POP6_YEAST
ID POP6_YEAST Reviewed; 158 AA.
AC P53218; D6VUG5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribonucleases P/MRP protein subunit POP6;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein POP6;
DE AltName: Full=RNases P/MRP 18.2 kDa subunit;
GN Name=POP6; OrderedLocusNames=YGR030C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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: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 P53218; P41812: POP1; NbExp=5; IntAct=EBI-13662, EBI-13621;
CC P53218; P38336: POP4; NbExp=4; IntAct=EBI-13662, EBI-13646;
CC P53218; P38291: POP7; NbExp=3; IntAct=EBI-13662, EBI-13670;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72815; CAA97018.1; -; Genomic_DNA.
DR EMBL; AY558324; AAS56650.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08126.1; -; Genomic_DNA.
DR PIR; S64321; S64321.
DR RefSeq; NP_011544.1; NM_001181159.1.
DR PDB; 3IAB; X-ray; 2.70 A; A=1-158.
DR PDB; 6AGB; EM; 3.48 A; F=1-158.
DR PDB; 6AH3; EM; 3.48 A; F=1-158.
DR PDB; 6W6V; EM; 3.00 A; F=1-158.
DR PDB; 7C79; EM; 2.50 A; F=1-158.
DR PDB; 7C7A; EM; 2.80 A; F=1-158.
DR PDBsum; 3IAB; -.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR PDBsum; 6W6V; -.
DR PDBsum; 7C79; -.
DR PDBsum; 7C7A; -.
DR AlphaFoldDB; P53218; -.
DR SMR; P53218; -.
DR BioGRID; 33275; 30.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR ComplexPortal; CPX-3284; Nucleolar ribonuclease MRP complex.
DR DIP; DIP-6775N; -.
DR IntAct; P53218; 12.
DR MINT; P53218; -.
DR STRING; 4932.YGR030C; -.
DR MaxQB; P53218; -.
DR PaxDb; P53218; -.
DR PRIDE; P53218; -.
DR EnsemblFungi; YGR030C_mRNA; YGR030C; YGR030C.
DR GeneID; 852918; -.
DR KEGG; sce:YGR030C; -.
DR SGD; S000003262; POP6.
DR VEuPathDB; FungiDB:YGR030C; -.
DR eggNOG; ENOG502S7W4; Eukaryota.
DR HOGENOM; CLU_115485_0_0_1; -.
DR InParanoid; P53218; -.
DR OMA; INKVETH; -.
DR BioCyc; YEAST:YGR030C-MON; -.
DR EvolutionaryTrace; P53218; -.
DR PRO; PR:P53218; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53218; 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: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:0042134; F:rRNA primary transcript 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 InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR Pfam; PF01918; Alba; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Hydrolase; Nucleus; Reference proteome;
KW rRNA processing; tRNA processing.
FT CHAIN 1..158
FT /note="Ribonucleases P/MRP protein subunit POP6"
FT /id="PRO_0000058517"
FT COILED 51..71
FT /evidence="ECO:0000255"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 29..34
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6W6V"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7C79"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:7C79"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 110..123
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:7C7A"
FT STRAND 130..144
FT /evidence="ECO:0007829|PDB:7C79"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:7C79"
SQ SEQUENCE 158 AA; 18210 MW; 6C27A73FAD521181 CRC64;
MINGVYYNEI SRDLDISSST QCLRFLKETV IPSLANNGNN STSIQYHGIS KNDNIKKSVN
KLDKQINMAD RSLGLQQVVC IFSYGPHIQK MLSILEIFKK GYIKNNKKIY QWNKLTSFDI
KREGRNELQE ERLKVPILVT LVSDSEIIDL NLHSFTKQ
