Protein Domain : IPR013758

Type:  Domain Name:  DNA topoisomerase, type IIA, subunit A/ C-terminal, alpha-beta
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 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 [].Type IIA topoisomerases together manage chromosome integrity and topology in cells. Topoisomerase II (called gyrase in bacteria) primarily introduces negative supercoils into DNA. In bacteria, topoisomerase II consists of two polypeptide subunits, gyrA and gyrB, which form a heterotetramer: (BA)2. In most eukaryotes, topoisomerase II consists of a single polypeptide, where the N- and C-terminal regions correspond to gyrB and gyrA, respectively; this topoisomerase II forms a homodimer that is equivalent to the bacterial heterotetramer. There are four functional domains in topoisomerase II: domain 1 (N-terminal of gyrB) is an ATPase, domain 2 (C-terminal of gyrB) is responsible for subunit interactions (differs between eukaryotic and bacterial enzymes), domain 3 (N-terminal of gyrA) is responsible for the breaking-rejoining function through its capacity to form protein-DNA bridges, and domain 4 (C-terminal of gyrA) is able to non-specifically bind DNA [].Topoisomerase IV primarily decatenates DNA and relaxes positive supercoils, which is important in bacteria, where the circular chromosome becomes catenated, or linked, during replication []. Topoisomerase IV consists of two polypeptide subunits, parE and parC, where parC is homologous to gyrA and parE is homologous to gyrB.This entry represents the alpha-beta domain of subunit A (gyrA and parC) of bacterial gyrase and topoisomerase IV, and the equivalent C-terminal region in eukaryotic topoisomerase II composed of a single polypeptide. Short Name:  Topo_IIA_A/C_ab
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0 Child Features

0 Contains

1 Cross References

Identifier
G3DSA:3.90.199.10

6 Found Ins

DB identifier Type Name
IPR005743 Family DNA gyrase, subunit A
IPR013760 Domain DNA topoisomerase, type IIA-like domain
IPR002205 Domain DNA topoisomerase, type IIA, subunit A/C-terminal
IPR001154 Family DNA topoisomerase II, eukaryotic-type
IPR005741 Family DNA topoisomerase IV subunit A, Gram-positive
IPR005742 Family DNA topoisomerase IV, subunit A, Gram-negative

5 GO Annotations

GO Term Gene Name
GO:0003677 IPR013758
GO:0003918 IPR013758
GO:0005524 IPR013758
GO:0006259 IPR013758
GO:0006265 IPR013758

5 Ontology Annotations

GO Term Gene Name
GO:0003677 IPR013758
GO:0003918 IPR013758
GO:0005524 IPR013758
GO:0006259 IPR013758
GO:0006265 IPR013758

0 Parent Features

947 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
evm.TU.contig_37237.1 PAC:16431005 Carica papaya 43  
evm.model.supercontig_1221.1 PAC:16407101 Carica papaya 144  
evm.model.supercontig_54.38 PAC:16422389 Carica papaya 96  
Thhalv10002141m V4MCE0 PAC:20200346 Eutrema salsugineum 71  
Lus10032156 PAC:23161149 Linum usitatissimum 72  
Gorai.005G101700.3 A0A0D2RCB2 PAC:26806631 Gossypium raimondii 627  
Gorai.005G101700.4 A0A0D2NAC7 PAC:26806632 Gossypium raimondii 574  
Araha.4052s0002.1.p PAC:28842919 Arabidopsis halleri 249  
Cagra.2460s0027.1.p PAC:28897512 Capsella grandiflora 380  
Brara.D00547.1.p A0A397ZI71 PAC:30621755 Brassica rapa FPsc 154  
Bradi3g38860.1.p PAC:31153086 Brachypodium distachyon 592  
Bradi3g38850.1.p PAC:31151296 Brachypodium distachyon 515  
Medtr0756s0010.1 A0A072TDW4 PAC:31105847 Medicago truncatula 996  
Traes_1BL_8F3BBD25E.33 PAC:31982175 Triticum aestivum 134  
Traes_1DL_013A3A113.4 PAC:31907140 Triticum aestivum 687  
Traes_1DL_013A3A113.5 PAC:31907141 Triticum aestivum 501  
Traes_6BL_FC1815242.3 PAC:31905495 Triticum aestivum 280  
Traes_6DL_2BA26E6A2.4 PAC:31877749 Triticum aestivum 851  
Bradi4g16893.1.p A0A0Q3EL23 PAC:32789143 Brachypodium distachyon 1004  
Pp3c21_11820V3.2.p PAC:32916881 Physcomitrium patens 124  
Pp3c22_6500V3.1.p A0A2K1IMH1 PAC:32905247 Physcomitrium patens 67  
Pp3c3_37370V3.1.p A9SMZ5 PAC:32941203 Physcomitrium patens 243  
Pp3c3_37370V3.2.p A9SMZ5 PAC:32941204 Physcomitrium patens 243  
LOC_Os01g59290.1 PAC:33124238 Oryza sativa 86  
Zosma18g01000.1 A0A0K9PPJ8 PAC:33169513 Zostera marina 193  
Brdisv1Per11029704m.p PAC:33211212 Brachypodium distachyon Per1 175  
Brdisv1Per11036150m.p A0A0Q3EL23 PAC:33239985 Brachypodium distachyon Per1 1004  
Brdisv1Uni21024899m.p PAC:33255790 Brachypodium distachyon Uni2 1004  
Brdisv1Uni21034521m.p PAC:33290263 Brachypodium distachyon Uni2 175  
Brdisv1Bd3-1_r1022598m.p PAC:33301131 Brachypodium distachyon Bd3-1 109  

7 Publications

First Author Title Year Journal Volume Pages PubMed ID
            7770916
            11395412
            12596227
            12042765
            7980433
            16023670
            8982450