|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-638 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 1360.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 1 MEQQHNSYDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGI 80
Cdd:PRK05644 1 KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIG 160
Cdd:PRK05644 81 PVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 161 ETDVTGTTTHFVPDPEIFtETIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKERRNEYCYEGGIKSYVEHLNRSKEVV 240
Cdd:PRK05644 161 ETDETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEKEETFHYEGGIKEYVEYLNRNKEPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 241 HEEPVYIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVR 320
Cdd:PRK05644 240 HEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKS 400
Cdd:PRK05644 320 EGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 401 ALEVSSLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK05644 400 ALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 481 GIGEDFTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGKRvEYVYNDKQLDELLK 560
Cdd:PRK05644 480 GIGDDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGK-EYAYSDEELDEILA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 561 TLPQ--TPKPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIEENAQYVKNLDI 638
Cdd:PRK05644 559 ELKLkgNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKYVRNLDI 638
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
6-638 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 1299.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 6 NSYDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIH 85
Cdd:COG0187 4 SNYDASSIQVLEGLEAVRKRPGMYIGSTDERGLHHLVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPVDIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 86 EKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIGETDVT 165
Cdd:COG0187 84 PKEGKSALEVVLTVLHAGGKFDGGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 166 GTTTHFVPDPEIFtETIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKERRNEYCYEGGIKSYVEHLNRSKEVVHEEPV 245
Cdd:COG0187 164 GTTVRFKPDPEIF-ETTEFDYETLAERLRELAFLNKGLTITLTDEREEEPKEETFHYEGGIKDFVEYLNEDKEPLHPEVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 246 YIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVREGLTA 325
Cdd:COG0187 243 YFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 326 IISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKSALEVS 405
Cdd:COG0187 323 VISVKLPEPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 406 SLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGED 485
Cdd:COG0187 403 GLPGKLADCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGDD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 486 FTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGKRVEYVYNDKQLDELLKTLPQT 565
Cdd:COG0187 483 FDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGHVYIAQPPLYRIKKGKKTYYAYSDAELDELLKELKGK 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2182436910 566 PKPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIEENAQYVKNLDI 638
Cdd:COG0187 563 KKVEIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSLLMGDKVEPRREFIEENAKFVRNLDI 635
|
|
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
2-638 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 1161.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 2 EQQHNSYDENQIQVLEGLEAVRKRPGMYIGSTS-AKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGI 80
Cdd:PRK14939 1 SMMSNSYGASSIKVLKGLDAVRKRPGMYIGDTDdGTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIG 160
Cdd:PRK14939 81 PTDIHPEEGVSAAEVIMTVLHAGGKFDQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 161 ETDVTGTTTHFVPDPEIFTeTIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKErrNEYCYEGGIKSYVEHLNRSKEVV 240
Cdd:PRK14939 161 ETDKTGTEVRFWPSPEIFE-NTEFDYDILAKRLRELAFLNSGVRIRLKDERDGKE--EEFHYEGGIKAFVEYLNRNKTPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 241 HEEPVYIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVR 320
Cdd:PRK14939 238 HPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 321 EGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKS 400
Cdd:PRK14939 318 EGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 401 ALEVSSLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:PRK14939 398 ALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGC 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 481 GIG-EDFTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGKRVEYVYNDKQLD--- 556
Cdd:PRK14939 478 GIGrDEFNPDKLRYHKIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVKKGKQEQYLKDDEALDdyl 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 --------------------------------------------------------------------------------
Cdd:PRK14939 558 ielalegatlhladgpaisgealeklvkeyravrkiidrlerrypravlealiyapaldlddladeaavaaldadfltsa 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 557 -----------------------------------ELLKTLPQTPKPGL--QRYKGLGEMNATQLWETTMDPDARTLLQV 599
Cdd:PRK14939 638 eyrrlvelaeklrglieegaylergerkqpvssfeEALDWLLAEARKGLsiQRYKGLGEMNPEQLWETTMDPENRRLLQV 717
|
730 740 750
....*....|....*....|....*....|....*....
