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Protein

Ribonucleases P/MRP protein subunit POP6

Gene

POP6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.1 Publication

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC
  2. rRNA primary transcript binding Source: SGD

GO - Biological processi

  1. intronic box C/D snoRNA processing Source: SGD
  2. mRNA cleavage Source: SGD
  3. RNA phosphodiester bond hydrolysis Source: GOC
  4. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  5. rRNA processing Source: SGD
  6. tRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

rRNA processing, tRNA processing

Enzyme and pathway databases

BioCyciYEAST:YGR030C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleases P/MRP protein subunit POP6 (EC:3.1.26.5)
Alternative name(s):
RNA-processing protein POP6
RNases P/MRP 18.2 kDa subunit
Gene namesi
Name:POP6
Ordered Locus Names:YGR030C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR030c.
SGDiS000003262. POP6.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleolar ribonuclease P complex Source: SGD
  3. nucleus Source: SGD
  4. ribonuclease MRP complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Ribonucleases P/MRP protein subunit POP6PRO_0000058517Add
BLAST

Proteomic databases

MaxQBiP53218.
PaxDbiP53218.
PeptideAtlasiP53218.

Expressioni

Gene expression databases

GenevestigatoriP53218.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POP7P382913EBI-13662,EBI-13670

Protein-protein interaction databases

BioGridi33275. 17 interactions.
DIPiDIP-6775N.
IntActiP53218. 10 interactions.
MINTiMINT-633018.
STRINGi4932.YGR030C.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi10 – 134Combined sources
Helixi19 – 2810Combined sources
Turni29 – 346Combined sources
Beta strandi38 – 4811Combined sources
Helixi55 – 6612Combined sources
Turni71 – 744Combined sources
Beta strandi76 – 849Combined sources
Helixi85 – 873Combined sources
Helixi88 – 10316Combined sources
Turni104 – 1063Combined sources
Beta strandi110 – 12011Combined sources
Beta strandi133 – 14715Combined sources
Beta strandi155 – 1573Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IABX-ray2.70A1-158[»]
ProteinModelPortaliP53218.
SMRiP53218. Positions 4-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53218.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili51 – 7121Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG69404.
HOGENOMiHOG000115608.
InParanoidiP53218.
KOiK14524.
OMAiWNNASET.
OrthoDBiEOG70CRK7.

Family and domain databases

InterProiIPR002775. DNA/RNA-bd_Alba-like.
IPR020224. RNase_P/MRP_POP6.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
ProDomiPD093696. RNase_P/MRP_su-POP6. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P53218-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MINGVYYNEI SRDLDISSST QCLRFLKETV IPSLANNGNN STSIQYHGIS
60 70 80 90 100
KNDNIKKSVN KLDKQINMAD RSLGLQQVVC IFSYGPHIQK MLSILEIFKK
110 120 130 140 150
GYIKNNKKIY QWNKLTSFDI KREGRNELQE ERLKVPILVT LVSDSEIIDL

NLHSFTKQ
Length:158
Mass (Da):18,210
Last modified:October 1, 1996 - v1
Checksum:i6C27A73FAD521181
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72815 Genomic DNA. Translation: CAA97018.1.
AY558324 Genomic DNA. Translation: AAS56650.1.
BK006941 Genomic DNA. Translation: DAA08126.1.
PIRiS64321.
RefSeqiNP_011544.1. NM_001181159.1.

Genome annotation databases

EnsemblFungiiYGR030C; YGR030C; YGR030C.
GeneIDi852918.
KEGGisce:YGR030C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72815 Genomic DNA. Translation: CAA97018.1.
AY558324 Genomic DNA. Translation: AAS56650.1.
BK006941 Genomic DNA. Translation: DAA08126.1.
PIRiS64321.
RefSeqiNP_011544.1. NM_001181159.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IABX-ray2.70A1-158[»]
ProteinModelPortaliP53218.
SMRiP53218. Positions 4-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33275. 17 interactions.
DIPiDIP-6775N.
IntActiP53218. 10 interactions.
MINTiMINT-633018.
STRINGi4932.YGR030C.

Proteomic databases

MaxQBiP53218.
PaxDbiP53218.
PeptideAtlasiP53218.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR030C; YGR030C; YGR030C.
GeneIDi852918.
KEGGisce:YGR030C.

Organism-specific databases

CYGDiYGR030c.
SGDiS000003262. POP6.

Phylogenomic databases

eggNOGiNOG69404.
HOGENOMiHOG000115608.
InParanoidiP53218.
KOiK14524.
OMAiWNNASET.
OrthoDBiEOG70CRK7.

Enzyme and pathway databases

BioCyciYEAST:YGR030C-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53218.
NextBioi972622.

Gene expression databases

GenevestigatoriP53218.

Family and domain databases

InterProiIPR002775. DNA/RNA-bd_Alba-like.
IPR020224. RNase_P/MRP_POP6.
[Graphical view]
PfamiPF01918. Alba. 1 hit.
[Graphical view]
ProDomiPD093696. RNase_P/MRP_su-POP6. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP."
    Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.
    Genes Dev. 12:1678-1690(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component."
    Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.
    J. Biol. Chem. 280:11352-11360(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPOP6_YEAST
AccessioniPrimary (citable) accession number: P53218
Secondary accession number(s): D6VUG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3180 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.