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O74918 (RRP45_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Exosome complex component rrp45
Alternative name(s):
Ribosomal RNA-processing protein 45
Gene names
Name:rrp45
ORF Names:SPCC757.08
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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. 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 By similarity.

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 By similarity.

Subcellular location

Cytoplasm. Nucleus › nucleolus Ref.2.

Sequence similarities

Belongs to the RNase PH family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Exosome
Nucleus
   LigandRNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processexonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from sequence orthology. Source: PomBase

nonfunctional rRNA decay

Inferred from sequence orthology. Source: PomBase

nuclear polyadenylation-dependent mRNA catabolic process

Inferred from sequence orthology. Source: PomBase

nuclear polyadenylation-dependent rRNA catabolic process

Inferred from sequence orthology. Source: PomBase

nuclear polyadenylation-dependent tRNA catabolic process

Inferred from sequence orthology. Source: PomBase

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

Inferred from sequence orthology. Source: PomBase

nuclear-transcribed mRNA catabolic process, non-stop decay

Inferred from sequence orthology. Source: PomBase

   Cellular_componentcytoplasmic exosome (RNase complex)

Inferred from sequence orthology. Source: PomBase

cytosol

Inferred from direct assay Ref.2. Source: PomBase

nuclear exosome (RNase complex)

Inferred from sequence orthology. Source: PomBase

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3'-5'-exoribonuclease activity

Inferred from sequence orthology. Source: PomBase

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Exosome complex component rrp45
PRO_0000139973

Sequences

Sequence LengthMass (Da)Tools
O74918 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: DA0E97C737EC3EAC

FASTA29132,378
        10         20         30         40         50         60 
MSRHLETSLN NKEFVLNSLE KGLRLDGRQL SDFRSLEIQF GKEYGQVDVS FGHTRVMARI 

        70         80         90        100        110        120 
TTEITKPYTD RPFDGIFSIT TELTPLAYSA FEAGRVSDQE IVISRLIEKA VRRSNALDTE 

       130        140        150        160        170        180 
SLCIISGQKC WHVRASVHFI NHDGNLVDAA CIAVIAALCH FRRPELTVVG EEVTVHPVEE 

       190        200        210        220        230        240 
RVPVPLSILH MPICVTFSFF NNGELAIVDA TLEEEDLCNG SMTITLNKNR EVCQIYKAGG 

       250        260        270        280        290 
IIIDPSKIIS CAKTAFDIAV SVCSVIQQAL DEDLRKKETQ YLGGSAENER S

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA21233.1.
PIRT41599.
RefSeqNP_587683.1. NM_001022678.2.

3D structure databases

ProteinModelPortalO74918.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPCC757.08-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC757.08.1; SPCC757.08.1:pep; SPCC757.08.
GeneID2539106.
KEGGspo:SPCC757.08.

Organism-specific databases

PomBaseSPCC757.08.

Phylogenomic databases

eggNOGCOG2123.
HOGENOMHOG000229504.
KOK03678.
OMALIDASCI.
OrthoDBEOG4X0R2H.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
ProtoNetSearch...

Other

NextBio20800278.

Entry information

Entry nameRRP45_SCHPO
AccessionPrimary (citable) accession number: O74918
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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