|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-591 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 1095.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:PRK05644 28 MYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGIPVDIHPKTGKPAVEVVLTVLHAGGKFG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFET 160
Cdd:PRK05644 108 GGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 161 LSRRFQEMAFLNKGLTIVVRDERpdhiNGEPKEITYHYEGGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWNS 240
Cdd:PRK05644 188 LATRLRELAFLNKGLKITLTDER----EGEEKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYND 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 241 SYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEgKDENLAGEDIREGLTAIISVKLADPQFEGQTKTK 320
Cdd:PRK05644 264 GYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKE-KDDNLTGEDVREGLTAVISVKHPEPQFEGQTKTK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 321 LGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLLESgSGLPGKLADCQWSDPEKC 400
Cdd:PRK05644 343 LGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALES-SSLPGKLADCSSKDPEES 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 401 ELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILMADA 480
Cdd:PRK05644 422 ELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGDDFDISKLRYHKIIIMTDA 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 481 DVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKWDRKGddasYAYSDAERDAIIadgvARGKRDPRQHDGIQRF 560
Cdd:PRK05644 502 DVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGKE----YAYSDEELDEIL----AELKLKGNPKYGIQRY 573
|
570 580 590
....*....|....*....|....*....|.
gi 559767661 561 KGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:PRK05644 574 KGLGEMNPEQLWETTMDPETRTLLQVTIEDA 604
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-591 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 1047.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:COG0187 26 MYIGSTDERGLHHLVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPVDIHPKEGKSALEVVLTVLHAGGKFD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFET 160
Cdd:COG0187 106 GGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYET 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 161 LSRRFQEMAFLNKGLTIVVRDERPDhingEPKEITYHYEGGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWNS 240
Cdd:COG0187 186 LAERLRELAFLNKGLTITLTDEREE----EPKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWND 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 241 SYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEgKDENLAGEDIREGLTAIISVKLADPQFEGQTKTK 320
Cdd:COG0187 262 GYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKE-KDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 321 LGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLLESgSGLPGKLADCQWSDPEKC 400
Cdd:COG0187 341 LGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALES-SGLPGKLADCSSKDPEES 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 401 ELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILMADA 480
Cdd:COG0187 420 ELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGDDFDLEKLRYHKIIIMTDA 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 481 DVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKWdrkGDDASYAYSDAERDAIIADGVARGKrdprqhDGIQRF 560
Cdd:COG0187 500 DVDGAHIRTLLLTFFYRYMRPLIEAGHVYIAQPPLYRIKK---GKKTYYAYSDAELDELLKELKGKKK------VEIQRY 570
|
570 580 590
....*....|....*....|....*....|.
gi 559767661 561 KGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:COG0187 571 KGLGEMNPEQLWETTMDPETRTLLQVTIEDA 601
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-591 |
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: 890.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:TIGR01059 21 MYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHPEEGISAVEVVLTVLHAGGKFD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFET 160
Cdd:TIGR01059 101 KDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 161 LSRRFQEMAFLNKGLTIVVRDERpdhiNGEPKEITYHYEGGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWNS 240
Cdd:TIGR01059 181 LAKRLRELAFLNSGVKISLEDER----DGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWND 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 241 SYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEgKDENLAGEDIREGLTAIISVKLADPQFEGQTKTK 320
Cdd:TIGR01059 257 GYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKE-SKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 321 LGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLLESGsGLPGKLADCQWSDPEKC 400
Cdd:TIGR01059 336 LGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSG-GLPGKLADCSSKDPSKS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 401 ELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILMADA 480
Cdd:TIGR01059 415 ELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFDLEKLRYHKIIIMTDA 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 481 DVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKWDRKG----DD--------------ASYAYSDAERDAIIAd 542
Cdd:TIGR01059 495 DVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKKEryikDDkekdlvgealedlkALYIYSDKEKEEAKT- 573
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 559767661 543 gvARGKRDPRQHDGIQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:TIGR01059 574 --QIPVHLGRKGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDA 620
|
|
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-591 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 847.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGE-RGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKF 79
