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Conserved domains on  [gi|357530985|gb|AET81546|]
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DNA topoisomerase IV subunit B, partial [Bradyrhizobium denitrificans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gyrB super family cl36442
DNA gyrase subunit B; Provisional
 1-145 9.14e-107

DNA gyrase subunit B; Provisional


The actual alignment was detected with superfamily member PRK14939:

Pssm-ID: 237860 [Multi-domain]  Cd Length: 756  Bit Score: 320.12  E-value: 9.14e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:PRK14939  41 MVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGIPTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:PRK14939 121 GVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGET-DKTGTEVRFWPSPEIFENTEFD 184
 
Name Accession Description Interval E-value
gyrB PRK14939
DNA gyrase subunit B; Provisional
 1-145 9.14e-107

DNA gyrase subunit B; Provisional


Pssm-ID: 237860 [Multi-domain]  Cd Length: 756  Bit Score: 320.12  E-value: 9.14e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:PRK14939  41 MVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGIPTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:PRK14939 121 GVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGET-DKTGTEVRFWPSPEIFENTEFD 184
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
1-145 6.30e-85

DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];


Pssm-ID: 439957 [Multi-domain]  Cd Length: 635  Bit Score: 260.35  E-value: 6.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:COG0187   39 LVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPVDIHPKEGKSALEVVLTVLHAGGKFDGGSYKVSGGLHGV 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:COG0187  119 GASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKT-DRTGTTVRFKPDPEIFETTEFD 182
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
 1-145 2.91e-84

Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.


Pssm-ID: 340405 [Multi-domain]  Cd Length: 180  Bit Score: 244.37  E-value: 2.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:cd16928    4 LVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGLHGV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAQgRRGTEVTFLASTETFKMVEYD 145
Cdd:cd16928   84 GVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETK-KTGTTVRFWPDPEIFEKTEFD 147
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
 1-141 1.18e-66

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 212.03  E-value: 1.18e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985     1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:smart00433   5 LVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGGLHGV 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357530985    81 GVSVVNALSSKLQLRIWREDKEHLIEF-AHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKM 141
Cdd:smart00433  85 GASVVNALSTEFEVEVARDGKEYKQSFsNNGKPLSEPKIIGDT-KKDGTKVTFKPDLEIFGM 145
parE_Gneg TIGR01055
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ...
 1-139 9.63e-49

DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. This protein is active as an alpha(2)beta(2) heterotetramer. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 130127 [Multi-domain]  Cd Length: 625  Bit Score: 165.09  E-value: 9.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985    1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:TIGR01055  34 LVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHPKEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGV 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAQGR-RGTEVTFLASTETF 139
Cdd:TIGR01055 114 GISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKRlTGTSVHFTPDPEIF 173
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 1-102 6.15e-15

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 66.24  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985    1 MVYEVVDNAIDEAlaGYASRVEVVLNADN--SVTVRDDGRGIPVDIHKgegvsaaevimtqlHAGGKFDQnSYKVSGGLH 78
Cdd:pfam02518   9 VLSNLLDNALKHA--AKAGEITVTLSEGGelTLTVEDNGIGIPPEDLP--------------RIFEPFST-ADKRGGGGT 71

                          90       100
                  ....*....|....*....|....
gi 357530985   79 GVGVSVVNALSSKLQLRIWREDKE 102
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEP 95
 
Name Accession Description Interval E-value
gyrB PRK14939
DNA gyrase subunit B; Provisional
 1-145 9.14e-107

DNA gyrase subunit B; Provisional


Pssm-ID: 237860 [Multi-domain]  Cd Length: 756  Bit Score: 320.12  E-value: 9.14e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:PRK14939  41 MVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGIPTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:PRK14939 121 GVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGET-DKTGTEVRFWPSPEIFENTEFD 184
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
1-145 6.30e-85

DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];


Pssm-ID: 439957 [Multi-domain]  Cd Length: 635  Bit Score: 260.35  E-value: 6.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:COG0187   39 LVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPVDIHPKEGKSALEVVLTVLHAGGKFDGGSYKVSGGLHGV 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:COG0187  119 GASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKT-DRTGTTVRFKPDPEIFETTEFD 182
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
 1-145 2.91e-84

Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.


