|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-642 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 1203.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 1 MDSDAGEYNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGI 80
Cdd:PRK05644 1 KEEKAQEYDASQIQVLEGLEAVRKRPGMYIGSTGERGLHHLVYEIVDNSIDEALAGYCDHIEVTINEDGSITVTDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 81 PVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLS 160
Cdd:PRK05644 81 PVDIHPKTGKPAVEVVLTVLHAGGKFGGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 161 ESapIERGTIVHFKPDPDIFqETTVFNYKTLLTRVRELAFLNKGLRISITDKRPEEPVSESFCYQGGIKEYVSYLDEGKE 240
Cdd:PRK05644 161 ET--DETGTTVTFKPDPEIF-ETTEFDYDTLATRLRELAFLNKGLKITLTDEREGEEKEETFHYEGGIKEYVEYLNRNKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 241 TLFPEPVYVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGED 320
Cdd:PRK05644 238 PLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 321 VREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRK 400
Cdd:PRK05644 318 VREGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 401 QSGLEIGNLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAM 480
Cdd:PRK05644 398 KSALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITAL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 481 GSGFGNDFDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGNNkelHYIDSDEELE 560
Cdd:PRK05644 478 GTGIGDDFDISKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGYVYIAQPPLYKIKKGGK---EYAYSDEELD 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 561 DYLAQLP--SNAKPKVQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAVFVE 638
Cdd:PRK05644 555 EILAELKlkGNPKYGIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSILMGDDVEPRREFIEENAKYVR 634
|
....
gi 2467955154 639 DLDI 642
Cdd:PRK05644 635 NLDI 638
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
3-642 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 1143.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 3 SDAGEYNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPV 82
Cdd:COG0187 1 AKKSNYDASSIQVLEGLEAVRKRPGMYIGSTDERGLHHLVWEIVDNSIDEALAGYCDRIEVTLHADGSVTVEDNGRGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 83 DIQTKTGKPALETVFTILHAggkfggggykvsggLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLSES 162
Cdd:COG0187 81 DIHPKEGKSALEVVLTVLHAggkfdggsykvsggLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 163 ApiERGTIVHFKPDPDIFqETTVFNYKTLLTRVRELAFLNKGLRISITDKRPEEPVSESFCYQGGIKEYVSYLDEGKETL 242
Cdd:COG0187 161 D--RTGTTVRFKPDPEIF-ETTEFDYETLAERLRELAFLNKGLTITLTDEREEEPKEETFHYEGGIKDFVEYLNEDKEPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 243 FPEPVYVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGEDVR 322
Cdd:COG0187 238 HPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 323 EGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRKQS 402
Cdd:COG0187 318 EGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 403 GLEIGNLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGS 482
Cdd:COG0187 398 ALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 483 GFGNDFDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGnnKELHYIDSDEELEDY 562
Cdd:COG0187 478 GIGDDFDLEKLRYHKIIIMTDADVDGAHIRTLLLTFFYRYMRPLIEAGHVYIAQPPLYRIKKG--KKTYYAYSDAELDEL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 563 LAQLPSNAKPKVQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAVFVEDLDI 642
Cdd:COG0187 556 LKELKGKKKVEIQRYKGLGEMNPEQLWETTMDPETRTLLQVTIEDAAEADEIFSLLMGDKVEPRREFIEENAKFVRNLDI 635
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
8-642 |
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: 960.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 8 YNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVDIQTK 87
Cdd:TIGR01059 1 YDASSIKVLEGLEAVRKRPGMYIGSTGETGLHHLVYEVVDNSIDEAMAGYCDTISVTINDDGSVTVEDNGRGIPVDIHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 88 TGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLSESApiER 167
Cdd:TIGR01059 81 EGISAVEVVLTVLHAGGKFDKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETK--KT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 168 GTIVHFKPDPDIFqETTVFNYKTLLTRVRELAFLNKGLRISITDKRPEEPVSESFCYQGGIKEYVSYLDEGKETLFPEPV 247
Cdd:TIGR01059 159 GTTVRFWPDPEIF-ETTEFDFDILAKRLRELAFLNSGVKISLEDERDGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 248 YVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGEDVREGMTA 327
Cdd:TIGR01059 238 YIKGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 328 IVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRKQSGLEIG 407
Cdd:TIGR01059 318 VISVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 408 NLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGND 487
Cdd:TIGR01059 398 GLPGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 488 FDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGNNK------------------- 548
Cdd:TIGR01059 478 FDLEKLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIENGYVYIAQPPLYKVKKGKKEryikddkekdlvgealedl 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 549 ELHYIDSDEELEDYLAQLPSNAKPK---VQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPP 625
Cdd:TIGR01059 558 KALYIYSDKEKEEAKTQIPVHLGRKgieIQRYKGLGEMNADQLWETTMDPESRTLLKVTIEDAVEADRIFSTLMGDEVEP 637
|
650
....*....|....*..