Cdd:PRK14939 27 MYIGDTDDgTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGIPTDIHPEEGVSAAEVIMTVLHAGGKF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 80 DSKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFE 159
Cdd:PRK14939 107 DQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 160 TLSRRFQEMAFLNKGLTIVVRDERPDhingepKEITYHYEGGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWN 239
Cdd:PRK14939 187 ILAKRLRELAFLNSGVRIRLKDERDG------KEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 240 SSYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEGKdENLAGEDIREGLTAIISVKLADPQFEGQTKT 319
Cdd:PRK14939 261 DSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAK-VSLTGDDAREGLTAVLSVKVPDPKFSSQTKD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 320 KLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLLEsGSGLPGKLADCQWSDPEK 399
Cdd:PRK14939 340 KLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALD-IAGLPGKLADCQEKDPAL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 400 CELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGV-HDEFDLAKLRYHKLILMA 478
Cdd:PRK14939 419 SELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIgRDEFNPDKLRYHKIIIMT 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 479 DADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKwdrKG---------------------DDASYAYSDAE-- 535
Cdd:PRK14939 499 DADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVK---KGkqeqylkddealddylielalEGATLHLADGPai 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 536 -------------------------------RDAIIADG----------------------------------------- 543
Cdd:PRK14939 576 sgealeklvkeyravrkiidrlerrypravlEALIYAPAldlddladeaavaaldadfltsaeyrrlvelaeklrgliee 655
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559767661 544 ---VARGKRDPRQHD----------------GIQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:PRK14939 656 gayLERGERKQPVSSfeealdwllaearkglSIQRYKGLGEMNPEQLWETTMDPENRRLLQVTIEDA 722
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-591 |
0e+00 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 815.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:PRK05559 28 MYIGSTDTRGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGIPVGIHPEEGKSGVEVILTKLHAGGKFS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGT--TTTFWADSDIFETTTWNF 158
Cdd:PRK05559 108 NKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTAGKRKTgtRVRFWPDPKIFDSPKFSP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 159 ETLSRRFQEMAFLNKGLTIVVRDERpdhingepKEITYHYEGGLSDFVRHLNSKKEPAHL-SVIDFEEHGEGIAVEIAMQ 237
Cdd:PRK05559 188 ERLKERLRSKAFLLPGLTITLNDER--------ERQTFHYENGLKDYLAELNEGKETLPEeFVGSFEGEAEGEAVEWALQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 238 WNSSYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKegKDENLAGEDIREGLTAIISVKLADPQFEGQT 317
Cdd:PRK05559 260 WTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLP--KGKKLEGEDVREGLAAVLSVKIPEPQFEGQT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 318 KTKLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQarDLTRRKslLESGSGLPGKLADCQWSDP 397
Cdd:PRK05559 338 KEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAK--KVKRKK--KTSGPALPGKLADCTSQDP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 398 EKCELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILM 477
Cdd:PRK05559 414 ERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDSFDLEDLRYGKIIIM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 478 ADADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIkwdRKGDDASYAYSDAERDAIIADGVARGKRDPrqhdgI 557
Cdd:PRK05559 494 TDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRV---DKGKKKIYALDEEEKEELLKKLGKKGGKPE-----I 565
|
570 580 590
....*....|....*....|....*....|....
gi 559767661 558 QRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:PRK05559 566 QRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDA 599
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
10-591 |
0e+00 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 783.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 10 GLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFDSKSYAVSGG 89
Cdd:smart00433 1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 90 LHGVGAAVVNALSTRLQVEIRREGHVWRQSYLR-GVPTAPLARGEATAETGTTTTFWADSDIFETTT-WNFETLSRRFQE 167
Cdd:smart00433 81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTTdDDFELLKRRLRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 168 MAFLNKGLTIVVRDERpdhingEPKEITYHYEGGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWNSSYSESVY 247
Cdd:smart00433 161 LAFLNKGVKITLNDER------SDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 248 TFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEgkdENLAGEDIREGLTAIISVKLADPQFEGQTKTKLGNTEAK 327
Cdd:smart00433 235 SFVNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKE---KNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 328 SFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLleSGSGLPGKLADCQWSDPEKCELFIVEG 407
Cdd:smart00433 312 FGVEKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKKKL--SSISLPGKLADASSAGPKKCELFLVEG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 408 DSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILMADADVDGQHI 487
Cdd:smart00433 390 DSAGGSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEKLRYGKIIIMTDADVDGSHI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 488 TTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKWDRKGDDASYAYSDAERDAIIADGVARGKrdprqhDGIQRFKGLGEMN 567
Cdd:smart00433 470 KGLLLTFFYRYMPPLIEAGFVYIAIPPLYKVTKGKKKYVYSFYSLDEYEKWLEKTEGNKSK------YEIQRYKGLGEMN 543
|
570 580
....*....|....*....|....
