|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-389 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 818.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDV 80
Cdd:PRK14939 108 QNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 81 LAKRLRELSFLNSGVRIVLKDERSGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQESI 160
Cdd:PRK14939 188 LAKRLRELAFLNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 161 FCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVK 240
Cdd:PRK14939 268 LCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 241 PAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVEGD 320
Cdd:PRK14939 348 PAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGD 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 321 SAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSEFNPDKLRYHSIII 389
Cdd:PRK14939 428 SAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDKLRYHKIII 496
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
2-389 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 635.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 2 NTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDVL 81
Cdd:COG0187 107 GSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 82 AKRLRELSFLNSGVRIVLKDERSG--KEEVYEYEGGLSAFVAFLNQNKTPINK-VLHFHSQReDGIAVEVALQWNDSFQE 158
Cdd:COG0187 187 AERLRELAFLNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPeVIYFEGEK-DGIEVEVALQWNDGYSE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:COG0187 266 NIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:COG0187 346 ARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVE 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:COG0187 426 GDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGD-DFDLEKLRYHKIII 495
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-389 |
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: 623.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDV 80
Cdd:TIGR01059 101 KDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 81 LAKRLRELSFLNSGVRIVLKDER--SGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQE 158
Cdd:TIGR01059 181 LAKRLRELAFLNSGVKISLEDERdgKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:TIGR01059 261 NILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:TIGR01059 341 VRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:TIGR01059 421 GDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGK-DFDLEKLRYHKIII 490
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-389 |
3.63e-171 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 490.53 E-value: 3.63e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQ-GVPQAPLGVVGESDSTGTTVHFKPSANTFSNI-EFHF 78
Cdd:smart00433 72 DDAYKVSGGLHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTtDDDF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 79 DVLAKRLRELSFLNSGVRIVLKDERSGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQE 158
Cdd:smart00433 152 ELLKRRLRELAFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVntTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:smart00433 232 NIVSFVNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI--KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKgALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:smart00433 310 VRFGVEKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVE 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:smart00433 389 GDSAGGSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGK-DFDIEKLRYGKIII 458
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
114-271 |
7.66e-75 |
|
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: 229.75 E-value: 7.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 114 GGLSAFVAFLNQNKTPIN-KVLHFhSQREDGIAVEVALQWNDSFQESIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIE 192
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHeEPIYI-EGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 193 REGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMID 271
Cdd:cd00822 80 KNNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
115-271 |
6.21e-64 |
|
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: 202.08 E-value: 6.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 115 GLSAFVAFLNQNKTPINK-VLHF-HSQREDGIAVEVALQWNDSFQESIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIE 192
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKeIIYFeGESPDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 193 REGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMID 271
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-389 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 818.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDV 80
