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A0A0J9V6Q0 · A0A0J9V6Q0_FUSO4

Function

function

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.

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 )

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 Componentnucleus
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
      FOXG_08257

Organism names

Accessions

  • Primary accession
    A0A0J9V6Q0

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-20
ChainPRO_500532455421-1737DNA topoisomerase 2

Keywords

Interaction

Subunit

Homodimer.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region86-169Disordered
Domain620-738Toprim
Region1251-1279Disordered
Region1359-1407Disordered
Compositional bias1368-1389Basic and acidic residues
Region1441-1737Disordered
Compositional bias1449-1464Polar residues
Compositional bias1470-1484Basic and acidic residues
Compositional bias1505-1519Basic and acidic residues
Compositional bias1521-1537Polar residues
Compositional bias1567-1582Basic and acidic residues
Compositional bias1594-1609Polar residues
Compositional bias1647-1661Polar residues
Compositional bias1718-1737Acidic residues

Sequence similarities

Belongs to the type II topoisomerase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,737
  • Mass (Da)
    194,405
  • Last updated
    2015-10-14 v1
  • MD5 Checksum
    C1D2CEEA64067FE187A2F5B84A084485
MGSLAPFISSFLLSRLCTRASPLARPGRPSFLTPLSLFYPSLRPLYSNSLSLNPALAPQARFFALTANNNKMDSDASMFSLGEESDGYVPETKAKPKAAPKKAAARPPVKKMVQTTLKTKSAPRKRPTPESDDDDISIASGFSNTPPKAKKQKKEPAVSKSSGAPLEELENDSMVIDSPAKPGKKKTATEMYTKLSQLEHILKRPDTYIGSVERTEQQMWVLNKESQLMEYKNVSFVPGLYKIFDEILVNAADNKQRDGSMTYMKINIDRENGVISVENNGKGIPIVIHEKEKIYIPELIFGHLLAGSNFDDDEKKTVGGRNGYGAKLCNVFSTEFNLECQDSEHGKRYKQTWRNNMQTMEKAKITSSKTSDFTRVTFKPDFKRFGMEDGIDDDLESLLHRRVYDMVGTIRGIKVFLNGEQIKIKDFKAYCDLYAKSIAKERSTEEGGAPTCTVEMDKDKSHPRWEVGFAVSDGTFQQVSFVNSIATTSGGTHVNYIADQVTEALLKALNKKRKGHALKQSHLKNHIFIFVNCYINNPAFTSQTKEQMTTKPSQFGSKCKLGEDFLKKIAKSDALQNILDFAEKKADKMLAKGDGNKRSRVNNAKLVEANFAGTRRGHECTLILTEGDSAKGLAVSGRAILDPDRIGVFPLRGKLLNVRDASVDQIMKNAEIQNIKQFLGLKHKQTYTDTKNLRYGHLMIMADQDHDGSHIKGLLINFLQVQFPSLLKIPDFFREFITPIVKVWQGPNPKKPQRLKSFFTQPEYEEWKEDHKNELTRWHSKYFKGLGTSSNEDAQVYFTNLDDHLKEFDTMKPEEADLLELAFSKKKADARKEWLGNFVPGTYLDHSTKSITYSDFINRELILFSMADNMRSIPSVLDGFKPGQRKVIYACFKRNLVKDKKVVELAGYVSEQTAYHHGEQSLQQTIIGLAQNFVGSNNINCLEPSGNFGSRLAGGSDAASPRYTFTRLSPFARKIFHPMDEPNLMHHYEDGKKIEPMVYAPIIPMVLVNGADGIGTGWSTSIPNYHPMDIVKNLKRRMGRLDDNDLEERPFETMMPWFRGWKGTPEVAGPDRYKFNGIAYHNEQKDNEVVITELPIRMWTDDFKGKLEKIIAGVDGPAWIKDYKEFNDHSTVHFEIAVDDKHMGKVLEEGVLERFKLTKQVATSNLVAFDTRGMIRKYEKVEDILEEFYLYRLDMYTDRKKHWLGVFHADYRKLKNQARFIKEIIDGQLVVGKKKKTVLVQELRDCDYEAFPPGGEKKKTADEEDDDADENQDVDGDLEGGARDYDYLLSMPIWSLTAERLEKLKQAIEKKKAEHDELLALSEKDLWCRDLDDFMAEWETQLAVDAEIKTSIRRMGRRVSKKIGAGTARGRKVKDDDEYEPDKKGRGRPKAAASKATVKTAPKVETKSAQRFAEMFSSKPKVKKEPSADVMELSDLSDDDYAALSRSKSSAPAIKTSQSPPTEAPENPRVKRAAASKVKTIIDDDSESDDDQMLGDVGALVKGIDKPAGDRERGRFSLHAMSRPDSSQGNAGVSGLSKSRPKSAKAFDFDDDSPDDTNYELLAKSSPHKTATKDDHIDSFLSDDEPFVAPSKSAATKSKPTSTDSEDPTPAGLATVKKGRGRPAGAKSKEPAKPKAAPKATKTAASKVASRPATKQTTLSPAAKAYAAKKAVKKSVLDDDSDEDMADPDSPPPKASSRVRPGRAAASRRPIVVDDDSSVMQQDDESDDPFEVDDDED

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0J9V5P8A0A0J9V5P8_FUSO4FOXG_082571296

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1368-1389Basic and acidic residues
Compositional bias1449-1464Polar residues
Compositional bias1470-1484Basic and acidic residues
Compositional bias1505-1519Basic and acidic residues
Compositional bias1521-1537Polar residues
Compositional bias1567-1582Basic and acidic residues
Compositional bias1594-1609Polar residues
Compositional bias1647-1661Polar residues
Compositional bias1718-1737Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS231705
EMBL· GenBank· DDBJ
KNB06843.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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