Pssm-ID: 340405 [Multi-domain]  Cd Length: 180  Bit Score: 244.37  E-value: 2.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:cd16928    4 LVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGLHGV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAQgRRGTEVTFLASTETFKMVEYD 145
Cdd:cd16928   84 GVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETK-KTGTTVRFWPDPEIFEKTEFD 147
gyrB PRK05644
DNA gyrase subunit B; Validated
 1-145 1.07e-82

DNA gyrase subunit B; Validated


Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 254.63  E-value: 1.07e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:PRK05644  41 LVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGIPVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKMVEYD 145
Cdd:PRK05644 121 GVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGET-DETGTTVTFKPDPEIFETTEFD 184
PRK05559 PRK05559
DNA topoisomerase IV subunit B; Reviewed
 1-140 6.93e-76

DNA topoisomerase IV subunit B; Reviewed


Pssm-ID: 235501 [Multi-domain]  Cd Length: 631  Bit Score: 236.92  E-value: 6.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:PRK05559  41 LVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGIPVGIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357530985  81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEA-QGRRGTEVTFLASTETFK 140
Cdd:PRK05559 121 GVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTAgKRKTGTRVRFWPDPKIFD 181
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
 1-141 1.18e-66

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 212.03  E-value: 1.18e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985     1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:smart00433   5 LVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGGLHGV 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357530985    81 GVSVVNALSSKLQLRIWREDKEHLIEF-AHGDAVAPLKVVGEAqGRRGTEVTFLASTETFKM 141
Cdd:smart00433  85 GASVVNALSTEFEVEVARDGKEYKQSFsNNGKPLSEPKIIGDT-KKDGTKVTFKPDLEIFGM 145
parE_Gneg TIGR01055
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ...
 1-139 9.63e-49

DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. This protein is active as an alpha(2)beta(2) heterotetramer. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 130127 [Multi-domain]  Cd Length: 625  Bit Score: 165.09  E-value: 9.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985    1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGV 80
Cdd:TIGR01055  34 LVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHPKEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGV 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   81 GVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVGEAQGR-RGTEVTFLASTETF 139
Cdd:TIGR01055 114 GISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKRlTGTSVHFTPDPEIF 173
PTZ00109 PTZ00109
DNA gyrase subunit b; Provisional
 1-133 2.51e-37

DNA gyrase subunit b; Provisional


Pssm-ID: 240272 [Multi-domain]  Cd Length: 903  Bit Score: 134.62  E-value: 2.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGYASRVEVVLNADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKF-------------- 66
Cdd:PTZ00109 133 LLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPCDVSEKTGKSGLETVLTVLHSGGKFqdtfpknsrsdkse 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985  67 DQNS--------------------------YKVSGGLHGVGVSVVNALSSKLQLRIWREDKEHLIEFAHGDAVAPLKVVG 120
Cdd:PTZ00109 213 DKNDtksskkgksshvkgpkeakekessqmYEYSSGLHGVGLSVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFS 292

                        170
                 ....*....|...
gi 357530985 121 EAQGRRGTEVTFL 133
Cdd:PTZ00109 293 CPLKKRGTTIHFL 305
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 1-102 9.42e-16

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 68.06  E-value: 9.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985     1 MVYEVVDNAIDEALAGyaSRVEVVLNADN---SVTVRDDGRGIPvdihkgegvsaAEVIMTQLHAGGKFDQNSYKVSGgl 77
Cdd:smart00387   9 VLSNLLDNAIKYTPEG--GRITVTLERDGdhvEITVEDNGPGIP-----------PEDLEKIFEPFFRTDKRSRKIGG-- 73

                           90       100
                   ....*....|....*....|....*
gi 357530985    78 HGVGVSVVNALSSKLQLRIWREDKE 102
Cdd:smart00387  74 TGLGLSIVKKLVELHGGEISVESEP 98
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 1-102 6.15e-15

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 66.24  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985    1 MVYEVVDNAIDEAlaGYASRVEVVLNADN--SVTVRDDGRGIPVDIHKgegvsaaevimtqlHAGGKFDQnSYKVSGGLH 78
Cdd:pfam02518   9 VLSNLLDNALKHA--AKAGEITVTLSEGGelTLTVEDNGIGIPPEDLP--------------RIFEPFST-ADKRGGGGT 71

                          90       100
                  ....*....|....*....|....
gi 357530985   79 GVGVSVVNALSSKLQLRIWREDKE 102
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEP 95
39 PHA02569
DNA topoisomerase II large subunit; Provisional
 4-91 3.92e-14

