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Conserved domains on  [gi|16077074|ref|NP_387887|]
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DNA gyrase (subunit B) [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

type IIA DNA topoisomerase subunit B (domain architecture ID 11481348)

type IIA DNA topoisomerase subunit B relaxes positive DNA supercoils generated during DNA replication

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
gyrB PRK05644
DNA gyrase subunit B; Validated
1-638 0e+00

DNA gyrase subunit B; Validated


:

Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 1363.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    1 MEQQQNSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGI 80
Cdd:PRK05644   1 KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIG 160
Cdd:PRK05644  81 PVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  161 ETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:PRK05644 161 ETDETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEKEETFHYEGGIKEYVEYLNRNKEPL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVR 320
Cdd:PRK05644 240 HEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:PRK05644 320 EGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK05644 400 ALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGT 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRvEYAYNDKELEELLK 560
Cdd:PRK05644 480 GIGDDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGK-EYAYSDEELDEILA 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  561 TLPQ--TPKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:PRK05644 559 ELKLkgNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKYVRNLDI 638
 
Name Accession Description Interval E-value
gyrB PRK05644
DNA gyrase subunit B; Validated
1-638 0e+00

DNA gyrase subunit B; Validated


Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 1363.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    1 MEQQQNSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGI 80
Cdd:PRK05644   1 KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIG 160
Cdd:PRK05644  81 PVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  161 ETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:PRK05644 161 ETDETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEKEETFHYEGGIKEYVEYLNRNKEPL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVR 320
Cdd:PRK05644 240 HEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:PRK05644 320 EGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK05644 400 ALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGT 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRvEYAYNDKELEELLK 560
Cdd:PRK05644 480 GIGDDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGK-EYAYSDEELDEILA 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  561 TLPQ--TPKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:PRK05644 559 ELKLkgNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKYVRNLDI 638
gyrB TIGR01059
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ...
8-638 0e+00

DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273421 [Multi-domain]  Cd Length: 654  Bit Score: 1173.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     8 YDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEK 87
Cdd:TIGR01059   1 YDASSIKVLEGLEAVRKRPGMYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    88 MGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGETDHTGT 167
Cdd:TIGR01059  81 EGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   168 TTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKNEYHYEGGIKSYVEYLNRSKEVVHEEPIYI 247
Cdd:TIGR01059 161 TVRFWPDPEIF-ETTEFDFDILAKRLRELAFLNSGVKISLEDERDGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   248 EGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVREGLTAII 327
Cdd:TIGR01059 240 KGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   328 SIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKSALEISNL 407
Cdd:TIGR01059 320 SVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   408 PGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFN 487
Cdd:TIGR01059 400 PGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFD 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   488 LEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGK---------------------RV 546
Cdd:TIGR01059 480 LEKLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKkeryikddkekdlvgealedlKA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   547 EYAYNDKELEELLKTLPQTP---KPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRR 623
Cdd:TIGR01059 560 LYIYSDKEKEEAKTQIPVHLgrkGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTLMGDEVEPRR 639
                         650
                  ....*....|....*
gi 16077074   624 NFIEANARYVKNLDI 638
Cdd:TIGR01059 640 EFIEANALDVKNLDV 654
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
4-638 0e+00

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


Pssm-ID: 223265 [Multi-domain]  Cd Length: 635  Bit Score: 1155.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   4 QQNSYDENQIQVLEGLEAVRKRPGMYIGSTNS-KGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPV 82
Cdd:COG0187   2 KTNNYDASSIQVLEGLEAVRKRPGMYIGSTGDgRGLHHLVWEVVDNSIDEALAGYADRIDVTLHEDGSISVEDNGRGIPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  83 GIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGET 162
Cdd:COG0187  82 DIHPKEKVSAVEVIFTVLHAGGKFDNDSYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYRQRFERGVPVTPLEVIGST 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 163 D--HTGTTTHFVPDPEIFSETtEYDYDLLANRVRELAFLTKGVNITIEDKREGqERKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:COG0187 162 DtkKTGTKVRFKPDPEIFGET-EFDYEILKRRLRELAFLNKGVKITLTDERTG-EEKKEFHYEGGLKDYVEYLNKGKTPL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDpnLSGDDVR 320
Cdd:COG0187 240 HEEIFYFNGEKDGIAVEVALQWNDGYSENILSFVNNIPTREGGTHEAGFRSALTRAINEYAKKKNLLKEGD--LTGDDIR 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:COG0187 318 EGLTAVISVKIPDPQFEGQTKEKLGNSEVRSIVEKLVSEAFSLFLEENPQEAKKIVEKAIAAAKAREAARKARELTRRKS 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:COG0187 398 ALDIPGLPGKLADCTSKDPEKSELFLVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIQTIITALGT 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRVEYAYNDKELEELLK 560
Cdd:COG0187 478 GIGKDFDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMPPLIENGHVYIAQPPLYKVKKGKKTFYAYDDEELEKLLE 557
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16077074 561 TLPQTPKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:COG0187 558 RLGKKKGYEIQRYKGLGEMNPDQLWETTMDPETRRLLQVTIEDADEADEIFSTLMGDKVEPRRNFIEENALFVENLDI 635
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
37-631 0e+00

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 966.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     37 GLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGG 116
Cdd:smart00433   1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    117 LHGVGASVVNALSTELDVTVHRDGKIHRQTYKR-GVPVTDLEIIGETDHTGTTTHFVPDPEIFSETTEYDYDLLANRVRE 195
Cdd:smart00433  81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTTDDDFELLKRRLRE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    196 LAFLTKGVNITIEDKREGQERknEYHYEGGIKSYVEYLNRSKEVVHEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTN 275
Cdd:smart00433 161 LAFLNKGVKITLNDERSDEEK--TFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    276 NINTYEGGTHEAGFKTGLTRVINDYARKKGLIKEndPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDT 355
Cdd:smart00433 239 NIATTEGGTHENGFKDALTRVINEYAKKKKKLKE--KNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEK 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    356 LFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKsALEISNLPGKLADCSSKDPSISELYIVEGDSAGGS 435
Cdd:smart00433 317 IVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGS 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    436 AKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLT 515
Cdd:smart00433 396 AKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEKLRYGKIIIMTDADVDGSHIKGLLLT 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    516 FFYRYMRQIIENGYVYIAQPPLYKVQQGKRvEYAYNDKELEELLKTLPQTP----KPGLQRYKGLGEMNATQLWETTMDP 591
Cdd:smart00433 476 FFYRYMPPLIEAGFVYIAIPPLYKVTKGKK-KYVYSFYSLDEYEKWLEKTEgnksKYEIQRYKGLGEMNADQLWETTMDP 554
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 16077074    592 SSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANAR 631
Cdd:smart00433 555 ERRTLLFVTLDDADEADLIFSALMGDKVEPRKEWIEENAP 594
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
38-216 6.27e-116