gi 2467955154 626 RRQFIEDNAVFVEDLDI 642
Cdd:TIGR01059 638 RREFIEANALDVKNLDV 654
|
|
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
2-642 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 934.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 2 DSDAGEYNADQIQVLEGLEAVRKRPGMYIG-TTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGI 80
Cdd:PRK14939 1 SMMSNSYGASSIKVLKGLDAVRKRPGMYIGdTDDGTGLHHMVYEVVDNAIDEALAGHCDDITVTIHADGSVSVSDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 81 PVDIQTKTGKPALETVFTILHAggkfggggykvsggLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLS 160
Cdd:PRK14939 81 PTDIHPEEGVSAAEVIMTVLHAggkfdqnsykvsggLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 161 ESApiERGTIVHFKPDPDIFqETTVFNYKTLLTRVRELAFLNKGLRISITDKRPEEpvSESFCYQGGIKEYVSYLDEGKE 240
Cdd:PRK14939 161 ETD--KTGTEVRFWPSPEIF-ENTEFDYDILAKRLRELAFLNSGVRIRLKDERDGK--EEEFHYEGGIKAFVEYLNRNKT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 241 TLFPEPVYVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGED 320
Cdd:PRK14939 236 PLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 321 VREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRK 400
Cdd:PRK14939 316 AREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 401 QSGLEIGNLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAM 480
Cdd:PRK14939 396 KGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITAL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 481 GSGFGND-FDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGnnKELHYIDSDEEL 559
Cdd:PRK14939 476 GCGIGRDeFNPDKLRYHKIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGHLYIAQPPLYKVKKG--KQEQYLKDDEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 560 EDYLAQL--------PSNAKP----------------------------------------------------------- 572
Cdd:PRK14939 554 DDYLIELalegatlhLADGPAisgealeklvkeyravrkiidrlerrypravlealiyapaldlddladeaavaaldadf 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 573 -----------------------------------------------------KVQRYKGLGEMDYDQLADTTMDPAHRR 599
Cdd:PRK14939 634 ltsaeyrrlvelaeklrglieegaylergerkqpvssfeealdwllaearkglSIQRYKGLGEMNPEQLWETTMDPENRR 713
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2467955154 600 LLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAVFVEDLDI 642
Cdd:PRK14939 714 LLQVTIEDAIAADEIFTTLMGDEVEPRREFIEENALNVANLDV 756
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-640 |
0e+00 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 884.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 1 MDSDAGEYNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGI 80
Cdd:PRK05559 1 AAMMTNNYNADSIEVLEGLEPVRKRPGMYIGSTDTRGLHHLVQEVIDNSVDEALAGHGKRIEVTLHADGSVSVRDNGRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 81 PVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLS 160
Cdd:PRK05559 81 PVGIHPEEGKSGVEVILTKLHAGGKFSNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 161 ESAPIERGTIVHFKPDPDIFqETTVFNYKTLLTRVRELAFLNKGLRISITDKRPEepvsESFCYQGGIKEYVSYLDEGKE 240
Cdd:PRK05559 161 TAGKRKTGTRVRFWPDPKIF-DSPKFSPERLKERLRSKAFLLPGLTITLNDERER----QTFHYENGLKDYLAELNEGKE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 241 TLFPEPV-YVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAEsLTGE 319
Cdd:PRK05559 236 TLPEEFVgSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLPKGKK-LEGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 320 DVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTR 399
Cdd:PRK05559 315 DVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKVKRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 400 KQSGLeigNLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTA 479
Cdd:PRK05559 395 KTSGP---ALPGKLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 480 MGSGFGNDFDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGNNKelHYIDSDEEL 559
Cdd:PRK05559 472 IGIGPGDSFDLEDLRYGKIIIMTDADVDGAHIATLLLTFFYRHFPPLVEAGHVYIALPPLYRVDKGKKK--IYALDEEEK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 560 EDYLAQL-PSNAKPKVQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAVFVE 638
Cdd:PRK05559 550 EELLKKLgKKGGKPEIQRFKGLGEMNPDQLWETTMDPETRRLVRVTIDDAEETEKLVDMLMGKKAEPRREWIEENGDFAE 629
|
..
gi 2467955154 639 DL 640
Cdd:PRK05559 630 EE 631
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
37-635 |
0e+00 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 834.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 37 GLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGG 116
Cdd:smart00433 1 GLHHLVDEIVDNAADEALAGYMDTIKVTIDKDNSISVEDNGRGIPVEIHPKEKKYAPEVIFTVLHAGGKFDDDAYKVSGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 117 LHGVGASVVNALSTNLDVKVVREGKVYYMDF-ATGRVKTPMTVLSESApiERGTIVHFKPDPDIFQETTVFNYKTLLTRV 195
Cdd:smart00433 81 LHGVGASVVNALSTEFEVEVARDGKEYKQSFsNNGKPLSEPKIIGDTK--KDGTKVTFKPDLEIFGMTTDDDFELLKRRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 196 RELAFLNKGLRISITDKRPEEPvsESFCYQGGIKEYVSYLDEGKETLFPEPVYVEGEEKDIVVEVALQYTTDIKENLRTF 275
Cdd:smart00433 159 RELAFLNKGVKITLNDERSDEE--KTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 276 TNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDgaESLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQAT 355
Cdd:smart00433 237 VNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKE--KNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 356 DRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRKqSGLEIGNLPGKLADNTSKDPEISELFIVEGDSAG 435
