|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-804 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 1612.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 1 MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPT 80
Cdd:PRK14939 3 MSNSYGASSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGIPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 81 GIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGET 160
Cdd:PRK14939 83 DIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 161 EQTGTRVRFWPSMDTFrNNTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNIEDHFHYEGGIKAFVEFLNKNKTPIHPNV 240
Cdd:PRK14939 163 DKTGTEVRFWPSPEIF-ENTEFDYDILAKRLRELAFLNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 241 FYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREGLV 320
Cdd:PRK14939 242 FYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 321 AVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKGALDL 400
Cdd:PRK14939 322 AVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 401 AGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGR 480
Cdd:PRK14939 402 AGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 481 DEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYIKDDEAMDEYQLSIA 560
Cdd:PRK14939 482 DEFNPDKLRYHKIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVKKGKQEQYLKDDEALDDYLIELA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 561 LDGASLYTNEhAPALKGEPLEKLVTEFNGVQKIIKRMERLYPLSLLNSLIYHPKLTEEALSDKAKVEEwiemlvtrlnds 640
Cdd:PRK14939 562 LEGATLHLAD-GPAISGEALEKLVKEYRAVRKIIDRLERRYPRAVLEALIYAPALDLDDLADEAAVAA------------ 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 641 eqngssysyrlhenrerqmyepvlcvrthgvdtdylLDFDFIHGGEYHRITQLSDKLRNLIEESAYIERGERRQPVSSFE 720
Cdd:PRK14939 629 ------------------------------------LDADFLTSAEYRRLVELAEKLRGLIEEGAYLERGERKQPVSSFE 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 721 QALNWLTKESRRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENALKAA 800
Cdd:PRK14939 673 EALDWLLAEARKGLSIQRYKGLGEMNPEQLWETTMDPENRRLLQVTIEDAIAADEIFTTLMGDEVEPRREFIEENALNVA 752
|
....
gi 2502825583 801 NIDI 804
Cdd:PRK14939 753 NLDV 756
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-804 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 1097.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 1 MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDgTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPT 80
Cdd:COG0187 2 KKSNYDASSIQVLEGLEAVRKRPGMYIGSTDE-RGLHHLVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 81 GIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGET 160
Cdd:COG0187 81 DIHPKEGKSALEVVLTVLHAGGKFDGGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 161 EQTGTRVRFWPSMDTFrNNTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNI--EDHFHYEGGIKAFVEFLNKNKTPIHP 238
Cdd:COG0187 161 DRTGTTVRFKPDPEIF-ETTEFDYETLAERLRELAFLNKGLTITLTDEREEEpkEETFHYEGGIKDFVEYLNEDKEPLHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 239 NVFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREG 318
Cdd:COG0187 240 EVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 319 LVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKGAL 398
Cdd:COG0187 320 LTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSAL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 399 DLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGI 478
Cdd:COG0187 400 ESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 479 GrDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYIKDDEAMDEyqls 558
Cdd:COG0187 480 G-DDFDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGHVYIAQPPLYRIKKGKKTYYAYSDAELDE---- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 559 ialdgaslytnehapalkgeplekLVTEFNGVQKIikrmerlyplsllnsliyhpklteealsdkakveewiemlvtrln 638
Cdd:COG0187 555 ------------------------LLKELKGKKKV--------------------------------------------- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 639 dseqngssysyrlhenrerqmyepvlcvrthgvdtdylldfdfihggeyhritqlsdklrnlieesayiergerrqpvss 718
Cdd:COG0187 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 719 feqalnwltkesrrglSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENALK 798
Cdd:COG0187 566 ----------------EIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSLLMGDKVEPRREFIEENAKF 629
|
....*.
gi 2502825583 799 AANIDI 804
Cdd:COG0187 630 VRNLDI 635
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
5-804 |
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: 1093.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 5 YDSSSIKVLKGLDAVRKRPGMYIGDTDDgTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGIHE 84
Cdd:TIGR01059 1 YDASSIKVLEGLEAVRKRPGMYIGSTGE-TGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 85 EEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGETEQTG 164
Cdd:TIGR01059 80 EEGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 165 TRVRFWPSMDTFRNnTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNI--EDHFHYEGGIKAFVEFLNKNKTPIHPNVFY 242
Cdd:TIGR01059 160 TTVRFWPDPEIFET-TEFDFDILAKRLRELAFLNSGVKISLEDERDGKgkKVTFHYEGGIKSFVKYLNRNKEPLHEEIIY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 243 FSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREGLVAV 322
Cdd:TIGR01059 239 IKGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 323 ISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKGALDLAG 402
Cdd:TIGR01059 319 ISVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 403 LPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDe 482
Cdd:TIGR01059 399 LPGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 483 YNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYIKDDEAMDeyqlsiald 562
Cdd:TIGR01059 478 FDLEKLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKKERYIKDDKEKD--------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 563 gaslytnehapaLKGEPLEKLvtefngvqkiikRMERLYplsllnsliyhpklteealSDKAKvEEWIemlvtrlndseq 642
Cdd:TIGR01059 549 ------------LVGEALEDL------------KALYIY-------------------SDKEK-EEAK------------ 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 643 ngssysyrlhenrerqmyepvlcvrthgvdtdylldfdfihggeyhritqlsdklrnlieesayiergerrqpvSSFEqa 722
Cdd:TIGR01059 573 --------------------------------------------------------------------------TQIP-- 576
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 723 lnwlTKESRRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENALKAANI 802
Cdd:TIGR01059 577 ----VHLGRKGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTLMGDEVEPRREFIEANALDVKNL 652
|
..
