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P46948 (RRP41_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 110. 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:
Exosome complex component SKI6
Alternative name(s):
Extracellular mutant protein 20
Ribosomal RNA-processing protein 41
Superkiller protein 6
Gene names
Name:SKI6
Synonyms:ECM20, RRP41
Ordered Locus Names:YGR195W
ORF Names:G7587
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 anti-sense 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. SKI6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation. Ref.5 Ref.11

Subunit structure

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. Ref.5 Ref.11

Subcellular location

Cytoplasm. Nucleusnucleolus Ref.7.

Miscellaneous

Present with 5150 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the RNase PH family.

Caution

Was originally (Ref.5) thought to have exonuclease activity but it was later shown (Ref.11 and Ref.9) that only DIS3/RRP44 subunit of the exosome core has this activity.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   LigandRNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processU1 snRNA 3'-end processing

Inferred from mutant phenotype. Source: SGD

U4 snRNA 3'-end processing

Inferred from mutant phenotype. Source: SGD

U5 snRNA 3'-end processing

Inferred from mutant phenotype. Source: SGD

exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.5. Source: SGD

nonfunctional rRNA decay

Inferred by curator Ref.6. Source: SGD

nuclear mRNA surveillance

Inferred from mutant phenotype. Source: SGD

nuclear polyadenylation-dependent CUT catabolic process

Inferred from mutant phenotype. Source: SGD

nuclear polyadenylation-dependent mRNA catabolic process

Inferred by curator Ref.6. Source: SGD

nuclear polyadenylation-dependent tRNA catabolic process

Inferred from direct assay. Source: SGD

nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay

Inferred from mutant phenotype. Source: SGD

nuclear-transcribed mRNA catabolic process, non-stop decay

Inferred by curator Ref.6. Source: SGD

polyadenylation-dependent snoRNA 3'-end processing

Inferred from mutant phenotype. Source: SGD

   Cellular componentcytoplasmic exosome (RNase complex)

Inferred from direct assay Ref.6. Source: SGD

nuclear exosome (RNase complex)

Inferred from direct assay Ref.6. Source: SGD

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DIS3Q081629EBI-1788,EBI-1740

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Exosome complex component SKI6
PRO_0000139962

Experimental info

Mutagenesis62 – 632KS → ED: Impairs RNA-binding (at the proposed ring entry site). Ref.12
Mutagenesis95 – 962RR → EE: Impairs RNA-binding (at the proposed ring exit site). Ref.12

Secondary structure

............................. 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46948 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C80EFFB528A43044

FASTA24627,561
        10         20         30         40         50         60 
MSRLEIYSPE GLRLDGRRWN ELRRFESSIN THPHAADGSS YMEQGNNKII TLVKGPKEPR 

        70         80         90        100        110        120 
LKSQMDTSKA LLNVSVNITK FSKFERSKSS HKNERRVLEI QTSLVRMFEK NVMLNIYPRT 

       130        140        150        160        170        180 
VIDIEIHVLE QDGGIMGSLI NGITLALIDA GISMFDYISG ISVGLYDTTP LLDTNSLEEN 

       190        200        210        220        230        240 
AMSTVTLGVV GKSEKLSLLL VEDKIPLDRL ENVLAIGIAG AHRVRDLMDE ELRKHAQKRV 


SNASAR 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of a 9000 bp fragment of the right arm of Saccharomyces cerevisiae chromosome VII contains four previously unknown open reading frames."
Guerreiro P., Maia e Silva A., Barreiros T., Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Rodrigues-Pousada C., Nombela C.
Yeast 11:1087-1091(1995) [PubMed: 7502584] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[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: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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: 9390555] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT.
[6]"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: 10465791] [Abstract]
Cited for: IDENTIFICATION IN THE RNA EXOSOME COMPLEX BY MASS SPECTROMETRY.
[7]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Reconstitution, activities, and structure of the eukaryotic RNA exosome."
Liu Q., Greimann J.C., Lima C.D.
Cell 127:1223-1237(2006) [PubMed: 17174896] [Abstract]
Cited for: RECONSTITUTION OF THE RNA EXOSOME COMPLEX, LACK OF EXONUCLEASE ACTIVITY.
[10]Erratum
Liu Q., Greimann J.C., Lima C.D.
Cell 131:188-189(2007)
[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: 17173052] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME COMPLEX, SUBUNIT.
[12]"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: 19879841] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH RRP45 AND DIS3, MUTAGENESIS OF 62-LYS-SER-63 AND 95-ARG-ARG-96.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82775 Genomic DNA. Translation: CAA58018.1.
Z72980 Genomic DNA. Translation: CAA97221.1.
Z72981 Genomic DNA. Translation: CAA97223.1.
AY558509 Genomic DNA. Translation: AAS56835.1.
BK006941 Genomic DNA. Translation: DAA08288.1.
PIRS59180.
RefSeqNP_011711.1. NM_001181324.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WP8X-ray3.00B1-246[»]
ProteinModelPortalP46948.
SMRP46948. Positions 3-239.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2083N.
IntActP46948. 24 interactions.
MINTMINT-555587.
STRINGP46948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR195W; YGR195W; YGR195W.
GeneID853109.
KEGGsce:YGR195W.
NMPDRfig|4932.3.peg.2838.

Organism-specific databases

CYGDYGR195w.
SGDS000003427. SKI6.

Phylogenomic databases

eggNOGfuNOG04193.
GeneTreeEFGT00050000004219.
HOGENOMHBG737187.
OMAHMAPFST.
OrthoDBEOG45MRFG.

Gene expression databases

ArrayExpressP46948.
GenevestigatorP46948.
GermOnlineYGR195W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
KOK11600.
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF55666. 3_ExoRNase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
ProtoNetSearch...

Other

NextBio973121.

Entry information

Entry nameRRP41_YEAST
AccessionPrimary (citable) accession number: P46948
Secondary accession number(s): D6VUX7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 14, 2011
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families