gi 559767661 568 AAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:smart00433 544 ADQLWETTMDPERRTLLFVTLDDA 567
|
|
| parE_Gpos |
TIGR01058 |
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II ... |
1-591 |
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: 615.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:TIGR01058 25 MYIGSTDSKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITVQDDGRGIPTGIHQDGNISTVETVFTVLHAGGKFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRG-VPTAPLARGEATAETGTTTTFWADSDIFETTTWNFE 159
Cdd:TIGR01058 105 QGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIYQQRFENGgKIVQSLKKIGTTKKTGTLVHFHPDPTIFKTTQFNSN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 160 TLSRRFQEMAFLNKGLTIVVRDERPDhingepKEITYHYEGGLSDFVRHLNSKKEPahLS-VIDFEEHGEGIAVEIAMQW 238
Cdd:TIGR01058 185 IIKERLKESAFLLKKLKLTFTDKRTN------KTTVFFYENGLVDFVDYINETKET--LSqVTYFEGEKNGIEVEVAFQF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 239 NSSYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEgKDENLAGEDIREGLTAIISVKLADP--QFEGQ 316
Cdd:TIGR01058 257 NDGDSENILSFANSVKTKEGGTHENGFKLAITDVINSYARKYNLLKE-KDKNLEGSDIREGLSAIISVRIPEEliQFEGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 317 TKTKLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKSLQAARARLAARQARDLTRR-KSLLESGSGLPGKLADCQWS 395
Cdd:TIGR01058 336 TKSKLFSPEARNVVDEIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKSgKKPKKEKGILSGKLTPAQSK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 396 DPEKCELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLI 475
Cdd:TIGR01058 416 NPAKNELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFCIGTGIGADFSIKDLKYDKII 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 476 LMADADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKwDRKGDDASYAYSDAERDAIiadgvargkRDPRQHD 555
Cdd:TIGR01058 496 IMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLS-KKDGKKVKYAWSDLELESV---------KKKLKNY 565
|
570 580 590
....*....|....*....|....*....|....*.
gi 559767661 556 GIQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:TIGR01058 566 TLQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDL 601
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
1-591 |
7.03e-158 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 475.14 E-value: 7.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKF- 79
Cdd:PTZ00109 120 MYIGNTDEKGLHQLLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPCDVSEKTGKSGLETVLTVLHSGGKFq 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 80 ----------------DSKS-----------------------YAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSY 120
Cdd:PTZ00109 200 dtfpknsrsdksedknDTKSskkgksshvkgpkeakekessqmYEYSSGLHGVGLSVVNALSSFLKVDVFKGGKIYSIEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 121 LRGVPTAPLA-RGEATAETGTTTTFWAD-SDIFETTT--------------WNFETLSRRFQEMAFLNKGLTIVVRDERP 184
Cdd:PTZ00109 280 SKGKVTKPLSvFSCPLKKRGTTIHFLPDyKHIFKTHHqhteteeeegckngFNLDLIKNRIHELSYLNPGLTFYLVDERI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 185 DHINGEPKEITYHYEGGLSDFVRHLNSKKEPAH--LSVIDFEEHGEGIAVEIAMQWNS-SYSESVYTFANTINTAeGGTH 261
Cdd:PTZ00109 360 ANENNFYPYETIKHEGGTREFLEELIKDKTPLYkdINIISIRGVIKNVNVEVSLSWSLeSYTALIKSFANNVSTT-AGTH 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 262 EEGFRAALTSIVNRYAREQKFLKeGKDENLAGEDIREGLTAIISVKLADPQFEGQTKTKLGNTEAKSFVQKACNDHLRDW 341
Cdd:PTZ00109 439 IDGFKYAITRCVNGNIKKNGYFK-GNFVNIPGEFIREGMTAIISVKLNGAEFDGQTKTKLGNHLLKTILESIVFEQLSEI 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 342 FERNPGEAKEIISKSLQAARARLAARQARDLTRRKSLLESGSGLPGKLADCQWSDPEKCELFIVEGDSAGGSAKGGRDSR 421
Cdd:PTZ00109 518 LEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSTILPGKLVDCISDDIERNELFIVEGESAAGNAKQARNRE 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 422 YQAILPIRGKILNVEKARID-KVLKNNEVQALITAMGTGVH-----------------DEF---------------DLAK 468
Cdd:PTZ00109 598 FQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNpvtwrqydlshgtkaskDESvqnnnstltkkknslFDTP 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 469 LRYHKLILMADADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKWDRKGDDAS---------YAYSDAERDAI 539
Cdd:PTZ00109 678 LRYGKIILLTDADVDGEHLRILLLTLLYRFCPSLYEHGRVYVACPPLYRITNNRMKQFNVstknskkyiYTWSDEELNVL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 540 IA------------DGVARGKRDPRQHDG--------------------------------------------------- 556
Cdd:PTZ00109 758 IKllnkdysskettRSVEEKGNAPDLDNEyedekldnknmrennvdevelktelgtnvadteqtdeldinkaffkfskhy 837
|
730 740 750
....*....|....*....|....*....|....*.