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: 343.36  E-value: 6.27e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  38 LHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGL 117
Cdd:cd16928   1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 118 HGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELA 197
Cdd:cd16928  81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIF-EKTEFDFDTLKRRLRELA 159
                       170
                ....*....|....*....
gi 16077074 198 FLTKGVNITIEDKREGQER 216
Cdd:cd16928 160 FLNKGLKIVLEDERTGKEE 178
DNA_gyraseB pfam00204
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ...
225-378 2.51e-77

DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.


Pssm-ID: 333922 [Multi-domain]  Cd Length: 173  Bit Score: 243.29  E-value: 2.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   225 GIKSYVEYLNRSKEVVHEEPIYIEGEK--DGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYAR 302
Cdd:pfam00204   1 GLKDYVEELNKDKKPLHKEIIYFEGEYpdDRIEVEVALQWTDSYSENILSFVNNIPTPEGGTHVDGFKSALTRAINEYAK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16077074   303 KKGLIKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDK 378
Cdd:pfam00204  81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLERFLEENPEIAKKILEK 156
 
Name Accession Description Interval E-value
gyrB PRK05644
DNA gyrase subunit B; Validated
1-638 0e+00

DNA gyrase subunit B; Validated


Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 1363.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    1 MEQQQNSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGI 80
Cdd:PRK05644   1 KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIG 160
Cdd:PRK05644  81 PVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  161 ETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:PRK05644 161 ETDETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEKEETFHYEGGIKEYVEYLNRNKEPL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVR 320
Cdd:PRK05644 240 HEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:PRK05644 320 EGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK05644 400 ALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGT 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRvEYAYNDKELEELLK 560
Cdd:PRK05644 480 GIGDDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGK-EYAYSDEELDEILA 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  561 TLPQ--TPKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:PRK05644 559 ELKLkgNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKYVRNLDI 638
gyrB TIGR01059
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ...
8-638 0e+00

DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273421 [Multi-domain]  Cd Length: 654  Bit Score: 1173.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     8 YDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEK 87
Cdd:TIGR01059   1 YDASSIKVLEGLEAVRKRPGMYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    88 MGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGETDHTGT 167
Cdd:TIGR01059  81 EGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   168 TTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKNEYHYEGGIKSYVEYLNRSKEVVHEEPIYI 247
Cdd:TIGR01059 161 TVRFWPDPEIF-ETTEFDFDILAKRLRELAFLNSGVKISLEDERDGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   248 EGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVREGLTAII 327
Cdd:TIGR01059 240 KGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   328 SIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKSALEISNL 407
Cdd:TIGR01059 320 SVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   408 PGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFN 487
Cdd:TIGR01059 400 PGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFD 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   488 LEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGK---------------------RV 546
Cdd:TIGR01059 480 LEKLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKkeryikddkekdlvgealedlKA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   547 EYAYNDKELEELLKTLPQTP---KPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRR 623
Cdd:TIGR01059 560 LYIYSDKEKEEAKTQIPVHLgrkGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTLMGDEVEPRR 639
                         650
                  ....*....|....*
gi 16077074   624 NFIEANARYVKNLDI 638
Cdd:TIGR01059 640 EFIEANALDVKNLDV 654
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
4-638 0e+00

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


Pssm-ID: 223265 [Multi-domain]  Cd Length: 635  Bit Score: 1155.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   4 QQNSYDENQIQVLEGLEAVRKRPGMYIGSTNS-KGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPV 82
Cdd:COG0187   2 KTNNYDASSIQVLEGLEAVRKRPGMYIGSTGDgRGLHHLVWEVVDNSIDEALAGYADRIDVTLHEDGSISVEDNGRGIPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  83 GIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGET 162
Cdd:COG0187  82 DIHPKEKVSAVEVIFTVLHAGGKFDNDSYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYRQRFERGVPVTPLEVIGST 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 163 D--HTGTTTHFVPDPEIFSETtEYDYDLLANRVRELAFLTKGVNITIEDKREGqERKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:COG0187 162 DtkKTGTKVRFKPDPEIFGET-EFDYEILKRRLRELAFLNKGVKITLTDERTG-EEKKEFHYEGGLKDYVEYLNKGKTPL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDpnLSGDDVR 320
Cdd:COG0187 240 HEEIFYFNGEKDGIAVEVALQWNDGYSENILSFVNNIPTREGGTHEAGFRSALTRAINEYAKKKNLLKEGD--LTGDDIR 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:COG0187 318 EGLTAVISVKIPDPQFEGQTKEKLGNSEVRSIVEKLVSEAFSLFLEENPQEAKKIVEKAIAAAKAREAARKARELTRRKS 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:COG0187 398 ALDIPGLPGKLADCTSKDPEKSELFLVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIQTIITALGT 477
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRVEYAYNDKELEELLK 560
Cdd:COG0187 478 GIGKDFDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMPPLIENGHVYIAQPPLYKVKKGKKTFYAYDDEELEKLLE 557
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16077074 561 TLPQTPKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:COG0187 558 RLGKKKGYEIQRYKGLGEMNPDQLWETTMDPETRRLLQVTIEDADEADEIFSTLMGDKVEPRRNFIEENALFVENLDI 635
gyrB PRK14939
DNA gyrase subunit B; Provisional
2-638 0e+00

