an RNA moiety and at least 10 protein subunits
CC including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and
CC SNM1, many of which are shared with the RNase P complex.
CC {ECO:0000269|PubMed:15637077, ECO:0000269|PubMed:9308968,
CC ECO:0000269|PubMed:9620854}.
CC -!- INTERACTION:
CC P38786; P41812: POP1; NbExp=3; IntAct=EBI-15968, EBI-13621;
CC P38786; P38336: POP4; NbExp=3; IntAct=EBI-15968, EBI-13646;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 3 family. {ECO:0000305}.
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DR EMBL; U95757; AAB96559.1; -; Genomic_DNA.
DR EMBL; U00061; AAB68389.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06755.1; -; Genomic_DNA.
DR PIR; S46710; S46710.
DR RefSeq; NP_011929.1; NM_001179192.1.
DR PDB; 6AGB; EM; 3.48 A; I/J=1-293.
DR PDB; 6AH3; EM; 3.48 A; I/J=1-293.
DR PDB; 6W6V; EM; 3.00 A; I/J=1-293.
DR PDB; 7C79; EM; 2.50 A; I/J=1-293.
DR PDB; 7C7A; EM; 2.80 A; I/J=1-293.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P38786; -.
DR SMR; P38786; -.
DR BioGRID; 36494; 228.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-5590N; -.
DR IntAct; P38786; 8.
DR MINT; P38786; -.
DR STRING; 4932.YHR062C; -.
DR MaxQB; P38786; -.
DR PaxDb; P38786; -.
DR PRIDE; P38786; -.
DR TopDownProteomics; P38786; -.
DR EnsemblFungi; YHR062C_mRNA; YHR062C; YHR062C.
DR GeneID; 856459; -.
DR KEGG; sce:YHR062C; -.
DR SGD; S000001104; RPP1.
DR VEuPathDB; FungiDB:YHR062C; -.
DR eggNOG; KOG2363; Eukaryota.
DR GeneTree; ENSGT00390000000883; -.
DR HOGENOM; CLU_048451_3_0_1; -.
DR InParanoid; P38786; -.
DR OMA; PWDVINL; -.
DR BioCyc; YEAST:YHR062C-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P38786; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38786; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0034965; P:intronic box C/D RNA processing; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IDA:ComplexPortal.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nucleus; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..293
FT /note="Ribonuclease P/MRP protein subunit RPP1"
FT /id="PRO_0000140034"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6W6V"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6AGB"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7C7A"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 218..241
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6W6V"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 293 AA; 32224 MW; E9C775D8C646B5C7 CRC64;
MLVDLNVPWP QNSYADKVTS QAVNNLIKTL STLHMLGYTH IAINFTVNHS EKFPNDVKLL
NPIDIKRRFG ELMDRTGLKL YSRITLIIDD PSKGQSLSKI SQAFDIVAAL PISEKGLTLS
TTNLDIDLLT FQYGSRLPTF LKHKSICSCV NRGVKLEIVY GYALRDVQAR RQFVSNVRSV
IRSSRSRGIV IGSGAMSPLE CRNILGVTSL IKNLGLPSDR CSKAMGDLAS LVLLNGRLRN
KSHKQTIVTG GGSGNGDDVV NDVQGIDDVQ TIKVVKRSMD AEQLGHASKR HKP
