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Q9P6Q6 (CET1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
mRNA-capping enzyme subunit beta

EC=3.1.3.33
Alternative name(s):
Polynucleotide 5'-triphosphatase
mRNA 5'-triphosphatase
Short name=TPase
Gene names
Name:pct1
ORF Names:SPAC644.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. Ref.2

Catalytic activity

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.

Cofactor

Divalent ions By similarity.

Subunit structure

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase. Ref.2

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the fungal TPase family.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentNucleus
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmRNA capping

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentmRNA cap methyltransferase complex

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Molecular functionpolynucleotide 5'-phosphatase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

protein homodimerization activity

Inferred from direct assay. Source: GeneDB_Spombe

transferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cdk9Q96WV92EBI-443547,EBI-443557

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303mRNA-capping enzyme subunit beta
PRO_0000210117

Sequences

Sequence LengthMass (Da)Tools
Q9P6Q6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 51A5A112CE927AED

FASTA30335,444
        10         20         30         40         50         60 
MDLKGLLHEE NELPSIEKRK IDENAVEHDK VERKRTKSVA VPKIEMNFLN KPIVPDTTKV 

        70         80         90        100        110        120 
ISNFLTHYLI TEPVEHVEIE AKLGTLIDLE TQNRFEFPVM NETILNPEFN LRTRFESDMT 

       130        140        150        160        170        180 
ASEHKYLNEF LNQAFRDSQK PGRLPFAYKH TKQVDLFYET EDNSRDKIRV SKNQSDNQVL 

       190        200        210        220        230        240 
ACVKKRRVAD LFLYCPNDAF DIRISISDEL PVSMPSGNQQ PSLTRLKDRV GYVHQEIKID 

       250        260        270        280        290        300 
LTKTTQNDPV YDTTERHELE VEFGNIADLR DRAQKAKDGM EAPLFRRVQL FMDNVRILRR 


EHS 

« Hide

References

« Hide 'large scale' 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases."
Hausmann S., Pei Y., Shuman S.
J. Biol. Chem. 278:30487-30496(2003) [PubMed: 12788946] [Abstract]
Cited for: FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB90131.1.
RefSeqNP_593872.1. NM_001019302.1.

3D structure databases

ProteinModelPortalQ9P6Q6.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9P6Q6. 2 interactions.
STRINGQ9P6Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC644.04.1; SPAC644.04.1:pep; SPAC644.04.
GeneID2543671.
GenomeReviewsGene locus pct1 in contig CU329670_GR.
KEGGspo:SPAC644.04.
NMPDRfig|4896.1.peg.3842.

Organism-specific databases

GeneDB_SpombeSPAC644.04.

Phylogenomic databases

eggNOGfuNOG08284.
GeneTreeEFGT00050000000198.
OMAVEPLDEF.
OrthoDBEOG42Z80Z.

Gene expression databases

ArrayExpressQ9P6Q6.

Family and domain databases

InterProIPR023577. CYTH-like_domain.
IPR004206. mRNA_capping_enz_bsu_dom.
[Graphical view]
Gene3DG3DSA:3.20.100.10. mRNA_capping_enz_bsu. 1 hit.
KOK01098.
PfamPF02940. mRNA_triPase. 1 hit.
[Graphical view]
SUPFAMSSF55154. mRNA_capping_enz_bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCET1_SCHPO
AccessionPrimary (citable) accession number: Q9P6Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 1, 2000
Last modified: December 14, 2011
This is version 57 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