Q9FLE2 · CLP5_ARATH

Function

function

Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.

Features

Showing features for binding site.

142450100150200250300350400
TypeIDPosition(s)Description
Binding site16ATP (UniProtKB | ChEBI)
Binding site56ATP (UniProtKB | ChEBI)
Binding site124-129ATP (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 ComponentmRNA cleavage factor complex
Molecular FunctionATP binding
Molecular Functionpolynucleotide 5'-hydroxyl-kinase activity
Biological ProcessmRNA 3'-end processing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein CLP1 homolog 5
  • Alternative names
    • CLP-like protein 5
    • Protein CLP-SIMILAR PROTEIN 5

Gene names

    • Name
      CLPS5
    • ORF names
      MYH19.12
    • Ordered locus names
      At5g39930

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
    Q9FLE2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004313521-424Protein CLP1 homolog 5

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Forms a complex with cleavage and polyadenylation specificity factor (CPSF) subunits PCFS1, FIPS3 and CPSF30.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the Clp1 family. Clp1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    47,489
  • Last updated
    2001-03-01 v1
  • Checksum
    50CC9AE9B42B32C9
MFGPQIRRVKLEKQSELRIELQPTSPLRLRLLDGKAEIFGYELPHEVWITFPPLMTFAVFTWYGATIEIDGITGNEYISCETPMVNYLGLHNSLQVQRHRVTSSTRDSASSQEGPRVIIVGDIDSGKSTLAKMLLNWAVKDGWKPTFVDLNVGQSSITIPGTIAAAPIKMLVDPVEGFPLDKALIHYFGLTNPSVNLRLYRTLVEELARELKEEFSANAESRASGMVIDTMGFIVREGYALLLHAIRTFNASLVIVVGQEEKLVYDLKKNLKFKKNLQVLNLEKSEGVFSRSSDFRKTLRNSNIQNYFYGVTNDLTVYTKTVKFSDVQVYRIGDFRVSGSTSAHQRGNDPLKITLVTIDEHLVNKVLAISYAIKPDQIISSIVAGFVCIKNVDISEERITYVSPSAAELPSKILILGTLTWHVT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB010077
EMBL· GenBank· DDBJ
BAB10217.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED94492.1
EMBL· GenBank· DDBJ
Genomic DNA
AY954872
EMBL· GenBank· DDBJ
AAX55198.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help