O61660 · TOP3_CAEEL

  • Protein
    DNA topoisomerase 3
  • Gene
    top-3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Releases the supercoiling and torsional tension of DNA 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 than 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 (By similarity).

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 active site, binding site.

1759100200300400500600700
Type
IDPosition(s)Description
Active site334O-(5'-phospho-DNA)-tyrosine intermediate
Binding site716Zn2+ (UniProtKB | ChEBI)
Binding site718Zn2+ (UniProtKB | ChEBI)
Binding site743Zn2+ (UniProtKB | ChEBI)
Binding site753Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular ComponentRecQ family helicase-topoisomerase III complex
Molecular FunctionDNA binding
Molecular FunctionDNA topoisomerase type I (single strand cut, ATP-independent) activity
Molecular Functionzinc ion binding
Biological ProcessDNA recombination
Biological ProcessDNA repair
Biological ProcessDNA topological change

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA topoisomerase 3
  • EC number
  • Alternative names
    • DNA topoisomerase III

Gene names

    • Name
      top-3
    • ORF names
      Y56A3A.27

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    O61660
  • Secondary accessions
    • Q9U223

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: Localizes to nuclear foci throughout pachynema in meiotic prophase I during meiotic recombination (PubMed:34252074).
Localization at nuclear foci is dependent on rmif-2 (PubMed:34252074).

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001451941-759DNA topoisomerase 3

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Component of the BTR double Holliday Junction dissolution complex composed of at least him-6, top-3, rmh-1 and rmif-2, which is involved in double strand break repair in the germline (Probable). May interact with rmh-1 (PubMed:27011106).

Complex viewer

View interactors in UniProtKB
View CPX-7361 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, zinc finger.

Type
IDPosition(s)Description
Domain3-147Toprim
Domain165-590Topo IA-type catalytic
Region609-715Disordered
Zinc finger716-759GRF-type

Sequence similarities

Belongs to the type IA topoisomerase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    759
  • Mass (Da)
    85,438
  • Last updated
    1998-08-01 v1
  • Checksum
    3D862412D72946BD
MKRALFVAEKNDVAKGVAAILSNGTANRREGRSKFNKIYTLNTELFGQQTAISVTSVSGHMMNFQFHENMSNWQTASMVELFRAPVRHVVTPEMKLIEQTLREQAQRHDILVVWTDCDREGEAIGAEIVKVCRDSNRRLDIFRARFSEITKAAITRAARNLIRLDEKTVAAVDCRSELDLRIGSAFTRLQTLHLRNRFRDLLGQNDTSQVISYGSCQFPTLGFVTDRYKMIENFVSEPFWKLIVEHTRESHKVEFLWDRNRLFDRDTVDILHDECKETKEAHVEKVAKKPKSKWRPQALDTVELEKLGISKLRMSAKQTMQVAEKLYSKGFISYPRTETNKFPAGLNLTPLVQQQTQSNIWGDFANEVLQNGVNPRNGRKSDEAHPPIHPLKFTEKHQLQGDDWKVYELVVRHFLACVSQDAQGEETMVNLTVGTEKFHASGLRIRDMGYLKVYVYEKWGNRLLPTYTEGERFTDFELKIGDGKTQAPDFLTEADLISLMDKYGIGTDATHAEHIEKIKTREYIGVRPDGKLIPSFLGLALVDGYDDMGFAMSKPDLRANLEIGLKEICDGRRQKQEVLDEQIGKYRAIFVESERKIGVLSQSLQRYLDKNNQAGGGPGGPGGGGGPPRGPGGGGGGGPTGPPAPPKPPAKPRGRPPRKSISPAVKNGHDDPENDTIVTLSEVFGSMSNPKPARKPRAPRKSAAPKEQEEEEEVFCQCPEPMRAVTKVVQKEGPNKGKKFYTCSLPYTSSEKCNFFKWA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF057032
EMBL· GenBank· DDBJ
AAC13567.1
EMBL· GenBank· DDBJ
mRNA
BX284603
EMBL· GenBank· DDBJ
CAB60518.2
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.
Help