InterPro : IPR013498

Name  DNA topoisomerase, type IA, zn finger Short Name  Topo_IA_Znf
Type  Domain Description  DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks []. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [, ]. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (; topoisomerases II, IV and VI) break double-strand DNA [].Type I topoisomerases are ATP-independent enzymes (except for reverse gyrase), and can be subdivided according to their structure and reaction mechanisms: type IA (bacterial and archaeal topoisomerase I, topoisomerase III and reverse gyrase) and type IB (eukaryotic topoisomerase I and topoisomerase V). These enzymes are primarily responsible for relaxing positively and/or negatively supercoiled DNA, except for reverse gyrase, which can introduce positive supercoils into DNA. This entry represents the zinc-finger domain found in type IA topoisomerases, including bacterial and archaeal topoisomerase I and III enzymes, and in eukaryotic topoisomerase III enzymes. Escherichia colitopoisomerase I proteins contain five copies of a zinc-ribbon-like domain at their C terminus, two of which have lost their cysteine residues and are therefore probably not able to bind zinc []. This domain is still considered to be a member of the zinc-ribbon superfamily despite not being able to bind zinc.
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Proteins

InterPro protein domain ID --> Contigs

 

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3 Found In

Id Name Short Name Type
IPR005733 DNA topoisomerase I, bacterial-type TopoI_bac-type Family
IPR005739 DNA topoisomerase I, archeal-type TopoI_arch Family
IPR014538 Uncharacterised conserved protein, topoisomerase zinc finger UCP028063_topo_Znf Family

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Roca J The mechanisms of DNA topoisomerases. 1995 Trends Biochem Sci 20 156-60
Champoux JJ DNA topoisomerases: structure, function, and mechanism. 2001 Annu Rev Biochem 70 369-413
Gadelle D Phylogenomics of type II DNA topoisomerases. 2003 Bioessays 25 232-42
Wang JC Cellular roles of DNA topoisomerases: a molecular perspective. 2002 Nat Rev Mol Cell Biol 3 430-40
Grishin NV C-terminal domains of Escherichia coli topoisomerase I belong to the zinc-ribbon superfamily. 2000 J Mol Biol 299 1165-77



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)