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   27-MAR-2024, entry version 169.
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   EMDB; EMD-21564; -.
DR   EMDB; EMD-30296; -.
DR   EMDB; EMD-30297; -.
DR   EMDB; EMD-9616; -.
DR   EMDB; EMD-9622; -.
DR   SMR; P53218; -.
DR   BioGRID; 33275; 35.
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; 4932-YGR030C; -.
DR   PeptideAtlas; P53218; -.
DR   EnsemblFungi; YGR030C_mRNA; YGR030C; YGR030C.
DR   GeneID; 852918; -.
DR   KEGG; sce:YGR030C; -.
DR   AGR; SGD:S000003262; -.
DR   SGD; S000003262; POP6.
DR   VEuPathDB; FungiDB:YGR030C; -.
DR   eggNOG; ENOG502S7W4; Eukaryota.
DR   HOGENOM; CLU_115485_0_0_1; -.
DR   InParanoid; P53218; -.
DR   OMA; KVETHNE; -.
DR   OrthoDB; 2012660at2759; -.
DR   BioCyc; YEAST:YGR030C-MONOMER; -.
DR   BioGRID-ORCS; 852918; 0 hits in 10 CRISPR screens.
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, RNase MRP-dependent; 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
//