Q8H0U8 · RH42_ARATH

Function

function

Helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance.

Catalytic activity

Features

Showing features for binding site.

111661002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site573-580ATP (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 Componentnucleus
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 42
  • EC number
  • Alternative names
    • DEAD-box RNA helicase RCF1
    • REGULATOR OF CBF GENE EXPRESSION 1

Gene names

    • Name
      RH42
    • Synonyms
      RCF1
    • ORF names
      F9H16.10
    • Ordered locus names
      At1g20920

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
    Q8H0U8
  • Secondary accessions
    • A8MQH2
    • Q9SYP6

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis687Loss of ATPase activity.
Mutagenesis808In rcf1-1; loss of function and reduced cold tolerance.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 46 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002391821-1166DEAD-box ATP-dependent RNA helicase 42
Modified residue210Phosphoserine
Modified residue324Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Induction

Up-regulated by cold.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

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

Type
IDPosition(s)Description
Compositional bias1-45Basic and acidic residues
Region1-460Disordered
Coiled coil14-95
Compositional bias68-83Basic and acidic residues
Compositional bias92-311Basic and acidic residues
Coiled coil130-302
Compositional bias325-346Acidic residues
Compositional bias416-430Basic and acidic residues
Motif529-557Q motif
Domain560-738Helicase ATP-binding
Motif686-689DEAD box
Domain749-910Helicase 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

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8H0U8-1

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
    1,166
  • Mass (Da)
    133,033
  • Last updated
    2006-05-30 v2
  • Checksum
    597BD171F02666B5
MEVEKSKYRSEDLDVVEEEADLKKSRRDRDRSNERKKDKGSEKRREKDRRKKRVKSSDSEDDYDRDDDEEREKRKEKERERRRRDKDRVKRRSERRKSSDSEDDVEEEDERDKRRVNEKERGHREHERDRGKDRKRDREREERKDKEREREKDRERREREREEREKERVKERERREREDGERDRREREKERGSRRNRERERSREVGNEESDDDVKRDLKRRRKEGGERKEKEREKSVGRSSRHEDSPKRKSVEDNGEKKEKKTREEELEDEQKKLDEEVEKRRRRVQEWQELKRKKEEAESESKGDADGNEPKAGKAWTLEGESDDEEGHPEEKSETEMDVDEETKPENDGDAKMVDLENETAATVSESGGDGAVDEEEIDPLDAFMNTMVLPEVEKFCNGAPPPAVNDGTLDSKMNGKESGDRPKKGFNKALGRIIQGEDSDSDYSEPKNDDDPSLDEDDEEFMKRVKKTKAEKLSLVDHSKIEYEPFRKNFYIEVKDISRMTQEEVNTYRKELELKVHGKDVPRPIKFWHQTGLTSKILDTMKKLNYEKPMPIQTQALPIIMSGRDCIGVAKTGSGKTLGFVLPMLRHIKDQPPVEAGDGPIGLVMAPTRELVQQIHSDIRKFSKPLGIRCVPVYGGSGVAQQISELKRGTEIVVCTPGRMIDILCTSSGKITNLRRVTFLVMDEADRMFDMGFEPQITRIIQNIRPERQTVLFSATFPRQVETLARKVLNKPVEIQVGGRSVVNKDITQLVEVRPESDRFLRLLELLGEWSEKGKILVFVQSQEKCDALYRDMIKSSYPCLSLHGGKDQTDRESTISDFKNDVCNLLIATSVAARGLDVKELELVVNFDAPNHYEDYVHRVGRTGRAGRKGCAVTFISEDDAKYAPDLVKALELSEQPVPDDLKALADGFMVKVKQGIEQAHGTGYGGSGFKFNEEEEEVRKAAKKAQAKEYGFEEDKSDSEDENDVVRKAGGGEISQQQATFAQIAAIAAAAKAAAAAPVSAPVTANQLLANGGGLAAMPGVLPVTVPTLPSEGAGRAAAMVAAMNLQHNLAKIQADAMPEHYEAELEINDFPQNARWKVTHKETLGPISEWTGAAITTRGQFYPTGRIPGPGERKLYLFIEGPSEKSVKHAKAELKRVLEDITNQAMSSLPGGASGRYSVL

Q8H0U8-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAN72041.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

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

Type
IDPosition(s)Description
Compositional bias1-45Basic and acidic residues
Alternative sequenceVSP_0535211-338in isoform 2
Compositional bias68-83Basic and acidic residues
Compositional bias92-311Basic and acidic residues
Compositional bias325-346Acidic residues
Compositional bias416-430Basic and acidic residues
Sequence conflict894in Ref. 3; AAN72041

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC007369
EMBL· GenBank· DDBJ
AAD30599.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE30040.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE30041.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM59668.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM59669.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM59670.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM59671.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM59672.1
EMBL· GenBank· DDBJ
Genomic DNA
BT002030
EMBL· GenBank· DDBJ
AAN72041.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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