24  structures 965  species 1  interaction 13560  sequences 20  architectures

Family: DNA_gyraseA_C (PF03989)

Summary

DNA gyrase C-terminal domain, beta-propeller Add an annotation

This repeat is found as 6 tandem copies at the C-termini of GyrA and ParC DNA gyrases. It is predicted to form 4 beta strands and to probably form a beta-propeller structure [1]. This region has been shown to bind DNA non-specifically and may stabilise the DNA-topoisomerase complex [2].


Literature references

  1. Qi Y, Pei J, Grishin NV; , Proteins 2002;47:258-264.: C-terminal domain of gyrase A is predicted to have a beta-propeller structure. PUBMED:11948780

  2. Reece RJ, Maxwell A; , Crit Rev Biochem Mol Biol 1991;26:335-375.: DNA gyrase: structure and function. PUBMED:1657531


InterPro entry IPR006691

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 PUBMED:12042765, PUBMED:11395412. 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 PUBMED:12596227.

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 PUBMED:7980433.

This entry represents the beta-pinwheel repeat found at the C-terminal end of subunit A of topoisomerase IV (ParC) and subunit A of DNA gyrase (GyrA). DNA gyrase is the topoisomerase II found primarily in bacteria and archaea that consists of two polypeptide subunits, gyrA and gyrB, which form a heterotetramer: (BA)2. This is distinct from the topoisomerase II found in most eukaryotes, which consists of a single polypeptide, with the N- and C-terminal regions corresponding to gyrB and gyrA, respectively, and which is not represented in this entry.

The ability of DNA gyrase to introduce negative supercoils into DNA is mediated in part by the C-terminal domain of subunit A, which forms a beta-pinwheel fold that is similar to a beta-propeller but with a different blade topology, and which forms a superhelical spiral domain PUBMED:15123801, PUBMED:15897198. This beta-pinwheel is capable of bending DNA by over 180 degrees over a 40 bp region, possibly by wrapping the DNA around the GyrA C-terminal beta-pinwheel domain.

In topoisomerase IV, although the C-terminal domain forms a similar superhelical spiral to that of DNA gyrase A, it assembles as a broken form of a beta-pinwheel as distinct from that of gyrA, due to the absence of a DNA gyrase-specific GyrA box motif PUBMED:15466871. This difference may account for parC being less efficient than gyrA in mediating DNA-bending, leading to their divergence in terms of activity, where topoisomerase IV acts to relax positive supercoils, and DNA gyrase acts to introduce negative supercoils PUBMED:16023670.

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

Gene Ontology

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

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Pfam alignments:
Full length sequences

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Trees

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Yeats C
Previous IDs: none
Type: Repeat
Author: Yeats C
Number in seed: 362
Number in full: 13560
Average length of the domain: 49.60 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 5.97 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.4 4.0
Trusted cut-off 20.4 4.0
Noise cut-off 20.3 3.9
Model length: 50
Family (HMM) version: 6
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Species distribution

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Interactions

There is 1 interaction for this family. More...

DNA_gyraseA_C

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DNA_gyraseA_C domain has been found.

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