gi 2182436910 600 TLEDAIDADETFEMLMGDKVEPRRNFIEENAQYVKNLDI 638
Cdd:PRK14939 718 TIEDAIAADEIFTTLMGDEVEPRREFIEENALNVANLDV 756
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
8-638 |
0e+00 |
|
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273421 [Multi-domain] Cd Length: 654 Bit Score: 1142.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 8 YDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIHEK 87
Cdd:TIGR01059 1 YDASSIKVLEGLEAVRKRPGMYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 88 MGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIGETDVTGT 167
Cdd:TIGR01059 81 EGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 168 TTHFVPDPEIFtETIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKERRNEYCYEGGIKSYVEHLNRSKEVVHEEPVYI 247
Cdd:TIGR01059 161 TVRFWPDPEIF-ETTEFDFDILAKRLRELAFLNSGVKISLEDERDGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 248 EGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVREGLTAII 327
Cdd:TIGR01059 240 KGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 328 SIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKSALEVSSL 407
Cdd:TIGR01059 320 SVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 408 PGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFT 487
Cdd:TIGR01059 400 PGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 488 LEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGK---------------------RV 546
Cdd:TIGR01059 480 LEKLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKkeryikddkekdlvgealedlKA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 547 EYVYNDKQLDELLKTLPQTP---KPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRR 623
Cdd:TIGR01059 560 LYIYSDKEKEEAKTQIPVHLgrkGIEIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTLMGDEVEPRR 639
|
650
....*....|....*
gi 2182436910 624 NFIEENAQYVKNLDI 638
Cdd:TIGR01059 640 EFIEANALDVKNLDV 654
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-630 |
0e+00 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 985.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 1 MEQQHNSYDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGI 80
Cdd:PRK05559 1 AAMMTNNYNADSIEVLEGLEPVRKRPGMYIGSTDTRGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 81 PVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIG 160
Cdd:PRK05559 81 PVGIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 161 ET--DVTGTTTHFVPDPEIFtETIEFDYDTLANRVRELAFLTKGVNIIIEDLREgkerRNEYCYEGGIKSYVEHLNRSKE 238
Cdd:PRK05559 161 TAgkRKTGTRVRFWPDPKIF-DSPKFSPERLKERLRSKAFLLPGLTITLNDERE----RQTFHYENGLKDYLAELNEGKE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 239 VVHEEPV-YIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKdGDSNLSGE 317
Cdd:PRK05559 236 TLPEEFVgSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLP-KGKKLEGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 318 DVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVmaARARMAAKKARELTR 397
Cdd:PRK05559 315 DVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAI--KAAQARLRAAKKVKR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 398 RKSALEvSSLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITA 477
Cdd:PRK05559 393 KKKTSG-PALPGKLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 478 LGTGIGEDFTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGKRVEYVYNDKQLDE 557
Cdd:PRK05559 472 IGIGPGDSFDLEDLRYGKIIIMTDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRVDKGKKKIYALDEEEKEE 551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182436910 558 LLKTLPQT-PKPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIEENA 630
Cdd:PRK05559 552 LLKKLGKKgGKPEIQRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDAEETEKLVDMLMGKKAEPRREWIEENG 625
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
37-630 |
0e+00 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 962.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 37 GLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGG 116
Cdd:smart00433 1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 117 LHGVGASVVNALSTTLDVTVYRDGKIHYQQFKR-GVPVGDLEVIGETDVTGTTTHFVPDPEIFTETIEFDYDTLANRVRE 195
Cdd:smart00433 81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTTDDDFELLKRRLRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 196 LAFLTKGVNIIIEDLREGKERrnEYCYEGGIKSYVEHLNRSKEVVHEEPVYIEGEKDGITVEVALQYNDSYTSNIYSFAN 275
Cdd:smart00433 161 LAFLNKGVKITLNDERSDEEK--TFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 276 NINTYEGGTHEAGFKTGLTRVINDYARKNGvfKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDS 355
Cdd:smart00433 239 NIATTEGGTHENGFKDALTRVINEYAKKKK--KLKEKNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 356 LFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKsALEVSSLPGKLADCSSKDPSISELYIVEGDSAGGS 435
Cdd:smart00433 317 IVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 436 AKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFTLEKARYHKIVIMTDADVDGAHIRTLLLT 515
Cdd:smart00433 396 AKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEKLRYGKIIIMTDADVDGSHIKGLLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 516 FFYRYMREIIENGYVYIAQPPLYKVQQGKRvEYVYNDKQLDELLKTLPQTP----KPGLQRYKGLGEMNATQLWETTMDP 591
Cdd:smart00433 476 FFYRYMPPLIEAGFVYIAIPPLYKVTKGKK-KYVYSFYSLDEYEKWLEKTEgnksKYEIQRYKGLGEMNADQLWETTMDP 554
|
570 580 590
....*....|....*....|....*....|....*....
gi 2182436910 592 DARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIEENA 630
Cdd:smart00433 555 ERRTLLFVTLDDADEADLIFSALMGDKVEPRKEWIEENA 593
|
|
| parE_Gpos |
TIGR01058 |
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II ... |
6-632 |
0e+00 |
|
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation step of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 130130 [Multi-domain] Cd Length: 637 Bit Score: 794.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 6 NSYDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIH 85
Cdd:TIGR01058 3 SKYNADAIKILEGLDAVRKRPGMYIGSTDSKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITVQDDGRGIPTGIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 86 EKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKR-GVPVGDLEVIGETDV 164
Cdd:TIGR01058 83 QDGNISTVETVFTVLHAGGKFDQGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIYQQRFENgGKIVQSLKKIGTTKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 165 TGTTTHFVPDPEIFTeTIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKerRNEYCYEGGIKSYVEHLNRSKEVVHEEp 244
Cdd:TIGR01058 163 TGTLVHFHPDPTIFK-TTQFNSNIIKERLKESAFLLKKLKLTFTDKRTNK--TTVFFYENGLVDFVDYINETKETLSQV- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 245 VYIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVREGLT 324