Cdd:PRK14939 108 QNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 81 LAKRLRELSFLNSGVRIVLKDERSGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQESI 160
Cdd:PRK14939 188 LAKRLRELAFLNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 161 FCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVK 240
Cdd:PRK14939 268 LCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 241 PAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVEGD 320
Cdd:PRK14939 348 PAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGD 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 321 SAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSEFNPDKLRYHSIII 389
Cdd:PRK14939 428 SAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDKLRYHKIII 496
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
2-389 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 635.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 2 NTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDVL 81
Cdd:COG0187 107 GSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 82 AKRLRELSFLNSGVRIVLKDERSG--KEEVYEYEGGLSAFVAFLNQNKTPINK-VLHFHSQReDGIAVEVALQWNDSFQE 158
Cdd:COG0187 187 AERLRELAFLNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPeVIYFEGEK-DGIEVEVALQWNDGYSE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:COG0187 266 NIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:COG0187 346 ARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVE 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:COG0187 426 GDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGD-DFDLEKLRYHKIII 495
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
2-389 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 630.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 2 NTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDVL 81
Cdd:PRK05644 109 GGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDTL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 82 AKRLRELSFLNSGVRIVLKDERSG--KEEVYEYEGGLSAFVAFLNQNKTPIN-KVLHFHSQReDGIAVEVALQWNDSFQE 158
Cdd:PRK05644 189 ATRLRELAFLNKGLKITLTDEREGeeKEETFHYEGGIKEYVEYLNRNKEPLHeEPIYFEGEK-DGIEVEVAMQYNDGYSE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:PRK05644 268 NILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHPEPQFEGQTKTKLGNSE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:PRK05644 348 VRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEESELYIVE 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:PRK05644 428 GDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGD-DFDISKLRYHKIII 497
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-389 |
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: 623.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDV 80
Cdd:TIGR01059 101 KDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 81 LAKRLRELSFLNSGVRIVLKDER--SGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQE 158
Cdd:TIGR01059 181 LAKRLRELAFLNSGVKISLEDERdgKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:TIGR01059 261 NILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:TIGR01059 341 VRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:TIGR01059 421 GDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGK-DFDLEKLRYHKIII 490
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-389 |
3.63e-171 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 490.53 E-value: 3.63e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQ-GVPQAPLGVVGESDSTGTTVHFKPSANTFSNI-EFHF 78
Cdd:smart00433 72 DDAYKVSGGLHGVGASVVNALSTEFEVEVARDGKEYKQSFSNnGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGMTtDDDF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 79 DVLAKRLRELSFLNSGVRIVLKDERSGKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQREDGIAVEVALQWNDSFQE 158
Cdd:smart00433 152 ELLKRRLRELAFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 159 SIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVntTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSE 238
Cdd:smart00433 232 NIVSFVNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI--KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 239 VKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKgALDIAGLPGKLADCQQKDPALSEIYLVE 318
Cdd:smart00433 310 VRFGVEKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVE 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83017277 319 GDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:smart00433 389 GDSAGGSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGK-DFDIEKLRYGKIII 458
