A0A978W5V3 · A0A978W5V3_ZIZJJ

Function

function

Severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
    EC:5.6.1.1 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site.

153650100150200250300350400450500
TypeIDPosition(s)Description
Binding site292-299ATP (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 Componentmicrotubule
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionisomerase activity
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule severing ATPase activity
Biological Processmicrotubule severing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Katanin p60 ATPase-containing subunit A1
  • EC number
  • Short names
    Katanin p60 subunit A1
  • Alternative names
    • p60 katanin

Gene names

    • Name
      KATNA1
    • ORF names
      FEM48_Zijuj01G0299000

Organism names

  • Taxonomic identifier
  • Strain
    • AT0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rhamnaceae > Paliureae > Ziziphus

Accessions

  • Primary accession
    A0A978W5V3

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region111-196Disordered
Compositional bias148-196Polar residues
Domain284-427AAA+ ATPase

Sequence similarities

Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    59,072
  • Last updated
    2023-02-22 v1
  • Checksum
    92154FA9F2A6BD92
MVGASLVGLQEHLKLAREYALEGLYDTSIIFFDGAIAQINKHLSTLDDPLVRAKWMNVKKALSEETEVVKQLDAERRAFKEIPMGRRPPSPPINSKSSFVFQPLDEYPTSSGAAMDDPDVWRPPSRDSNRRPARAGQVGMRKSSQDGAWARGGSTRTSTTARGAKTGGSSRVNSGVRASTTGKKGSGSGKSSKSDSAVSSTGCDYNFWILKLKNGDAEDGKSKRSQYEGPDPDLAAMLERDVLETSPGVRWDDVAGLTEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNARGASGEHESSRRVKSELLVQVDGVNNTSTNEDGSRKIVMVLAATNFPWDIDEALRRRLEKRIYIPLPNFESRKELIRINLKTVEVAPDVNIDDVARRTEGYSGDDLTNVCRDASLNGMRRKIAGKTRDEIKNMSKDEISKDPVAMCDFEEALVKVQRSVSAADIEKHEKWFAEFGSA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias148-196Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEACU010000001
EMBL· GenBank· DDBJ
KAH7547337.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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