Q3E9C3 · RH58_ARATH

Function

Catalytic activity

Features

Showing features for binding site.

147250100150200250300350400450
TypeIDPosition(s)Description
Binding site120-127ATP (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 Componentchloroplast
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DEAD-box ATP-dependent RNA helicase 58, chloroplastic
  • EC number

Gene names

    • Name
      RH58
    • ORF names
      T24G5.110
    • Ordered locus names
      At5g19210

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q3E9C3
  • Secondary accessions
    • Q84W18

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-54Chloroplast
ChainPRO_000023919755-472DEAD-box ATP-dependent RNA helicase 58, chloroplastic

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif, domain.

Type
IDPosition(s)Description
Motif76-104Q motif
Domain107-286Helicase ATP-binding
Motif231-234DEAD box
Domain314-472Helicase 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

Belongs to the DEAD box helicase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q3E9C3-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    472
  • Mass (Da)
    52,811
  • Last updated
    2005-11-08 v1
  • Checksum
    074057EA6DB630BB
MASQLLNVPHLAFFPKISYASVFSTLKPSFFHSTSTRRALKSSPSSRIINLQAVAETSSEIESNSVTETTVPLTLRQICQGFVPEHILHRMEEIGFVFPTDIQREALPTLFTGRDCILHAQTGSGKTLTYLLLIFSLINPQRSSVQAVIVVPTRELGMQVTKVARMLAAKSEIDVKGCTVMALLDGGTLRRHKSWLKAEPPAILVATVASLCHMLEKHIFRIDSVRVLVVDEVDFLFYSSKQVGSVRKLLTSFSSCDKRQTVFASASIPQHKHFVHDCIQQKWTKRDVVHVHVSAIMPMPLCLLHRFVMCEKTNKHQVLLALLESDAPESAIIFVGEQSEKSKKAGNDPSTTLLMEFLKTSYKGSLEILLLEGDMNFNSRAASLTEIRQGGGFLLVSTDIAARGIDLPETTHIFNFDLPQTVTDYLHRAGRAGRKPFSDRKCIVANLITSEERFVLQRYENELMFSCEEMML

Q3E9C3-2

  • Name
    2
  • Note
    May be due to a competing acceptor splice site.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0191071-157in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC069326
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CP002688
EMBL· GenBank· DDBJ
AED92670.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED92671.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
ANM69255.1
EMBL· GenBank· DDBJ
Genomic DNA
BT004328
EMBL· GenBank· DDBJ
AAO42322.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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