Cdd:smart00433 315 EKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRK-KKLSSISLPGKLADASSAGPKKCELFLVEGDSAG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 436 GSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTKANYHKVIIMTDADVDGAHIRTLL 515
Cdd:smart00433 394 GSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEKLRYGKIIIMTDADVDGSHIKGLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 516 LTLFYRYMRPLVDAGYIYIAQPPLYGVSLGNNKELHYIDSDEELEDYLAQLPSN-AKPKVQRYKGLGEMDYDQLADTTMD 594
Cdd:smart00433 474 LTFFYRYMPPLIEAGFVYIAIPPLYKVTKGKKKYVYSFYSLDEYEKWLEKTEGNkSKYEIQRYKGLGEMNADQLWETTMD 553
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2467955154 595 PAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAV 635
Cdd:smart00433 554 PERRTLLFVTLDDADEADLIFSALMGDKVEPRKEWIEENAP 594
|
|
| parE_Gpos |
TIGR01058 |
DNA topoisomerase IV, B subunit, Gram-positive; Operationally, topoisomerase IV is a type II ... |
5-636 |
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: 720.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 5 AGEYNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVDI 84
Cdd:TIGR01058 2 ASKYNADAIKILEGLDAVRKRPGMYIGSTDSKGLHHLVWEIVDNSVDEVLAGYADNITVTLHKDNSITVQDDGRGIPTGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 85 QTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVVREGKVYYMDF-ATGRVKTPMTVLSESA 163
Cdd:TIGR01058 82 HQDGNISTVETVFTVLHAGGKFDQGGYKTAGGLHGVGASVVNALSSWLEVTVKRDGQIYQQRFeNGGKIVQSLKKIGTTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 164 piERGTIVHFKPDPDIFQeTTVFNYKTLLTRVRELAFLNKGLRISITDKRPEEpvSESFCYQGGIKEYVSYLDEGKETLF 243
Cdd:TIGR01058 162 --KTGTLVHFHPDPTIFK-TTQFNSNIIKERLKESAFLLKKLKLTFTDKRTNK--TTVFFYENGLVDFVDYINETKETLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 244 PEpVYVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGEDVRE 323
Cdd:TIGR01058 237 QV-TYFEGEKNGIEVEVAFQFNDGDSENILSFANSVKTKEGGTHENGFKLAITDVINSYARKYNLLKEKDKNLEGSDIRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 324 GMTAIVSIKHPDP--QFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRKQ 401
Cdd:TIGR01058 316 GLSAIISVRIPEEliQFEGQTKSKLFSPEARNVVDEIVQDHLFFFLEENNNDAKLLIDKAIKARDAKEAAKKAREEKKSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 402 SGL--EIGNLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTA 479
Cdd:TIGR01058 396 KKPkkEKGILSGKLTPAQSKNPAKNELFLVEGDSAGGSAKQGRDRKFQAILPLRGKVLNVEKAKLADILKNEEINTIIFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 480 MGSGFGNDFDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLGNNKELHYIDSDEEL 559
Cdd:TIGR01058 476 IGTGIGADFSIKDLKYDKIIIMTDADTDGAHIQVLLLTFFYRYMRPLIELGHVYIALPPLYKLSKKDGKKVKYAWSDLEL 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2467955154 560 EDYLAQLpSNAkpKVQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIEDNAVF 636
Cdd:TIGR01058 556 ESVKKKL-KNY--TLQRYKGLGEMNADQLWETTMNPETRTLVRVKIDDLARAERQINTLMGDKVEPRKKWIEANINF 629
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
4-634 |
0e+00 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 536.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 4 DAGEYNADQIQVLEGLEAVRKRPGMYIGTTTAQGLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVD 83
Cdd:PTZ00109 96 RCSEYDADDIVVLEGLEAVRKRPGMYIGNTDEKGLHQLLFEILDNSVDEYLAGECNKITVVLHKDGSVEISDNGRGIPCD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 84 IQTKTGKPALETVFTILH----------------------------------------AGGKFGGGGYKVSGGLHGVGAS 123
Cdd:PTZ00109 176 VSEKTGKSGLETVLTVLHsggkfqdtfpknsrsdksedkndtksskkgksshvkgpkeAKEKESSQMYEYSSGLHGVGLS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 124 VVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLSEsaPI-ERGTIVHFKPD-PDIFQETT-------------VFNY 188
Cdd:PTZ00109 256 VVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSC--PLkKRGTTIHFLPDyKHIFKTHHqhteteeeegcknGFNL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 189 KTLLTRVRELAFLNKGLRISITDKRPEEPVS----ESFCYQGGIKEYVSYLDEGKETLFPEPVYV--EGEEKDIVVEVAL 262
Cdd:PTZ00109 334 DLIKNRIHELSYLNPGLTFYLVDERIANENNfypyETIKHEGGTREFLEELIKDKTPLYKDINIIsiRGVIKNVNVEVSL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 263 QYTTD-IKENLRTFTNNINTyEGGTHETGFKSALTRVINDYAHKSGQLKDGAESLTGEDVREGMTAIVSIKHPDPQFEGQ 341
Cdd:PTZ00109 414 SWSLEsYTALIKSFANNVST-TAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISVKLNGAEFDGQ 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 342 TKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAKRAREMTRKQSGLEIGN-LPGKLADNTSKD 420
Cdd:PTZ00109 493 TKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSTiLPGKLVDCISDD 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 421 PEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLD-RVLANEEIRSLFTAMG------------------ 481
Cdd:PTZ00109 573 IERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGlsvnpvtwrqydlshgtk 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 482 --------------SGFGNDFDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLY------- 540
Cdd:PTZ00109 653 askdesvqnnnstlTKKKNSLFDTPLRYGKIILLTDADVDGEHLRILLLTLLYRFCPSLYEHGRVYVACPPLYritnnrm 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 541 ---GVSLGNNKELHYIDSDEELEDYLAQLPSNAKPK-------------------------------------------- 573
Cdd:PTZ00109 733 kqfNVSTKNSKKYIYTWSDEELNVLIKLLNKDYSSKettrsveekgnapdldneyedekldnknmrennvdevelktelg 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 574 --------------------------VQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRR 627
Cdd:PTZ00109 813 tnvadteqtdeldinkaffkfskhyeIQRFKGLGEMMADQLWETTMDPKKRILIRITVSDAMRASELIFLLMGEDVQSRK 892
|
....*..