gi 2502825583 803 DI 804
Cdd:TIGR01059 653 DV 654
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-804 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 1073.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 1 MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDgTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPT 80
Cdd:PRK05644 4 KAQEYDASQIQVLEGLEAVRKRPGMYIGSTGE-RGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 81 GIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGET 160
Cdd:PRK05644 83 DIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 161 EQTGTRVRFWPSMDTFrNNTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNIE--DHFHYEGGIKAFVEFLNKNKTPIHP 238
Cdd:PRK05644 163 DETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEkeETFHYEGGIKEYVEYLNRNKEPLHE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 239 NVFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREG 318
Cdd:PRK05644 242 EPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 319 LVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKGAL 398
Cdd:PRK05644 322 LTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSAL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 399 DLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGI 478
Cdd:PRK05644 402 ESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 479 GrDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEqYIKDDEAMDEyqls 558
Cdd:PRK05644 482 G-DDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGKE-YAYSDEELDE---- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 559 ialdgaslytnehapalkgepleklvtefngvqkIIKRMErlyplsllnsliyhpklteealsdkakveewiemlvtrln 638
Cdd:PRK05644 556 ----------------------------------ILAELK---------------------------------------- 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 639 dseqngssysyrlhenrerqmyepvlcvrthgvdtdylldfdfihggeyhritqlsdklrnlieesayiergerrqpvss 718
Cdd:PRK05644 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 719 feqalnwltKESRRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENALK 798
Cdd:PRK05644 562 ---------LKGNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKY 632
|
....*.
gi 2502825583 799 AANIDI 804
Cdd:PRK05644 633 VRNLDI 638
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-796 |
0e+00 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 862.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 1 MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDgTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPT 80
Cdd:PRK05559 4 MTNNYNADSIEVLEGLEPVRKRPGMYIGSTDT-RGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 81 GIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGET 160
Cdd:PRK05559 83 GIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 161 --EQTGTRVRFWPSMDTFRnNTEFQHDILAKRLRELSFLNSGVSIRLIDKRTniEDHFHYEGGIKAFVEFLNKNKTPIHP 238
Cdd:PRK05559 163 gkRKTGTRVRFWPDPKIFD-SPKFSPERLKERLRSKAFLLPGLTITLNDERE--RQTFHYENGLKDYLAELNEGKETLPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 239 N-VFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKvSATGDDARE 317
Cdd:PRK05559 240 EfVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLPKGK-KLEGEDVRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 318 GLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKARemTRRKGA 397
Cdd:PRK05559 319 GLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKV--KRKKKT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 398 LDLAgLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCG 477
Cdd:PRK05559 397 SGPA-LPGKLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 478 IGrDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYikddeAMDEYQL 557
Cdd:PRK05559 476 PG-DSFDLEDLRYGKIIIMTDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRVDKGKKKIY-----ALDEEEK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 558 sialdgaslytnehapalkgepleklvtefngvQKIIKRMERLyplsllnsliyhpklteealsdKAKVEewiemlvtrl 637
Cdd:PRK05559 550 ---------------------------------EELLKKLGKK----------------------GGKPE---------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 638 ndseqngssysyrlhenrerqmyepvlcvrthgvdtdylldfdfihggeyhritqlsdklrnlieesayiergerrqpvs 717
Cdd:PRK05559 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502825583 718 sfeqalnwltkesrrglsIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENA 796
Cdd:PRK05559 565 ------------------IQRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDAEETEKLVDMLMGKKAEPRREWIEENG 625
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
35-796 |
0e+00 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 807.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 35 GLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGG 114
