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Q08162

- RRP44_YEAST

UniProt

Q08162 - RRP44_YEAST

Protein

Exosome complex exonuclease DIS3

Gene

DIS3

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 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    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. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by DIS3. Plays a role in mitotic control.3 Publications

    Cofactori

    Mg2+.1 Publication

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: SGD
    2. endoribonuclease activity Source: SGD
    3. protein binding Source: IntAct
    4. tRNA binding Source: SGD

    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. ncRNA 3'-end processing Source: SGD
    3. nonfunctional rRNA decay Source: SGD
    4. nuclear mRNA surveillance Source: SGD
    5. nuclear polyadenylation-dependent CUT catabolic process Source: SGD
    6. nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
    7. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
    8. nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
    9. nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
    10. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
    11. polyadenylation-dependent snoRNA 3'-end processing Source: SGD
    12. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    13. rRNA catabolic process Source: SGD

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33437-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exosome complex exonuclease DIS3 (EC:3.1.13.-, EC:3.1.26.-)
    Alternative name(s):
    Chromosome disjunction protein 3
    Ribosomal RNA-processing protein 44
    Gene namesi
    Name:DIS3
    Synonyms:RRP44
    Ordered Locus Names:YOL021C
    ORF Names:O2197
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL021c.
    SGDiS000005381. DIS3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic exosome (RNase complex) Source: SGD
    2. mitochondrion Source: UniProtKB-SubCell
    3. nuclear exosome (RNase complex) Source: SGD
    4. nucleolus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Exosome, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471C → S: Slow growth; when associated with S-52 and S-55. 1 Publication
    Mutagenesisi52 – 521C → S: Slow growth; when associated with S-47 and S-55. 1 Publication
    Mutagenesisi55 – 551C → S: Slow growth; when associated with S-47 and S-52. 1 Publication
    Mutagenesisi171 – 1711D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication
    Mutagenesisi198 – 1981D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication
    Mutagenesisi551 – 5511D → N: Exoribonucleolytic activity abolished. Accumulation of partially processed 5.8S rRNA and partially degraded 5' ETS. No growth; when associated with A-171. No growth; when associated with A-198. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10011001Exosome complex exonuclease DIS3PRO_0000166423Add
    BLAST

    Proteomic databases

    MaxQBiQ08162.
    PaxDbiQ08162.
    PeptideAtlasiQ08162.
    PRIDEiQ08162.

    Expressioni

    Gene expression databases

    GenevestigatoriQ08162.

    Interactioni

    Subunit structurei

    Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate 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. DIS3 associates at the respective bottom side with Exo-9. Interacts with GSP1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RRP4P387926EBI-1740,EBI-1757
    RRP40Q082854EBI-1740,EBI-1831
    RRP46P532566EBI-1740,EBI-1842
    SKI6P4694810EBI-1740,EBI-1788

    Protein-protein interaction databases

    BioGridi34381. 61 interactions.
    DIPiDIP-2355N.
    IntActiQ08162. 21 interactions.
    MINTiMINT-614156.
    STRINGi4932.YOL021C.