gi 559767661 557 -IQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:PTZ00109 838 eIQRFKGLGEMMADQLWETTMDPKKRILIRITVSDA 873
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
1-590 |
5.49e-152 |
|
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: 450.91 E-value: 5.49e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGergLHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFD 80
Cdd:TIGR01055 24 MYTDTTR---PNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHPKEGVSAVEVILTTLHAGGKFS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 81 SKSYAVSGGLHGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPL--ARGEATAETGTTTTFWADSDIFETTTWNF 158
Cdd:TIGR01055 101 NKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLisAGTCGKRLTGTSVHFTPDPEIFDSLHFSV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 159 ETLSRRFQEMAFLNKGLTIVVRDERpdhingEPKEITYHYEGGLSDFVRHLNSKKE--PAHLSVIDFEehGEGIAVEIAM 236
Cdd:TIGR01055 181 SRLYHILRAKAVLCRGVEIEFEDEV------NNTKALWNYPDGLKDYLSEAVNGDNtlPPKPFSGNFE--GDDEAVEWAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 237 QWNSSYSESVY-TFANTINTAEGGTHEEGFRAALTSIVNRYAREQKFLKEGKdeNLAGEDIREGLTAIISVKLADPQFEG 315
Cdd:TIGR01055 253 LWLPEGGELFMeSYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRNNLPRGV--KLTAEDIWDRCSYVLSIKMQDPQFAG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 316 QTKTKLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIIskSLQAARARLAARQARDLTRRKslLESGSGLPGKLADCQWS 395
Cdd:TIGR01055 331 QTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLA--EHAISSAQRRKRAAKKVVRKK--LTSGPALPGKLADCTRQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 396 DPEKCELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGvHDEFDLAKLRYHKLI 475
Cdd:TIGR01055 407 DLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGID-PDSNDLSQLRYGKIC 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 476 LMADADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCPPLYKIKwdrKGDDASYAYSDAERDAIIaDGVARGKRDPRqhd 555
Cdd:TIGR01055 486 ILADADSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRID---LSKEVYYALDEEEKEKLL-YKLKKKKGKPN--- 558
|
570 580 590
....*....|....*....|....*....|....*
gi 559767661 556 gIQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDD 590
Cdd:TIGR01055 559 -VQRFKGLGEMNPAQLRETTMDPNTRRLVQLTLDD 592
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
11-183 |
2.87e-96 |
|
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: 291.75 E-value: 2.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 11 LHHLVYEVVDNSVDEALAGHADRIEVTLLADNGVRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFDSKSYAVSGGL 90
Cdd:cd16928 1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 91 HGVGAAVVNALSTRLQVEIRREGHVWRQSYLRGVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFETLSRRFQEMAF 170
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIFEKTEFDFDTLKRRLRELAF 160
|
170
....*....|...
gi 559767661 171 LNKGLTIVVRDER 183
Cdd:cd16928 161 LNKGLKIVLEDER 173
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
200-355 |
4.06e-76 |
|
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: 239.38 E-value: 4.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 200 GGLSDFVRHLNSKKEPAHLSVIDFEEHGEGIAVEIAMQWNSSYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYARE 279
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559767661 280 QKFLKEgKDENLAGEDIREGLTAIISVKLADPQFEGQTKTKLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISK 355
Cdd:cd00822 81 NNLLKK-KDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEK 155
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
201-356 |
8.57e-69 |
|
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: 425522 [Multi-domain] Cd Length: 173 Bit Score: 220.18 E-value: 8.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 201 GLSDFVRHLNSKKEPAHLSVIDF--EEHGEGIAVEIAMQWNSSYSESVYTFANTINTAEGGTHEEGFRAALTSIVNRYAR 278
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFegESPDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559767661 279 EQKFLKEgKDENLAGEDIREGLTAIISVKLADPQFEGQTKTKLGNTEAKSFVQKACNDHLRDWFERNPGEAKEIISKS 356
Cdd:pfam00204 81 KKGLLKK-KDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKA 157
|
|
| TOPRIM_TopoIIA_GyrB |
cd03366 |
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
400-513 |
1.04e-68 |
|
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: 217.91 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 400 CELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAKLRYHKLILMAD 479
Cdd:cd03366 1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKLRYHKIIIMTD 80
|
90 100 110
....*....|....*....|....*....|....