Cdd:smart00433 1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 115 LHGVGVSVVNALSEKLELVIRRDGKVHEQTYH-LGVPQSPLKVVGETEQTGTRVRFWPSMDTFRNNTEFQHDILAKRLRE 193
Cdd:smart00433 81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTTDDDFELLKRRLRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 194 LSFLNSGVSIRLIDKRTNIEDHFHYEGGIKAFVEFLNKNKTPIHPNVFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNI 273
Cdd:smart00433 161 LAFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 274 PQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVsaTGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLM 353
Cdd:smart00433 241 ATTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI--KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 354 NEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKgALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAK 433
Cdd:smart00433 319 SECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 434 QGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGrDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTF 513
Cdd:smart00433 398 SGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEKLRYGKIIIMTDADVDGSHIKGLLLTF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 514 FYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYIKDDEaMDEYqlsialdgaslytnehapalkgepleklvtefngvqki 593
Cdd:smart00433 477 FYRYMPPLIEAGFVYIAIPPLYKVTKGKKKYVYSFYS-LDEY-------------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 594 ikrmerlyplsllnsliyhpklteealsdkakvEEWIEmlvtrlndseqngssysyrlhenrerqmyepvlcvrthgvdt 673
Cdd:smart00433 518 ---------------------------------EKWLE------------------------------------------ 522
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 674 dylldfdfihggeyhritqlsdklrnlieesayiergerrqpvssfeqalnwLTKESRRGLSIQRYKGLGEMNPEQLWET 753
Cdd:smart00433 523 ----------------------------------------------------KTEGNKSKYEIQRYKGLGEMNADQLWET 550
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2502825583 754 TMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIEENA 796
Cdd:smart00433 551 TMDPERRTLLFVTLDDADEADLIFSALMGDKVEPRKEWIEENA 593
|
|
| parE_Gpos |
TIGR01058 |
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II ... |
1-795 |
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: 649.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 1 MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDdGTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPT 80
Cdd:TIGR01058 1 MASKYNADAIKILEGLDAVRKRPGMYIGSTD-SKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITVQDDGRGIPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 81 GIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLG-VPQSPLKVVGE 159
Cdd:TIGR01058 80 GIHQDGNISTVETVFTVLHAGGKFDQGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIYQQRFENGgKIVQSLKKIGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 160 TEQTGTRVRFWPSMDTFRNnTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNIEDHFHYEGGIKAFVEFLNKNKTPIHPn 239
Cdd:TIGR01058 160 TKKTGTLVHFHPDPTIFKT-TQFNSNIIKERLKESAFLLKKLKLTFTDKRTNKTTVFFYENGLVDFVDYINETKETLSQ- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 240 VFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREGL 319
Cdd:TIGR01058 238 VTYFEGEKNGIEVEVAFQFNDGDSENILSFANSVKTKEGGTHENGFKLAITDVINSYARKYNLLKEKDKNLEGSDIREGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 320 VAVISVKVPDP--KFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTR--RK 395
Cdd:TIGR01058 318 SAIISVRIPEEliQFEGQTKSKLFSPEARNVVDEIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKsgKK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 396 GALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALG 475
Cdd:TIGR01058 398 PKKEKGILSGKLTPAQSKNPAKNELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFCIG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 476 CGIGRDeYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKV--KKGKQEQYIKDDEAMD 553
Cdd:TIGR01058 478 TGIGAD-FSIKDLKYDKIIIMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLskKDGKKVKYAWSDLELE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 554 Eyqlsialdgaslytnehapalkgepleklvtefngvqkiikrmerlyplsllnsliyhpklteealsdkakveewieml 633
Cdd:TIGR01058 557 S------------------------------------------------------------------------------- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 634 vtrlndseqngssysyrlhenrerqmyepvlcvrthgvdtdylldfdfihggeyhritqlsdklrnlieesayiergerr 713
Cdd:TIGR01058 --------------------------------------------------------------------------------
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 714 qpvssfeqalnwlTKESRRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIE 793
Cdd:TIGR01058 558 -------------VKKKLKNYTLQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDLARAERQINTLMGDKVEPRKKWIE 624
|
..