DNA gyrase subunit B; Provisional


Pssm-ID: 237860 [Multi-domain]  Cd Length: 756  Bit Score: 1152.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    2 EQQQNSYDENQIQVLEGLEAVRKRPGMYIGSTN-SKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGI 80
Cdd:PRK14939   1 SMMSNSYGASSIKVLKGLDAVRKRPGMYIGDTDdGTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIG 160
Cdd:PRK14939  81 PTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  161 ETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGqeRKNEYHYEGGIKSYVEYLNRSKEVV 240
Cdd:PRK14939 161 ETDKTGTEVRFWPSPEIF-ENTEFDYDILAKRLRELAFLNSGVRIRLKDERDG--KEEEFHYEGGIKAFVEYLNRNKTPL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  241 HEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVR 320
Cdd:PRK14939 238 HPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKS 400
Cdd:PRK14939 318 EGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKG 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK14939 398 ALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGC 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  481 GIG-EDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRVEYAYNDKELE--- 556
Cdd:PRK14939 478 GIGrDEFNPDKLRYHKIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVKKGKQEQYLKDDEALDdyl 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074      --------------------------------------------------------------------------------
Cdd:PRK14939 558 ielalegatlhladgpaisgealeklvkeyravrkiidrlerrypravlealiyapaldlddladeaavaaldadfltsa 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  557 -----------------------------------ELLKTLPQTPKPGL--QRYKGLGEMNATQLWETTMDPSSRTLLQV 599
Cdd:PRK14939 638 eyrrlvelaeklrglieegaylergerkqpvssfeEALDWLLAEARKGLsiQRYKGLGEMNPEQLWETTMDPENRRLLQV 717
                        730       740       750
                 ....*....|....*....|....*....|....*....
gi 16077074  600 TLEDAMDADETFEMLMGDKVEPRRNFIEANARYVKNLDI 638
Cdd:PRK14939 718 TIEDAIAADEIFTTLMGDEVEPRREFIEENALNVANLDV 756
PRK05559 PRK05559
DNA topoisomerase IV subunit B; Reviewed
1-633 0e+00

DNA topoisomerase IV subunit B; Reviewed


Pssm-ID: 235501 [Multi-domain]  Cd Length: 631  Bit Score: 990.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    1 MEQQQNSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGI 80
Cdd:PRK05559   1 AAMMTNNYNADSIEVLEGLEPVRKRPGMYIGSTDTRGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIG 160
Cdd:PRK05559  81 PVGIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  161 ET--DHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELAFLTKGVNITIEDKREGQErkneYHYEGGIKSYVEYLNRSKE 238
Cdd:PRK05559 161 TAgkRKTGTRVRFWPDPKIF-DSPKFSPERLKERLRSKAFLLPGLTITLNDERERQT----FHYENGLKDYLAELNEGKE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  239 VVHEEPI-YIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKeNDPNLSGD 317
Cdd:PRK05559 236 TLPEEFVgSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLP-KGKKLEGE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  318 DVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKarELTR 397
Cdd:PRK05559 315 DVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAK--KVKR 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  398 RKSALEiSNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITA 477
Cdd:PRK05559 393 KKKTSG-PALPGKLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVA 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  478 LGTGIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRVEYAYNDKELEE 557
Cdd:PRK05559 472 IGIGPGDSFDLEDLRYGKIIIMTDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRVDKGKKKIYALDEEEKEE 551
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16077074  558 LLKTLPQT-PKPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARYV 633
Cdd:PRK05559 552 LLKKLGKKgGKPEIQRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDAEETEKLVDMLMGKKAEPRREWIEENGDFA 628
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
37-631 0e+00

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 966.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     37 GLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGG 116
Cdd:smart00433   1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    117 LHGVGASVVNALSTELDVTVHRDGKIHRQTYKR-GVPVTDLEIIGETDHTGTTTHFVPDPEIFSETTEYDYDLLANRVRE 195
Cdd:smart00433  81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTTDDDFELLKRRLRE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    196 LAFLTKGVNITIEDKREGQERknEYHYEGGIKSYVEYLNRSKEVVHEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTN 275
Cdd:smart00433 161 LAFLNKGVKITLNDERSDEEK--TFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    276 NINTYEGGTHEAGFKTGLTRVINDYARKKGLIKEndPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDT 355
Cdd:smart00433 239 NIATTEGGTHENGFKDALTRVINEYAKKKKKLKE--KNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEK 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    356 LFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKsALEISNLPGKLADCSSKDPSISELYIVEGDSAGGS 435
Cdd:smart00433 317 IVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGS 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    436 AKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLT 515
Cdd:smart00433 396 AKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEKLRYGKIIIMTDADVDGSHIKGLLLT 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    516 FFYRYMRQIIENGYVYIAQPPLYKVQQGKRvEYAYNDKELEELLKTLPQTP----KPGLQRYKGLGEMNATQLWETTMDP 591
Cdd:smart00433 476 FFYRYMPPLIEAGFVYIAIPPLYKVTKGKK-KYVYSFYSLDEYEKWLEKTEgnksKYEIQRYKGLGEMNADQLWETTMDP 554
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 16077074    592 SSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANAR 631
Cdd:smart00433 555 ERRTLLFVTLDDADEADLIFSALMGDKVEPRKEWIEENAP 594
parE_Gpos TIGR01058
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II ...
6-632 0e+00

DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation step 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. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 130130 [Multi-domain]  Cd Length: 637  Bit Score: 805.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     6 NSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIH 85
Cdd:TIGR01058   3 SKYNADAIKILEGLDAVRKRPGMYIGSTDSKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITVQDDGRGIPTGIH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    86 EKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKR-GVPVTDLEIIGETDH 164
Cdd:TIGR01058  83 QDGNISTVETVFTVLHAGGKFDQGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIYQQRFENgGKIVQSLKKIGTTKK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   165 TGTTTHFVPDPEIFSeTTEYDYDLLANRVRELAFLTKGVNITIEDKREGQerKNEYHYEGGIKSYVEYLNRSKEVVHEEp 244
Cdd:TIGR01058 163 TGTLVHFHPDPTIFK-TTQFNSNIIKERLKESAFLLKKLKLTFTDKRTNK--TTVFFYENGLVDFVDYINETKETLSQV- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   245 IYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVREGLT 324
Cdd:TIGR01058 239 TYFEGEKNGIEVEVAFQFNDGDSENILSFANSVKTKEGGTHENGFKLAITDVINSYARKYNLLKEKDKNLEGSDIREGLS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   325 AIISIKHPDP--QFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTR--RKS 400
Cdd:TIGR01058 319 AIISVRIPEEliQFEGQTKSKLFSPEARNVVDEIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKsgKKP 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   401 ALEISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:TIGR01058 399 KKEKGILSGKLTPAQSKNPAKNELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFCIGT 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   481 GIGEDFNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQ--GKRVEYAYNDKELEEL 558
Cdd:TIGR01058 479 GIGADFSIKDLKYDKIIIMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLSKkdGKKVKYAWSDLELESV 558
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16077074   559 LKTLPQTPkpgLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIEANARY 632
Cdd:TIGR01058 559 KKKLKNYT---LQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDLARAERQINTLMGDKVEPRKKWIEANINF 629
PTZ00109 PTZ00109
DNA gyrase subunit b; Provisional
3-630 0e+00