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
4-389 |
3.23e-163 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 471.89 E-value: 3.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 4 YKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDS--TGTTVHFKPSANTFSNIEFHFDVL 81
Cdd:PRK05559 111 YKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTAGKrkTGTRVRFWPDPKIFDSPKFSPERL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 82 AKRLRELSFLNSGVRIVLKDERsgKEEVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQRE-DGIAVEVALQWNDSFQESI 160
Cdd:PRK05559 191 KERLRSKAFLLPGLTITLNDER--ERQTFHYENGLKDYLAELNEGKETLPEEFVGSFEGEaEGEAVEWALQWTDEGGENI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 161 FCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKvNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVK 240
Cdd:PRK05559 269 ESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLPKGK-KLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREAR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 241 PAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKARemTRRKGALDIAgLPGKLADCQQKDPALSEIYLVEGD 320
Cdd:PRK05559 348 RFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKV--KRKKKTSGPA-LPGKLADCTSQDPERTELFLVEGD 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 321 SAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSeFNPDKLRYHSIII 389
Cdd:PRK05559 425 SAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDS-FDLEDLRYGKIII 492
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
1-389 |
1.84e-83 |
|
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: 266.78 E-value: 1.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESD--STGTTVHFKPSANTFSNIEFHF 78
Cdd:TIGR01055 101 NKNYHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGkrLTGTSVHFTPDPEIFDSLHFSV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 79 DVLAKRLRELSFLNSGVRIVLKDERSGKEEVYEYEGGLSAFVA-FLNQNKTPINKVL--HFHSqreDGIAVEVALQW--- 152
Cdd:TIGR01055 181 SRLYHILRAKAVLCRGVEIEFEDEVNNTKALWNYPDGLKDYLSeAVNGDNTLPPKPFsgNFEG---DDEAVEWALLWlpe 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 153 -NDSFQESifcYTNNIPQRDGGTHLAGFRAALTRGLNSYIEREGLgKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTK 231
Cdd:TIGR01055 258 gGELFMES---YVNLIPTPQGGTHVNGLRQGLLDALREFCEMRNN-LPRGVKLTAEDIWDRCSYVLSIKMQDPQFAGQTK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 232 DKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREmtrRKGALDIAGLPGKLADCQQKDPAL 311
Cdd:TIGR01055 334 ERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKKVV---RKKLTSGPALPGKLADCTRQDLEG 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83017277 312 SEIYLVEGDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSEFnpDKLRYHSIII 389
Cdd:TIGR01055 411 TELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGIDPDSNDL--SQLRYGKICI 486
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
2-374 |
1.36e-82 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 270.21 E-value: 1.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 2 NTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDS-TGTTVHFKPSA-NTFSN------ 73
Cdd:PTZ00109 241 QMYEYSSGLHGVGLSVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCPLKkRGTTIHFLPDYkHIFKThhqhte 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 74 --------IEFHFDVLAKRLRELSFLNSGVRIVLKDERSGKE------EVYEYEGGLSAFVAFLNQNKTPINKVLHFHSQ 139
Cdd:PTZ00109 321 teeeegckNGFNLDLIKNRIHELSYLNPGLTFYLVDERIANEnnfypyETIKHEGGTREFLEELIKDKTPLYKDINIISI 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 140 R--EDGIAVEVALQWN-DSFQESIFCYTNNIpQRDGGTHLAGFRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAI 216
Cdd:PTZ00109 401 RgvIKNVNVEVSLSWSlESYTALIKSFANNV-STTAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAI 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 217 ISVKVPDPKFSSQTKDKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGALDIA- 295
Cdd:PTZ00109 480 ISVKLNGAEFDGQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYSt 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 296 GLPGKLADCQQKDPALSEIYLVEGDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFD-KMLSSAEVGTLITALGCGIGK 374
Cdd:PTZ00109 560 ILPGKLVDCISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNP 639
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
114-271 |
7.66e-75 |
|
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: 229.75 E-value: 7.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 114 GGLSAFVAFLNQNKTPIN-KVLHFhSQREDGIAVEVALQWNDSFQESIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIE 192