gi 2502825583 794 EN 795
Cdd:TIGR01058 625 AN 626
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
3-796 |
2.32e-172 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 520.21 E-value: 2.32e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 3 NTYDSSSIKVLKGLDAVRKRPGMYIGDTDDgTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGI 82
Cdd:PTZ00109 98 SEYDADDIVVLEGLEAVRKRPGMYIGNTDE-KGLHQLLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPCDV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 83 HEEEGVSAAEVIMTVLHAGGKFDD----------------------------------------NSYKVSGGLHGVGVSV 122
Cdd:PTZ00109 177 SEKTGKSGLETVLTVLHSGGKFQDtfpknsrsdksedkndtksskkgksshvkgpkeakekessQMYEYSSGLHGVGLSV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 123 VNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGE-TEQTGTRVRFWPSMDT-FRNNTE-------------FQHDIL 187
Cdd:PTZ00109 257 VNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCpLKKRGTTIHFLPDYKHiFKTHHQhteteeeegckngFNLDLI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 188 AKRLRELSFLNSGVSIRLIDKRTNIEDHF------HYEGGIKAFVEFLNKNKTPIHP--NVFYFSTEKDGIGVEISMQWN 259
Cdd:PTZ00109 337 KNRIHELSYLNPGLTFYLVDERIANENNFypyetiKHEGGTREFLEELIKDKTPLYKdiNIISIRGVIKNVNVEVSLSWS 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 260 DG-FQENIYCFTNNIpQRDGGTHLVGFRTAMTRTLNSYMDKEGYNKKSKVSATGDDAREGLVAVISVKVPDPKFSSQTKD 338
Cdd:PTZ00109 417 LEsYTALIKSFANNV-STTAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISVKLNGAEFDGQTKT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 339 KLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIDAARAREAARKAREMTRRKGALDLA-GLPGKLADCQERDPAL 417
Cdd:PTZ00109 496 KLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYStILPGKLVDCISDDIER 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 418 SELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFD-KMLSSQEVATLITALGCGIGRDEYNPD---------- 486
Cdd:PTZ00109 576 NELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNPVTWRQYdlshgtkask 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 487 ---------------------KLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQY 545
Cdd:PTZ00109 656 desvqnnnstltkkknslfdtPLRYGKIILLTDADVDGEHLRILLLTLLYRFCPSLYEHGRVYVACPPLYRITNNRMKQF 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 546 IKDDEAMDEYQLSialdgaslYTNEHAPALkgepleklvtefngvqkiikrmerlypLSLLNSliyhpklteealsdkak 625
Cdd:PTZ00109 736 NVSTKNSKKYIYT--------WSDEELNVL---------------------------IKLLNK----------------- 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 626 veewiemlvtrlndseqngssySYRLHENRERQMYEPVLCVRTHGVDTDYLLDFDFIHGGEyhRITQLSDKLRNLIEESA 705
Cdd:PTZ00109 764 ----------------------DYSSKETTRSVEEKGNAPDLDNEYEDEKLDNKNMRENNV--DEVELKTELGTNVADTE 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 706 yiergerrqpvSSFEQALNWLTKESRRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAV 785
Cdd:PTZ00109 820 -----------QTDELDINKAFFKFSKHYEIQRFKGLGEMMADQLWETTMDPKKRILIRITVSDAMRASELIFLLMGEDV 888
|
890
....*....|.
gi 2502825583 786 EPRRAFIEENA 796
Cdd:PTZ00109 889 QSRKQFIFENS 899
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
4-550 |
4.31e-150 |
|
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: 453.61 E-value: 4.31e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 4 TYDSSSIKVLKGLDAVRKRPGMYIgdtdDGTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGIH 83
Cdd:TIGR01055 3 NYSAKDIEVLDGLEPVRKRPGMYT----DTTRPNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 84 EEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGETEQ- 162
Cdd:TIGR01055 79 PKEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 163 -TGTRVRFWPSmDTFRNNTEFQHDILAKRLRELSFLNSGVSIRLIDKRTNIEDHFHYEGGIKAFV-EFLNKNKTPIhPNV 240
Cdd:TIGR01055 159 lTGTSVHFTPD-PEIFDSLHFSVSRLYHILRAKAVLCRGVEIEFEDEVNNTKALWNYPDGLKDYLsEAVNGDNTLP-PKP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 241 FYFSTEKDGIGVEISMQW-NDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDKEGyNKKSKVSATGDDAREGL 319
Cdd:TIGR01055 237 FSGNFEGDDEAVEWALLWlPEGGELFMESYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRN-NLPRGVKLTAEDIWDRC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 320 VAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIIdaARAREAARKAREMTRRKGALD 399
Cdd:TIGR01055 316 SYVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAI--SSAQRRKRAAKKVVRKKLTSG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 400 LAgLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCgiG 479
Cdd:TIGR01055 394 PA-LPGKLADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGI--D 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502825583 480 RDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQPPLYKVKKGKQEQYIKDDE 550
Cdd:TIGR01055 471 PDSNDLSQLRYGKICILADADSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRIDLSKEVYYALDEE 541
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
36-216 |
3.27e-106 |
|
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: 323.33 E-value: 3.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 36 LHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGL 115
Cdd:cd16928 1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 116 HGVGVSVVNALSEKLELVIRRDGKVHEQTYHLGVPQSPLKVVGETEQTGTRVRFWPSMDTFrNNTEFQHDILAKRLRELS 195
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIF-EKTEFDFDTLKRRLRELA 159
|
170 180
....*....|....*....|.