gi 559767661 480 ADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCP 513
Cdd:cd03366 81 ADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP 114
|
|
| TOPRIM_TopoIIA_like |
cd01030 |
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
400-513 |
1.49e-56 |
|
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: 185.79 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 400 CELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVH-DEFDLAKLRYHKLILMA 478
Cdd:cd01030 1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGkDDFDLDKLRYGKIIIMT 80
|
90 100 110
....*....|....*....|....*....|....*
gi 559767661 479 DADVDGQHITTLLLTLLFRFMRPLIEAGHVYLSCP 513
Cdd:cd01030 81 DADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT 115
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
1-487 |
4.43e-37 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 147.93 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTGERGLHHLVYE---VVDNSV----------DEALAGHAD---------RIEVTLLADNG-VRVVDNGRGIPVGE 57
Cdd:PLN03128 22 TYIGSTEKHTQTLWVYEggeMVNREVtyvpglykifDEILVNAADnkqrdpsmdSLKVDIDVEQNtISVYNNGKGIPVEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 58 HPVEKKPAVELVMTTLHAGGKFDSKSYAVSGGLHGVGAAVVNALSTRLQVEI------RREGHVWRQSYlrGVPTAPLAR 131
Cdd:PLN03128 102 HKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFSTEFTVETadgnrgKKYKQVFTNNM--SVKSEPKIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 132 GEATAETGTTTTFWADSDIFETTTWNFET---LSRRFQEMA-FLNKGLTIvvrderpdHINGEPKEItyhyeGGLSDFVR 207
Cdd:PLN03128 180 SCKASENWTKITFKPDLAKFNMTRLDEDVvalMSKRVYDIAgCLGKKLKV--------ELNGKKLPV-----KSFQDYVG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 208 -HLNSKKEPAHLSVIdFEEHGEGIAVEIAMqwnSSYSESVYTFANTINTAEGGTHEEgfraALTSIVNRYAREQKFLKEG 286
Cdd:PLN03128 247 lYLGPNSREDPLPRI-YEKVNDRWEVCVSL---SDGSFQQVSFVNSIATIKGGTHVD----YVADQIVKHIQEKVKKKNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 287 KDENLAGEDIREGLTAIISVKLADPQFEGQTKTKLgNTEAKSFVQKAcndHLRDWFER---NPGEAKEIISKSLQAARAR 363
Cdd:PLN03128 319 NATHVKPFQIKNHLWVFVNCLIENPTFDSQTKETL-TTRPSSFGSKC---ELSEEFLKkveKCGVVENILSWAQFKQQKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 364 LAARqarDLTRRKSLLesgsGLPgKLADCQWS---DPEKCELFIVEGDSAGGSAKGG-----RDsrYQAILPIRGKILNV 435
Cdd:PLN03128 395 LKKK---DGAKRQRLT----GIP-KLDDANDAggkKSKDCTLILTEGDSAKALAMSGlsvvgRD--HYGVFPLRGKLLNV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 559767661 436 EKARIDKVLKNNEVQALITAMG---TGVHDEFDLAKLRYHKLILMADADVDGQHI 487
Cdd:PLN03128 465 REASHKQIMKNAEITNIKQILGlqfGKTYDEENTKSLRYGHLMIMTDQDHDGSHI 519
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
20-487 |
1.44e-34 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 140.18 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 20 DNSVDEALAGHADRIEVTLLADNG-VRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFDSKSYAVSGGLHGVGAAVV 98
Cdd:PTZ00108 71 DNKARDKGGHRMTYIKVTIDEENGeISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 99 NALSTRLQVEIR-----REGH-VWRQSYLRGvpTAPLARGEATAETGTTTTFWADSDIFETTTWNFETLS---RRFQEMA 169
Cdd:PTZ00108 151 NIFSTKFTVECVdsksgKKFKmTWTDNMSKK--SEPRITSYDGKKDYTKVTFYPDYAKFGMTEFDDDMLRllkKRVYDLA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 170 FLNKGLTIvvrderpdHINGEPKEITyhyegGLSDFVRhLNSKKEPAHLSVIDFEEHGE-GIAVEIAMqwnsSYSESVYT 248
Cdd:PTZ00108 229 GCFGKLKV--------YLNGERIAIK-----SFKDYVD-LYLPDGEEGKKPPYPFVYTSvNGRWEVVV----SLSDGQFQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 249 ---FANTINTAEGGTHeegFRAALTSIVNRYAREQKFLKEGKDEnLAGEDIREGLTAIISVKLADPQFEGQTKTKLgNTE 325
Cdd:PTZ00108 291 qvsFVNSICTTKGGTH---VNYILDQLISKLQEKAKKKKKKGKE-IKPNQIKNHLWVFVNCLIVNPSFDSQTKETL-TTK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 326 AKSFVQK-ACNDHLRDWFERNPgeakeIISKSLQAARARLAARQARDL-TRRKSLLesgSGLPgKLADCQWSDP---EKC 400
Cdd:PTZ00108 366 PSKFGSTcELSEKLIKYVLKSP-----ILENIVEWAQAKLAAELNKKMkAGKKSRI---LGIP-KLDDANDAGGknsEEC 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 401 ELFIVEGDSAGGSAKGGRDS---RYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGTGVHDEFDLAK-LRYHKLIL 476
Cdd:PTZ00108 437 TLILTEGDSAKALALAGLSVvgrDYYGVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEDPKgLRYGSLMI 516
|
490
....*....|.
