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 27-MAR-2024, entry version 177. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-21564; -. DR EMDB; EMD-30296; -. DR EMDB; EMD-30297; -. DR EMDB; EMD-9616; -. DR EMDB; EMD-9622; -. DR SMR; P28005; -. DR BioGRID; 31733; 135. 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; 4932-YAL033W; -. DR PeptideAtlas; P28005; -. DR EnsemblFungi; YAL033W_mRNA; YAL033W; YAL033W. DR GeneID; 851200; -. DR KEGG; sce:YAL033W; -. DR AGR; SGD:S000000031; -. 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; MQNYLDK; -. DR OrthoDB; 2787248at2759; -. DR BioCyc; YEAST:YAL033W-MONOMER; -. DR BioGRID-ORCS; 851200; 3 hits in 10 CRISPR screens. 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:MGI. 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, RNase MRP-dependent; 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; Ribonuclease P, Pop5 subunit; 1. DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like. DR InterPro; IPR016819; RNase_P/MRP_POP5. DR InterPro; IPR038085; Rnp2-like_sf. DR PANTHER; PTHR48326; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1. DR PANTHER; PTHR48326:SF1; RIBONUCLEASE P_MRP PROTEIN SUBUNIT POP5; 1. DR Pfam; PF01900; RNase_P_Rpp14; 1. DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 1. DR SUPFAM; SSF160350; Rnp2-like; 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 //