DNA gyrase subunit b; Provisional


Pssm-ID: 240272 [Multi-domain]  Cd Length: 903  Bit Score: 552.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    3 QQQNSYDENQIQVLEGLEAVRKRPGMYIGSTNSKGLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPV 82
Cdd:PTZ00109  95 QRCSEYDADDIVVLEGLEAVRKRPGMYIGNTDEKGLHQLLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPC 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   83 GIHEKMGRPAVEVIMTVLHAGGKF-DGSG---------------------------------------YKVSGGLHGVGA 122
Cdd:PTZ00109 175 DVSEKTGKSGLETVLTVLHSGGKFqDTFPknsrsdksedkndtksskkgksshvkgpkeakekessqmYEYSSGLHGVGL 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  123 SVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGE-TDHTGTTTHFVPD-PEIFSETTE-------------YDYD 187
Cdd:PTZ00109 255 SVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCpLKKRGTTIHFLPDyKHIFKTHHQhteteeeegckngFNLD 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  188 LLANRVRELAFLTKGVNITIEDKREGQErKNEYHYE-----GGIKSYVEYLNRSKEVVHEEP--IYIEGEKDGITVEVAL 260
Cdd:PTZ00109 335 LIKNRIHELSYLNPGLTFYLVDERIANE-NNFYPYEtikheGGTREFLEELIKDKTPLYKDIniISIRGVIKNVNVEVSL 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  261 QYN-DSYTSNIYSFTNNINTyEGGTHEAGFKTGLTRVINDYARKKGLIKENDPNLSGDDVREGLTAIISIKHPDPQFEGQ 339
Cdd:PTZ00109 414 SWSlESYTALIKSFANNVST-TAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISVKLNGAEFDGQ 492
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  340 TKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKARELTRRKSALEISN-LPGKLADCSSKD 418
Cdd:PTZ00109 493 TKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSTiLPGKLVDCISDD 572
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  419 PSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLD-KILSNNEVRSMITALGTGIGED------------ 485
Cdd:PTZ00109 573 IERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNPVtwrqydlshgtk 652
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  486 --------------------FNLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKV----- 540
Cdd:PTZ00109 653 askdesvqnnnstltkkknsLFDTPLRYGKIILLTDADVDGEHLRILLLTLLYRFCPSLYEHGRVYVACPPLYRItnnrm 732
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  541 -------QQGKRVEYAYNDKELEELLKTL-----------------------------------------PQTPKPG--- 569
Cdd:PTZ00109 733 kqfnvstKNSKKYIYTWSDEELNVLIKLLnkdysskettrsveekgnapdldneyedekldnknmrennvDEVELKTelg 812
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  570 --------------------------LQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRR 623
Cdd:PTZ00109 813 tnvadteqtdeldinkaffkfskhyeIQRFKGLGEMMADQLWETTMDPKKRILIRITVSDAMRASELIFLLMGEDVQSRK 892

                 ....*..
gi 16077074  624 NFIEANA 630
Cdd:PTZ00109 893 QFIFENS 899
parE_Gneg TIGR01055
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ...
7-628 0e+00

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: 547.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     7 SYDENQIQVLEGLEAVRKRPGMYIGSTNskgLHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHE 86
Cdd:TIGR01055   3 NYSAKDIEVLDGLEPVRKRPGMYTDTTR---PNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    87 KMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGETDH-- 164
Cdd:TIGR01055  80 KEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKrl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   165 TGTTTHFVPDPEIFSEtTEYDYDLLANRVRELAFLTKGVNITIEDKREGQERKneYHYEGGIKSYVEYLNRSKEVVHEEP 244
Cdd:TIGR01055 160 TGTSVHFTPDPEIFDS-LHFSVSRLYHILRAKAVLCRGVEIEFEDEVNNTKAL--WNYPDGLKDYLSEAVNGDNTLPPKP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   245 IYIEGEKDGITVEVALQYNDSYTSNIY-SFTNNINTYEGGTHEAGFKTGLTRVINDYARKKGlIKENDPNLSGDDVREGL 323
Cdd:TIGR01055 237 FSGNFEGDDEAVEWALLWLPEGGELFMeSYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRN-NLPRGVKLTAEDIWDRC 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   324 TAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDKGLMAARARMAAKKArelTRRKSALE 403
Cdd:TIGR01055 316 SYVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKK---VVRKKLTS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   404 ISNLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALgtGIG 483
Cdd:TIGR01055 393 GPALPGKLADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVAL--GID 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   484 EDFN-LEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQPPLYKVQQGKRVEYAYNDKELEELLKTL 562
Cdd:TIGR01055 471 PDSNdLSQLRYGKICILADADSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRIDLSKEVYYALDEEEKEKLLYKL 550
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   563 PQTP-KPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMD--ADETFEMLMGDKV-EPRRNFIEA 628
Cdd:TIGR01055 551 KKKKgKPNVQRFKGLGEMNPAQLRETTMDPNTRRLVQLTLDDVQDqrVDKIMDMLLAKKRsEDRFNWLQE 620
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
38-216 6.27e-116

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: 343.36  E-value: 6.27e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  38 LHHLVWEIVDNSIDEALAGYCTDINIQIEKDNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGL 117
Cdd:cd16928   1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 118 HGVGASVVNALSTELDVTVHRDGKIHRQTYKRGVPVTDLEIIGETDHTGTTTHFVPDPEIFsETTEYDYDLLANRVRELA 197
Cdd:cd16928  81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIF-EKTEFDFDTLKRRLRELA 159
                       170
                ....*....|....*....
gi 16077074 198 FLTKGVNITIEDKREGQER 216
Cdd:cd16928 160 FLNKGLKIVLEDERTGKEE 178
TopoII_Trans_DNA_gyrase cd00822
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ...
224-378 2.01e-89

TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to the B subunits of E. coli DNA gyrase and E. coli Topoisomerase IV which are heterodimers composed of two subunits. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. E.coli DNA gyrase is a heterodimer composed of two subunits. E. coli DNA gyrase B subunit is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes.