Cdd:TIGR01058 239 TYFEGEKNGIEVEVAFQFNDGDSENILSFANSVKTKEGGTHENGFKLAITDVINSYARKYNLLKEKDKNLEGSDIREGLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 325 AIISIKHPDP--QFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTR--RKS 400
Cdd:TIGR01058 319 AIISVRIPEEliQFEGQTKSKLFSPEARNVVDEIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKsgKKP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 401 ALEVSSLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGT 480
Cdd:TIGR01058 399 KKEKGILSGKLTPAQSKNPAKNELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFCIGT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 481 GIGEDFTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQ--GKRVEYVYNDKQLDEL 558
Cdd:TIGR01058 479 GIGADFSIKDLKYDKIIIMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLSKkdGKKVKYAWSDLELESV 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2182436910 559 LKTLPQTPkpgLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIEENAQY 632
Cdd:TIGR01058 559 KKKLKNYT---LQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDLARAERQINTLMGDKVEPRKKWIEANINF 629
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
3-631 |
0e+00 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 566.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 3 QQHNSYDENQIQVLEGLEAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPV 82
Cdd:PTZ00109 95 QRCSEYDADDIVVLEGLEAVRKRPGMYIGNTDEKGLHQLLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 83 GIHEKMGRPAVEVIMTVLHAGGKF-DGSG---------------------------------------YKVSGGLHGVGA 122
Cdd:PTZ00109 175 DVSEKTGKSGLETVLTVLHSGGKFqDTFPknsrsdksedkndtksskkgksshvkgpkeakekessqmYEYSSGLHGVGL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 123 SVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIGE-TDVTGTTTHFVPD-PEIFTETIE-------------FDYD 187
Cdd:PTZ00109 255 SVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCpLKKRGTTIHFLPDyKHIFKTHHQhteteeeegckngFNLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 188 TLANRVRELAFLTKGVNIIIEDLREGKERrNEYCYE-----GGIKSYVEHLNRSKEVVHEEPVYI--EGEKDGITVEVAL 260
Cdd:PTZ00109 335 LIKNRIHELSYLNPGLTFYLVDERIANEN-NFYPYEtikheGGTREFLEELIKDKTPLYKDINIIsiRGVIKNVNVEVSL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 261 QYN-DSYTSNIYSFANNINTyEGGTHEAGFKTGLTRVINDYARKNGVFKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQ 339
Cdd:PTZ00109 414 SWSlESYTALIKSFANNVST-TAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISVKLNGAEFDGQ 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 340 TKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKARELTRRKSALEVSS-LPGKLADCSSKD 418
Cdd:PTZ00109 493 TKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSTiLPGKLVDCISDD 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 419 PSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLD-KILSNNEVRSMITALGTGIGED------------ 485
Cdd:PTZ00109 573 IERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNPVtwrqydlshgtk 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 486 --------------------FTLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKV----- 540
Cdd:PTZ00109 653 askdesvqnnnstltkkknsLFDTPLRYGKIILLTDADVDGEHLRILLLTLLYRFCPSLYEHGRVYVACPPLYRItnnrm 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 541 -------QQGKRVEYVYNDKQLDELLKTL-----------------------------------------PQTPKPG--- 569
Cdd:PTZ00109 733 kqfnvstKNSKKYIYTWSDEELNVLIKLLnkdysskettrsveekgnapdldneyedekldnknmrennvDEVELKTelg 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 570 --------------------------LQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRR 623
Cdd:PTZ00109 813 tnvadteqtdeldinkaffkfskhyeIQRFKGLGEMMADQLWETTMDPKKRILIRITVSDAMRASELIFLLMGEDVQSRK 892
|
....*...
gi 2182436910 624 NFIEENAQ 631
Cdd:PTZ00109 893 QFIFENSP 900
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
7-628 |
0e+00 |
|
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. This protein is active as an alpha(2)beta(2) heterotetramer. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 130127 [Multi-domain] Cd Length: 625 Bit Score: 549.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 7 SYDENQIQVLEGLEAVRKRPGMYIGSTSakgLHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIHE 86
Cdd:TIGR01055 3 NYSAKDIEVLDGLEPVRKRPGMYTDTTR---PNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 87 KMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIGETD--V 164
Cdd:TIGR01055 80 KEGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGkrL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 165 TGTTTHFVPDPEIFTEtIEFDYDTLANRVRELAFLTKGVNIIIEDLREGKERRneYCYEGGIKSYVEHLNRSKEVVHEEP 244
Cdd:TIGR01055 160 TGTSVHFTPDPEIFDS-LHFSVSRLYHILRAKAVLCRGVEIEFEDEVNNTKAL--WNYPDGLKDYLSEAVNGDNTLPPKP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 245 VYIEGEKDGITVEVALQYNDSYTSNIY-SFANNINTYEGGTHEAGFKTGLTRVINDYARKNGVFKDGdSNLSGEDVREGL 323
Cdd:TIGR01055 237 FSGNFEGDDEAVEWALLWLPEGGELFMeSYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRNNLPRG-VKLTAEDIWDRC 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 324 TAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEKGVMAARARMAAKKArelTRRKSALE 403
Cdd:TIGR01055 316 SYVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKK---VVRKKLTS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 404 VSSLPGKLADCSSKDPSISELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIG 483
Cdd:TIGR01055 393 GPALPGKLADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGIDPD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 484 EDFtLEKARYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQPPLYKVQQGKRVEYVYNDKQLDELLKTLP 563
Cdd:TIGR01055 473 SND-LSQLRYGKICILADADSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRIDLSKEVYYALDEEEKEKLLYKLK 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2182436910 564 QTP-KPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAID--ADETFEMLMGDKV-EPRRNFIEE 628
Cdd:TIGR01055 552 KKKgKPNVQRFKGLGEMNPAQLRETTMDPNTRRLVQLTLDDVQDqrVDKIMDMLLAKKRsEDRFNWLQE 620
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
38-216 |
1.76e-114 |
|
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: 339.90 E-value: 1.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 38 LHHLVWEIVDNSIDEALAGYCTDITVQIEKDNSITVKDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGL 117
Cdd:cd16928 1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 118 HGVGASVVNALSTTLDVTVYRDGKIHYQQFKRGVPVGDLEVIGETDVTGTTTHFVPDPEIFtETIEFDYDTLANRVRELA 197
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIF-EKTEFDFDTLKRRLRELA 159
|
170
....*....|....*....