    Structurei

    Secondary structure

    1
    1001
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 2811
    Beta strandi31 – 4313
    Beta strandi49 – 513
    Helixi55 – 573
    Turni80 – 834
    Beta strandi84 – 907
    Helixi92 – 976
    Turni99 – 1024
    Turni105 – 1073
    Beta strandi110 – 1145
    Helixi115 – 12410
    Helixi126 – 13712
    Beta strandi144 – 1485
    Turni150 – 1523
    Turni154 – 1563
    Helixi166 – 18419
    Helixi186 – 1883
    Beta strandi190 – 1956
    Helixi199 – 2068
    Beta strandi214 – 2163
    Helixi218 – 2225
    Helixi228 – 2314
    Helixi232 – 2343
    Helixi261 – 2699
    Beta strandi272 – 2809
    Beta strandi282 – 2843
    Beta strandi287 – 2904
    Beta strandi293 – 2975
    Beta strandi299 – 3035
    Helixi304 – 3074
    Beta strandi315 – 3206
    Helixi323 – 3253
    Turni336 – 3383
    Helixi367 – 38317
    Beta strandi385 – 3873
    Beta strandi389 – 3979
    Beta strandi402 – 4076
    Helixi409 – 4113
    Beta strandi420 – 4289
    Beta strandi434 – 4385
    Helixi441 – 4444
    Beta strandi447 – 4559
    Beta strandi464 – 47512
    Helixi478 – 48710
    Helixi497 – 5004
    Helixi507 – 5093
    Helixi519 – 5246
    Helixi526 – 5305
    Beta strandi531 – 5333
    Beta strandi540 – 5467
    Beta strandi552 – 5587
    Beta strandi564 – 5718
    Helixi573 – 5764
    Beta strandi579 – 5813
    Helixi582 – 5909
    Beta strandi594 – 5963
    Beta strandi599 – 6013
    Helixi606 – 6094
    Turni610 – 6123
    Beta strandi619 – 63012
    Beta strandi636 – 65318
    Helixi654 – 6629
    Beta strandi663 – 6653
    Helixi669 – 69022
    Beta strandi701 – 7055
    Beta strandi707 – 7104
    Beta strandi712 – 7176
    Helixi722 – 74524
    Turni747 – 7493
    Beta strandi751 – 7555
    Helixi760 – 7634
    Helixi764 – 77411
    Helixi783 – 7919
    Helixi801 – 81010
    Beta strandi817 – 8204
    Helixi821 – 8233
    Helixi826 – 8294
    Turni832 – 8354
    Beta strandi836 – 8383
    Turni845 – 8473
    Helixi849 – 86113
    Helixi869 – 8724
    Helixi874 – 90835
    Beta strandi912 – 92211
    Beta strandi925 – 9295
    Turni931 – 9333
    Beta strandi936 – 9405
    Helixi941 – 9444
    Helixi948 – 9503
    Beta strandi952 – 9543
    Turni955 – 9584
    Beta strandi959 – 9624
    Beta strandi971 – 9744
    Beta strandi978 – 9836
    Beta strandi985 – 9873
    Turni989 – 9913
    Beta strandi995 – 9973
    Beta strandi998 – 10003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VNUX-ray2.30D242-1001[»]
    2WP8X-ray3.00J25-1001[»]
    4IFDX-ray2.80J1-1001[»]
    ProteinModelPortaliQ08162.
    SMRiQ08162. Positions 9-1001.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08162.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini904 – 100198S1 motifPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 235235EndoribonucleaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RNR ribonuclease family.Curated
    Contains 1 S1 motif domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0557.
    GeneTreeiENSGT00530000063106.
    HOGENOMiHOG000191945.
    KOiK12585.
    OMAiENANDRN.
    OrthoDBiEOG7FR7R3.

    Family and domain databases

    Gene3Di3.40.50.1010. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR022967. RNA-binding_domain_S1.
    IPR022966. RNase_II/R_CS.
    [Graphical view]
    PfamiPF13638. PIN_4. 1 hit.
    [Graphical view]
    SMARTiSM00670. PINc. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 4 hits.
    SSF88723. SSF88723. 1 hit.
    PROSITEiPS01175. RIBONUCLEASE_II. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q08162-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVPAIAPRR KRLADGLSVT QKVFVRSRNG GATKIVREHY LRSDIPCLSR     50
    SCTKCPQIVV PDAQNELPKF ILSDSPLELS APIGKHYVVL DTNVVLQAID 100
    LLENPNCFFD VIVPQIVLDE VRNKSYPVYT RLRTLCRDSD DHKRFIVFHN 150
    EFSEHTFVER LPNETINDRN DRAIRKTCQW YSEHLKPYDI NVVLVTNDRL 200
    NREAATKEVE SNIITKSLVQ YIELLPNADD IRDSIPQMDS FDKDLERDTF 250
    SDFTFPEYYS TARVMGGLKN GVLYQGNIQI SEYNFLEGSV SLPRFSKPVL 300
    IVGQKNLNRA FNGDQVIVEL LPQSEWKAPS SIVLDSEHFD VNDNPDIEAG 350
    DDDDNNESSS NTTVISDKQR RLLAKDAMIA QRSKKIQPTA KVVYIQRRSW 400
    RQYVGQLAPS SVDPQSSSTQ NVFVILMDKC LPKVRIRTRR AAELLDKRIV 450
    ISIDSWPTTH KYPLGHFVRD LGTIESAQAE TEALLLEHDV EYRPFSKKVL 500
    ECLPAEGHDW KAPTKLDDPE AVSKDPLLTK RKDLRDKLIC SIDPPGCVDI 550
    DDALHAKKLP NGNWEVGVHI ADVTHFVKPG TALDAEGAAR GTSVYLVDKR 600
    IDMLPMLLGT DLCSLKPYVD RFAFSVIWEL DDSANIVNVN FMKSVIRSRE 650
    AFSYEQAQLR IDDKTQNDEL TMGMRALLKL SVKLKQKRLE AGALNLASPE 700
    VKVHMDSETS DPNEVEIKKL LATNSLVEEF MLLANISVAR KIYDAFPQTA 750
    MLRRHAAPPS TNFEILNEML NTRKNMSISL ESSKALADSL DRCVDPEDPY 800
    FNTLVRIMST RCMMAAQYFY SGAYSYPDFR HYGLAVDIYT HFTSPIRRYC 850
    DVVAHRQLAG AIGYEPLSLT HRDKNKMDMI CRNINRKHRN AQFAGRASIE 900
    YYVGQVMRNN ESTETGYVIK VFNNGIVVLV PKFGVEGLIR LDNLTEDPNS 950
    AAFDEVEYKL TFVPTNSDKP RDVYVFDKVE VQVRSVMDPI TSKRKAELLL 1000
    K 1001
    Length:1,001
    Mass (Da):113,707
    Last modified:November 1, 1997 - v1
    Checksum:i00DD31BD2D6904F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D76430 Genomic DNA. Translation: BAA11176.1.
    Z74763 Genomic DNA. Translation: CAA99021.1.
    BK006948 Genomic DNA. Translation: DAA10760.1.
    PIRiS66704.
    RefSeqiNP_014621.1. NM_001183275.1.

