A1C5V3 · DBP3_ASPCL

Function

function

ATP-dependent RNA helicase required for 60S ribosomal subunit synthesis. Involved in efficient pre-rRNA processing, predominantly at site A3, which is necessary for the normal formation of 25S and 5.8S rRNAs (By similarity).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site129-136ATP (UniProtKB | ChEBI)

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 Componentnucleolus
Cellular Componentpreribosome, large subunit precursor
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Biological Processendonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent RNA helicase dbp3
  • EC number

Gene names

    • Name
      dbp3
    • ORF names
      ACLA_068010

Organism names

Accessions

  • Primary accession
    A1C5V3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002816951-503ATP-dependent RNA helicase dbp3

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, motif, domain.

TypeIDPosition(s)Description
Compositional bias1-32Basic and acidic residues
Region1-37Disordered
Motif104-112Q motif
Domain116-292Helicase ATP-binding
Motif239-242DEAD box
Domain323-472Helicase C-terminal

Domain

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    503
  • Mass (Da)
    54,695
  • Last updated
    2007-01-23 v1
  • Checksum
    486F0EF1718B8C5F
MGKRVSHNEGADRRPKKKAKNEKPEKETMESPAADVTVDFGSKSDATYVQSQVLSDMPQSEIDQFLATHSIKVTDTSDAPAVRPIISFSHLPSCDSKLYSSLSSFASPTPIQSATWPLLFAGRDVIGIAETGSGKTLAFGLPCLKKILDSGKIKFKNARPAAVIISPTRELAMQIYDQISKYAGSIGIKATCIFGGVKKDEQREALKSAAIVVATPGRLKDLQNDGSVDLGKVKYLVLDEADRMLDKGFEQDIKDIISSTPDSKRQTVMFTATWPPSVRDLAATFMTSAVTVTIGGDPSADPRANTRIKQTVEVVQSHDKEYRLVQLLSENQRGAAALDKVLVFCLYKKEAMRVERLLRNKNFKVAGIHGDLNQHERFKSLDAFKSGAATVLVATDVAARGLDIPSVKLVINVTFPLTVEDYVHRIGRTGRAGAEGRAITLFTETDKAQSGALINVLKAAKQEVPQELLKFGTTVKKKQHGAYGAFFKEADSGKSATKIVFDD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-32Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027045
EMBL· GenBank· DDBJ
EAW13774.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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