gi 559767661 477 MADADVDGQHI 487
Cdd:PTZ00108 517 MTDQDHDGSHI 527
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
1-590 |
1.32e-29 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 123.71 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 1 MYIGSTG----ER-------------GLHHLVYEVVDNSVDEALAG---HADRIEVTLlADNGVRVVDNGRGIPvgEHPV 60
Cdd:PHA02569 19 MYIGSVAyeahERflfgkftqveyvpGLVKIIDEIIDNSVDEAIRTnfkFANKIDVTI-KNNQVTVSDNGRGIP--QAMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 61 EKKPAVEL-----VMTTLHAGGKFDSKSyAVSGGLHGVGAAVVNALSTRL---------QVEIR----REGHVWRQSYLR 122
Cdd:PHA02569 96 TTPEGEEIpgpvaAWTRTKAGSNFDDTN-RVTGGMNGVGSSLTNFFSVLFigetcdgknEVTVNcsngAENISWSTKPGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 123 GVPTaplargeataetgtTTTFWADSDIFETTTWNFETL---SRRFQEMAflnkgltiVVRDERPDHINGEpkeityHYE 199
Cdd:PHA02569 175 GKGT--------------SVTFIPDFSHFEVNGLDQQYLdiiLDRLQTLA--------VVFPDIKFTFNGK------KVS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 200 GGLSDFVRHLNSKKepahlsvIDFEEHGEGIAVEiamqwNSSYSESVYTFANTINTAEGGTHEEGFRAALTS-IVNRYAR 278
Cdd:PHA02569 227 GKFKKYAKQFGDDT-------IVQENDNVSIALA-----PSPDGFRQLSFVNGLHTKNGGHHVDCVMDDICEeLIPMIKK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 279 EQKFlkegkdeNLAGEDIREGLTAIISVK-LADPQFEGQTKTKLGNT--EAKSFVQ----KACNDHLRDwfernpgeaKE 351
Cdd:PHA02569 295 KHKI-------EVTKARVKECLTIVLFVRnMSNPRFDSQTKERLTSPfgEIRNHIDldykKIAKQILKT---------EA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 352 IISKSLQAARARLAARQARDLTRRKSllesgSGLPGKLAD----CQWSDPEKCELFIVEGDSAGGSAKGGRDSRYQAILP 427
Cdd:PHA02569 359 IIMPIIEAALARKLAAEKAAETKAAK-----KAKKAKVAKhikaNLIGKDAETTLFLTEGDSAIGYLIEVRDEELHGGYP 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 428 IRGKILNVEKARIDKVLKNNEVqALITAMgTGVHDEFDLAKLRYHKLILMADADVDGQHITTLLLTLLFRFMRPLIEAGH 507
Cdd:PHA02569 434 LRGKVLNTWGMSYADILKNKEL-FDICAI-TGLVLGEKAENMNYKNIAIMTDADVDGKGSIYPLLLAFFSRWPELFEQGR 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 508 VYLSCPPLYkIKWDRKGDDASYAYSDAERDaiiadgvargKRDPRQHDgIQRFKGLGEMNAAQLWETTMNPdtrLLRQVT 587
Cdd:PHA02569 512 IRFVKTPVI-IAQVGKETKWFYSLDEFEKA----------KDSLKKWS-IRYIKGLGSLRKSEYRRVINNP---VYDVVV 576
|
...