gi 2182436910 198 FLTKGVNIIIEDLREGKER 216
Cdd:cd16928 160 FLNKGLKIVLEDERTGKEE 178
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
224-378 |
8.98e-90 |
|
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: 275.98 E-value: 8.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 224 GGIKSYVEHLNRSKEVVHEEPVYIEGEKDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYARK 303
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2182436910 304 NGVFKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEK 378
Cdd:cd00822 81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEK 155
|
|
| TOPRIM_TopoIIA_GyrB |
cd03366 |
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
422-535 |
1.86e-85 |
|
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: 262.59 E-value: 1.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 422 SELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFTLEKARYHKIVIMTD 501
Cdd:cd03366 1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKLRYHKIIIMTD 80
|
90 100 110
....*....|....*....|....*....|....
gi 2182436910 502 ADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQP 535
Cdd:cd03366 81 ADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP 114
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
225-378 |
2.32e-77 |
|
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
Pssm-ID: 425522 [Multi-domain] Cd Length: 173 Bit Score: 243.68 E-value: 2.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 225 GIKSYVEHLNRSKEVVHEEPVYIEGE--KDGITVEVALQYNDSYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINDYAR 302
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2182436910 303 KNGVFKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEALEKFLLENPDAAKKIVEK 378
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEK 156
|
|
| TOPRIM_TopoIIA_like |
cd01030 |
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
422-535 |
2.42e-70 |
|
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: 223.15 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 422 SELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIG-EDFTLEKARYHKIVIMT 500
Cdd:cd01030 1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGkDDFDLDKLRYGKIIIMT 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2182436910 501 DADVDGAHIRTLLLTFFYRYMREIIENGYVYIAQP 535
Cdd:cd01030 81 DADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT 115
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
11-626 |
5.54e-59 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 208.45 E-value: 5.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 11 NQIQVLEGLEAVRKRPGMYIGSTSAK-----------------GLHHLVWEIVDNSIDEALAG---YCTDITVQIeKDNS 70
Cdd:PHA02569 2 DEFKVLSDREHILKRPGMYIGSVAYEaherflfgkftqveyvpGLVKIIDEIIDNSVDEAIRTnfkFANKIDVTI-KNNQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 71 ITVKDNGRGIPVGI-----HEKMGRPavEVIMTVLHAGGKFDGSGyKVSGGLHGVGASVVNALSTTLdVTVYRDGKihyq 145
Cdd:PHA02569 81 VTVSDNGRGIPQAMvttpeGEEIPGP--VAAWTRTKAGSNFDDTN-RVTGGMNGVGSSLTNFFSVLF-IGETCDGK---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 146 qfkRGVPV----GDLEVIGETDVT---GTTTHFVPDPEIF-TETIEFDY-DTLANRVRELAFLTKGVNIIIEdlreGKEr 216
Cdd:PHA02569 153 ---NEVTVncsnGAENISWSTKPGkgkGTSVTFIPDFSHFeVNGLDQQYlDIILDRLQTLAVVFPDIKFTFN----GKK- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 217 rneycYEGGIKSYVEHLNrskevvhEEPVYIEGEKDGITVEVAlqyNDSYTSNiySFANNINTYEGGTHEAGFKTGLT-R 295
Cdd:PHA02569 225 -----VSGKFKKYAKQFG-------DDTIVQENDNVSIALAPS---PDGFRQL--SFVNGLHTKNGGHHVDCVMDDICeE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 296 VINDYARKNGVfkdgdsNLSGEDVREGLTAIISIKH-PDPQFEGQTKTKLGNS--EARTITDsLFSEALEKFLLENPDAA 372
Cdd:PHA02569 288 LIPMIKKKHKI------EVTKARVKECLTIVLFVRNmSNPRFDSQTKERLTSPfgEIRNHID-LDYKKIAKQILKTEAII 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 373 KKIVEKGVMAARARMAAkkarELTR-RKSALEV-------SSLPGKLADcsskdpsiSELYIVEGDSAGGSAKQGRDRHF 444
Cdd:PHA02569 361 MPIIEAALARKLAAEKA----AETKaAKKAKKAkvakhikANLIGKDAE--------TTLFLTEGDSAIGYLIEVRDEEL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 445 QAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDftLEKARYHKIVIMTDADVDG-AHIRTLLLTFFYRYmRE 523
Cdd:PHA02569 429 HGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEK--AENMNYKNIAIMTDADVDGkGSIYPLLLAFFSRW-PE 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 524 IIENGYVYIAQPPLYKVQQGKRVEYVYNdkqLDELLKTLPQTPKPGLQRYKGLGEMNATQLWETTMDPdarTLLQVTLED 603
Cdd:PHA02569 506 LFEQGRIRFVKTPVIIAQVGKETKWFYS---LDEFEKAKDSLKKWSIRYIKGLGSLRKSEYRRVINNP---VYDVVVLPD 579
|
650 660
....*....|....*....|...
