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Q05636

- RRP45_YEAST

UniProt

Q05636 - RRP45_YEAST

Protein

Exosome complex component RRP45

Gene

RRP45

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP45 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
    2. nonfunctional rRNA decay Source: SGD
    3. nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
    4. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
    5. nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
    6. nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
    7. nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' Source: SGD
    8. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
    9. polyadenylation-dependent snoRNA 3'-end processing Source: SGD
    10. U1 snRNA 3'-end processing Source: SGD
    11. U4 snRNA 3'-end processing Source: SGD
    12. U5 snRNA 3'-end processing Source: SGD

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29845-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex component RRP45
    Alternative name(s):
    Ribosomal RNA-processing protein 45
    Gene namesi
    Name:RRP45
    Ordered Locus Names:YDR280W
    ORF Names:D9954.1
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR280w.
    SGDiS000002688. RRP45.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytoplasmic exosome (RNase complex) Source: SGD
    2. nuclear exosome (RNase complex) Source: SGD
    3. nucleolus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Exosome complex component RRP45PRO_0000139974Add
    BLAST

    Proteomic databases

    MaxQBiQ05636.
    PaxDbiQ05636.
    PeptideAtlasiQ05636.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05636.

    Interactioni

    Subunit structurei

    Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. Interacts with LRP1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSL4P538597EBI-1810,EBI-1731
    SKI6P469488EBI-1810,EBI-1788

    Protein-protein interaction databases

    BioGridi32333. 38 interactions.
    DIPiDIP-2084N.
    IntActiQ05636. 28 interactions.
    MINTiMINT-555570.
    STRINGi4932.YDR280W.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2012
    Beta strandi36 – 405
    Beta strandi46 – 516
    Beta strandi54 – 6512
    Beta strandi76 – 805
    Helixi85 – 873
    Helixi99 – 11113
    Turni112 – 1165
    Helixi120 – 1234
    Beta strandi124 – 1263
    Turni127 – 1293
    Beta strandi130 – 14213
    Helixi147 – 16115
    Beta strandi167 – 1704
    Beta strandi173 – 1764
    Turni179 – 1813
    Beta strandi194 – 2018
    Helixi206 – 2105
    Beta strandi218 – 2225
    Helixi225 – 2284
    Beta strandi232 – 2409
    Turni241 – 2433
    Beta strandi244 – 2507
    Beta strandi252 – 2543
    Helixi258 – 29942

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WP8X-ray3.00A1-305[»]
    4IFDX-ray2.80A2-305[»]
    ProteinModelPortaliQ05636.
    SMRiQ05636. Positions 2-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05636.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RNase PH family.Curated

    Phylogenomic databases

    eggNOGiCOG2123.
    GeneTreeiENSGT00530000063093.
    HOGENOMiHOG000229504.
    KOiK03678.
    OMAiCWSVRVD.
    OrthoDBiEOG79CZ8V.

    Family and domain databases

    InterProiIPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PfamiPF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF55666. SSF55666. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q05636-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKDIEISAS ESKFILEALR QNYRLDGRSF DQFRDVEITF GKEFGDVSVK    50
    MGNTKVHCRI SCQIAQPYED RPFEGLFVIS TEISPMAGSQ FENGNITGED 100
    EVLCSRIIEK SVRRSGALDV EGLCIVAGSK CWAVRADVHF LDCDGGFIDA 150
    SCIAVMAGLM HFKKPDITVH GEQIIVHPVN EREPVPLGIL HIPICVTFSF 200
    FNPQDTEENI KGETNSEISI IDATLKEELL RDGVLTVTLN KNREVVQVSK 250
    AGGLPMDALT LMKCCHEAYS IIEKITDQIL QLLKEDSEKR NKYAAMLTSE 300
    NAREI 305
    Length:305
    Mass (Da):33,962
    Last modified:November 1, 1996 - v1
    Checksum:i65C9DB5A63678F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51030 Genomic DNA. Translation: AAB64446.1.
    AY557748 Genomic DNA. Translation: AAS56074.1.
    BK006938 Genomic DNA. Translation: DAA12120.1.
    PIRiS70136.
    RefSeqiNP_010566.1. NM_001180588.1.

    Genome annotation databases

    EnsemblFungiiYDR280W; YDR280W; YDR280W.
    GeneIDi851874.
    KEGGisce:YDR280W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51030 Genomic DNA. Translation: AAB64446.1 .
    AY557748 Genomic DNA. Translation: AAS56074.1 .
    BK006938 Genomic DNA. Translation: DAA12120.1 .
    PIRi S70136.
    RefSeqi NP_010566.1. NM_001180588.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WP8 X-ray 3.00 A 1-305 [» ]
    4IFD X-ray 2.80 A 2-305 [» ]
    ProteinModelPortali Q05636.
    SMRi Q05636. Positions 2-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32333. 38 interactions.
    DIPi DIP-2084N.
    IntActi Q05636. 28 interactions.
    MINTi MINT-555570.
    STRINGi 4932.YDR280W.

    Proteomic databases

    MaxQBi Q05636.
    PaxDbi Q05636.
    PeptideAtlasi Q05636.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR280W ; YDR280W ; YDR280W .
    GeneIDi 851874.
    KEGGi sce:YDR280W.

    Organism-specific databases

    CYGDi YDR280w.
    SGDi S000002688. RRP45.

    Phylogenomic databases

    eggNOGi COG2123.
    GeneTreei ENSGT00530000063093.
    HOGENOMi HOG000229504.
    KOi K03678.
    OMAi CWSVRVD.
    OrthoDBi EOG79CZ8V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29845-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q05636.
    NextBioi 969829.
    PROi Q05636.

    Gene expression databases

    Genevestigatori Q05636.

    Family and domain databases

    InterProi IPR001247. ExoRNase_PH_dom1.
    IPR015847. ExoRNase_PH_dom2.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    Pfami PF01138. RNase_PH. 1 hit.
    PF03725. RNase_PH_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 2 hits.
    SSF55666. SSF55666. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
      Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
      Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    5. Cited for: INTERACTION WITH LRP1.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
      Liu Q., Greimann J.C., Lima C.D.
      Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECONSTITUTION OF THE RNA EXOSOME COMPLEX, LACK OF EXONUCLEASE ACTIVITY.
    9. Erratum
      Liu Q., Greimann J.C., Lima C.D.
      Cell 131:188-189(2007)
    10. "A single subunit, Dis3, is essentially responsible for yeast exosome core activity."
      Dziembowski A., Lorentzen E., Conti E., Seraphin B.
      Nat. Struct. Mol. Biol. 14:15-22(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME COMPLEX, SUBUNIT.
    11. "The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation."
      Bonneau F., Basquin J., Ebert J., Lorentzen E., Conti E.
      Cell 139:547-559(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SKI6 AND DIS3.

    Entry informationi

    Entry nameiRRP45_YEAST
    AccessioniPrimary (citable) accession number: Q05636
    Secondary accession number(s): D6VSR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 121 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 4800 molecules/cell in log phase SD medium.1 Publication

    Caution

    According to PubMed:17173052 and PubMed:17174896, only DIS3/RRP44 subunit of the exosome core has exonuclease activity.Curated

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

    External Data

    Dasty 3