gi 559767661 588 LDD 590
Cdd:PHA02569 577 LPD 579
|
|
| DNA_gyraseB_C |
pfam00986 |
DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA ... |
557-591 |
3.88e-22 |
|
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: 460016 [Multi-domain] Cd Length: 63 Bit Score: 89.74 E-value: 3.88e-22
10 20 30
....*....|....*....|....*....|....*
gi 559767661 557 IQRFKGLGEMNAAQLWETTMNPDTRLLRQVTLDDA 591
Cdd:pfam00986 6 IQRYKGLGEMNPEQLWETTMDPETRRLLQVTIEDA 40
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
10-487 |
2.27e-21 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 99.17 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 10 GLHHLVYEVVDNSVDEALAG-HADRIEVTLLADNG-VRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFDSKSYAVS 87
Cdd:PLN03237 77 GLYKIFDEILVNAADNKQRDpKMDSLRVVIDVEQNlISVYNNGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 88 GGLHGVGAAVVNALSTRLQVEI---RREGHvWRQSYLR--GVPTAPLARGEATAETGTTTTFWADSDIFETTTWNFET-- 160
Cdd:PLN03237 157 GGRNGYGAKLTNIFSTEFVIETadgKRQKK-YKQVFSNnmGKKSEPVITKCKKSENWTKVTFKPDLAKFNMTHLEDDVva 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 161 -LSRRFQEMAFlNKGLTIVVrderpdHINGEPKEITyhyegGLSDFVR-HLNSKKEPAhlsvidfEEHGEGIAVEIAMQW 238
Cdd:PLN03237 236 lMKKRVVDIAG-CLGKTVKV------ELNGKRIPVK-----SFSDYVDlYLESANKSR-------PENLPRIYEKVNDRW 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 239 N--SSYSESVY---TFANTINTAEGGTHEEgfraALTSIVNRYAREqKFLKEGKDENLAGEDIREGLTAIISVKLADPQF 313
Cdd:PLN03237 297 EvcVSLSEGQFqqvSFVNSIATIKGGTHVD----YVTNQIANHVME-AVNKKNKNANIKAHNVKNHLWVFVNALIDNPAF 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 314 EGQTKTKLgNTEAKSFVQKAcndhlrdwfernpgEAKEIISKSLQAARARLAARQARDLTRRKSLLESG-------SGLP 386
Cdd:PLN03237 372 DSQTKETL-TLRQSSFGSKC--------------ELSEDFLKKVMKSGIVENLLSWADFKQSKELKKTDgakttrvTGIP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 387 gKLADCQWS---DPEKCELFIVEGDSA-----GGSAKGGRDsrYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGT 458
Cdd:PLN03237 437 -KLEDANEAggkNSEKCTLILTEGDSAkalavAGLSVVGRN--YYGVFPLRGKLLNVREASHKQIMNNAEIENIKQILGL 513
|
490 500 510
....*....|....*....|....*....|
gi 559767661 459 GVHDEFDLAK-LRYHKLILMADADVDGQHI 487
Cdd:PLN03237 514 QHGKQYESVKsLRYGHLMIMTDQDHDGSHI 543
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
400-487 |
1.09e-19 |
|
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: 85.04 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 400 CELFIVEGDSAGGSAKGGR---DSRYQAILPIRGKILNVEKARIDKVLKNNEVQALITAMGT--GVHDEFDLAKLRYHKL 474
Cdd:cd03365 1 CTLILTEGDSAKALAVAGLsvvGRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLqhGKSDYESTKSLRYGRL 80
|
90
....*....|...
gi 559767661 475 ILMADADVDGQHI 487
Cdd:cd03365 81 MIMTDQDHDGSHI 93
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
202-322 |
2.35e-19 |
|
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: 83.46 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 202 LSDFVRHLNSKKEPAHLsvIDFEEHGEGIAVEIAMQWNS---SYSESVYTFANTINTAEGGTHEEGFRAALTSIVNryar 278
Cdd:cd00329 1 LKDRLAEILGDKVADKL--IYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 559767661 279 eqkflkegkdenlaGEDIREGLTAIISVKL--ADPQFE-GQTKTKLG 322
Cdd:cd00329 75 --------------GDDVRRYPVAVLSLKIppSLVDVNvHPTKEEVR 107
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
8-117 |
5.30e-16 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 74.22 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 8 ERGLHHLVYEVVDNSVDEALAGhaDRIEVTLLADNG---VRVVDNGRGIPvgehpvekkpaVELVMTTLHAGGKFDSKSY 84
Cdd:smart00387 3 PDRLRQVLSNLLDNAIKYTPEG--GRITVTLERDGDhveITVEDNGPGIP-----------PEDLEKIFEPFFRTDKRSR 69
|
90 100 110
....*....|....*....|....*....|...
gi 559767661 85 AVSGglHGVGAAVVNALSTRLQVEIRREGHVWR 117
Cdd:smart00387 70 KIGG--TGLGLSIVKKLVELHGGEISVESEPGG 100
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
8-112 |
4.91e-15 |
|
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 71.25 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 8 ERGLHHLVYEVVDNSVDEAlaGHADRIEVTLLADNG--VRVVDNGRGIPVGEHPvekkpavelvmttlHAGGKFDSKSyA 85
Cdd:pfam02518 3 ELRLRQVLSNLLDNALKHA--AKAGEITVTLSEGGEltLTVEDNGIGIPPEDLP--------------RIFEPFSTAD-K 65
|
90 100
....*....|....*....|....*..
