A0A2H9QBB2 · A0A2H9QBB2_9ARCH

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

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.

Type
IDPosition(s)Description
Site116Interaction with DNA
Site228Interaction with DNA
Site232Interaction with DNA
Active site377O-(5'-phospho-DNA)-tyrosine intermediate
Site379Interaction with DNA
Site565Interaction 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
      COX84_04255

Organism names

Accessions

  • Primary accession
    A0A2H9QBB2

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-18Basic and acidic residues
Region1-60Disordered
Compositional bias23-50Polar residues
Domain64-203Toprim
Region257-262Interaction with DNA

Sequence similarities

Belongs to the type IA topoisomerase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    754
  • Mass (Da)
    83,778
  • Last updated
    2018-02-28 v1
  • Checksum
    48B846CC94794502
MPKLKNDASIMPKEKRKTTKPKATAKSSAANFEPQAITVSGSGDMSERVSSTSSRDSKPETHYDALIVTEKPSVAEKVAYALSDSTVAKKRYAGPVSYFIITRDGKRMCVAPAVGHILTLTEKKKNSGYPSFDIGWVESYKVNKKAAFTKDYAESLRFLGKQSNDFIVACDYDIEGSLIGYNILKYLCGSEKGRRMKFSALTKTDLLEAYATLSPQLDYGNIFAGESRHILDWYYGINLSRALMQAIRTGGMYSILSIGRVQGPTLHLMVVKEREIRAFVSTPYWEVVAFYGPAEAAVEFFYEKGKLSAEAEALRLVAIVKQGGIVESVETAQKKIPPLFPFDLTSLQLESFSTFHFPPSKTLRVAQSLYEQSYISYPRTSSQQLPPTLNTRNIISDLSHQPAYSEYASMLISQNRTRPHNGQKTDPAHPAIYPTGIAPKGIDSDQAKLYDLIARRFLATFSEWAERENNKVAVNCSGERFIASATHTTYKGWFAIYAPFLKYEEKYLSGFTQGQPISFTDVQSLAKMTKPPKRYTPASLISELEKLGLGTKSTRSMIIDILHDRGYVRGKSLKVTDLGMSVASVLEKHCPKILDEQMTRDVEAELDRITEGSVDREKIINTGKQLLIEILQSFREHEQAIGSELASTIMNQKSEESHLGKCPACSNGLLKIIELRSRGTQFIGCTNYPNCRNSFPLPKGARVRSAKSACKRCGLPEVVISGFNGKGSEFTKCISPKCNAEAYAQRQKEQGGKT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Basic and acidic residues
Compositional bias23-50Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PFPH01000253
EMBL· GenBank· DDBJ
PIZ95710.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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