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Q9UU90 (POP5_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. 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:
Ribonucleases P/MRP protein subunit POP5

EC=3.1.26.5
Gene names
ORF Names:SPCC830.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences By similarity.

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from sequence orthology. Source: PomBase

tRNA processing

Inferred from sequence orthology. Source: PomBase

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleolar ribonuclease P complex

Inferred from sequence orthology. Source: PomBase

ribonuclease MRP complex

Inferred from sequence orthology. Source: PomBase

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Ribonucleases P/MRP protein subunit POP5
PRO_0000140014

Sequences

Sequence LengthMass (Da)Tools
Q9UU90 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3E581179B769E589

FASTA13915,680
        10         20         30         40         50         60 
MVRFKSRYLL FEVLYPEAKE FFDYPTIPSD SSITTSSLSK IIRTMVAENF GDVGIGKVAS 

        70         80         90        100        110        120 
SLTVKYFSPN TSTGILRVSR QHFRLAWAAL VLIRELYGKP VIIRVVRVSG TIKKAELAAI 

       130 
ERNKSEIHNI SLMDEPIEV 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAB52882.1.
PIRT41635.
RefSeqNP_588479.1. NM_001023470.2.

3D structure databases

ProteinModelPortalQ9UU90.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPCC830.09c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC830.09c.1; SPCC830.09c.1:pep; SPCC830.09c.
GeneID2538895.
KEGGspo:SPCC830.09c.

Organism-specific databases

PomBaseSPCC830.09c.

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000216538.
KOK03537.
OMAITKLCII.
OrthoDBEOG4M9522.

Family and domain databases

InterProIPR002759. RNase_P/MRP_subunit.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800074.

Entry information

Entry namePOP5_SCHPO
AccessionPrimary (citable) accession number: Q9UU90
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 64 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