Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P38291

- POP7_YEAST

UniProt

P38291 - POP7_YEAST

Protein

Ribonucleases P/MRP protein subunit POP7

Gene

POP7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribonuclease P activity Source: UniProtKB-EC

    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    rRNA processing, tRNA processing

    Enzyme and pathway databases

    BioCyciYEAST:YBR167C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:POP7
    Synonyms:RPP2
    Ordered Locus Names:YBR167C
    ORF Names:YBR1219
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR167c.
    SGDiS000000371. POP7.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleolar ribonuclease P complex Source: SGD
    2. ribonuclease MRP complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 140140Ribonucleases P/MRP protein subunit POP7PRO_0000058519Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38291.
    PaxDbiP38291.

    Expressioni

    Gene expression databases

    GenevestigatoriP38291.

    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
    POP6P532183EBI-13670,EBI-13662

    Protein-protein interaction databases

    BioGridi32867. 109 interactions.
    DIPiDIP-5462N.
    IntActiP38291. 9 interactions.
    MINTiMINT-570982.
    STRINGi4932.YBR167C.

    Structurei

    Secondary structure

    1
    140
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 294
    Beta strandi32 – 343
    Helixi41 – 5818
    Beta strandi61 – 688
    Helixi69 – 713
    Helixi72 – 8413
    Beta strandi90 – 10213
    Beta strandi126 – 13914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IABX-ray2.70B1-140[»]
    ProteinModelPortaliP38291.
    SMRiP38291. Positions 14-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38291.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone-like Alba family.Curated

    Phylogenomic databases

    eggNOGiNOG45117.
    HOGENOMiHOG000248080.
    KOiK14526.
    OMAiMVSYVEL.
    OrthoDBiEOG7PGF3J.

    Family and domain databases

    InterProiIPR020241. RNase_P/MRP_POP7.
    [Graphical view]
    ProDomiPD085500. Ribonuclease_P/MRP_su_POP7. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    P38291-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALKKNTHNK STKRVTKHPS LKTLTHKQIH TTIFVKSTTP YVSALKRINK    50
    FLDSVHKQGS SYVAVLGMGK AVEKTLALGC HFQDQKNKKI EVYTKTIEVL 100
    DEVITEGQAD IDMESDVEDD DKETQLKKRA VSGVELRIYV 140
    Length:140
    Mass (Da):15,814
    Last modified:October 1, 1994 - v1
    Checksum:iB507BFDC7ED9C95C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921V → I in AAT92849. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055991 Genomic DNA. Translation: AAC24226.1.
    Z36036 Genomic DNA. Translation: CAA85128.1.
    AY692830 Genomic DNA. Translation: AAT92849.1.
    BK006936 Genomic DNA. Translation: DAA07283.1.
    PIRiS46038.
    RefSeqiNP_009726.3. NM_001178515.3.

    Genome annotation databases

    EnsemblFungiiYBR167C; YBR167C; YBR167C.
    GeneIDi852465.
    KEGGisce:YBR167C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055991 Genomic DNA. Translation: AAC24226.1 .
    Z36036 Genomic DNA. Translation: CAA85128.1 .
    AY692830 Genomic DNA. Translation: AAT92849.1 .
    BK006936 Genomic DNA. Translation: DAA07283.1 .
    PIRi S46038.
    RefSeqi NP_009726.3. NM_001178515.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IAB X-ray 2.70 B 1-140 [» ]
    ProteinModelPortali P38291.
    SMRi P38291. Positions 14-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32867. 109 interactions.
    DIPi DIP-5462N.
    IntActi P38291. 9 interactions.
    MINTi MINT-570982.
    STRINGi 4932.YBR167C.

    Proteomic databases

    MaxQBi P38291.
    PaxDbi P38291.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR167C ; YBR167C ; YBR167C .
    GeneIDi 852465.
    KEGGi sce:YBR167C.

    Organism-specific databases

    CYGDi YBR167c.
    SGDi S000000371. POP7.

    Phylogenomic databases

    eggNOGi NOG45117.
    HOGENOMi HOG000248080.
    KOi K14526.
    OMAi MVSYVEL.
    OrthoDBi EOG7PGF3J.

    Enzyme and pathway databases

    BioCyci YEAST:YBR167C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38291.
    NextBioi 971411.

    Gene expression databases

    Genevestigatori P38291.

    Family and domain databases

    InterProi IPR020241. RNase_P/MRP_POP7.
    [Graphical view ]
    ProDomi PD085500. Ribonuclease_P/MRP_su_POP7. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. "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].

    Entry informationi

    Entry nameiPOP7_YEAST
    AccessioniPrimary (citable) accession number: P38291
    Secondary accession number(s): D6VQG3, E9P8X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3