POP5_YEAST
ID POP5_YEAST Reviewed; 173 AA.
AC P28005; D6VPI5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ribonuclease P/MRP protein subunit POP5;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein POP5;
DE AltName: Full=RNase P/MRP 19.6 kDa subunit;
GN Name=POP5; OrderedLocusNames=YAL033W; ORFNames=FUN53;
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].
RX PubMed=1583694; DOI=10.1016/0022-2836(92)91025-k;
RA Harris S.D., Cheng J., Pugh T.A., Pringle J.R.;
RT "Molecular analysis of Saccharomyces cerevisiae chromosome I. On the number
RT of genes and the identification of essential genes using temperature-
RT sensitive-lethal mutations.";
RL J. Mol. Biol. 225:53-65(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
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 [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 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 [6]
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 [7]
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 [8]
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: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:9620854}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000305}.
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DR EMBL; X62577; CAA44457.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04999.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06955.1; -; Genomic_DNA.
DR PIR; S23411; S23411.
DR RefSeq; NP_009369.1; NM_001178178.1.
DR PDB; 6AGB; EM; 3.48 A; E=1-173.
DR PDB; 6AH3; EM; 3.48 A; E=1-173.
DR PDB; 6W6V; EM; 3.00 A; E=1-173.
DR PDB; 7C79; EM; 2.50 A; E=1-173.
DR PDB; 7C7A; EM; 2.80 A; E=1-173.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P28005; -.
DR SMR; P28005; -.
DR BioGRID; 31733; 129.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-3789N; -.
DR IntAct; P28005; 11.
DR MINT; P28005; -.
DR STRING; 4932.YAL033W; -.
DR iPTMnet; P28005; -.
DR MaxQB; P28005; -.
DR PaxDb; P28005; -.
DR PRIDE; P28005; -.
DR EnsemblFungi; YAL033W_mRNA; YAL033W; YAL033W.
DR GeneID; 851200; -.
DR KEGG; sce:YAL033W; -.
DR SGD; S000000031; POP5.
DR VEuPathDB; FungiDB:YAL033W; -.
DR eggNOG; KOG4639; Eukaryota.
DR GeneTree; ENSGT00970000196581; -.
DR HOGENOM; CLU_086710_1_2_1; -.
DR InParanoid; P28005; -.
DR OMA; FLDRAMG; -.
DR BioCyc; YEAST:YAL033W-MON; -.
DR PRO; PR:P28005; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P28005; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0000171; F:ribonuclease MRP activity; IDA:MGI.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IEA:InterPro.
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:0006364; P:rRNA processing; IDA:MGI.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR Gene3D; 3.30.70.3250; -; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR016819; RNase_P/MRP_POP5.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Reference proteome;
KW rRNA processing; tRNA processing.
FT CHAIN 1..173
FT /note="Ribonuclease P/MRP protein subunit POP5"
FT /id="PRO_0000140015"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 123..145
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:6W6V"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:6W6V"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6W6V"
SQ SEQUENCE 173 AA; 19574 MW; 918193631BD790DD CRC64;
MVRLKSRYIL FEIIFPPTDT NVEESVSKAD ILLSHHRASP ADVSIKSILQ EIRRSLSLNL
GDYGSAKCNS LLQLKYFSNK TSTGIIRCHR EDCDLVIMAL MLMSKIGDVD GLIVNPVKVS
GTIKKIEQFA MRRNSKILNI IKCSQSSHLS DNDFIINDFK KIGRENENEN EDD