gi 2502825583 196 FLNSGVSIRLIDKRTNIEDHF 216
Cdd:cd16928 160 FLNKGLKIVLEDERTGKEEVF 180
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
220-377 |
9.91e-81 |
|
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: 256.33 E-value: 9.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 220 GGIKAFVEFLNKNKTPIHPNVFYFSTEKDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMDK 299
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502825583 300 EGYNKKSKVSATGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIID 377
Cdd:cd00822 81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| TOPRIM_TopoIIA_GyrB |
cd03366 |
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
418-532 |
1.43e-77 |
|
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: 245.64 E-value: 1.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 418 SELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGrDEYNPDKLRYHSIIIMT 497
Cdd:cd03366 1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIG-EDFDLEKLRYHKIIIMT 79
|
90 100 110
....*....|....*....|....*....|....*
gi 2502825583 498 DADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQP 532
Cdd:cd03366 80 DADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP 114
|
|
| TOPRIM_TopoIIA_like |
cd01030 |
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
418-532 |
1.73e-68 |
|
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: 221.23 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 418 SELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMT 497
Cdd:cd01030 1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGKDDFDLDKLRYGKIIIMT 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2502825583 498 DADVDGSHIRTLLLTFFYRQMPEIIERGHVFIAQP 532
Cdd:cd01030 81 DADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT 115
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
221-377 |
5.92e-67 |
|
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: 219.41 E-value: 5.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 221 GIKAFVEFLNKNKTPIHPNVFYFSTE--KDGIGVEISMQWNDGFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNSYMD 298
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502825583 299 KEGYNKKSKVSATGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLENPNDAKTVVSKIID 377
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| GyrB_insert |
pfam18053 |
DNA gyrase B subunit insert domain; This is the insert domain found in DNA gyrase B subunit ... |
564-729 |
1.06e-62 |
|
DNA gyrase B subunit insert domain; This is the insert domain found in DNA gyrase B subunit proteins. Studies indicate that the insert has two functions, acting as a steric buttress to pre-configure the primary DNA-binding site, and serving as a relay that may help coordinate communication between different functional domains.
Pssm-ID: 465629 Cd Length: 167 Bit Score: 207.76 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 564 ASLYTNEHAPALKGEPLEKLVTEFNGVQKIIKRMERLYPLSLLNSLIYHPKLTEEALSDKAKVEEWIEMLVTRLNDSEQN 643
Cdd:pfam18053 1 AALYPNEGAPPISGEALEELARQYRLAEAIIKRLSRRYDPAVLEALLYLPPLDAEDLDDEAAAEAWAAALEARLNQDGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 644 GSSYSYRLHENRERQMYEPVLCVRTHGVDTDYLLDFDFIHGGEYHRITQLSDKLRNLIEESAYIERGERRQPVSSFEQAL 723
Cdd:pfam18053 81 GPRYRVSVEEDTERGKYLLRVTRRHHGNETVYVLDADFFESGDYRALAELGETLDGLIGEGAYIKRGEKEQPVESFKEAL 160
|
....*.
gi 2502825583 724 NWLTKE 729
Cdd:pfam18053 161 DWLMEE 166
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
22-543 |
1.99e-52 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 198.35 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 22 RPGMYIGDTDDGT----------------------GLHHMVFEVVDNAID----EALAGHCSEVIVTI-HADNSVSVQDD 74
Cdd:PTZ00108 22 RPDTYIGSIETQTedmwvydeeknrmvyktityvpGLYKIFDEILVNAADnkarDKGGHRMTYIKVTIdEENGEISVYND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 75 GRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIR--RDGKVHEQTY--HLGVP 150
Cdd:PTZ00108 102 GEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLTNIFSTKFTVECVdsKSGKKFKMTWtdNMSKK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 151 QSPLKVVGETEQTGTRVRFWPSMDTFrNNTEFQHDILA---KRLRELSFLNSGVSIRLIDKRTNIEDHFHYeggIKAFVE 227
Cdd:PTZ00108 182 SEPRITSYDGKKDYTKVTFYPDYAKF-GMTEFDDDMLRllkKRVYDLAGCFGKLKVYLNGERIAIKSFKDY---VDLYLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 228 FLNKNKTPIHPNVFYFSTEKDGIGVEISmqwNDGFQenIYCFTNNIPQRDGGTHLvgfrTAMTRTLNSYMDKE--GYNKK 305
Cdd:PTZ00108 258 DGEEGKKPPYPFVYTSVNGRWEVVVSLS---DGQFQ--QVSFVNSICTTKGGTHV----NYILDQLISKLQEKakKKKKK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 306 SKVSATGDdAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLEnpndaktvvSKIIDAARAREAA 385
Cdd:PTZ00108 329 GKEIKPNQ-IKNHLWVFVNCLIVNPSFDSQTKETLTTKPSKFGSTCELSEKLIKYVLK---------SPILENIVEWAQA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 386 RKAREMTRRKGALD---LAGLPgKLADCQERDPALSE---LYLVEGDSAGGSAKQG---RNRKNQAILPLKGKILNVEKA 456
Cdd:PTZ00108 399 KLAAELNKKMKAGKksrILGIP-KLDDANDAGGKNSEectLILTEGDSAKALALAGlsvVGRDYYGVFPLRGKLLNVRDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 457 RFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIE-RGhvFIAQ--PP 533
Cdd:PTZ00108 478 SLKQLMNNKEIQNLFKILGLDIGKKYEDPKGLRYGSLMIMTDQDHDGSHIKGLLINMIHHFWPSLLKnPG--FLKEfiTP 555
|
570
....*....|.