Pssm-ID: 238419 [Multi-domain]  Cd Length: 172  Bit Score: 274.82  E-value: 2.01e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 224 GGIKSYVEYLNRSKEVVHEEPIYIEGEKDGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYARK 303
Cdd:cd00822   1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16077074 304 KGLIKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDK 378
Cdd:cd00822  81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEK 155
TOPRIM_TopoIIA_GyrB cd03366
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
422-535 6.60e-86

TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to the Escherichia coli GyrB subunit. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. DNA gyrase is more effective at relaxing supercoils than decatentating DNA. DNA gyrase in addition inserts negative supercoils in the presence of ATP. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173786 [Multi-domain]  Cd Length: 114  Bit Score: 263.36  E-value: 6.60e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 422 SELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFNLEKARYHKVVIMTD 501
Cdd:cd03366   1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKLRYHKIIIMTD 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 16077074 502 ADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQP 535
Cdd:cd03366  81 ADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP 114
DNA_gyraseB pfam00204
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ...
225-378 2.51e-77

DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.


Pssm-ID: 333922 [Multi-domain]  Cd Length: 173  Bit Score: 243.29  E-value: 2.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   225 GIKSYVEYLNRSKEVVHEEPIYIEGEK--DGITVEVALQYNDSYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINDYAR 302
Cdd:pfam00204   1 GLKDYVEELNKDKKPLHKEIIYFEGEYpdDRIEVEVALQWTDSYSENILSFVNNIPTPEGGTHVDGFKSALTRAINEYAK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16077074   303 KKGLIKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDTLFSTAMETFMLENPDAAKKIVDK 378
Cdd:pfam00204  81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLERFLEENPEIAKKILEK 156
TOPRIM_TopoIIA_like cd01030
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
422-535 7.55e-71

TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173780 [Multi-domain]  Cd Length: 115  Bit Score: 224.31  E-value: 7.55e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 422 SELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIG-EDFNLEKARYHKVVIMT 500
Cdd:cd01030   1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGkDDFDLDKLRYGKIIIMT 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16077074 501 DADVDGAHIRTLLLTFFYRYMRQIIENGYVYIAQP 535
Cdd:cd01030  81 DADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT 115
39 PHA02569
DNA topoisomerase II large subunit; Provisional
11-626 6.29e-60

DNA topoisomerase II large subunit; Provisional


Pssm-ID: 177398 [Multi-domain]  Cd Length: 602  Bit Score: 210.77  E-value: 6.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   11 NQIQVLEGLEAVRKRPGMYIGSTNSK-----------------GLHHLVWEIVDNSIDEALAG---YCTDINIQIeKDNS 70
Cdd:PHA02569   2 DEFKVLSDREHILKRPGMYIGSVAYEaherflfgkftqveyvpGLVKIIDEIIDNSVDEAIRTnfkFANKIDVTI-KNNQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   71 ITVVDNGRGIPVGI-----HEKMGRPavEVIMTVLHAGGKFDGSGyKVSGGLHGVGASVVNALSTELdVTVHRDGkihrq 145
Cdd:PHA02569  81 VTVSDNGRGIPQAMvttpeGEEIPGP--VAAWTRTKAGSNFDDTN-RVTGGMNGVGSSLTNFFSVLF-IGETCDG----- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  146 tyKRGVPVT---DLEIIGETDH----TGTTTHFVPDPEIFSETT--EYDYDLLANRVRELAFLTKGVNITIEDKRegqer 216
Cdd:PHA02569 152 --KNEVTVNcsnGAENISWSTKpgkgKGTSVTFIPDFSHFEVNGldQQYLDIILDRLQTLAVVFPDIKFTFNGKK----- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  217 kneyhYEGGIKSYVEYLNrskevvhEEPIYIEGEKDGITVEVAlqyNDSYTSNiySFTNNINTYEGGTHEAGFKTGLTRV 296
Cdd:PHA02569 225 -----VSGKFKKYAKQFG-------DDTIVQENDNVSIALAPS---PDGFRQL--SFVNGLHTKNGGHHVDCVMDDICEE 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  297 INDYARKKGLIKENDPNlsgddVREGLTAIISIKH-PDPQFEGQTKTKLGNS--EARTITDtLFSTAMETFMLENPDAAK 373
Cdd:PHA02569 288 LIPMIKKKHKIEVTKAR-----VKECLTIVLFVRNmSNPRFDSQTKERLTSPfgEIRNHID-LDYKKIAKQILKTEAIIM 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  374 KIVDKGLMAAR---ARMAAKKARELTRRKSALEI-SNLPGKLADcsskdpsiSELYIVEGDSAGGSAKQGRDRHFQAILP 449
Cdd:PHA02569 362 PIIEAALARKLaaeKAAETKAAKKAKKAKVAKHIkANLIGKDAE--------TTLFLTEGDSAIGYLIEVRDEELHGGYP 433
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  450 LRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDfnLEKARYHKVVIMTDADVDG-AHIRTLLLTFFYRYmRQIIENG 528
Cdd:PHA02569 434 LRGKVLNTWGMSYADILKNKELFDICAITGLVLGEK--AENMNYKNIAIMTDADVDGkGSIYPLLLAFFSRW-PELFEQG 510
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  529 YVYIAQPPLYKVQQGKRVEYAYNDKELEELLKTLpqtPKPGLQRYKGLGEMNATQLWETTMDPssrTLLQVTLEDamDAD 608
Cdd:PHA02569 511 RIRFVKTPVIIAQVGKETKWFYSLDEFEKAKDSL---KKWSIRYIKGLGSLRKSEYRRVINNP---VYDVVVLPD--DWK 582
                        650
                 ....*....|....*...
gi 16077074  609 ETFEMLMGDKVEPRRNFI 626
Cdd:PHA02569 583 ELFEMLFGDDADLRKDWM 600
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
9-577 6.87e-47