gi 2467955154 628 QFIEDNA 634
Cdd:PTZ00109 893 QFIFENS 899
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
8-632 |
1.32e-178 |
|
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: 521.02 E-value: 1.32e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 8 YNADQIQVLEGLEAVRKRPGMYIGTTTaqgLHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVDIQTK 87
Cdd:TIGR01055 4 YSAKDIEVLDGLEPVRKRPGMYTDTTR---PNHLVQEVIDNSVDEALAGFASIIMVILHQDQSIEVFDNGRGMPVDIHPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 88 TGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLSESAPIER 167
Cdd:TIGR01055 81 EGVSAVEVILTTLHAGGKFSNKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKRLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 168 GTIVHFKPDPDIFQETTvFNYKTLLTRVRELAFLNKGLRISITDKRpeEPVSESFCYQGGIKEYVSYLDEGKETLFPEPV 247
Cdd:TIGR01055 161 GTSVHFTPDPEIFDSLH-FSVSRLYHILRAKAVLCRGVEIEFEDEV--NNTKALWNYPDGLKDYLSEAVNGDNTLPPKPF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 248 YVEGEEKDIVVEVALQYTTDIKENL-RTFTNNINTYEGGTHETGFKSALTRVINDYAHKSGQLKDGAEsLTGEDVREGMT 326
Cdd:TIGR01055 238 SGNFEGDDEAVEWALLWLPEGGELFmESYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRNNLPRGVK-LTAEDIWDRCS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 327 AIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQKVRLSAkrAREMTRKQ--SGL 404
Cdd:TIGR01055 317 YVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRA--AKKVVRKKltSGP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 405 EignLPGKLADNTSKDPEISELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGF 484
Cdd:TIGR01055 395 A---LPGKLADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGIDP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 485 GNDfDVTKANYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQPPLYGVSLgnNKELHYIDSDEELEDYLA 564
Cdd:TIGR01055 472 DSN-DLSQLRYGKICILADADSDGLHIATLLCALFFLHFPKLVEEGHVYVAKPPLYRIDL--SKEVYYALDEEEKEKLLY 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2467955154 565 QLP-SNAKPKVQRYKGLGEMDYDQLADTTMDPAHRRLLRV--DPADAQEADAVIDMLMGGDVPP-RRQFIED 632
Cdd:TIGR01055 549 KLKkKKGKPNVQRFKGLGEMNPAQLRETTMDPNTRRLVQLtlDDVQDQRVDKIMDMLLAKKRSEdRFNWLQE 620
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
226-397 |
2.71e-84 |
|
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: 261.73 E-value: 2.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 226 GGIKEYVSYLDEGKETLFPEPVYVEGEEKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAHK 305
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 306 SGQLKDGAESLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILAQ 385
Cdd:cd00822 81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAILAA 160
|
170
....*....|..
gi 2467955154 386 KVRLSAKRAREM 397
Cdd:cd00822 161 KAREAARKAREL 172
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
38-219 |
1.76e-82 |
|
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: 257.47 E-value: 1.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 38 LHHLVWEIVDNGIDEALAGFASHISVTIEKDNSITVTDDGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGL 117
Cdd:cd16928 1 LHHLVWEIVDNSIDEALAGYATEIEVTLHEDNSITVEDNGRGIPVDIHPKTGKSAVEVVLTVLHAGGKFDGGSYKVSGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 118 HGVGASVVNALSTNLDVKVVREGKVYYMDFATGRVKTPMTVLSESApiERGTIVHFKPDPDIFqETTVFNYKTLLTRVRE 197
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETK--KTGTTVRFWPDPEIF-EKTEFDFDTLKRRLRE 157
|
170 180
....*....|....*....|..
gi 2467955154 198 LAFLNKGLRISITDKRPEEPVS 219
Cdd:cd16928 158 LAFLNKGLKIVLEDERTGKEEV 179
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
227-397 |
1.04e-78 |
|
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: 247.14 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 227 GIKEYVSYLDEGKETLFPEPVYVEGE--EKDIVVEVALQYTTDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYAH 304
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 305 KSGQLKDGAESLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPSVAKRIVEKGILA 384
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQA 160
|
170
....*....|...
gi 2467955154 385 QKVRLSAKRAREM 397
Cdd:pfam00204 161 AKARLAARKAREA 173
|
|
| TOPRIM_TopoIIA_GyrB |
cd03366 |
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
424-537 |
5.42e-74 |
|
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: 232.93 E-value: 5.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 424 SELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTKANYHKVIIMTD 503
Cdd:cd03366 1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKLRYHKIIIMTD 80
|
90 100 110
....*....|....*....|....*....|....
