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InterPro: IPR018522 DNA topoisomerase, type IIA, conserved site

Protein matchesHelp
UniProtKB
Matches:
7224 proteins
AccessionHelp IPR018522 TopoIIA_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR000565 DNA topoisomerase, type IIA, subunit B
IPR001154 DNA topoisomerase II, eukaryotic-type
IPR001241 DNA topoisomerase, type IIA, subunit B or N-terminal
IPR005737 DNA topoisomerase IV, subunit B, Gram-negative
IPR005740 DNA topoisomerase IV, subunit B, Gram-positive
IPR006171 Toprim domain
IPR011557 DNA gyrase, subunit B
IPR013759 DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
IPR013760 DNA topoisomerase, type IIA, central
GO Term annotationHelp
Process GO:0006265 DNA topological change
Function GO:0003677 DNA binding
GO:0003918 DNA topoisomerase (ATP-hydrolyzing) activity
GO:0005524 ATP binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 [1, 2]. DNA topoisomerases are divided into two classes: type I enzymes (EC:5.99.1.2; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (EC:5.99.1.3; topoisomerases II, IV and VI) break double-strand DNA [3].

Type II topoisomerases are ATP-dependent enzymes, and can be subdivided according to their structure and reaction mechanisms: type IIA (topoisomerase II or gyrase, and topoisomerase IV) and type IIB (topoisomerase VI). These enzymes are responsible for relaxing supercoiled DNA as well as for introducing both negative and positive supercoils [4].

DNA topoisomerase II (EC:5.99.1.3) [5, 6, 7] is one of the two types of enzyme that catalyze the interconversion of topological DNA isomers. Type II topoisomerases are ATP-dependent and act by passing a DNA segment through a transient double-strand break. Topoisomerase II is found in phages, archaebacteria, prokaryotes, eukaryotes, and in African Swine Fever virus (ASF). Bacteriophage T4 topoisomerase II consists of three subunits (the product of genes 39, 52 and 60). In prokaryotes and in archaebacteria the enzyme, known as DNA gyrase, consists of two subunits (genes GyrA and GyrB). In some bacteria, a second type II topoisomerase has been identified; it is known as topoisomerase IV and is required for chromosome segregation, it also consists of two subunits (genes parC and parE). In eukaryotes, type II topoisomerase is a homodimer.

There are many regions of sequence homology between the different subtypes of topoisomerase II. The signature pattern used in this entry is a highly conserved pentapeptide, which is located in GyrB, in ParE, and in protein 39 of phage T4 topoisomerase.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase [8].

Structural linksHelp
SCOP: e.11.1.1
CATH: 3.40.50.670
Database linksHelp
Enzyme: EC:5.99.1.3

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR018522 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P06786 DNA topoisomerase 2

P11388 DNA topoisomerase 2-alpha

P15348 DNA topoisomerase 2

P34534 Putative DNA topoisomerase 2, mitochondrial

Q01320 DNA topoisomerase 2-alpha

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001241 DNA topoisomerase, type IIA, subunit B or N-terminal
IPR020568 Ribosomal protein S5 domain 2-type fold
IPR001154 DNA topoisomerase II, eukaryotic-type
IPR013506 DNA topoisomerase, type IIA, subunit B, region 2
IPR003594 ATPase-like, ATP-binding domain
IPR013760 DNA topoisomerase, type IIA, central
IPR018522 DNA topoisomerase, type IIA, conserved site
IPR012542 DTHCT
IPR013758 DNA topoisomerase, type IIA, subunit A or C-terminal, alpha-beta
IPR013757 DNA topoisomerase, type IIA, subunit A, alpha-helical
IPR013759 DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
IPR002205 DNA topoisomerase, type IIA, subunit A or C-terminal
IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Wang JC.
Cellular roles of DNA topoisomerases: a molecular perspective.
Nat. Rev. Mol. Cell Biol. 3 430-40 2002 [PubMed: 12042765]
http://dx.doi.org/10.1038/nrm831
2. Champoux JJ.
DNA topoisomerases: structure, function, and mechanism.
Annu. Rev. Biochem. 70 369-413 2001 [PubMed: 11395412]
http://dx.doi.org/10.1146/annurev.biochem.70.1.369
3. Gadelle D, Filee J, Buhler C, Forterre P.
Phylogenomics of type II DNA topoisomerases.
Bioessays 25 232-42 2003 [PubMed: 12596227]
http://dx.doi.org/10.1002/bies.10245
4. Watt PM, Hickson ID.
Structure and function of type II DNA topoisomerases.
Biochem. J. 303 ( Pt 3) 681-95 1994 [PubMed: 7980433]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7980433
5. Sternglanz R.
DNA topoisomerases.
Curr. Opin. Cell Biol. 1 533-5 1989 [PubMed: 2560656]
http://dx.doi.org/10.1016/0955-0674(89)90016-1
6. Sharma A, Mondragon A.
DNA topoisomerases.
Curr. Opin. Struct. Biol. 5 39-47 1995 [PubMed: 7773745]
http://dx.doi.org/10.1016/0959-440X(95)80007-N
7. Roca J.
The mechanisms of DNA topoisomerases.
Trends Biochem. Sci. 20 156-60 1995 [PubMed: 7770916]
http://dx.doi.org/10.1016/S0968-0004(00)88993-8
8. McDowall J.
Protein of the Month: DNA Topoisomerase.
2006

Additional ReadingHelp
Dong KC, Berger JM.
Structural basis for gate-DNA recognition and bending by type IIA topoisomerases.
Nature 450 2007 1201-5 [PubMed: 18097402]
http://dx.doi.org/10.1038/nature06396
Berger JM, Gamblin SJ, Harrison SC, Wang JC.
Structure and mechanism of DNA topoisomerase II.
Nature 379 1996 225-32 [PubMed: 8538787]
http://dx.doi.org/10.1038/379225a0
Fass D, Bogden CE, Berger JM.
Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands.
Nat. Struct. Biol. 6 1999 322-6 [PubMed: 10201398]
http://dx.doi.org/10.1038/7556
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InterPro 23.1