gi 2502825583 534 LYKV-KKGKQE 543
Cdd:PTZ00108 556 IVKAtKKGNQV 566
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
7-555 |
3.41e-50 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 186.50 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 7 SSSIKVLKGLDAVRKRPGMYIGDTDDGT----------------GLHHMVFEVVDNAIDEALAG---HCSEVIVTIHaDN 67
Cdd:PHA02569 1 KDEFKVLSDREHILKRPGMYIGSVAYEAherflfgkftqveyvpGLVKIIDEIIDNSVDEAIRTnfkFANKIDVTIK-NN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 68 SVSVQDDGRGIPTGI---HEEEGVSAAEVIMTVLHAGGKFDDNSyKVSGGLHGVGVSVVNALSE---------KLELVIR 135
Cdd:PHA02569 80 QVTVSDNGRGIPQAMvttPEGEEIPGPVAAWTRTKAGSNFDDTN-RVTGGMNGVGSSLTNFFSVlfigetcdgKNEVTVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 136 RDGKVHEQTYHlgvpQSPLKVvgeteqTGTRVRFWPSMDTFRNNTEFQH--DILAKRLRELSflnsgVSIRLIDKRTNIE 213
Cdd:PHA02569 159 CSNGAENISWS----TKPGKG------KGTSVTFIPDFSHFEVNGLDQQylDIILDRLQTLA-----VVFPDIKFTFNGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 214 DHfhyEGGIKAFVEFLNKNKtpihpnvfyFSTEKDGIGVEISMQwNDGFQENiyCFTNNIPQRDGGTHLVGFRTAMTRTL 293
Cdd:PHA02569 224 KV---SGKFKKYAKQFGDDT---------IVQENDNVSIALAPS-PDGFRQL--SFVNGLHTKNGGHHVDCVMDDICEEL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 294 nsymdKEGYNKKSKVSATGDDAREGLVAVISVK-VPDPKFSSQTKDKLVSS--EVKTAVEtLMNEKLVEYLLENPNdakt 370
Cdd:PHA02569 289 -----IPMIKKKHKIEVTKARVKECLTIVLFVRnMSNPRFDSQTKERLTSPfgEIRNHID-LDYKKIAKQILKTEA---- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 371 VVSKIIDAARAREAARKAREMTR-RKGALDL-------AGLPGKLADcqerdpalSELYLVEGDSAGGSAKQGRNRKNQA 442
Cdd:PHA02569 359 IIMPIIEAALARKLAAEKAAETKaAKKAKKAkvakhikANLIGKDAE--------TTLFLTEGDSAIGYLIEVRDEELHG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 443 ILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEynpDKLRYHSIIIMTDADVDG-SHIRTLLLTFFYRqMPEI 521
Cdd:PHA02569 431 GYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKA---ENMNYKNIAIMTDADVDGkGSIYPLLLAFFSR-WPEL 506
|
570 580 590
....*....|....*....|....*....|....
