A0A1D8MRB5 · A0A1D8MRB5_9EURY

Function

function

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
    EC:5.6.2.1 (UniProtKB | ENZYME | Rhea)

Features

Showing features for site, active site.

168350100150200250300350400450500550600650
TypeIDPosition(s)Description
Site52Interaction with DNA
Site165Interaction with DNA
Site169Interaction with DNA
Active site320O-(5'-phospho-DNA)-tyrosine intermediate
Site322Interaction with DNA
Site508Interaction with DNA

GO annotations

AspectTerm
Cellular Componentchromosome
Molecular FunctionDNA binding
Molecular FunctionDNA topoisomerase type I (single strand cut, ATP-independent) activity
Molecular Functionmetal ion binding
Biological ProcessDNA topological change

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA topoisomerase 1
  • EC number
  • Alternative names
    • DNA topoisomerase I

Gene names

    • Name
      topA
    • ORF names
      AQV86_01315

Organism names

Accessions

  • Primary accession
    A0A1D8MRB5

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain3-141Toprim
Region194-199Interaction with DNA
Compositional bias359-374Basic and acidic residues
Region359-385Disordered
Coiled coil538-587

Sequence similarities

Belongs to the type IA topoisomerase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    683
  • Mass (Da)
    78,506
  • Last updated
    2017-01-18 v1
  • Checksum
    B334896742C317F1
MQTAVMVGEKPKVASRIAQALGNYSVEENRGVKNYVLEKNGKKIIIAPAVGHIFNLEEHEEGWDYPVFEVQWEPIFENEDGADYVKKYYNNLRDQLDKADEYINACDFDLEGSVIGANVIKQLANADEGRIKRMKFSTLTPDDLNEAFDDLEDFDKGMTEAGLTRHVLDFYYGVNVSRALMQAVRENDRYKTLSTGRVQGPSLKMLADKERSIIEFEPDPYWEIFLHHSEFRAKFQDPEADHEKNDRIWEEEIAEGIFDQVQDEDEAEVSNIKVNNYKHNPPIPFNLTGLQSEASSQFNINPKTTQSIAQTLYENGLISYPRTESQKLPKKLGYSNLLKKLKGQEEYEGLAQKVLDKDDIYPRQGKKEDDAHPAIYPTGESPGSLSKKERKVYDLIVKRFLAVFGDAAKRQSLTLTLDVRGYEFNAKSKITKERNWFNLYDPYVNVEEAELPGVEEGEVLDIEEFELADKETKPPRRYSQSSIVNELEKRELGTKATRAQIVDRLYDREYIEGDPIEVTDLGLAIVETLEDHSPAVVSEELTREFEEKMEAIREEKNSREEVIEEAKEELTETLSKFKEKEKEIGRELVDTIDQERKRKRQLGPCDQCEDGTLRMIKSSGSRFVGCSNYPDCENSFPLPNNGDISKTDETCDECNTPKIQVYREKSSNYKMCIDPDCPTKDDW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias359-374Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP012986
EMBL· GenBank· DDBJ
AOV94548.1
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.
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.
FeedbackHelp