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 178.32  E-value: 6.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     9 DENQIQVLEGLEAVRKRPGMYIGSTNSK-----------------------GLHHLVWEI----VDNSIDEALAGYCTDI 61
Cdd:PTZ00108    6 VEERYQKKTQIEHILLRPDTYIGSIETQtedmwvydeeknrmvyktityvpGLYKIFDEIlvnaADNKARDKGGHRMTYI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    62 NIQI-EKDNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDVTV--HR 138
Cdd:PTZ00108   86 KVTIdEENGEISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLTNIFSTKFTVECvdSK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   139 DGKIHRQTYKRGVPVTDLEII----GETDHTGTTthFVPDPEIF--SETTEYDYDLLANRVRELAFLTKGVNITIEDKRE 212
Cdd:PTZ00108  166 SGKKFKMTWTDNMSKKSEPRItsydGKKDYTKVT--FYPDYAKFgmTEFDDDMLRLLKKRVYDLAGCFGKLKVYLNGERI 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   213 gqerkneyhyegGIKSYVEY-----LNRSKEVVHEEPIYIEGEKDGitVEVALQYNDSyTSNIYSFTNNINTYEGGTHEA 287
Cdd:PTZ00108  244 ------------AIKSFKDYvdlylPDGEEGKKPPYPFVYTSVNGR--WEVVVSLSDG-QFQQVSFVNSICTTKGGTHVN 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   288 GFKTGLTRVINDYARKKgliKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTK-------TKLGNSeaRTITDTLFSTA 360
Cdd:PTZ00108  309 YILDQLISKLQEKAKKK---KKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKetlttkpSKFGST--CELSEKLIKYV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   361 METFMLEN----------PDAAKKIvdKGlmaararmaakkarelTRRKSALEISnlpgKLADCSSKDPSISE---LYIV 427
Cdd:PTZ00108  384 LKSPILENivewaqaklaAELNKKM--KA----------------GKKSRILGIP----KLDDANDAGGKNSEectLILT 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   428 EGDSA-----GGSAKQGRDRHfqAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDF-NLEKARYHKVVIMTD 501
Cdd:PTZ00108  442 EGDSAkalalAGLSVVGRDYY--GVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYeDPKGLRYGSLMIMTD 519
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16077074   502 ADVDGAHIRTLLLTFFYRYMRQIIE-NGYVYIAQPPLYKVQQ-GKRVEYAYNDKELEELLKTLPqTPKPGLQRYKGLG 577
Cdd:PTZ00108  520 QDHDGSHIKGLLINMIHHFWPSLLKnPGFLKEFITPIVKATKkGNQVISFFTIPDFEKWKQTVG-LKGWKIKYYKGLG 596
PLN03128 PLN03128
DNA topoisomerase 2; Provisional
19-577 9.74e-47

DNA topoisomerase 2; Provisional


Pssm-ID: 215593 [Multi-domain]  Cd Length: 1135  Bit Score: 177.59  E-value: 9.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    19 LEAVRKRPGMYIGST-----------NSK----------GLHHLVWEIVDNSIDEALAGYCTD---INIQIEKdNSITVV 74
Cdd:PLN03128   13 LEHILLRPDTYIGSTekhtqtlwvyeGGEmvnrevtyvpGLYKIFDEILVNAADNKQRDPSMDslkVDIDVEQ-NTISVY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    75 DNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDV-TVH-RDGKIHRQTYKRGVP 152
Cdd:PLN03128   92 NNGKGIPVEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFSTEFTVeTADgNRGKKYKQVFTNNMS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   153 VTDLEIIG--ETDHTGTTTHFVPDPEIFSETT--EYDYDLLANRVRELA-FLTKGVNITIEDKREgqerkneyhyegGIK 227
Cdd:PLN03128  172 VKSEPKITscKASENWTKITFKPDLAKFNMTRldEDVVALMSKRVYDIAgCLGKKLKVELNGKKL------------PVK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   228 SYVEYLN---RSKEVVHEEPIYIEGEKDGITVEVALQyNDSYTSniYSFTNNINTYEGGTHEAGFKTGLTRVINDYARKK 304
Cdd:PLN03128  240 SFQDYVGlylGPNSREDPLPRIYEKVNDRWEVCVSLS-DGSFQQ--VSFVNSIATIKGGTHVDYVADQIVKHIQEKVKKK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   305 gliKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKLgnsearTITDTLFSTAMETfmleNPDAAKKIVDKGLMAAR 384
Cdd:PLN03128  317 ---NKNATHVKPFQIKNHLWVFVNCLIENPTFDSQTKETL------TTRPSSFGSKCEL----SEEFLKKVEKCGVVENI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   385 ARMAAKKARELTRRKSALEISNLPG--KLADCS---SKDPSISELYIVEGDSA-----GGSAKQGRDRHfqAILPLRGKI 454
Cdd:PLN03128  384 LSWAQFKQQKELKKKDGAKRQRLTGipKLDDANdagGKKSKDCTLILTEGDSAkalamSGLSVVGRDHY--GVFPLRGKL 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   455 LNVEKARLDKILSNNEVRSMITALGTGIGEDFNLEKA---RYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQIIE-NGYV 530
Cdd:PLN03128  462 LNVREASHKQIMKNAEITNIKQILGLQFGKTYDEENTkslRYGHLMIMTDQDHDGSHIKGLIINFFHSFWPSLLKiPGFL 541
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 16077074   531 YIAQPPLYKVQQGKRVEYAYNDKELEELLKTL-PQTPKPGLQRYKGLG 577
Cdd:PLN03128  542 VEFITPIVKATKGGKSLSFYTMPEYEAWKESLeGETKGWTIKYYKGLG 589
DNA_gyraseB_C pfam00986
DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA ...
567-627 2.90e-39

DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA topoisomerase II are similar, but they have a different carboxyl terminus. The amino-terminal portion of the DNA gyrase B protein is thought to catalyze the ATP-dependent super-coiling of DNA. See pfam00204. The carboxyl-terminal end supports the complexation with the DNA gyrase A protein and the ATP-independent relaxation. This family also contains Topoisomerase IV. This is a bacterial enzyme that is closely related to DNA gyrase,.


