Q0ILZ4 · RH9_ORYSJ

Function

Catalytic activity

Features

Showing features for binding site.

162850100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site142-149ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Biological ProcessGroup II intron splicing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DEAD-box ATP-dependent RNA helicase 9
  • EC number

Gene names

    • Ordered locus names
      Os12g0611200, LOC_Os12g41715

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q0ILZ4
  • Secondary accessions
    • A0A0P0YBZ7

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00002824751-628UniProtDEAD-box ATP-dependent RNA helicase 9
Modified residue (large scale data)168PTMeXchangePhosphoserine
Modified residue (large scale data)503PTMeXchangePhosphoserine
Modified residue (large scale data)596PTMeXchangePhosphoserine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Motif98-126Q motif
Domain129-302Helicase ATP-binding
Motif250-253DEAD box
Domain331-478Helicase C-terminal
Region496-548Disordered
Region571-628Disordered
Compositional bias601-628Polar residues

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
    628
  • Mass (Da)
    65,595
  • Last updated
    2006-10-03 v1
  • Checksum
    EFBFE0AC2784EF9A
MYSILRRAAPLRRRAVSALAAAVLRREEAAAEVVVSRRATIPAAWFHSSPAWLGFRETGAAGAAARPQYAADEGLFYEEDKRGAKAGGVAAGGAEEGLEVAKLGISPKIVSQLASRGITKLFPIQRAVLEPAMQGKDMVGRAKTGTGKTLAFGIPILDAIIRHNEKNSPGKFPLAIVLAPTRELAKQVEREFSDSSNVETICVYGGTPISQQIRQLNYGVDVVIGTPGRVIDLLKRGALNLSEVRFVVLDEADQMLSVGFDEDVETILDRVPPKRQTLMFSATMPTWIQRLTQKYLKNPVTIDLVGEDDQKLAEGISLYSIASEGHAKPAVLGELIKEHAKGGKCIVFTQTKRDADRLSYTMGRSFQCQALHGDITQAQRERTLKGFREGHFNILIATDVAARGLDIPNVDLVIHFELPNSSELFVHRSGRTGRAGKKGKAIVMHSYQQSRAIRMVENDVGCKFTELPKINVEGSDLMSGGFDSFGGGGFGREGGGSYGRRGSFGSSSSRGGGFGDSGFGRSGGGFGRSGGGGFGRSSGGGFGDSGFGRSGGGGFGDSGFGRSGGGGYGDSGFGSSGGGSGRSGFGRSGGFGDSGSGRFGGGFGNSGSGSFGNFGGNNSGQSGGFGSS

Sequence caution

The sequence BAF30271.2 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias601-628Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP008218
EMBL· GenBank· DDBJ
BAF30271.2
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AP014968
EMBL· GenBank· DDBJ
BAT18038.1
EMBL· GenBank· DDBJ
Genomic DNA
AK287833
EMBL· GenBank· DDBJ
-mRNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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