gi 2467955154 504 ADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQP 537
Cdd:cd03366 81 ADVDGAHIRTLLLTFFFRYMRPLIENGHVYIAQP 114
|
|
| TOPRIM_TopoIIA_like |
cd01030 |
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
424-537 |
4.37e-64 |
|
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: 206.59 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 424 SELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFG-NDFDVTKANYHKVIIMT 502
Cdd:cd01030 1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGkDDFDLDKLRYGKIIIMT 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2467955154 503 DADVDGAHIRTLLLTLFYRYMRPLVDAGYIYIAQP 537
Cdd:cd01030 81 DADVDGSHIRTLLLTFFYRFWPSLLENGFLYIAQT 115
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
11-630 |
7.62e-53 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 191.51 E-value: 7.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 11 DQIQVLEGLEAVRKRPGMYIGTTTAQ-----------------GLHHLVWEIVDNGIDEALAG---FASHISVTIeKDNS 70
Cdd:PHA02569 2 DEFKVLSDREHILKRPGMYIGSVAYEaherflfgkftqveyvpGLVKIIDEIIDNSVDEAIRTnfkFANKIDVTI-KNNQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 71 ITVTDDGRGIPVD-IQTKTGK--PALETVFTILHAGGKFGGGGYKVSGgLHGVGASVVNALStnldVKVVREgkvyymdf 147
Cdd:PHA02569 81 VTVSDNGRGIPQAmVTTPEGEeiPGPVAAWTRTKAGSNFDDTNRVTGG-MNGVGSSLTNFFS----VLFIGE-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 148 aTGRVKTPMTV----------LSESAPIERGTIVHFKPDPDIFQETTVFN--YKTLLTRVRELAFLNKGLRISITDKRpe 215
Cdd:PHA02569 148 -TCDGKNEVTVncsngaenisWSTKPGKGKGTSVTFIPDFSHFEVNGLDQqyLDIILDRLQTLAVVFPDIKFTFNGKK-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 216 epvsesfcYQGGIKEYVSYLDEgketlfpEPVYVEGEEkdivVEVALQYTTDIKENLrTFTNNINTYEGGTHETGfksal 295
Cdd:PHA02569 225 --------VSGKFKKYAKQFGD-------DTIVQENDN----VSIALAPSPDGFRQL-SFVNGLHTKNGGHHVDC----- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 296 trVIND-YAHKSGQLKDGAE-SLTGEDVREGMTAIVSIKH-PDPQFEGQTKTKLGNS--DARQATDRTFSEtFSRFMMEN 370
Cdd:PHA02569 280 --VMDDiCEELIPMIKKKHKiEVTKARVKECLTIVLFVRNmSNPRFDSQTKERLTSPfgEIRNHIDLDYKK-IAKQILKT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 371 PSVAKRIVEkGILAQKVrlsAKRAREMTRKQSGLE--------IGNLPGKLADNTskdpeiseLFIVEGDSAGGSAKQGR 442
Cdd:PHA02569 357 EAIIMPIIE-AALARKL---AAEKAAETKAAKKAKkakvakhiKANLIGKDAETT--------LFLTEGDSAIGYLIEVR 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 443 NRLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTkaNYHKVIIMTDADVDG-AHIRTLLLTLFYR 521
Cdd:PHA02569 425 DEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKAENM--NYKNIAIMTDADVDGkGSIYPLLLAFFSR 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 522 YMRpLVDAGYIYIAQPPLYGVSLGNNKELHYidsdeELEDYLAQLPSNAKPKVQRYKGLG---EMDYDQ-LADTTMDPAh 597
Cdd:PHA02569 503 WPE-LFEQGRIRFVKTPVIIAQVGKETKWFY-----SLDEFEKAKDSLKKWSIRYIKGLGslrKSEYRRvINNPVYDVV- 575
|
650 660 670
....*....|....*....|....*....|...
