POP8_YEAST
ID POP8_YEAST Reviewed; 133 AA.
AC P38208; D6VPY2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ribonucleases P/MRP protein subunit POP8;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein POP8;
DE AltName: Full=RNases P/MRP 15.5 kDa subunit;
GN Name=POP8; OrderedLocusNames=YBL018C; ORFNames=YBL0301;
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=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 [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 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 [4]
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 [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).
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).
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: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z35779; CAA84837.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07102.1; -; Genomic_DNA.
DR PIR; S45752; S45752.
DR RefSeq; NP_009535.1; NM_001178258.1.
DR PDB; 6AGB; EM; 3.48 A; H=1-133.
DR PDB; 6AH3; EM; 3.48 A; H=1-133.
DR PDB; 6W6V; EM; 3.00 A; H=1-133.
DR PDB; 7C79; EM; 2.50 A; H=1-133.
DR PDB; 7C7A; EM; 2.80 A; H=1-133.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P38208; -.
DR SMR; P38208; -.
DR BioGRID; 32680; 115.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-2033N; -.
DR IntAct; P38208; 9.
DR STRING; 4932.YBL018C; -.
DR MaxQB; P38208; -.
DR PaxDb; P38208; -.
DR PRIDE; P38208; -.
DR EnsemblFungi; YBL018C_mRNA; YBL018C; YBL018C.
DR GeneID; 852263; -.
DR KEGG; sce:YBL018C; -.
DR SGD; S000000114; POP8.
DR VEuPathDB; FungiDB:YBL018C; -.
DR eggNOG; ENOG502SCWV; Eukaryota.
DR HOGENOM; CLU_153352_0_0_1; -.
DR InParanoid; P38208; -.
DR OMA; RQWLNNA; -.
DR BioCyc; YEAST:YBL018C-MON; -.
DR PRO; PR:P38208; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38208; 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: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:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR InterPro; IPR020347; Pop8.
DR PANTHER; PTHR28173; PTHR28173; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nucleus; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..133
FT /note="Ribonucleases P/MRP protein subunit POP8"
FT /id="PRO_0000058521"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 115..132
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 133 AA; 15512 MW; 9605CC5BD74AFA21 CRC64;
MGKKTFREWQ YFKLSITSFD QDVDDAHAID QMTWRQWLNN ALKRSYGIFG EGVEYSFLHV
DDKLAYIRVN HADKDTFSSS ISTYISTDEL VGSPLTVSIL QESSSLRLLE VTDDDRLWLK
KVMEEEEQDC KCI
