A0A974CIT1 · A0A974CIT1_XENLA

Function

function

Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand.

Catalytic activity

  • ATP-dependent breakage, passage and rejoining of double-stranded DNA.
    EC:5.6.2.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
Molecular Functionmetal ion binding
Biological ProcessDNA topological change
Biological Processresolution of meiotic recombination intermediates
Biological Processsister chromatid segregation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA topoisomerase 2
  • EC number

Gene names

    • ORF names
      XELAEV_18033124mg

Organism names

  • Taxonomic identifier
  • Strain
    • J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    A0A974CIT1

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Homodimer.

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain474-591Toprim
Region1108-1139Disordered
Coiled coil1158-1201
Region1278-1681Disordered
Compositional bias1297-1312Basic and acidic residues
Compositional bias1326-1350Basic and acidic residues
Compositional bias1358-1372Basic and acidic residues
Compositional bias1410-1427Basic and acidic residues
Compositional bias1472-1486Polar residues
Compositional bias1487-1505Basic and acidic residues
Compositional bias1524-1542Basic and acidic residues
Compositional bias1548-1571Polar residues
Compositional bias1572-1592Basic and acidic residues
Compositional bias1617-1631Basic and acidic residues
Compositional bias1654-1670Polar residues

Sequence similarities

Belongs to the type II topoisomerase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,695
  • Mass (Da)
    191,382
  • Last updated
    2023-02-22 v1
  • Checksum
    69025162C3A1A667
MSKSAGGCGGAGGGSVGLTWVTLFDNQNNALKKEETESNNKNDSKKMSVERVYQKKTQLEHILLRPDTYIGSVETVTQSMWVYDEEVGMNCRDITFVPGLYKIFDEILVNAADNKQRDKNMNCIKISIDPDSNIISIWNNGKGIPVVEHKVEKMYVPALIFGHLLTSSNYDDEEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWANNMLKTTDPKIKYFDGDDYTCITFQPDLAKFKMEKLDKDTVALLTRRAYDVAGSLKGVKVVLNGKKLPVNGFRSYVDLYVKDKIDETGIALKVIHEVSSERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQIVSKLIEVVKKKNKAGVSVKPFQVKNHIWVFVNCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFSKAASNCGIVESILNWVKFKAQTQLNKKCSSVKHSKIKGIPKLDDANDAGGKHSLDCTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDNESLKTLRYGKIMIMTDQDQDGSHIKGLLINFFHHNWPSLLKHSFLEEFITPIVKATKNKQELSFYSIPEFEEWKKQIENQKLWKIKYYKGLGTSTAKEAKEYFADMDRHRIIFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKYLTYNDFINKELILFSNSDNERSIPSLVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNVSLLQPIGQFGTRLHGGKDAASPRYIFTMLSPLARLLFPSVDDNLLKFLYDDNQRVEPEWYIPIIPIVLVNGAEGIGTGWACKLPNYDTREIVNNVKRMLDGLDPYPMLPSYKNFKGTIQELGQNQYAMSGEIFVLDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPSLISDYKEYHTDTTVKFVVKMTEEKLAQAEAVGLHKVFKLQTSLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLHYYTLRKEWLIGMLGAEAARLSNQARFILEKIQGKITIENKSKRDLIQMLVQKGFESDPVKAWKEAQEKATEEDDLLQDPNEDNSSDSGTGSGPDFNYILNMSLWSLSKEKVDELVRQRDIKTKELNDLKRKSPSDLWKEDLAAFVEELERVEAQEREDVMAGFAGKAIKGKIGKPKIKKLQLEETLPSLYGRRVEPQISAMKADASKKMLKKKKGEMDSIALKMEFDEEFGSAPAEGGAEDSLTTTPVKPVKPKREKKEPGPRVKKNVSSPKSSTKKLKKRNPWSDVESKSESDLEEAEPEPVVIPRDSLLRRAAAERPKYTFDFSEEEDADDDDDEGVISRNNNNNFDDLKPPSSPAANSRDDDDVLSDSQEKDDYEFSSFKSTPAPQKPSESQKKKDYIFSSSEKVEASSKYNSDDDDNDEPSPLYSSYSFKTSDKTTGKGSSKKESAKYNSDDDDDEPSPLYSSYSFKSTEKPTSKGSSEKESTRYNSDEDDNDDLPFSSFTFKSSEKPASKGSTKKAKTLSDGTPKPKRPPKPKKSETSLNLDSDLLEFGSSKKSATPKAKGRGKKRKTSDSENEGEYNPGKKPTKPASSSKKSKKASLEQDSDADLFSSEVASETTSRQRPGRARKEVKYFADSDDDDDFVMF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1297-1312Basic and acidic residues
Compositional bias1326-1350Basic and acidic residues
Compositional bias1358-1372Basic and acidic residues
Compositional bias1410-1427Basic and acidic residues
Compositional bias1472-1486Polar residues
Compositional bias1487-1505Basic and acidic residues
Compositional bias1524-1542Basic and acidic residues
Compositional bias1548-1571Polar residues
Compositional bias1572-1592Basic and acidic residues
Compositional bias1617-1631Basic and acidic residues
Compositional bias1654-1670Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM004477
EMBL· GenBank· DDBJ
OCT74168.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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