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Q05636

- RRP45_YEAST

UniProt

Q05636 - RRP45_YEAST

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Protein

Exosome complex component RRP45

Gene
RRP45, YDR280W, D9954.1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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. Nucleusnucleolus 1 Publication

GO - Cellular componenti

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

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 LRP1.3 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.

Miscellaneous databases

EvolutionaryTraceiQ05636.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 120 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.

Caution

According to 1 Publication and 1 Publication, only DIS3/RRP44 subunit of the exosome core has exonuclease 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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