A0A1J4MFP8 · A0A1J4MFP8_9CRYT

Function

function

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

Caution

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

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
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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA topoisomerase 2
  • EC number

Gene names

    • ORF names
      cubi_01624

Organism names

  • Taxonomic identifier
  • Strain
    • 39726
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Cryptosporidiidae > Cryptosporidium

Accessions

  • Primary accession
    A0A1J4MFP8

Proteomes

Organism-specific databases

Interaction

Subunit

Homodimer.

Family & Domains

Features

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

TypeIDPosition(s)Description
Compositional bias313-347Basic and acidic residues
Region313-406Disordered
Compositional bias348-362Acidic residues
Compositional bias381-406Polar residues
Domain589-704Toprim
Coiled coil1371-1428
Region1442-1599Disordered
Compositional bias1449-1464Basic and acidic residues
Compositional bias1509-1542Acidic residues
Compositional bias1562-1598Polar residues
Compositional bias1664-1694Polar residues
Region1664-1789Disordered
Compositional bias1711-1731Polar residues
Compositional bias1746-1773Acidic residues
Compositional bias1774-1789Polar residues

Sequence similarities

Belongs to the type II topoisomerase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,789
  • Mass (Da)
    203,891
  • Last updated
    2017-02-15 v1
  • Checksum
    21C77C9A8735E791
MIFEENQMENNELISNSKITGKPKMVNRSKKTVEERYQKKTQIEHILLRPDTYIGSTEFHEQTLWVWDDSNKKMVYRTINYVPGLYKIFDEILVNAADVKAREISTKSNHFIEKCTCIKVEINREKKEITVYNDGEGIPIEIHRDHQVYVPELIFGHLLTSDNYDDNEDRVTGGRNGFGAKLTNIFSKEFKIECGDNNTGRIFKMTWYNNMSKKSEENIKENYSGKSYVKITFKPDLSRFGNMSDFDDDIVSLLNKRVYDISGTSGVRVYLNGTLIPIKDFKSYTLLYLKSKINNNKESSDIAHEDNINTIENNEKRNNTRKLRNANKKNVKSDGEDENSNGFNENDHDESFEEDFMEDDEWDDEPKTSRSKKKSSVSNSKKKKSGQNISSSFFSSSSSSSSSLLLSGGGNDTNSPLIIYESVPKWEIVISESEGGQFQHVSFVNSICTIKGGTHISYVLDPLINAILKKVQTKNKGGMDVKSHHVKNHIWIFIKCLIVNPSFDSQTKETLTTKVSKFGSTCLLSEKTINSVVKSSIVENVLMWAQLKQSMELKKKMKSNQKNTVTSRLLGIPKLEDANEAGGPHSKKCTLILTEGDSAKTSCLAGLSIVGRDYFGVFPLRGKLLNVREASFKQQIGNVEIQNILKILGLGIGQKYDNGPVNLRYGSLMLMTDQDHDGSHIKGLIINLIHYYWPSLIHFRGFLKQFVTPIVKAKKGQNEISFFTLYEYEQWRKNNSSKLTGWKFKYYKGLGTSTDLEFKEYFTKIENHSIEFDWMDEQDDEAIDMAFSKKRTEDRKNWIESYKEGTYVDYSINNQCRNLRYFDFIHKELVLFSRYDTTRSIPNLLDGLKPGQRKVLFATFKKKLNNELKVVQLAGYVAEHSAYHHGESSLQSTIVNMAQNFVGSNNLNLLEPCGQFGSRKEGGKDASAARYIFTKLSKWTRYIFPEADDPLLTYLYDDGQQIEPLYYVPIIPMILVNGTDGIGTGWSSSVPNYNPKDIIMNLKRMLKGEIMVPMTPWYKSFKGKIVPIKQKSKKSTINNGGNNNNRRRTAVSGFGIGSNSNILAGSQIDVEDEDFQQIQKTNITNSGVVEESLELGANYETFGNWYKKNEETLVITELPVRRWTQDYKEWLESTLLPAPNADSDNIENSWILDYRDNSSHENVHITVRMRPEKLQQAELEGIEKIFKLKSTLSTSNMTLFDHNSRIVRYETELDILKEFIPIRLEMYEKRKKYLLSKLNYEKCILEQKILFLRLVIQGFIGLSNKNKEALVSELKKNNIKSIKQVQDLTQWKGGNLVQEIGGIENLASDGPGDTLTDDTQFISDSLDYLESSQHDGVMKSSYSREGSQGNELKLFDYLLSMPLWSLTKERMELLEAELLKKTEEYEKLLKTGIEEIWNIELDELLKVIEEEETQEEMIEAEHNSLIQKRRLSVDWNDLKKKTGTSRKRRNETAKKQENIKAKHPQKTNSKKTTKPTKKSRIGDSESDEYIEGDDYSEEDHHYGDFDDVLDGSDDSNDFDDIDNFESSDSEKEGIDDPESEFEDFSDSGKTSKGRRTQKVSIKKSKSGVQGKTNSSNVKKAKNISSSLSNSSKENKQGLFKSSACIEGDSLSAGNINSSITNLGKSKNTSNINKEVLKSSSPKPLESISLLQRLQQRTNLVNSFNQSHSSFSSSLNKVTSTDNSSKENGPVSKQTKITDIFKKGAIGDSENGVAKSVNQKKQNNQISRTKGVPTSKRGRRKTIIESEDEEEEEEEEEEEEEEEEEEDGIEDNESFSDVSSDSLMESDFSE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias313-347Basic and acidic residues
Compositional bias348-362Acidic residues
Compositional bias381-406Polar residues
Compositional bias1449-1464Basic and acidic residues
Compositional bias1509-1542Acidic residues
Compositional bias1562-1598Polar residues
Compositional bias1664-1694Polar residues
Compositional bias1711-1731Polar residues
Compositional bias1746-1773Acidic residues
Compositional bias1774-1789Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LRBP01000025
EMBL· GenBank· DDBJ
OII72291.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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