gi 559767661 86 VSGGLHGVGAAVVNALSTRLQVEIRRE 112
Cdd:pfam02518 66 RGGGGTGLGLSIVRKLVELLGGTITVE 92
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
401-487 |
1.41e-14 |
|
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: 396354 [Multi-domain] Cd Length: 93 Bit Score: 69.31 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 401 ELFIVEGDSAGGSAKGGRDSRYQAILPIRGKILNVEKARIDKVLKnnevqalitamgtgvhdEFDLAKLRYHKLILMADA 480
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALK-----------------ALKELALKAKEVILATDP 63
|
....*..
gi 559767661 481 DVDGQHI 487
Cdd:pfam01751 64 DREGEAI 70
|
|
| HATPase_TopII-like |
cd16930 |
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ... |
23-120 |
7.25e-11 |
|
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the histidine kinase-like ATPase (HATpase) domains of human topoisomerase IIA (TopIIA) and TopIIB, Saccharomyces cerevisae TOP2p, and related proteins. These proteins catalyze the passage of DNA double strands through a transient double-strand break in the presence of ATP.
Pssm-ID: 340407 [Multi-domain] Cd Length: 147 Bit Score: 60.43 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 23 VDEALAGHAD---------RIEVTLLADNG-VRVVDNGRGIPVGEHPVEKKPAVELVMTTLHAGGKFDSKSYAVSGGLHG 92
Cdd:cd16930 9 FDEILVNAADnkqrdksmtCIKVTIDPENNeISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVTGGRNG 88
|
90 100 110
....*....|....*....|....*....|
gi 559767661 93 VGAAVVNALSTRLQVEI--RREGHVWRQSY 120
Cdd:cd16930 89 YGAKLCNIFSTEFTVETadSESKKKFKQTW 118
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
11-110 |
2.22e-06 |
|
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.
Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 46.44 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 11 LHHLVYEVVDNSVDEALAGhaDRIEVTLLADNG---VRVVDNGRGIPVGEHPvekkpavelvmttlHAGGKFDSKSYAVS 87
Cdd:cd00075 1 LEQVLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEEDLE--------------RIFERFYRGDKSRE 64
|
90 100
....*....|....*....|...
gi 559767661 88 GGLHGVGAAVVNALSTRLQVEIR 110
Cdd:cd00075 65 GGGTGLGLAIVRRIVEAHGGRIT 87
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
400-487 |
1.40e-03 |
|
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: 37.79 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 400 CELFIVEGDSAGGSAKGGRDSRYqAILPIRGKILNVEKARIDKVLKnnevqalitamgtgvhdefdlaklRYHKLILMAD 479
Cdd:cd00188 1 KKLIIVEGPSDALALAQAGGYGG-AVVALGGHALNKTRELLKRLLG------------------------EAKEVIIATD 55
|
....*...
gi 559767661 480 ADVDGQHI 487
Cdd:cd00188 56 ADREGEAI 63
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
17-54 |
1.60e-03 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 41.18 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 559767661 17 EVVDNSVDealAGhADRIEVTLlADNGV---RVVDNGRGIP 54
Cdd:COG0323 30 ELVENAID---AG-ATRIEVEI-EEGGKsliRVTDNGCGMS 65
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
15-54 |
2.31e-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: 39.34 E-value: 2.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 559767661 15 VYEVVDNSVDealAGhADRIEVTLlaDNG----VRVVDNGRGIP 54
Cdd:cd16926 18 VKELVENSID---AG-ATRIDVEI--EEGglklIRVTDNGSGIS 55
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| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
9-110 |
6.99e-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: 38.10 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559767661 9 RGLHHLVYEVVDNSVDEA-LAGHADRIEVTL-LADNG---VRVVDNGRGIPVGEHPvekkpaveLVMTTLHAGGKFDSKS 83
Cdd:cd16933 18 RSLYTTVRELVENSLDATeEAGILPDIKVEIeEIGKDhykVIVEDNGPGIPEEQIP--------KVFGKVLYGSKYHNKQ 89
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90 100 110
....*....|....*....|....*....|
gi 559767661 84 yavSGGLHGVG--AAVVNA-LSTRLQVEIR 110
Cdd:cd16933 90 ---SRGQQGLGisAAVLYSqMTTGKPVEII 116
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| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
15-54 |
7.93e-03 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 39.04 E-value: 7.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 559767661 15 VYEVVDNSVDealAGhADRIEVTLlaDNG----VRVVDNGRGIP 54
Cdd:PRK00095 27 VKELVENALD---AG-ATRIDIEI--EEGglklIRVRDNGCGIS 64
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