DNA topoisomerase II large subunit; Provisional


Pssm-ID: 177398 [Multi-domain]  Cd Length: 602  Bit Score: 68.24  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   4 EVVDNAIDEALAG---YASRVEVVLNaDNSVTVRDDGRGIPVDIHK---GEGVSAAEVIMTQLHAGGKFDqNSYKVSGGL 77
Cdd:PHA02569  52 EIIDNSVDEAIRTnfkFANKIDVTIK-NNQVTVSDNGRGIPQAMVTtpeGEEIPGPVAAWTRTKAGSNFD-DTNRVTGGM 129

                         90
                 ....*....|....
gi 357530985  78 HGVGVSVVNALSSK 91
Cdd:PHA02569 130 NGVGSSLTNFFSVL 143
HATPase_TopII-like cd16930
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ...
 19-91 3.31e-12

Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the histidine kinase-like ATPase (HATpase) domains of human topoisomerase IIA (TopIIA) and TopIIB, Saccharomyces cerevisae TOP2p, and related proteins. These proteins catalyze the passage of DNA double strands through a transient double-strand break in the presence of ATP.


Pssm-ID: 340407 [Multi-domain]  Cd Length: 147  Bit Score: 60.04  E-value: 3.31e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357530985  19 SRVEVVLNAD-NSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGVGVSVVNALSSK 91
Cdd:cd16930   27 TCIKVTIDPEnNEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTE 100
PLN03128 PLN03128
DNA topoisomerase 2; Provisional
 20-90 5.47e-12

DNA topoisomerase 2; Provisional


Pssm-ID: 215593 [Multi-domain]  Cd Length: 1135  Bit Score: 62.03  E-value: 5.47e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357530985   20 RVEVVLNAD-NSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGVGVSVVNALSS 90
Cdd:PLN03128   76 SLKVDIDVEqNTISVYNNGKGIPVEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFST 147
PLN03237 PLN03237
DNA topoisomerase 2; Provisional
 21-143 2.79e-10

DNA topoisomerase 2; Provisional


Pssm-ID: 215641 [Multi-domain]  Cd Length: 1465  Bit Score: 57.18  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   21 VEVVLNAD-NSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGVGVSVVNALSSklqlriwre 99
Cdd:PLN03237  102 LRVVIDVEqNLISVYNNGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTTGGRNGYGAKLTNIFST--------- 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 357530985  100 dkEHLIEFAHGDAVAPLKVV-----GEA---------QGRRGTEVTFLASTETFKMVE 143
Cdd:PLN03237  173 --EFVIETADGKRQKKYKQVfsnnmGKKsepvitkckKSENWTKVTFKPDLAKFNMTH 228
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 26-91 2.38e-09

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 54.28  E-value: 2.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357530985   26 NADNSVTVRDDGRGIPVDIHKGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGVGVSVVNALSSK 91
Cdd:PTZ00108   91 EENGEISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLTNIFSTK 156
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 1-97 3.99e-06

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 42.98  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357530985   1 MVYEVVDNAIDEALAGyaSRVEVVLNADNS---VTVRDDGRGIPVDIhkgegvsaaevimtQLHAGGKFDQNSYKVSGGL 77
Cdd:cd00075    4 VLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEED--------------LERIFERFYRGDKSREGGG 67

                         90       100
                 ....*....|....*....|
gi 357530985  78 HGVGVSVVNALSSKLQLRIW 97
Cdd:cd00075   68 TGLGLAIVRRIVEAHGGRIT 87
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
4-43 3.20e-04

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 39.26  E-value: 3.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 357530985   4 EVVDNAIDealAGyASRVEVVLNAD--NSVTVRDDGRGIPVD 43
Cdd:COG0323   30 ELVENAID---AG-ATRIEVEIEEGgkSLIRVTDNGCGMSPE 67
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 2-43 1.22e-03

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 37.03  E-value: 1.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 357530985   2 VYEVVDNAIDealAGyASRVEVVLNAD--NSVTVRDDGRGIPVD 43
Cdd:cd16926   18 VKELVENSID---AG-ATRIDVEIEEGglKLIRVTDNGSGISRE 57
mutL PRK00095
DNA mismatch repair endonuclease MutL;
2-43 4.06e-03

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 36.35  E-value: 4.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 357530985   2 VYEVVDNAIDealAGyASRVEV-VLNAD-NSVTVRDDGRGIPVD 43
Cdd:PRK00095  27 VKELVENALD---AG-ATRIDIeIEEGGlKLIRVRDNGCGISKE 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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