    Genome annotation databases

    EnsemblFungiiYOL021C; YOL021C; YOL021C.
    GeneIDi854138.
    KEGGisce:YOL021C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D76430 Genomic DNA. Translation: BAA11176.1 .
    Z74763 Genomic DNA. Translation: CAA99021.1 .
    BK006948 Genomic DNA. Translation: DAA10760.1 .
    PIRi S66704.
    RefSeqi NP_014621.1. NM_001183275.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VNU X-ray 2.30 D 242-1001 [» ]
    2WP8 X-ray 3.00 J 25-1001 [» ]
    4IFD X-ray 2.80 J 1-1001 [» ]
    ProteinModelPortali Q08162.
    SMRi Q08162. Positions 9-1001.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34381. 61 interactions.
    DIPi DIP-2355N.
    IntActi Q08162. 21 interactions.
    MINTi MINT-614156.
    STRINGi 4932.YOL021C.

    Proteomic databases

    MaxQBi Q08162.
    PaxDbi Q08162.
    PeptideAtlasi Q08162.
    PRIDEi Q08162.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL021C ; YOL021C ; YOL021C .
    GeneIDi 854138.
    KEGGi sce:YOL021C.

    Organism-specific databases

    CYGDi YOL021c.
    SGDi S000005381. DIS3.

    Phylogenomic databases

    eggNOGi COG0557.
    GeneTreei ENSGT00530000063106.
    HOGENOMi HOG000191945.
    KOi K12585.
    OMAi ENANDRN.
    OrthoDBi EOG7FR7R3.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33437-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q08162.
    NextBioi 975871.
    PROi Q08162.

    Gene expression databases

    Genevestigatori Q08162.

    Family and domain databases

    Gene3Di 3.40.50.1010. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR003029. Rbsml_prot_S1_RNA-bd_dom.
    IPR022967. RNA-binding_domain_S1.
    IPR022966. RNase_II/R_CS.
    [Graphical view ]
    Pfami PF13638. PIN_4. 1 hit.
    [Graphical view ]
    SMARTi SM00670. PINc. 1 hit.
    SM00316. S1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 4 hits.
    SSF88723. SSF88723. 1 hit.
    PROSITEi PS01175. RIBONUCLEASE_II. 1 hit.
    PS50126. S1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1."
      Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N., Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.
      EMBO J. 15:5595-5605(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH GSP1.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(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. "The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases."
      Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D.
      Cell 91:457-466(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
    5. "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: IDENTIFICATION IN THE EXOSOME COMPLEX BY MASS SPECTROMETRY.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    9. "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: EXOSOME EXONUCLEASE ACTIVITY, SUBUNIT.
    10. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
      Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
      J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. "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, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, INTERACTION OF THE EXOSOME WITH RRP6 AND SKI7, SUBUNIT, MUTAGENESIS OF ASP-551.
    12. "The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities."
      Schaeffer D., Tsanova B., Barbas A., Reis F.P., Dastidar E.G., Sanchez-Rotunno M., Arraiano C.M., van Hoof A.
      Nat. Struct. Mol. Biol. 16:56-62(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY AS ENDONUCLEASE, MUTAGENESIS OF CYS-47; CYS-52; CYS-55; ASP-171; ASP-198 AND ASP-551.
    13. "Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family."
      Lorentzen E., Basquin J., Tomecki R., Dziembowski A., Conti E.
      Mol. Cell 29:717-728(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 242-1001 IN COMPLEX WITH SINGLE-STRANDED RNA AND MAGNESIUM ION, MUTAGENESIS OF ASP-551.
    14. "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 RRP45.

    Entry informationi

    Entry nameiRRP44_YEAST
    AccessioniPrimary (citable) accession number: Q08162
    Secondary accession number(s): D6W244
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 123 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 606 molecules/cell in log phase SD medium.1 Publication
    Mn2+ doesn't support the hydrolytic activity. Activity is KCl or NaCl dependent and activity is slightly increased in the presence of reducing agents such as DTT or beta-mercaptoethanol and doesn't vary notably between pH 6.8 and 8.8.

    Caution

    It was originally thought that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only this DIS3/RRP44 subunit of the exosome core has this activity.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. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3