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P38291 (POP7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleases P/MRP protein subunit POP7

EC=3.1.26.5
Alternative name(s):
RNA-processing protein POP7
RNases P/MRP 15.8 kDa subunit
Gene names
Name:POP7
Synonyms:RPP2
Ordered Locus Names:YBR167C
ORF Names:YBR1219
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Catalytic activity

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

Subunit structure

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. Ref.5 Ref.7

Subcellular location

Nucleus Ref.6.

Sequence similarities

Belongs to the histone-like Alba family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

POP6P532183EBI-13670,EBI-13662

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Ribonucleases P/MRP protein subunit POP7
PRO_0000058519

Amino acid modifications

Modified residue1151Phosphoserine Ref.8

Experimental info

Sequence conflict921V → I in AAT92849. Ref.4

Secondary structure

............... 140
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38291 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: B507BFDC7ED9C95C

FASTA14015,814
        10         20         30         40         50         60 
MALKKNTHNK STKRVTKHPS LKTLTHKQIH TTIFVKSTTP YVSALKRINK FLDSVHKQGS 

        70         80         90        100        110        120 
SYVAVLGMGK AVEKTLALGC HFQDQKNKKI EVYTKTIEVL DEVITEGQAD IDMESDVEDD 

       130        140 
DKETQLKKRA VSGVELRIYV 

« Hide

References

« Hide 'large scale' references
[1]"Rpp2, an essential protein subunit of nuclear RNase P, is required for processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces cerevisiae."
Stolc V., Katz A., Altman S.
Proc. Natl. Acad. Sci. U.S.A. 95:6716-6721(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055991 Genomic DNA. Translation: AAC24226.1.
Z36036 Genomic DNA. Translation: CAA85128.1.
AY692830 Genomic DNA. Translation: AAT92849.1.
BK006936 Genomic DNA. Translation: DAA07283.1.
PIRS46038.
RefSeqNP_009726.3. NM_001178515.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IABX-ray2.70B1-140[»]
ProteinModelPortalP38291.
SMRP38291. Positions 14-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32867. 109 interactions.
DIPDIP-5462N.
IntActP38291. 9 interactions.
MINTMINT-570982.
STRING4932.YBR167C.

Proteomic databases

PaxDbP38291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR167C; YBR167C; YBR167C.
GeneID852465.
KEGGsce:YBR167C.

Organism-specific databases

CYGDYBR167c.
SGDS000000371. POP7.

Phylogenomic databases

eggNOGNOG45117.
HOGENOMHOG000248080.
KOK14526.
OMAYITVKGM.
OrthoDBEOG7PGF3J.

Enzyme and pathway databases

BioCycYEAST:YBR167C-MONOMER.

Gene expression databases

GenevestigatorP38291.

Family and domain databases

InterProIPR020241. RNase_P/MRP_POP7.
[Graphical view]
ProDomPD085500. Ribonuclease_P/MRP_su_POP7. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP38291.
NextBio971411.

Entry information

Entry namePOP7_YEAST
AccessionPrimary (citable) accession number: P38291
Secondary accession number(s): D6VQG3, E9P8X7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references