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Q08162

- RRP44_YEAST

UniProt

Q08162 - RRP44_YEAST

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Protein

Exosome complex exonuclease DIS3

Gene
DIS3, RRP44, YOL021C, O2197
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Cytoplasm. Mitochondrion. Nucleusnucleolus 3 Publications

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
Complete GO annotation...

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 GSP1.5 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.

Miscellaneous databases

EvolutionaryTraceiQ08162.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini904 – 100198S1 motifAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the RNR ribonuclease family.
Contains 1 S1 motif domain.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 122 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.
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 (1 Publication) that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (1 Publication and 1 Publication) that only this DIS3/RRP44 subunit of the exosome core has this activity.

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

Similar proteinsi