Pssm-ID: 334335 [Multi-domain]  Cd Length: 63  Bit Score: 137.87  E-value: 2.90e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16077074   567 KPGLQRYKGLGEMNATQLWETTMDPSSRTLLQVTLEDAMDADETFEMLMGDKVEPRRNFIE 627
Cdd:pfam00986   3 KVEIQRYKGLGEMNPEQLWETTMDPETRRLLQVTIEDAAEADEIFSMLMGDKVEPRREFIE 63
PLN03237 PLN03237
DNA topoisomerase 2; Provisional
19-577 9.93e-31

DNA topoisomerase 2; Provisional


Pssm-ID: 215641 [Multi-domain]  Cd Length: 1465  Bit Score: 128.83  E-value: 9.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    19 LEAVRKRPGMYIGS---------------------TNSKGLHHLVWEIVDNSIDEALAGYCTD-INIQIEKD-NSITVVD 75
Cdd:PLN03237   38 LEHILLRPDTYIGSiekhtqtlwvyetdkmvqrsvTYVPGLYKIFDEILVNAADNKQRDPKMDsLRVVIDVEqNLISVYN 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    76 NGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELdVTVHRDG---KIHRQTYKRGVP 152
Cdd:PLN03237  118 NGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTTGGRNGYGAKLTNIFSTEF-VIETADGkrqKKYKQVFSNNMG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   153 VTDLEIIGETDHTG--TTTHFVPDPEIFSeTTEYDYD---LLANRVRELA-FLTKGVNITIEDKREgqerkneyhyegGI 226
Cdd:PLN03237  197 KKSEPVITKCKKSEnwTKVTFKPDLAKFN-MTHLEDDvvaLMKKRVVDIAgCLGKTVKVELNGKRI------------PV 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   227 KSYVEYLN---RSKEVVHEEPIYIEGEKDGITVEVALQYNDSYTSNIySFTNNINTYEGGTHeagfKTGLTRVINDYARK 303
Cdd:PLN03237  264 KSFSDYVDlylESANKSRPENLPRIYEKVNDRWEVCVSLSEGQFQQV-SFVNSIATIKGGTH----VDYVTNQIANHVME 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   304 KGLIKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKtklgnsEARTITDTLFSTAMETfmleNPDAAKKIVDKGLMAA 383
Cdd:PLN03237  339 AVNKKNKNANIKAHNVKNHLWVFVNALIDNPAFDSQTK------ETLTLRQSSFGSKCEL----SEDFLKKVMKSGIVEN 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   384 RARMAAKKARELTRRKSALEISNLPG--KLADCSSKDPSISE---LYIVEGDSAGGSAKQGR---DRHFQAILPLRGKIL 455
Cdd:PLN03237  409 LLSWADFKQSKELKKTDGAKTTRVTGipKLEDANEAGGKNSEkctLILTEGDSAKALAVAGLsvvGRNYYGVFPLRGKLL 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   456 NVEKARLDKILSNNEVRSMITALGTGIGEDF-NLEKARYHKVVIMTDADVDGAHIRTLLLTFFYRYMRQI--IENGYVYI 532
Cdd:PLN03237  489 NVREASHKQIMNNAEIENIKQILGLQHGKQYeSVKSLRYGHLMIMTDQDHDGSHIKGLLINFIHSFWPSLlkVPSFLVEF 568
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 16077074   533 AQPPLYKVQQGKRVEYAYNDKELEELLKTLPQTPKP-GLQRYKGLG 577
Cdd:PLN03237  569 ITPIVKATRRGKKVLSFYSMPEYEEWKESLGGNATGwSIKYYKGLG 614
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
226-345 3.46e-25

MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.


Pssm-ID: 238202 [Multi-domain]  Cd Length: 107  Bit Score: 100.03  E-value: 3.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 226 IKSYVEYLNRSKevVHEEPIYIEGEKDGITVEVALQYND---SYTSNIYSFTNNINTYEGGTHEAGFKTGLTRVINdyar 302
Cdd:cd00329   1 LKDRLAEILGDK--VADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 16077074 303 kkglikendpnlsGDDVREGLTAIISIKHPD--PQFE-GQTKTKLG 345
Cdd:cd00329  75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEVR 107
TOPRIM_TopoIIA cd03365
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
424-520 1.34e-20

TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173785 [Multi-domain]  Cd Length: 120  Bit Score: 87.36  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 424 LYIVEGDSAGGSAKQGR---DRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDF--NLEKARYHKVVI 498
Cdd:cd03365   3 LILTEGDSAKALAVAGLsvvGRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDyeSTKSLRYGRLMI 82
                        90       100
                ....*....|....*....|..
gi 16077074 499 MTDADVDGAHIRTLLLTFFYRY 520
Cdd:cd03365  83 MTDQDHDGSHIKGLLINFIHSF 104
Toprim pfam01751
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ...
423-535 6.99e-18

Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesizes the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases. Type II DNA topoisomerases catalyze the relaxation of DNA supercoiling by causing transient double strand breaks.


Pssm-ID: 334664 [Multi-domain]  Cd Length: 90  Bit Score: 78.51  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   423 ELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILsnnevrsmitalgtgigedfNLEKARYHKVVIMTDA 502
Cdd:pfam01751   1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLATKDKLKAL--------------------KELALKAKEVILATDP 60
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16077074   503 DVDGAHIRTLLLTffyryMRQIIEN--GYVYIAQP 535
Cdd:pfam01751  61 DREGEAIALKLLT-----LKELLEAagGRVKISEL 90
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
33-146 9.52e-17

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.15  E-value: 9.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074     33 TNSKGLHHLVWEIVDNSIDEALAGycTDINIQIEKDN---SITVVDNGRGIPvgihekmgrpaVEVIMTVLHAGGKFDGS 109
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG--GRITVTLERDGdhvEITVEDNGPGIP-----------PEDLEKIFEPFFRTDKR 67
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 16077074    110 GYKVSGglHGVGASVVNALSTELDVTVHRDGKIHRQT 146
Cdd:smart00387  68 SRKIGG--TGLGLSIVKKLVELHGGEISVESEPGGGT 102
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
33-146 1.99e-16