gi 2502825583 522 IERGHVFIAQPPLYKVKKGKQEQYIKDdeaMDEY 555
Cdd:PHA02569 507 FEQGRIRFVKTPVIIAQVGKETKWFYS---LDEF 537
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
22-542 |
3.93e-43 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 169.50 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 22 RPGMYIGDTDDGT--------------------GLHHMVFEVVDNAIDEALAG-HCSEVIVTIHAD-NSVSVQDDGRGIP 79
Cdd:PLN03128 19 RPDTYIGSTEKHTqtlwvyeggemvnrevtyvpGLYKIFDEILVNAADNKQRDpSMDSLKVDIDVEqNTISVYNNGKGIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 80 TGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSE--KLELVIRRDGKVHEQTY--HLGVPQSPLK 155
Cdd:PLN03128 99 VEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFSTefTVETADGNRGKKYKQVFtnNMSVKSEPKI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 156 VVGETEQTGTRVRFWPSMDTFrNNTEFQHDI---LAKRLRELS-FLNSGVSIRLIDKRTNIedhfhyeGGIKAFVE-FLN 230
Cdd:PLN03128 179 TSCKASENWTKITFKPDLAKF-NMTRLDEDVvalMSKRVYDIAgCLGKKLKVELNGKKLPV-------KSFQDYVGlYLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 231 KNKTPIHPNVFYfstEKDGIGVEISMQWNDG-FQEniYCFTNNIPQRDGGTHLvgfrTAMTRTLNSYMdKEGYNKKSK-- 307
Cdd:PLN03128 251 PNSREDPLPRIY---EKVNDRWEVCVSLSDGsFQQ--VSFVNSIATIKGGTHV----DYVADQIVKHI-QEKVKKKNKna 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 308 VSATGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEYLLEnpndaktvvSKIIDAARAREAARK 387
Cdd:PLN03128 321 THVKPFQIKNHLWVFVNCLIENPTFDSQTKETLTTRPSSFGSKCELSEEFLKKVEK---------CGVVENILSWAQFKQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 388 AREMTRRKGA--LDLAGLPgKLADCQERDPALSE---LYLVEGDSAGGSAKQGR---NRKNQAILPLKGKILNVEKARFD 459
Cdd:PLN03128 392 QKELKKKDGAkrQRLTGIP-KLDDANDAGGKKSKdctLILTEGDSAKALAMSGLsvvGRDHYGVFPLRGKLLNVREASHK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 460 KMLSSQEVATLITALGCGIGR--DEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGHvFIAQ--PPLY 535
Cdd:PLN03128 471 QIMKNAEITNIKQILGLQFGKtyDEENTKSLRYGHLMIMTDQDHDGSHIKGLIINFFHSFWPSLLKIPG-FLVEfiTPIV 549
|
....*..
gi 2502825583 536 KVKKGKQ 542
Cdd:PLN03128 550 KATKGGK 556
|
|
| DNA_gyraseB_C |
pfam00986 |
DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA ... |
731-793 |
3.99e-41 |
|
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: 144.44 E-value: 3.99e-41
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502825583 731 RRGLSIQRYKGLGEMNPEQLWETTMNPETRRMMRVTVKDAIATDQLFTTLMGDAVEPRRAFIE 793
Cdd:pfam00986 1 KKKVEIQRYKGLGEMNPEQLWETTMDPETRRLLQVTIEDAAEADEIFSTLMGDKVEPRREFIE 63
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
65-523 |
5.70e-33 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 137.69 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 65 ADNSVSVQDDGRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEklELVIRR-DGKvHEQ 143
Cdd:PLN03237 109 EQNLISVYNNGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTTGGRNGYGAKLTNIFST--EFVIETaDGK-RQK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 144 TY------HLGVPQSPLKVVGETEQTGTRVRFWPSMDTFrNNTEFQHDILA---KRLRELS-FLNSGVSIRLIDKRTNIe 213
Cdd:PLN03237 186 KYkqvfsnNMGKKSEPVITKCKKSENWTKVTFKPDLAKF-NMTHLEDDVVAlmkKRVVDIAgCLGKTVKVELNGKRIPV- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 214 dhfhyeggiKAFVEFLN---KNKTPIHPNVFYFSTEKDGIGVEISMQWNDG-FQEniYCFTNNIPQRDGGTHLVGFRTAM 289
Cdd:PLN03237 264 ---------KSFSDYVDlylESANKSRPENLPRIYEKVNDRWEVCVSLSEGqFQQ--VSFVNSIATIKGGTHVDYVTNQI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 290 TRTLNSYMDKEgyNKKSKVSATgdDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLVEyllenpndaK 369
Cdd:PLN03237 333 ANHVMEAVNKK--NKNANIKAH--NVKNHLWVFVNALIDNPAFDSQTKETLTLRQSSFGSKCELSEDFLK---------K 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 370 TVVSKIIDAARAREAARKAREMTRRKGA--LDLAGLPgKLADCQE---RDPALSELYLVEGDSAGGSAKQGRN---RKNQ 441
Cdd:PLN03237 400 VMKSGIVENLLSWADFKQSKELKKTDGAktTRVTGIP-KLEDANEaggKNSEKCTLILTEGDSAKALAVAGLSvvgRNYY 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 442 AILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEI 521
Cdd:PLN03237 479 GVFPLRGKLLNVREASHKQIMNNAEIENIKQILGLQHGKQYESVKSLRYGHLMIMTDQDHDGSHIKGLLINFIHSFWPSL 558
|
..
gi 2502825583 522 IE 523
Cdd:PLN03237 559 LK 560
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
420-524 |
2.79e-24 |
|
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: 98.53 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 420 LYLVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEY-NPDKLRYHSIII 495
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYeSTKSLRYGRLMI 82
|
90 100
....*....|....*....|....*....