gi 2467955154 598 rrllrVDPADAQEadaVIDMLMGGDVPPRRQFI 630
Cdd:PHA02569 576 -----VLPDDWKE---LFEMLFGDDADLRKDWM 600
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
10-581 |
1.46e-42 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 165.60 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 10 ADQIQVLEGLEAVRKRPGMYIGTTTAQ-----------------------GLHHLVWEI----VDNGIDEALAGFASHIS 62
Cdd:PTZ00108 7 EERYQKKTQIEHILLRPDTYIGSIETQtedmwvydeeknrmvyktityvpGLYKIFDEIlvnaADNKARDKGGHRMTYIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 63 VTI-EKDNSITVTDDGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVV--RE 139
Cdd:PTZ00108 87 VTIdEENGEISVYNDGEGIPVQIHKEHKIYVPEMIFGHLLTSSNYDDTEKRVTGGRNGFGAKLTNIFSTKFTVECVdsKS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 140 GKVYYMDFATGRVKTPMTVLSESAPIERGTIVHFKPDPDIFQeTTVFN---YKTLLTRVRELAFLNKGLRISITDKRPEe 216
Cdd:PTZ00108 167 GKKFKMTWTDNMSKKSEPRITSYDGKKDYTKVTFYPDYAKFG-MTEFDddmLRLLKKRVYDLAGCFGKLKVYLNGERIA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 217 pvSESFcyqggiKEYVS--YLDEGKETLFPEPVyvEGEEKDIVVEVALQYTtDIKENLRTFTNNINTYEGGTHETGFKSA 294
Cdd:PTZ00108 245 --IKSF------KDYVDlyLPDGEEGKKPPYPF--VYTSVNGRWEVVVSLS-DGQFQQVSFVNSICTTKGGTHVNYILDQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 295 LTRVINDYAHKsgqLKDGAESLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPsva 374
Cdd:PTZ00108 314 LISKLQEKAKK---KKKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTKPSKFGSTCELSEKLIKYVLKSP--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 375 krIVEKGILAQKVRLSAKRAREMTRKQSGLEIGnLPgKLADNTSKDPEISE---LFIVEGDSA-----GGSAKQGRNRLt 446
Cdd:PTZ00108 388 --ILENIVEWAQAKLAAELNKKMKAGKKSRILG-IP-KLDDANDAGGKNSEectLILTEGDSAkalalAGLSVVGRDYY- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 447 qAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTKA-NYHKVIIMTDADVDGAHIRTLLLTLFYRYMRP 525
Cdd:PTZ00108 463 -GVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEDPKGlRYGSLMIMTDQDHDGSHIKGLLINMIHHFWPS 541
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2467955154 526 LVDA-GYIYIAQPPLYGVSLGNNKELHYIdsdeELEDYL--AQLPSNAKPKVQRYKGLG 581
Cdd:PTZ00108 542 LLKNpGFLKEFITPIVKATKKGNQVISFF----TIPDFEkwKQTVGLKGWKIKYYKGLG 596
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
19-581 |
7.05e-36 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 144.85 E-value: 7.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 19 LEAVRKRPGMYIGTTTAQGLHHLVWE---IVDNGI----------DEALAGFA---------SHISVTIEKD-NSITVTD 75
Cdd:PLN03128 13 LEHILLRPDTYIGSTEKHTQTLWVYEggeMVNREVtyvpglykifDEILVNAAdnkqrdpsmDSLKVDIDVEqNTISVYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 76 DGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVV--REGKVYYMDFATGRVK 153
Cdd:PLN03128 93 NGKGIPVEIHKEEGVYVPELIFGHLLTSSNFDDNEKKTTGGRNGYGAKLANIFSTEFTVETAdgNRGKKYKQVFTNNMSV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 154 TPMTVLSESAPIERGTIVHFKPDPDIFQETTVFN--YKTLLTRVRELA-FLNKGLRISITDKRPEepvSESFcyqggiKE 230
Cdd:PLN03128 173 KSEPKITSCKASENWTKITFKPDLAKFNMTRLDEdvVALMSKRVYDIAgCLGKKLKVELNGKKLP---VKSF------QD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 231 YVS-YLDEGKETLFPEPVYVEGEEK-DIVVEValqytTDIKENLRTFTNNINTYEGGTHetgfKSALTRVINDYAHKSGQ 308
Cdd:PLN03128 244 YVGlYLGPNSREDPLPRIYEKVNDRwEVCVSL-----SDGSFQQVSFVNSIATIKGGTH----VDYVADQIVKHIQEKVK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 309 LKD-GAESLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLgnsdarqatdrTFSET-F-SRFMMeNPSVAKRIVEKGILAQ 385
Cdd:PLN03128 315 KKNkNATHVKPFQIKNHLWVFVNCLIENPTFDSQTKETL-----------TTRPSsFgSKCEL-SEEFLKKVEKCGVVEN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 386 KVRLSAKRAREMTRKQSGLEIGNLPG--KLADNT---SKDPEISELFIVEGDSA-----GGSAKQGRNRLtqAILPIRGK 455
Cdd:PLN03128 383 ILSWAQFKQQKELKKKDGAKRQRLTGipKLDDANdagGKKSKDCTLILTEGDSAkalamSGLSVVGRDHY--GVFPLRGK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 456 ILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTKAN---YHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVD-AGY 531
Cdd:PLN03128 461 LLNVREASHKQIMKNAEITNIKQILGLQFGKTYDEENTKslrYGHLMIMTDQDHDGSHIKGLIINFFHSFWPSLLKiPGF 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2467955154 532 IYIAQPPLYGVSLGNNKELHYidSDEELEDYLAQLPSNAKP-KVQRYKGLG 581
Cdd:PLN03128 541 LVEFITPIVKATKGGKSLSFY--TMPEYEAWKESLEGETKGwTIKYYKGLG 589
|
|
| DNA_gyraseB_C |
pfam00986 |
DNA gyrase B subunit, carboxyl terminus; The amino terminus of eukaryotic and prokaryotic DNA ... |
569-631 |
1.06e-31 |
|
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: 117.09 E-value: 1.06e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2467955154 569 NAKPKVQRYKGLGEMDYDQLADTTMDPAHRRLLRVDPADAQEADAVIDMLMGGDVPPRRQFIE 631
Cdd:pfam00986 1 KKKVEIQRYKGLGEMNPEQLWETTMDPETRRLLQVTIEDAAEADEIFSTLMGDKVEPRREFIE 63