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: 334955 [Multi-domain]  Cd Length: 110  Bit Score: 75.11  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074    33 TNSKGLHHLVWEIVDNSIDEALAGYCTdINIQIEKDN-SITVVDNGRGIPVGIHEKMgrpavevimtvlhaGGKFDGSGY 111
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAKAGEIT-VTLSADGGDlTLTVEDNGIGIPPEDLPRI--------------FEPFSTDSS 65
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16077074   112 KVSGGLHGVGASVVNALSTELDVTVHRDGKIHRQT 146
Cdd:pfam02518  66 TRGGGGTGLGLSIVRKLVELMGGTITVESEPGGGT 100
HATPase_TopII-like cd16930
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ...
58-174 1.26e-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: 65.44  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  58 CTDINIQIEKdNSITVVDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTELDV-TV 136
Cdd:cd16930  28 CIKVTIDPEN-NEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFTVeTA 106
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16077074 137 HRD-GKIHRQTY-----KRGVPVTdLEIIGETDHTGTTthFVPD 174
Cdd:cd16930 107 DSEsKKKFKQTWtnnmgKASEPKI-TPYEKGKDYTKVT--FKPD 147
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
422-525 2.18e-07

Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173773 [Multi-domain]  Cd Length: 83  Bit Score: 48.58  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 422 SELYIVEGDSAGGSAKQGRDrHFQAILPLRGKILNVEKARLDKILSnnevrsmitalgtgigedfnlekaRYHKVVIMTD 501
Cdd:cd00188   1 KKLIIVEGPSDALALAQAGG-YGGAVVALGGHALNKTRELLKRLLG------------------------EAKEVIIATD 55
                        90       100
                ....*....|....*....|....
gi 16077074 502 ADVDGAHIRTLLLTFFYRYMRQII 525
Cdd:cd00188  56 ADREGEAIALRLLELLKSLGKKVR 79
TopoIIA_Trans_ScTopoIIA cd03481
TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ...
224-344 1.44e-05

TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topo IIA. S. cerevisiae Topo IIA is a homodimer encoded by a single gene. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes.


Pssm-ID: 239563  Cd Length: 153  Bit Score: 45.36  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074 224 GGIKSYVEYLNRSKEVVHEEPIYIEGEKDGITVEVALQYNDSYTSNIySFTNNINTYEGGTHEAGFKTGLTRVINDYARK 303
Cdd:cd03481   1 KSFKDYVKLYLKDANKEDGPPPPVVYEPVNDRWEVAVALSDGQFQQV-SFVNSIATTKGGTHVDYVADQIVKKLDEVVKK 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16077074 304 KgliKENDPNLSGDDVREGLTAIISIKHPDPQFEGQTKTKL 344
Cdd:cd03481  80 K---NKGGINVKPFQVKNHLWIFVNCLIENPSFDSQTKETL 117
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
38-137 8.64e-05

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: 41.82  E-value: 8.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  38 LHHLVWEIVDNSIDEALAGycTDINIQIEKDNS---ITVVDNGRGIPVGIHEKMGRPavevimtvlhaggkFDGSGYKVS 114
Cdd:cd00075   1 LEQVLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEEDLERIFER--------------FYRGDKSRE 64
                        90       100
                ....*....|....*....|...
gi 16077074 115 GGLHGVGASVVNALSTELDVTVH 137
Cdd:cd00075  65 GGGTGLGLAIVRRIVEAHGGRIT 87
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
44-81 1.93e-04

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


Pssm-ID: 223400 [Multi-domain]  Cd Length: 638  Bit Score: 44.25  E-value: 1.93e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 16077074  44 EIVDNSIDealAGyCTDINIQIEKD--NSITVVDNGRGIP 81
Cdd:COG0323  30 ELVENSLD---AG-ATRIDIEVEGGglKLIRVRDNGSGID 65
mutL PRK00095
DNA mismatch repair protein; Reviewed
44-81 1.38e-03

DNA mismatch repair protein; Reviewed


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 41.36  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 16077074   44 EIVDNSIDealAGyCTDINIQIEKD--NSITVVDNGRGIP 81
Cdd:PRK00095  29 ELVENALD---AG-ATRIDIEIEEGglKLIRVRDNGCGIS 64
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
44-81 1.43e-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: 40.11  E-value: 1.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 16077074  44 EIVDNSIDealAGyCTDINIQIEKD--NSITVVDNGRGIP 81
Cdd:cd16926  20 ELVENSID---AG-ATRIDVEIEEGglKLIRVTDNGSGIS 55
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
20-125 1.64e-03

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 40.02  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  20 EAVRKRPGMyIGSTN-SKGLHHLVWEIVDNSIDEA-LAGYCTDINIQIEKDN----SITVVDNGRGIPvgiHEKMGRpav 93
Cdd:cd16933   2 EFFRKNKEM-LGFDNpIRSLYTTVRELVENSLDATeEAGILPDIKVEIEEIGkdhyKVIVEDNGPGIP---EEQIPK--- 74
                        90       100       110
                ....*....|....*....|....*....|..
gi 16077074  94 eVIMTVLhAGGKFdgsGYKVSGGLHGVGASVV 125
Cdd:cd16933  75 -VFGKVL-YGSKY---HNKQSRGQQGLGISAA 101
COG1389 COG1389
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
20-125 1.71e-03

DNA topoisomerase VI, subunit B [Replication, recombination and repair];


Pssm-ID: 224307 [Multi-domain]  Cd Length: 538  Bit Score: 41.23  E-value: 1.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074  20 EAVRKRPGMyIGSTN-SKGLHHLVWEIVDNSIDEA-LAGYCTDINIQIEKDN----SITVVDNGRGIPVgihEKMGRpav 93
Cdd:COG1389  19 EFFRKNKEM-LGFDGpIRSLTTTVHELVTNSLDACeEAGILPDIKVEIERIGkdhyKVIVEDNGPGIPE---EQIPK--- 91
                        90       100       110
                ....*....|....*....|....*....|..
gi 16077074  94 eVIMTVLhAGGKFDGSgyKVSGGLHGVGASVV 125
Cdd:COG1389  92 -VFGKML-YGSKFHRN--IQSRGQQGIGISAA 119
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
36-125 2.33e-03

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 40.65  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16077074   36 KGLHHLVWEIVDNSIDEA-LAGYCTDINIQIEKDN------SITVVDNGRGIPvgihekmgrpaVEVIMTVLhagGK-FD 107
Cdd:PRK04184  35 RALYTTVKELVDNSLDACeEAGILPDIKIEIKRVDegkdhyRVTVEDNGPGIP-----------PEEIPKVF---GKlLY 100
                         90       100
                 ....*....|....*....|.
gi 16077074  108 GSGYKV---SGGLHGVGASVV 125
Cdd:PRK04184 101 GSKFHNlrqSRGQQGIGISAA 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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