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Reviewed, UniProtKB/Swiss-Prot Q755F7 (CET1_ASHGO)

Last modified November 3, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CET1
Ordered Locus Names: AFL134W
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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 By similarity.

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
Gene Ontology (GO)
   Biological processmRNA capping

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmRNA cap methyltransferase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionpolynucleotide 5'-phosphatase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478mRNA-capping enzyme subunit beta
PRO_0000210111

Sequences

Sequence LengthMass (Da)Tools
Q755F7-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1D734613FA2401FC

FASTA47853,999
        10         20         30         40         50         60 
MSSEKQEGSP RRVLSLSDLV NREDSKDASG NTAGAALKPL SNDEVRRRLA HEDYSSNTVS 

        70         80         90        100        110        120 
QVDDETDTDD GLGEVAFDRA DFRFDFEGHQ RSGGRASGEA EAESGGPGHE KATQQPSDAI 

       130        140        150        160        170        180 
ATSPDRESTE PRAMDIFEER ASLESKKNNL RKDLRVLNEI ASTARPGRYK VAPIWAQKWK 

       190        200        210        220        230        240 
PTVRALQNVN SKDLMKIDVS FTQVIPDDDL TKSVQDWVYA TLLSIPPEQR QYVEVEMKFG 

       250        260        270        280        290        300 
ILMDRSSDSQ RVTPPVSSQT VYMEADARMK PDVDERVFVE LNRYVKGISE LTENTGKFNI 

       310        320        330        340        350        360 
IESHNKDEMY RAGINTQRPR FLRMSKDVKT GRVGEFIEKR RISQLLLFSP KDSYDVKISI 

       370        380        390        400        410        420 
NVELPVPEND PPEKYMGQAP LNSRTKERIS YIHNDSCTRI DITKVTNHNK GKRDDAEVTH 

       430        440        450        460        470 
EIELELNSQA LLAAFDKIAQ DSKDYATIVR TFLNNGTIIR RKLTSLSYEI FEGGKKVV 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

Cross-references

Sequence databases

AE016819 Genomic DNA. Translation: AAS53240.1.
RefSeqNP_985416.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ755F7.

Genome annotation databases

GeneID4621643.
GenomeReviewsGene locus AFL134W in contig AE016819_GR.
KEGGago:AGOS_AFL134W.
NMPDRfig|33169.1.peg.3061.

Organism-specific databases

AGDAFL134W.

Phylogenomic databases

OMAVELEINT.

Enzyme and pathway databases

BRENDA3.1.3.33. 279361.

Family and domain databases

InterProIPR004206. mRNA_capping_enz_bsu.
[Graphical view]
Gene3DG3DSA:3.20.100.10. mRNA_capping_enz_bsu. 1 hit.
PfamPF02940. mRNA_triPase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCET1_ASHGO
AccessionPrimary (citable) accession number: Q755F7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents