POP7_YEAST
ID POP7_YEAST Reviewed; 140 AA.
AC P38291; D6VQG3; E9P8X7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ribonucleases P/MRP protein subunit POP7;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein POP7;
DE AltName: Full=RNases P/MRP 15.8 kDa subunit;
GN Name=POP7; Synonyms=RPP2; OrderedLocusNames=YBR167C; ORFNames=YBR1219;
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], AND FUNCTION.
RX PubMed=9618478; DOI=10.1073/pnas.95.12.6716;
RA Stolc V., Katz A., Altman S.;
RT "Rpp2, an essential protein subunit of nuclear RNase P, is required for
RT processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6716-6721(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [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 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 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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:9618478, 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 -!- INTERACTION:
CC P38291; P41812: POP1; NbExp=4; IntAct=EBI-13670, EBI-13621;
CC P38291; P38336: POP4; NbExp=3; IntAct=EBI-13670, EBI-13646;
CC P38291; P53218: POP6; NbExp=3; IntAct=EBI-13670, EBI-13662;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; AF055991; AAC24226.1; -; Genomic_DNA.
DR EMBL; Z36036; CAA85128.1; -; Genomic_DNA.
DR EMBL; AY692830; AAT92849.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07283.1; -; Genomic_DNA.
DR PIR; S46038; S46038.
DR RefSeq; NP_009726.3; NM_001178515.3.
DR PDB; 3IAB; X-ray; 2.70 A; B=1-140.
DR PDB; 6AGB; EM; 3.48 A; G=1-140.
DR PDB; 6AH3; EM; 3.48 A; G=1-140.
DR PDB; 6W6V; EM; 3.00 A; G=1-140.
DR PDB; 7C79; EM; 2.50 A; G=1-140.
DR PDB; 7C7A; EM; 2.80 A; G=1-140.
DR PDBsum; 3IAB; -.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P38291; -.
DR SMR; P38291; -.
DR BioGRID; 32867; 497.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-5462N; -.
DR IntAct; P38291; 11.
DR MINT; P38291; -.
DR STRING; 4932.YBR167C; -.
DR iPTMnet; P38291; -.
DR MaxQB; P38291; -.
DR PaxDb; P38291; -.
DR PRIDE; P38291; -.
DR TopDownProteomics; P38291; -.
DR EnsemblFungi; YBR167C_mRNA; YBR167C; YBR167C.
DR GeneID; 852465; -.
DR KEGG; sce:YBR167C; -.
DR SGD; S000000371; POP7.
DR VEuPathDB; FungiDB:YBR167C; -.
DR eggNOG; ENOG502S59H; Eukaryota.
DR HOGENOM; CLU_133944_0_0_1; -.
DR InParanoid; P38291; -.
DR OMA; GQADIDM; -.
DR BioCyc; YEAST:YBR167C-MON; -.
DR EvolutionaryTrace; P38291; -.
DR PRO; PR:P38291; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38291; protein.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:SGD.
DR GO; GO:0005697; C:telomerase holoenzyme 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: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 Gene3D; 3.30.110.20; -; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR014612; Pop7/Rpp20.
DR InterPro; IPR020241; RNase_P/MRP_Pop7_fungi.
DR PANTHER; PTHR28256; PTHR28256; 2.
DR Pfam; PF12328; Rpp20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nucleus; Phosphoprotein; Reference proteome;
KW rRNA processing; tRNA processing.
FT CHAIN 1..140
FT /note="Ribonucleases P/MRP protein subunit POP7"
FT /id="PRO_0000058519"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 92
FT /note="V -> I (in Ref. 4; AAT92849)"
FT /evidence="ECO:0000305"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 90..103
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 125..138
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 140 AA; 15814 MW; B507BFDC7ED9C95C CRC64;
MALKKNTHNK STKRVTKHPS LKTLTHKQIH TTIFVKSTTP YVSALKRINK FLDSVHKQGS
SYVAVLGMGK AVEKTLALGC HFQDQKNKKI EVYTKTIEVL DEVITEGQAD IDMESDVEDD
DKETQLKKRA VSGVELRIYV