gi 2182436910 604 aiDADETFEMLMGDKVEPRRNFI 626
Cdd:PHA02569 580 --DWKELFEMLFGDDADLRKDWM 600
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
9-638 |
1.66e-45 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 174.46 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 9 DENQIQVLEGLEAVRKRPGMYIGSTSAK-----------------------GLHHLVWEI----VDNSIDEALAGYCTDI 61
Cdd:PTZ00108 6 VEERYQKKTQIEHILLRPDTYIGSIETQtedmwvydeeknrmvyktityvpGLYKIFDEIlvnaADNKARDKGGHRMTYI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 62 TVQI-EKDNSITVKDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLDVTVyRDG 140
Cdd:PTZ00108 86 KVTIdEENGEISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLTNIFSTKFTVEC-VDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 141 KIHyQQFK-------------RGVPVGdleviGETDVTGTTthFVPDPEIFTETiEFDYDTLA---NRVRELAFLTKGVN 204
Cdd:PTZ00108 165 KSG-KKFKmtwtdnmskksepRITSYD-----GKKDYTKVT--FYPDYAKFGMT-EFDDDMLRllkKRVYDLAGCFGKLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 205 IIIEDLREgkerrneycyegGIKSYVEHLN-RSKEVVHEEPVYIEGEKDGIT--VEVALQYNDSyTSNIYSFANNINTYE 281
Cdd:PTZ00108 236 VYLNGERI------------AIKSFKDYVDlYLPDGEEGKKPPYPFVYTSVNgrWEVVVSLSDG-QFQQVSFVNSICTTK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 282 GGTHEAGFKTGLTRVINDYARKngvFKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSEAL 361
Cdd:PTZ00108 303 GGTHVNYILDQLISKLQEKAKK---KKKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTKPSKFGSTCELSEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 362 EKFLLENPdaakkIVEKGVMAARARMAAKKAREL-TRRKSALevSSLPgKLADCSSKDPSISE---LYIVEGDSA----- 432
Cdd:PTZ00108 380 IKYVLKSP-----ILENIVEWAQAKLAAELNKKMkAGKKSRI--LGIP-KLDDANDAGGKNSEectLILTEGDSAkalal 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 433 GGSAKQGRDRHfqAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFT-LEKARYHKIVIMTDADVDGAHIRT 511
Cdd:PTZ00108 452 AGLSVVGRDYY--GVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEdPKGLRYGSLMIMTDQDHDGSHIKG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 512 LLLTFFYRYMREIIE-NGYVYIAQPPLYKVQQ-GKRVEYVYNDKQLDELLKTLPqTPKPGLQRYKGLGEMNATQLWE--T 587
Cdd:PTZ00108 530 LLINMIHHFWPSLLKnPGFLKEFITPIVKATKkGNQVISFFTIPDFEKWKQTVG-LKGWKIKYYKGLGTSTDKEGKEyfS 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2182436910 588 TMDpdaRTLLQVTLEDAIDaDETFEMLMG-DKVEPRRNFIeenAQYVKNLDI 638
Cdd:PTZ00108 609 NID---KHRIRFVYVDDSD-DDSIDLAFSkKRVEDRKEWI---TNYKGGTYV 653
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
19-593 |
2.02e-42 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 164.88 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 19 LEAVRKRPGMYIGSTS---------------------AKGLHHLVWEIVDNSIDEALAGYCTD-ITVQIEKD-NSITVKD 75
Cdd:PLN03128 13 LEHILLRPDTYIGSTEkhtqtlwvyeggemvnrevtyVPGLYKIFDEILVNAADNKQRDPSMDsLKVDIDVEqNTISVYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 76 NGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALST-----TLDVTVYRdgkiHYQQ-FKR 149
Cdd:PLN03128 93 NGKGIPVEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFSTeftveTADGNRGK----KYKQvFTN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 150 GVPVGDLEVIGETDVTGTTTH--FVPDPEIFTETiEFDYDT---LANRVRELA-FLTKGVNIIIEDlregkerrnEYCYE 223
Cdd:PLN03128 169 NMSVKSEPKITSCKASENWTKitFKPDLAKFNMT-RLDEDVvalMSKRVYDIAgCLGKKLKVELNG---------KKLPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 224 GGIKSYVEHLNRSKEVVHEEPVYIEGEKDGITVEVALQyNDSYTSniYSFANNINTYEGGTHEAGFKTGLTRVINDYA-R 302
Cdd:PLN03128 239 KSFQDYVGLYLGPNSREDPLPRIYEKVNDRWEVCVSLS-DGSFQQ--VSFVNSIATIKGGTHVDYVADQIVKHIQEKVkK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 303 KNGvfkdGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLGNSEARTITDSLFSealEKFLlenpdaaKKIVEKGVMA 382
Cdd:PLN03128 316 KNK----NATHVKPFQIKNHLWVFVNCLIENPTFDSQTKETLTTRPSSFGSKCELS---EEFL-------KKVEKCGVVE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 383 ARARMAAKKARELTRRKSALEVSSLPG--KLADCS---SKDPSISELYIVEGDSA-----GGSAKQGRDRHfqAILPLRG 452
Cdd:PLN03128 382 NILSWAQFKQQKELKKKDGAKRQRLTGipKLDDANdagGKKSKDCTLILTEGDSAkalamSGLSVVGRDHY--GVFPLRG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 453 KILNVEKARLDKILSNNEVRSMITALGTGIGEDFTLEKA---RYHKIVIMTDADVDGAHIRTLLLTFFYRYMREIIE-NG 528
Cdd:PLN03128 460 KLLNVREASHKQIMKNAEITNIKQILGLQFGKTYDEENTkslRYGHLMIMTDQDHDGSHIKGLIINFFHSFWPSLLKiPG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 529 YVYIAQPPLYKVQQGKRVEYVYNDKQLDELLKTL-PQTPKPGLQRYKGLGEMNATQ---------------LWETTMDPD 592
Cdd:PLN03128 540 FLVEFITPIVKATKGGKSLSFYTMPEYEAWKESLeGETKGWTIKYYKGLGTSTSEEakeyfsnldihkkefLWQSDEDGD 619
|
.
