Essential maintenance is planned to begin on Tue Jan 28 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ during this time.

Q2UGU4 · Q2UGU4_ASPOR

Function

function

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentmRNA capping enzyme complex
Molecular Functionpolynucleotide 5'-phosphatase activity
Biological Process7-methylguanosine mRNA capping
Biological Processpolynucleotide 5' dephosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    mRNA-capping enzyme subunit beta
  • EC number
  • Alternative names
    • mRNA 5'-phosphatase
    • mRNA 5'-triphosphate monophosphatase

Gene names

    • ORF names
      AO090023000709

Organism names

Accessions

  • Primary accession
    Q2UGU4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-378Disordered
Compositional bias7-32Polar residues
Compositional bias68-155Polar residues
Compositional bias163-218Polar residues
Compositional bias231-250Polar residues
Compositional bias264-339Polar residues
Compositional bias412-429Polar residues
Region412-452Disordered
Compositional bias430-446Pro residues
Domain465-711mRNA triphosphatase Cet1-like

Sequence similarities

Belongs to the fungal TPase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    752
  • Mass (Da)
    82,255
  • Last updated
    2006-01-24 v1
  • MD5 Checksum
    6334CB0C3AF8557BFD7BFC6311C6688C
MDLRTIMNNDASGTSDAPSTAPLQSPSQVSRKPSDPMYAPRDQQRTSSYPSAYSSHPPQPPPLQRPHASPERSSSYGSLQSPYQYHPPSAQIAGAQSQRGPSPPPYGSSASRDSFSTYGHPQQHQQQQSPFAQQRSQSIQSVLTPSSTSTYSFHPRESPPAVASQPYPSQQFSPPAQGSVPNTPRGSVAASYTRQTPPSARPQSSGHESLSNRASSPWVGPDAQVHMSPTAIPRVSRQDSRPLEQTPRQNSSATDRRDSDESVSPKTAFPSGSRQGSTAGYTDLASSSQPKPTENGISLKESPPNLQTSQPAPAASNFDSSPPARKSLTDDTSAIDQARSLPTKMDMTPDATANSSPQAPRVKRRRYEEPPIYAQRSVRTKGRIPMIPNRCPPIPKHARNSMQNPFVMRQQTVSAQASATDSPAKLKSETPPTNGPPAPRRPPEPAQAGSLGPWEPSIYGYIPHEEVTKTVCDFLFQHVVMRNDATAAPAGATATGQGAMIEVEAKLGQLVDMDRGERLLLPISTEGIVNKENTRLRTAFESTMTIAQHQAMNNFLNEAVKMSMPQANPGRIPLSYTHKKERDTFYEISPSELPPVIRQNLNPRHKPKVRVTLDQRTGEVLAKIVKCRIADLDVYSPRTCVDWRISVNLEMSYEGDVSHLPVVDPGRGRGGERNKDRMSYRHLAYQIDLTQVAKSEPPSKGEFEHELEVEISAAEIRRQGQLAIAGDPKNQYEELVKGFVDNIRILARAVPP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-32Polar residues
Compositional bias68-155Polar residues
Compositional bias163-218Polar residues
Compositional bias231-250Polar residues
Compositional bias264-339Polar residues
Compositional bias412-429Polar residues
Compositional bias430-446Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP007157
EMBL· GenBank· DDBJ
BAE59221.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help