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
19-581 |
5.82e-23 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 104.56 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 19 LEAVRKRPGMYIGT---------------------TTAQGLHHLVWEIVDNGIDEALAGfASHISVTIEKD---NSITVT 74
Cdd:PLN03237 38 LEHILLRPDTYIGSiekhtqtlwvyetdkmvqrsvTYVPGLYKIFDEILVNAADNKQRD-PKMDSLRVVIDveqNLISVY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 75 DDGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVSGGLHGVGASVVNALSTNLDVKVV--REGKVYYMDFATGRV 152
Cdd:PLN03237 117 NNGDGVPVEIHQEEGVYVPEMIFGHLLTSSNYDDNEKKTTGGRNGYGAKLTNIFSTEFVIETAdgKRQKKYKQVFSNNMG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 153 KTPMTVLSESAPIERGTIVHFKPDPDIFQETTVFNYKTLLT--RVRELA-FLNKGLRISITDKRPeePVSesfcyqgGIK 229
Cdd:PLN03237 197 KKSEPVITKCKKSENWTKVTFKPDLAKFNMTHLEDDVVALMkkRVVDIAgCLGKTVKVELNGKRI--PVK-------SFS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 230 EYVSYLDEGKETLFPEPVYVEGEEKDIVVEVALQyTTDIKENLRTFTNNINTYEGGTHETGFKSALT----RVINDyAHK 305
Cdd:PLN03237 268 DYVDLYLESANKSRPENLPRIYEKVNDRWEVCVS-LSEGQFQQVSFVNSIATIKGGTHVDYVTNQIAnhvmEAVNK-KNK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 306 SGQLKdgaesltGEDVREGMTAIVSIKHPDPQFEGQTKTKLGNSDARQATDRTFSETFSRFMMENPsvakrIVEKgILAQ 385
Cdd:PLN03237 346 NANIK-------AHNVKNHLWVFVNALIDNPAFDSQTKETLTLRQSSFGSKCELSEDFLKKVMKSG-----IVEN-LLSW 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 386 KvrlSAKRAREMtRKQSGLEIGNLPG--KLADNTS---KDPEISELFIVEGDSA-----GGSAKQGRNRLtqAILPIRGK 455
Cdd:PLN03237 413 A---DFKQSKEL-KKTDGAKTTRVTGipKLEDANEaggKNSEKCTLILTEGDSAkalavAGLSVVGRNYY--GVFPLRGK 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 456 ILNVGKASLDRVLANEEIRSLFTAMGSGFGNDFDVTKA-NYHKVIIMTDADVDGAHIRTLLLTLFYRYMRPLVDA-GYIY 533
Cdd:PLN03237 487 LLNVREASHKQIMNNAEIENIKQILGLQHGKQYESVKSlRYGHLMIMTDQDHDGSHIKGLLINFIHSFWPSLLKVpSFLV 566
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2467955154 534 IAQPPLYGVSLGNNKELHYIdSDEELEDYLAQLPSNAKP-KVQRYKGLG 581
Cdd:PLN03237 567 EFITPIVKATRRGKKVLSFY-SMPEYEEWKESLGGNATGwSIKYYKGLG 614
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
228-347 |
4.31e-21 |
|
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: 88.47 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 228 IKEYVSYLDEGKETlfPEPVYVEGEEKDIVVEVALQYTTDI---KENLRTFTNNINTYEGGTHETGFKSALTRVINdyah 304
Cdd:cd00329 1 LKDRLAEILGDKVA--DKLIYVEGESDGFRVEGAISYPDSGrssKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2467955154 305 ksgqlkdgaesltGEDVREGMTAIVSIKHPD--PQFE-GQTKTKLG 347
Cdd:cd00329 75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEVR 107
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
426-522 |
1.90e-19 |
|
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.
Pssm-ID: 173785 [Multi-domain] Cd Length: 120 Bit Score: 84.27 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 426 LFIVEGDSAGGSAKQGRN---RLTQAILPIRGKILNVGKASLDRVLANEEIRSLFTAMGSGFGNDF--DVTKANYHKVII 500
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDyeSTKSLRYGRLMI 82
|
90 100
....*....|....*....|..
gi 2467955154 501 MTDADVDGAHIRTLLLTLFYRY 522
Cdd:cd03365 83 MTDQDHDGSHIKGLLINFIHSF 104
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
425-537 |
5.17e-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: 70.85 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 425 ELFIVEGDSAGGSAKQGRNRLTQAILPIRGKILNVGKASLDRVLaneeirslftamgsgfgNDFDVTKANYHKVIIMTDA 504
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKAL-----------------KALKELALKAKEVILATDP 63
|
90 100 110
....*....|....*....|....*....|...
gi 2467955154 505 DVDGAHIRTLLLTlFYRYMRPLVdaGYIYIAQP 537
Cdd:pfam01751 64 DREGEAIALKLLE-LKELLENAG--GRVEFSEL 93
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
37-179 |
1.40e-12 |
|
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: 64.31 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 37 GLHHLVWEIVDNGIDEAlaGFASHISVTIEKDN--SITVTDDGRGIPVDIQTKTGKPaletvFTilhaggkfggGGYKVS 114
Cdd:pfam02518 5 RLRQVLSNLLDNALKHA--AKAGEITVTLSEGGelTLTVEDNGIGIPPEDLPRIFEP-----FS----------TADKRG 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2467955154 115 GGLHGVGASVVNALSTNLDvkvvreGKVYYmdfatgrvktpmtvlsESAPiERGTIVHFKPDPDI 179
Cdd:pfam02518 68 GGGTGLGLSIVRKLVELLG------GTITV----------------ESEP-GGGTTVTLTLPLAQ 109
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
37-142 |
1.80e-11 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 61.13 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 37 GLHHLVWEIVDNGIDEALAGfaSHISVTIEKDN---SITVTDDGRGIPVDIQTKTGKPALETvftilhaggkfggGGYKV 113
Cdd:smart00387 5 RLRQVLSNLLDNAIKYTPEG--GRITVTLERDGdhvEITVEDNGPGIPPEDLEKIFEPFFRT-------------DKRSR 69
|
90 100
....*....|....*....|....*....