gi 2182436910 593 A 593
Cdd:PLN03128 620 L 620
|
|
| DNA_gyraseB_C |
pfam00986 |
DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA ... |
567-627 |
8.28e-40 |
|
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: 139.44 E-value: 8.28e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182436910 567 KPGLQRYKGLGEMNATQLWETTMDPDARTLLQVTLEDAIDADETFEMLMGDKVEPRRNFIE 627
Cdd:pfam00986 3 KVEIQRYKGLGEMNPEQLWETTMDPETRRLLQVTIEDAAEADEIFSTLMGDKVEPRREFIE 63
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
19-593 |
2.09e-29 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 124.97 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 19 LEAVRKRPGMYIGS---------------------TSAKGLHHLVWEIVDNSIDEALAGYCTD-ITVQIEKD-NSITVKD 75
Cdd:PLN03237 38 LEHILLRPDTYIGSiekhtqtlwvyetdkmvqrsvTYVPGLYKIFDEILVNAADNKQRDPKMDsLRVVIDVEqNLISVYN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 76 NGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVSGGLHGVGASVVNALSTTLdVTVYRDGKIH--YQQF------ 147
Cdd:PLN03237 118 NGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTTGGRNGYGAKLTNIFSTEF-VIETADGKRQkkYKQVfsnnmg 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 148 KRGVPVgdLEVIGETDvTGTTTHFVPDPEIFTETiEFDYDTLA---NRVRELA-FLTKGVNIIIEDLREGKERRNEYCY- 222
Cdd:PLN03237 197 KKSEPV--ITKCKKSE-NWTKVTFKPDLAKFNMT-HLEDDVVAlmkKRVVDIAgCLGKTVKVELNGKRIPVKSFSDYVDl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 223 --EGGIKSYVEHLNRSKEVVHEEpvyiegekdgitVEVALQYNDSYTSNIySFANNINTYEGGTHEAGFKTGLTRVINDY 300
Cdd:PLN03237 273 ylESANKSRPENLPRIYEKVNDR------------WEVCVSLSEGQFQQV-SFVNSIATIKGGTHVDYVTNQIANHVMEA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 301 ARKngvfKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKtklgnsEARTITDSLFS---EALEKFLlenpdaaKKIVE 377
Cdd:PLN03237 340 VNK----KNKNANIKAHNVKNHLWVFVNALIDNPAFDSQTK------ETLTLRQSSFGskcELSEDFL-------KKVMK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 378 KGVMAARAR-MAAKKAREL--TRRKSALEVSSLPgKLADCSSKDPSISE---LYIVEGDSAGGSAKQGR---DRHFQAIL 448
Cdd:PLN03237 403 SGIVENLLSwADFKQSKELkkTDGAKTTRVTGIP-KLEDANEAGGKNSEkctLILTEGDSAKALAVAGLsvvGRNYYGVF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 449 PLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDFTLEKA-RYHKIVIMTDADVDGAHIRTLLLTFFYRYMREI--I 525
Cdd:PLN03237 482 PLRGKLLNVREASHKQIMNNAEIENIKQILGLQHGKQYESVKSlRYGHLMIMTDQDHDGSHIKGLLINFIHSFWPSLlkV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 526 ENGYVYIAQPPLYKVQQGKRVEYVYNDKQLDELLKTL----------------PQTPKPGLQRYKGLGEMNATQLWETTM 589
Cdd:PLN03237 562 PSFLVEFITPIVKATRRGKKVLSFYSMPEYEEWKESLggnatgwsikyykglgTSTAKEGKEYFKNLGKHKKDFVWEDEQ 641
|
....
gi 2182436910 590 DPDA 593
Cdd:PLN03237 642 DGDA 645
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
226-345 |
6.74e-25 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.
Pssm-ID: 238202 [Multi-domain] Cd Length: 107 Bit Score: 99.26 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 226 IKSYVEHLNRSKevVHEEPVYIEGEKDGITVEVALQYND---SYTSNIYSFANNINTYEGGTHEAGFKTGLTRVINdyar 302
Cdd:cd00329 1 LKDRLAEILGDK--VADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2182436910 303 kngvfkdgdsnlsGEDVREGLTAIISIKHPD--PQFE-GQTKTKLG 345
Cdd:cd00329 75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEVR 107
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
424-520 |
3.19e-20 |
|
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.
