Q5JKF2 · RH40_ORYSJ

Function

function

ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.

Catalytic activity

Features

Showing features for binding site.

1792100200300400500600700
TypeIDPosition(s)Description
Binding site194-201ATP (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
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionmRNA binding
Molecular FunctionRNA helicase activity
Biological Processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Biological ProcessrRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DEAD-box ATP-dependent RNA helicase 40
  • EC number

Gene names

    • ORF names
      B1156H12.12-1, B1156H12.12-2, OsJ_02174
    • Ordered locus names
      Os01g0549400, LOC_Os01g36860

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
    Q5JKF2
  • Secondary accessions
    • A0A0P0V3W2
    • Q5JKF3

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
ChainPRO_00002824571-792UniProtDEAD-box ATP-dependent RNA helicase 40
Modified residue (large scale data)86PTMeXchangePhosphothreonine
Modified residue (large scale data)550PTMeXchangePhosphoserine
Modified residue (large scale data)552PTMeXchangePhosphoserine
Modified residue (large scale data)588PTMeXchangePhosphoserine
Modified residue (large scale data)608PTMeXchangePhosphoserine
Modified residue (large scale data)656PTMeXchangePhosphoserine
Modified residue (large scale data)658PTMeXchangePhosphothreonine
Modified residue (large scale data)660PTMeXchangePhosphoserine
Modified residue (large scale data)675PTMeXchangePhosphothreonine
Modified residue (large scale data)688PTMeXchangePhosphoserine
Modified residue (large scale data)709PTMeXchangePhosphoserine
Modified residue (large scale data)720PTMeXchangePhosphoserine
Modified residue (large scale data)728PTMeXchangePhosphoserine
Modified residue (large scale data)730PTMeXchangePhosphoserine
Modified residue (large scale data)732PTMeXchangePhosphoserine
Modified residue (large scale data)753PTMeXchangePhosphoserine
Modified residue (large scale data)754PTMeXchangePhosphoserine

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

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

Type
IDPosition(s)Description
Region1-25Disordered
Domain17-51WW
Region44-118Disordered
Compositional bias51-68Pro residues
Compositional bias69-112Basic and acidic residues
Motif150-178Q motif
Domain181-355Helicase ATP-binding
Motif303-306DEAD box
Domain384-528Helicase C-terminal
Region523-792Disordered
Compositional bias529-558Basic and acidic residues
Compositional bias573-610Basic and acidic residues
Compositional bias611-646Basic residues
Compositional bias667-710Basic and acidic residues
Compositional bias713-748Polar 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 & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q5JKF2-1

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
    792
  • Mass (Da)
    87,980
  • Last updated
    2007-04-03 v2
  • Checksum
    B0A866D5D26EBBFC
MSAGTAPAAPRYAPDDPSLPKPWRGLVDGTTGYLYYWNPETNITQYEKPLPPEDQLPPPPPLPPPPPRSGRGDRDRDRRDRSRSRTPPRRDHRDRDRDRDRRHDDHRSAPSHHHPLPAAAAIAADDPSTEAYRHRHEITVVGDNVPAPITSFETGGFPPEILKEIQRAGFSSPTPIQAQSWPIALQCQDVVAIAKTGSGKTLGYLLPGFMHIKRLQNNPRSGPTVLVLAPTRELATQILEEAVKFGRSSRISSTCLYGGAPKGPQLRDLDRGVDVVVATPGRLNDILEMRRISLKQVSYLVLDEADRMLDMGFEPQIRKIVKEIPPRRQTLMYTATWPKEVRRIAEDLLVHPVQVTIGSVDELVANSAITQNVELITPSEKLRRLEQILRSQDSGSKVLIFCTTKRMCDQLARTLTRQFGASAIHGDKSQSEREKVLSHFRSGRSPILVATDVAARGLDIKDIRVVINYDFPTGIEDYVHRIGRTGRAGATGVAYTFFCDQDSKYAADLIKILEGANQRVPRDLADMASRGGRGGRKRNRWATRSDRGGSHSELDSRYGGRDGLSGSSGRLDSSRSSRRHDYGDDGRSRRSGRGRSRSRSRSDSDRYSRSPKRSRRHSRSRTRSRSRSRSRSYTRNRRASRSRSRSPGASRRHERSATGSGSALPDSGHGERKRTPEADPSRNHTNHSDPKDDRHPEDGKVGKVDLDRSPTPQDKSGPYSPAYNGKTSRSVSPGNQVEGNNKAAEVSKNPDPSSPPHHGKTREDEEEGMIDEDGEIADDPRANATVQNGGDN

Q5JKF2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-141: Missing
    • 142-164: GDNVPAPITSFETGGFPPEILKE → MLLEPFLLHLAHASQHILDALSF

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0P0V3W4A0A0P0V3W4_ORYSJOs01g0549400639
A0A0P0V3W9A0A0P0V3W9_ORYSJOs01g0549400266

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0241591-141in isoform 2
Compositional bias51-68Pro residues
Compositional bias69-112Basic and acidic residues
Alternative sequenceVSP_024160142-164in isoform 2
Sequence conflict344in Ref. 6; AK122104
Sequence conflict512in Ref. 6; AK102720
Compositional bias529-558Basic and acidic residues
Compositional bias573-610Basic and acidic residues
Compositional bias611-646Basic residues
Compositional bias667-710Basic and acidic residues
Compositional bias713-748Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP004225
EMBL· GenBank· DDBJ
BAD88050.1
EMBL· GenBank· DDBJ
Genomic DNA
AP004225
EMBL· GenBank· DDBJ
BAD88051.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008207
EMBL· GenBank· DDBJ
BAF05209.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014957
EMBL· GenBank· DDBJ
BAS72626.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014957
EMBL· GenBank· DDBJ
BAS72627.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000138
EMBL· GenBank· DDBJ
EAZ12284.1
EMBL· GenBank· DDBJ
Genomic DNA
AK102720
EMBL· GenBank· DDBJ
-mRNA No translation available.
AK122104
EMBL· GenBank· DDBJ
-mRNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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