A0A2N2CP04 · A0A2N2CP04_9FIRM

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

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
Site36Interaction with DNA
Site142Interaction with DNA
Site143Interaction with DNA
Site146Interaction with DNA
Site151Interaction with DNA
Site158Interaction with DNA
Active site303O-(5'-phospho-DNA)-tyrosine intermediate
Site305Interaction with DNA
Site495Interaction 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
      CVU91_11555

Organism names

Accessions

  • Primary accession
    A0A2N2CP04

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain6-116Toprim
Region166-171Interaction with DNA
Compositional bias425-453Basic and acidic residues
Region425-461Disordered
Region708-780Disordered
Compositional bias750-764Polar residues

Sequence similarities

Belongs to the type IA topoisomerase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    780
  • Mass (Da)
    87,550
  • Last updated
    2018-04-25 v1
  • Checksum
    F25C8F6736CC0070
MAQTRTDLVIVESPAKARTIEKYLGPNYHVVASMGHLRDLPKSTMGVDIENGFEPDYQPVAARKDVIDELKKKSKAAGIVYLATDPDREGEAISWHLKELLELPDEKAKRVTFNEITKKVVNESIAAPREIDQDLVDAQQARRILDRIVGYKLSPLLWRKVRRGLSAGRVQSVATRMVVDREKEIREFKTEEYWLLDATLDRVEKEGSFVARFHGTEAKKIELHSEAEVDKIIKEISEDEFYIKSVKRGEKQRSPSPPFITSTLQQEASRRLGMTPKRTMSIAQQLYEGVDISGEGTVGLITYMRTDSLRLSDVATSAAKDFIIGRYGREYYPEKTRVFKTKSGAQDAHEAIRPSSVELTPELIKKDLTADQYRLYRLIWGRFTACQMANAVYDGVTIDASSAGYIFRANYSELKFAGYTAVYEESKDEEQTERERPLPDLREGEKAKLAKTDKEQQFTQPASRYTEATLIRAMEEKGIGRPSTYAPTISTITTREYVVKEGKYLRPTVLGEVVTDLMETRFPDIVDLKFTARMEETLDNVEEGKRAWKDILSEFYGNFDNELKDAETALEGQHIKIPDEESDEICDKCGRKMVVKTGRFGRFLACPGYPECDFTKPIVVEMPGKCPKCSGRILKRTSKKGYAYYACEHVGDKTCDFMSWDVPVKETCTECGRTLFKLSGKGKKTPFCINDACPNFLPEDKRGYKKKAVAAEGESDTTSDKTVANKTPAKSAAKKPAAKKTAANKTAAKKTAAKKTTATKTVAKPTAAKKTPAKTGAKAK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias425-453Basic and acidic residues
Compositional bias750-764Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PGZZ01000011
EMBL· GenBank· DDBJ
PKM71952.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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