Pssm-ID: 173785 [Multi-domain] Cd Length: 120 Bit Score: 86.59 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 424 LYIVEGDSAGGSAKQGR---DRHFQAILPLRGKILNVEKARLDKILSNNEVRSMITALGTGIGEDF--TLEKARYHKIVI 498
Cdd:cd03365 3 LILTEGDSAKALAVAGLsvvGRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDyeSTKSLRYGRLMI 82
|
90 100
....*....|....*....|..
gi 2182436910 499 MTDADVDGAHIRTLLLTFFYRY 520
Cdd:cd03365 83 MTDQDHDGSHIKGLLINFIHSF 104
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
423-535 |
2.73e-17 |
|
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: 77.40 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 423 ELYIVEGDSAGGSAKQGRDRHFQAILPLRGKILNVEKARLDKILSNnevrsmitalgtgigedFTLEKARYHKIVIMTDA 502
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALKA-----------------LKELALKAKEVILATDP 63
|
90 100 110
....*....|....*....|....*....|....*
gi 2182436910 503 DVDGAHIRTLLLTFfyrymREIIEN--GYVYIAQP 535
Cdd:pfam01751 64 DREGEAIALKLLEL-----KELLENagGRVEFSEL 93
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
35-141 |
1.98e-16 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 75.38 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 35 AKGLHHLVWEIVDNSIDEALAGycTDITVQIEKDN---SITVKDNGRGIPvgihekmgrpaVEVIMTVLHAGGKFDGSGY 111
Cdd:smart00387 3 PDRLRQVLSNLLDNAIKYTPEG--GRITVTLERDGdhvEITVEDNGPGIP-----------PEDLEKIFEPFFRTDKRSR 69
|
90 100 110
....*....|....*....|....*....|
gi 2182436910 112 KVSGglHGVGASVVNALSTTLDVTVYRDGK 141
Cdd:smart00387 70 KIGG--TGLGLSIVKKLVELHGGEISVESE 97
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
35-139 |
6.29e-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: 73.94 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 35 AKGLHHLVWEIVDNSIDEAlaGYCTDITVQIEKDN--SITVKDNGRGIPVGIHEKMgrpavevimtvlhaGGKFDgSGYK 112
Cdd:pfam02518 3 ELRLRQVLSNLLDNALKHA--AKAGEITVTLSEGGelTLTVEDNGIGIPPEDLPRI--------------FEPFS-TADK 65
|
90 100
....*....|....*....|....*..
gi 2182436910 113 VSGGLHGVGASVVNALSTTLDVTVYRD 139
Cdd:pfam02518 66 RGGGGTGLGLSIVRKLVELLGGTITVE 92
|
|
| HATPase_TopII-like |
cd16930 |
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ... |
37-174 |
9.07e-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: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 37 GLHHLVWEIVDNSID-EALAGYCTDITVQIEKD-NSITVKDNGRGIPVGIHEKMGRPAVEVIMTVLHAGGKFDGSGYKVS 114
Cdd:cd16930 4 GLYKIFDEILVNAADnKQRDKSMTCIKVTIDPEnNEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVT 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2182436910 115 GGLHGVGASVVNALSTTLDV-TVYRDGKIHYQQ------FKRGVPVgDLEVIGETDVTGTTthFVPD 174
Cdd:cd16930 84 GGRNGYGAKLCNIFSTEFTVeTADSESKKKFKQtwtnnmGKASEPK-ITPYEKGKDYTKVT--FKPD 147
|
|
| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
422-525 |
5.07e-07 |
|
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.
Pssm-ID: 173773 [Multi-domain] Cd Length: 83 Bit Score: 47.81 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 422 SELYIVEGDSAGGSAKQGRDrHFQAILPLRGKILNVEKARLDKILSnnevrsmitalgtgigedftlekaRYHKIVIMTD 501
Cdd:cd00188 1 KKLIIVEGPSDALALAQAGG-YGGAVVALGGHALNKTRELLKRLLG------------------------EAKEVIIATD 55
|
90 100
....*....|....*....|....
gi 2182436910 502 ADVDGAHIRTLLLTFFYRYMREII 525
Cdd:cd00188 56 ADREGEAIALRLLELLKSLGKKVR 79
|
|
| COG1389 |
COG1389 |
DNA topoisomerase VI, subunit B [Replication, recombination and repair]; |
32-148 |
3.92e-05 |
|
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
Pssm-ID: 440999 [Multi-domain] Cd Length: 530 Bit Score: 46.75 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 32 STSAKGLHHLVWEIVDNSIDEA-LAGYCTDITVQIEKDNS-----ITVKDNGRGIPvgiHEKMGRpaveVIMTVLhAGGK 105
Cdd:COG1389 30 DSPARALYTTVKEAVDNSLDACeEAGILPDIKVSIERVDGkdiyrVTVEDNGPGIP---PEQIPK----VFGKLL-YGSK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2182436910 106 FdgSGYKVSGGLHGVGAS--VVNALSTT-LDVTVY----RDGKIHYQQFK 148
Cdd:COG1389 102 F--HVLRQSRGQQGIGISaaVLYAQMTTgKPVEVIsktgGSEPAYYFELK 149
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
38-128 |
6.16e-05 |
|
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.
Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 42.20 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 38 LHHLVWEIVDNSIDEALAGycTDITVQIEKDNS---ITVKDNGRGIPVGIHEKMGRPavevimtvlhaggkFDGSGYKVS 114
Cdd:cd00075 1 LEQVLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEEDLERIFER--------------FYRGDKSRE 64
|
90
....*....|....
gi 2182436910 115 GGLHGVGASVVNAL 128
Cdd:cd00075 65 GGGTGLGLAIVRRI 78
|
|
| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
32-148 |
1.97e-04 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 44.50 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 32 STSAKGLHHLVWEIVDNSIDEA-LAGYCTDITVQIEKDN------SITVKDNGRGIPvgihekmgrpaVEVIMTVLhagG 104
Cdd:PRK04184 31 DNPARALYTTVKELVDNSLDACeEAGILPDIKIEIKRVDegkdhyRVTVEDNGPGIP-----------PEEIPKVF---G 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2182436910 105 K-FDGSGYKV---SGGLHGVGAS--VVNALSTT-LDVTVY----RDGKIHYQQFK 148
Cdd:PRK04184 97 KlLYGSKFHNlrqSRGQQGIGISaaVLYAQMTTgKPVRVIsstgGSKKAYYFELK 151
|
|
| TopoIIA_Trans_ScTopoIIA |
cd03481 |
TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
224-378 |
3.73e-04 |
|
TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topo IIA. S. cerevisiae Topo IIA is a homodimer encoded by a single gene. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes.
Pssm-ID: 239563 [Multi-domain] Cd Length: 153 Bit Score: 41.50 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 224 GGIKSYVEHLNRSKEVVHEEPVYIEGEKDGITVEVALQYNDSYTSNIySFANNINTYEGGTHEAGFKTGLTRVINDYARK 303
Cdd:cd03481 1 KSFKDYVKLYLKDANKEDGPPPPVVYEPVNDRWEVAVALSDGQFQQV-SFVNSIATTKGGTHVDYVADQIVKKLDEVVKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 304 NgvfKDGDSNLSGEDVREGLTAIISIKHPDPQFEGQTKTKLgnsearTITDSLFS---EALEKFLlenpDAAKK--IVEK 378
Cdd:cd03481 80 K---NKGGINVKPFQVKNHLWIFVNCLIENPSFDSQTKETL------TTKPKSFGskcELSEKFL----KKAVKsgIVES 146
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|
| HATPase_TopVIB-like |
cd16933 |
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ... |
20-125 |
3.86e-04 |
|
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: 41.95 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 20 EAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEA-LAGYCTDITVQIEKDN----SITVKDNGRGIPvgiHEKMGRpave 94
Cdd:cd16933 2 EFFRKNKEMLGFDNPIRSLYTTVRELVENSLDATeEAGILPDIKVEIEEIGkdhyKVIVEDNGPGIP---EEQIPK---- 74
|
90 100 110
....*....|....*....|....*....|.
gi 2182436910 95 VIMTVLhAGGKFdgsGYKVSGGLHGVGASVV 125
Cdd:cd16933 75 VFGKVL-YGSKY---HNKQSRGQQGLGISAA 101
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
44-81 |
1.46e-03 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 40.11 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2182436910 44 EIVDNSIDealAGyCTDITVQIEKD--NSITVKDNGRGIP 81
Cdd:cd16926 20 ELVENSID---AG-ATRIDVEIEEGglKLIRVTDNGSGIS 55
|
|
| top6b |
TIGR01052 |
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type ... |
20-162 |
2.72e-03 |
|
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type II DNA topoisomerase (DNA gyrase). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273417 [Multi-domain] Cd Length: 488 Bit Score: 40.58 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2182436910 20 EAVRKRPGMYIGSTSAKGLHHLVWEIVDNSIDEA-LAGYCTDITVQIEKDNS----ITVKDNGRGIPvgihekmgrpaVE 94
Cdd:TIGR01052 11 EFFRKNKHMLGYSGKIRSLTTVIHELVTNSLDACeEAGILPDIKVEIEKIGKdhykVTVEDNGPGIP-----------EE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2182436910 95 VIMTVLhaGGKFDGSGYKV---SGGLHGVGASvvnalsttldvtvyrdGKIHYQQFKRGVPVgdlEVIGET 162
Cdd:TIGR01052 80 YIPKVF--GKMLAGSKFHRiiqSRGQQGIGIS----------------GAVLYSQMTTGKPV---KVISST 129
|
|
| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
44-81 |
3.33e-03 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 40.41 E-value: 3.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2182436910 44 EIVDNSIDealAGyCTDITVQIEKD--NSITVKDNGRGIP 81
Cdd:COG0323 30 ELVENAID---AG-ATRIEVEIEEGgkSLIRVTDNGCGMS 65
|
|
| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
44-81 |
3.59e-03 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 40.59 E-value: 3.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2182436910 44 EIVDNSIDealAGyCTDITVQIEKD--NSITVKDNGRGIP 81
Cdd:PRK00095 29 ELVENALD---AG-ATRIDIEIEEGglKLIRVRDNGCGIS 64
|
|
| HATPase_LytS-like |
cd16957 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
45-94 |
6.94e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.
Pssm-ID: 340433 [Multi-domain] Cd Length: 106 Bit Score: 36.63 E-value: 6.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2182436910 45 IVDNSIDEALAG--YCTDITVQIEKDNS---ITVKDNGRGIPVGIHEKMGRPAVE 94
Cdd:cd16957 9 LVENAIRHAFPKrkENNEVRVVVKKDQHkvhVSVSDNGQGIPEERLDLLGKTTVT 63
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