gi 2502825583 496 MTDADVDGSHIRTLLLTFFYRQMPEIIER 524
Cdd:cd03365 83 MTDQDHDGSHIKGLLINFIHSFWPSLLKI 111
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
222-340 |
1.57e-20 |
|
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: 87.32 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 222 IKAFVEFLNKNKTpiHPNVFYFSTEKDGIGVEISMQWND---GFQENIYCFTNNIPQRDGGTHLVGFRTAMTRTLNsymd 298
Cdd:cd00329 1 LKDRLAEILGDKV--ADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2502825583 299 kegynkkskvsatGDDAREGLVAVISVKVPD--PKFS-SQTKDKL 340
Cdd:cd00329 75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
32-144 |
1.86e-18 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 81.54 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 32 DGTGLHHMVFEVVDNAIDEALAGhcSEVIVTIHADN---SVSVQDDGRGIPtgiheeegvsaAEVIMTVLHAGGKFDDNS 108
Cdd:smart00387 2 DPDRLRQVLSNLLDNAIKYTPEG--GRITVTLERDGdhvEITVEDNGPGIP-----------PEDLEKIFEPFFRTDKRS 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 2502825583 109 YKVSGglHGVGVSVVNALSEKLELVIRRDGKVHEQT 144
Cdd:smart00387 69 RKIGG--TGLGLSIVKKLVELHGGEISVESEPGGGT 102
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
31-171 |
1.20e-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: 460579 [Multi-domain] Cd Length: 109 Bit Score: 76.25 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 31 DDGTGLHHMVFEVVDNAIDEALAGHCSEVIVTIHADNSVSVQDDGRGIPTGIHEeegvsaaevimtvlHAGGKFDDnSYK 110
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLP--------------RIFEPFST-ADK 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502825583 111 VSGGLHGVGVSVVNALSEKLelvirrDGKVHeqtyhlgvpqsplkvVGETEQTGTRVRFWP 171
Cdd:pfam02518 66 RGGGGTGLGLSIVRKLVELL------GGTIT---------------VESEPGGGTTVTLTL 105
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
419-532 |
1.21e-15 |
|
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: 72.77 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 419 ELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLssqevatlitalgcgigrDEYNPDKLRYHSIIIMTD 498
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKAL------------------KALKELALKAKEVILATD 62
|
90 100 110
....*....|....*....|....*....|....*.
gi 2502825583 499 ADVDGSHIRTLLLTFFyrqmpEIIER--GHVFIAQP 532
Cdd:pfam01751 63 PDREGEAIALKLLELK-----ELLENagGRVEFSEL 93
|
|
| HATPase_TopII-like |
cd16930 |
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ... |
35-171 |
4.61e-13 |
|
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: 67.36 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 35 GLHHMVFEVVDNAID-EALAGHCSEVIVTIHAD-NSVSVQDDGRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVS 112
Cdd:cd16930 4 GLYKIFDEILVNAADnKQRDKSMTCIKVTIDPEnNEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVT 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502825583 113 GGLHGVGVSVVNALSEK--LELVIRRDGKVHEQTY--HLGVPQSPLKVVGETEQTGTRVRFWP 171
Cdd:cd16930 84 GGRNGYGAKLCNIFSTEftVETADSESKKKFKQTWtnNMGKASEPKITPYEKGKDYTKVTFKP 146
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
36-170 |
1.08e-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: 47.60 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 36 LHHMVFEVVDNAIDEALAGhcSEVIVTIHADNS---VSVQDDGRGIPTGIHEeegvsaaevimtvlHAGGKFDDNSYKVS 112
Cdd:cd00075 1 LEQVLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEEDLE--------------RIFERFYRGDKSRE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2502825583 113 GGLHGVGVSVVNALSEKLelvirrDGKVHeqtyhlgvpqsplkvVGETEQTGTRVRFW 170
Cdd:cd00075 65 GGGTGLGLAIVRRIVEAH------GGRIT---------------VESEPGGGTTFTVT 101
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
418-522 |
1.46e-05 |
|
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: 43.95 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502825583 418 SELYLVEGDSAGGSAKQGRnRKNQAILPLKGKILNvekarfdkmlssQEVATLITALGcgigrdeynpdklRYHSIIIMT 497
Cdd:cd00188 1 KKLIIVEGPSDALALAQAG-GYGGAVVALGGHALN------------KTRELLKRLLG-------------EAKEVIIAT 54
|
90 100
....*....|....*....|....*
gi 2502825583 498 DADVDGSHIRTLLLTFFYRQMPEII 522
Cdd:cd00188 55 DADREGEAIALRLLELLKSLGKKVR 79
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