A0A076ETH3 · A0A076ETH3_RHOOP

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.

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.

1972100200300400500600700800900
Type
IDPosition(s)Description
Site50Interaction with DNA
Site169Interaction with DNA
Site170Interaction with DNA
Site173Interaction with DNA
Site178Interaction with DNA
Site185Interaction with DNA
Active site340O-(5'-phospho-DNA)-tyrosine intermediate
Site342Interaction with DNA
Site543Interaction with DNA

GO annotations

AspectTerm
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
      EP51_19650

Organism names

Accessions

  • Primary accession
    A0A076ETH3

Proteomes

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region1-21Disordered
Domain20-144Toprim
Region193-198Interaction with DNA
Region736-785Disordered
Region891-972Disordered
Compositional bias905-933Basic and acidic residues
Compositional bias934-961Basic residues

Sequence similarities

Belongs to the type IA topoisomerase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    972
  • Mass (Da)
    105,924
  • Last updated
    2014-10-29 v1
  • Checksum
    59076101D2FB997E
MAKGDNGSAQGAAGASGQPRRLVIVESPTKARKIAPYLGKNYVVEASVGHIRDLPRGAADVPAKYKGESWARLGVNVDHDFEPLYVVSPEKKSKVTELKSLLKDADELFLATDPDREGEAIAWHLLETLKPKIPVRRMVFHEITEPAIRAAAEDTRELDNDLVDAQETRRILDRLYGYEVSPVLWKKVMPRLSAGRVQSVATRVIVQRERERMAFRSASYWDISATLDAGADASPRSFGARLVSVDGSRVATGRDFGADGQLKTSTVTVLDEARAQRLAGSLAGVDLTVSSAESKPYTRKPYAPFMTSTLQQEAGRKLRFTSERTMRIAQRLYENGYITYMRTDSTTLSSSAIAAARAQATELYGAEYVHDTPRQYTRKVKNAQEAHEAIRPAGDVFQTPGQLHSRLDTDEFRLYELIWQRTVASQMADARGTTLTLRITGTAGTGEECTFSASGRTITFAGFLKAYVESVDEEAGGQSDDAESRLPVLVEGQAVTATKLDPDGHTTNPPARYTEASLIKTLEELGIGRPSTYSSIIKTILDRGYVYKRGSALVPSWVAFAVIGLLEMHFGRLVDFDFTAGMEDDLDAIAGGREQRGNWLSSFYFGGDHGAEGSVAREGGLKKMVGVNLEEIDAREVNSIRLFDDAEGREVHVRVGRFGPYLERMVQNPDDPEGDLISQRANLPDDLPPDELTPEYAEKLFSTPQEGRKLGVDPLTGHEIVAKEGRFGPYVTEILPEPEPEPEPAVVPVTDESGDGTTKTKTAAKKAPAKKAAKKATGPKPRTGSLLKSMDLATVTLDDALKLLSLPRVVGVDPESKEEITAQNGRYGPYLKKGTDSRSLATEDQMFTVTLDEALKIYAEPKRRGRQAAATPPLRELGVDSVSEKPMVIKDGRFGPYVTDGETNASLRKGDEVESITDARASELLADRRARGPVKKKAAAKKAPAKKAAKKTAAKKAPAKKAAAKKAADKKA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias905-933Basic and acidic residues
Compositional bias934-961Basic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP008947
EMBL· GenBank· DDBJ
AII06729.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help