gi 2467955154 114 SGGLHGVGASVVNALSTNLDVKVVREGKV 142
Cdd:smart00387 70 KIGGTGLGLSIVKKLVELHGGEISVESEP 98
|
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| TOPRIM |
cd00188 |
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ... |
424-522 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 424 SELFIVEGDSAGGSAKQGRNRlTQAILPIRGKILNvgkasldrvlanEEIRSLFTAMGsgfgndfdvtkaNYHKVIIMTD 503
Cdd:cd00188 1 KKLIIVEGPSDALALAQAGGY-GGAVVALGGHALN------------KTRELLKRLLG------------EAKEVIIATD 55
|
90
....*....|....*....
gi 2467955154 504 ADVDGAHIRTLLLTLFYRY 522
Cdd:cd00188 56 ADREGEAIALRLLELLKSL 74
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| HATPase_TopII-like |
cd16930 |
Histidine kinase-like ATPase domain of eukaryotic topoisomerase II; This family includes the ... |
37-176 |
7.37e-05 |
|
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: 43.10 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 37 GLHHLVWEIVDNGID-EALAGFASHISVTIEKD-NSITVTDDGRGIPVDIQTKTGKPALETVFTILHAGGKFGGGGYKVS 114
Cdd:cd16930 4 GLYKIFDEILVNAADnKQRDKSMTCIKVTIDPEnNEISVWNNGKGIPVVIHKEEKIYVPEMIFGHLLTSSNYDDDEKKVT 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2467955154 115 GGLHGVGASVVNALSTNLDVKVV--REGKVYYMDFATGRVKTPMTVLSESAPIERGTIVHFKPD 176
Cdd:cd16930 84 GGRNGYGAKLCNIFSTEFTVETAdsESKKKFKQTWTNNMGKASEPKITPYEKGKDYTKVTFKPD 147
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| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
38-85 |
2.11e-04 |
|
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: 40.66 E-value: 2.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2467955154 38 LHHLVWEIVDNGIDEALAGfaSHISVTIEKDNS---ITVTDDGRGIPVDIQ 85
Cdd:cd00075 1 LEQVLSNLLDNALKYSPPG--GTIEISLRQEGDgvvLEVEDNGPGIPEEDL 49
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| TopoIIA_Trans_ScTopoIIA |
cd03481 |
TopoIIA_Trans_ScTopoIIA: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
226-385 |
8.02e-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: 40.35 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 226 GGIKEYVS-YL-DEGKETLFPEPVYVEgeEKDIVVEVALQYTtDIKENLRTFTNNINTYEGGTHETGFKSALTRVINDYA 303
Cdd:cd03481 1 KSFKDYVKlYLkDANKEDGPPPPVVYE--PVNDRWEVAVALS-DGQFQQVSFVNSIATTKGGTHVDYVADQIVKKLDEVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2467955154 304 HKSgqLKDGAEsLTGEDVREGMTAIVSIKHPDPQFEGQTKTKLgNSDARQ-ATDRTFSETFsrfmmenpsvAKRIVEKGI 382
Cdd:cd03481 78 KKK--NKGGIN-VKPFQVKNHLWIFVNCLIENPSFDSQTKETL-TTKPKSfGSKCELSEKF----------LKKAVKSGI 143
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...
gi 2467955154 383 LAQ 385
Cdd:cd03481 144 VES 146
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| MutL |
COG0323 |
DNA mismatch repair ATPase MutL [Replication, recombination and repair]; |
44-83 |
1.24e-03 |
|
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
Pssm-ID: 440092 [Multi-domain] Cd Length: 515 Bit Score: 41.95 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2467955154 44 EIVDNGIDealAGfASHISVTIEKD--NSITVTDDGRGIPVD 83
Cdd:COG0323 30 ELVENAID---AG-ATRIEVEIEEGgkSLIRVTDNGCGMSPE 67
|
|
| HATPase_MutL-MLH-PMS-like |
cd16926 |
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ... |
44-83 |
1.74e-03 |
|
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Pssm-ID: 340403 [Multi-domain] Cd Length: 188 Bit Score: 39.73 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2467955154 44 EIVDNGIDealAGfASHISVTIEKD--NSITVTDDGRGIPVD 83
Cdd:cd16926 20 ELVENSID---AG-ATRIDVEIEEGglKLIRVTDNGSGISRE 57
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| mutL |
PRK00095 |
DNA mismatch repair endonuclease MutL; |
44-83 |
2.46e-03 |
|
DNA mismatch repair endonuclease MutL;
Pssm-ID: 234630 [Multi-domain] Cd Length: 617 Bit Score: 40.97 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2467955154 44 EIVDNGIDealAGfASHISVTIEKD--NSITVTDDGRGIPVD 83
Cdd:PRK00095 29 ELVENALD---AG-ATRIDIEIEEGglKLIRVRDNGCGISKE 66
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