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHeEPIYI-EGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 193 REGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMID 271
Cdd:cd00822 80 KNNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
115-271 |
6.21e-64 |
|
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: 202.08 E-value: 6.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 115 GLSAFVAFLNQNKTPINK-VLHF-HSQREDGIAVEVALQWNDSFQESIFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIE 192
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKeIIYFeGESPDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83017277 193 REGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKPAVEQEMGQHFNDYLLENPQEAKSVVTKMID 271
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
1-110 |
2.20e-53 |
|
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: 175.03 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIRRAGRIYEQTYHQGVPQAPLGVVGESDSTGTTVHFKPSANTFSNIEFHFDV 80
Cdd:cd16928 71 GGSYKVSGGLHGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIFEKTEFDFDT 150
|
90 100 110
....*....|....*....|....*....|
gi 83017277 81 LAKRLRELSFLNSGVRIVLKDERSGKEEVY 110
Cdd:cd16928 151 LKRRLRELAFLNKGLKIVLEDERTGKEEVF 180
|
|
| TOPRIM_TopoIIA_GyrB |
cd03366 |
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ... |
312-389 |
2.18e-48 |
|
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: 159.74 E-value: 2.18e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83017277 312 SEIYLVEGDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKsEFNPDKLRYHSIII 389
Cdd:cd03366 1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGE-DFDLEKLRYHKIII 77
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1-389 |
9.02e-26 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 109.75 E-value: 9.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIR--RAGRIYEQTYHQGVPQAPLGVVGESDSTG--TTVHFKPSANTFSNIEF 76
Cdd:PTZ00108 133 DTEKRVTGGRNGFGAKLTNIFSTKFTVECVdsKSGKKFKMTWTDNMSKKSEPRITSYDGKKdyTKVTFYPDYAKFGMTEF 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 77 ---HFDVLAKRLRELSFLNSGVRIVLKDERSGKEEVYEY-----EGGLSAFVAFLNQNKTPINKvlhfhsqredgiAVEV 148
Cdd:PTZ00108 213 dddMLRLLKKRVYDLAGCFGKLKVYLNGERIAIKSFKDYvdlylPDGEEGKKPPYPFVYTSVNG------------RWEV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 149 ALQWNDS-FQesIFCYTNNIPQRDGGTHLagfRAALTRGLNSYIEREGLGKKDKVNTTGDDAREGLTAIISVKVPDPKFS 227
Cdd:PTZ00108 281 VVSLSDGqFQ--QVSFVNSICTTKGGTHV---NYILDQLISKLQEKAKKKKKKGKEIKPNQIKNHLWVFVNCLIVNPSFD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 228 SQTKDKLVSSEVKPAVEQEMGQHFNDYLLENP-----------QEAKSVVTKMidaakareaarkarEMTRRKGaldIAG 296
Cdd:PTZ00108 356 SQTKETLTTKPSKFGSTCELSEKLIKYVLKSPilenivewaqaKLAAELNKKM--------------KAGKKSR---ILG 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 297 LPgKLADCQQKDPALSEI---YLVEGDSAGGSAKQG---RDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGC 370
Cdd:PTZ00108 419 IP-KLDDANDAGGKNSEEctlILTEGDSAKALALAGlsvVGRDYYGVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGL 497
|
410
....*....|....*....
gi 83017277 371 GIGKSEFNPDKLRYHSIII 389
Cdd:PTZ00108 498 DIGKKYEDPKGLRYGSLMI 516
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
1-389 |
2.90e-18 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 87.07 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTIR--RAGRIYEQTYHQGVPQA--PLGVVGESDSTGTTVHFKPSANTFSNIEF 76
Cdd:PLN03128 125 DNEKKTTGGRNGYGAKLANIFSTEFTVETAdgNRGKKYKQVFTNNMSVKsePKITSCKASENWTKITFKPDLAKFNMTRL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 77 HFDV---LAKRLRELS-FLNSGVRIVLKDERSGKEEVYEYEGglsafvAFLNQNKTPINKVLHFHsQREDGIAVEVALQw 152
Cdd:PLN03128 205 DEDVvalMSKRVYDIAgCLGKKLKVELNGKKLPVKSFQDYVG------LYLGPNSREDPLPRIYE-KVNDRWEVCVSLS- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 153 NDSFQESIFCytNNIPQRDGGTHLAgfraALTRGLNSYIErEGLGKKDK--VNTTGDDAREGLTAIISVKVPDPKFSSQT 230
Cdd:PLN03128 277 DGSFQQVSFV--NSIATIKGGTHVD----YVADQIVKHIQ-EKVKKKNKnaTHVKPFQIKNHLWVFVNCLIENPTFDSQT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 231 KDKLVSSEVKpaveqeMGQHFNdylLENPQEAKSVVTKMIDAAKAREAARKAREMTRRKGA--LDIAGLPgKLADCQQKD 308
Cdd:PLN03128 350 KETLTTRPSS------FGSKCE---LSEEFLKKVEKCGVVENILSWAQFKQQKELKKKDGAkrQRLTGIP-KLDDANDAG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 309 PALSE---IYLVEGDSA-----GGSAKQGRDRrtQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKS--EFN 378
Cdd:PLN03128 420 GKKSKdctLILTEGDSAkalamSGLSVVGRDH--YGVFPLRGKLLNVREASHKQIMKNAEITNIKQILGLQFGKTydEEN 497
|
410
....*....|.
gi 83017277 379 PDKLRYHSIII 389
Cdd:PLN03128 498 TKSLRYGHLMI 508
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
116-234 |
3.49e-18 |
|
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: 79.23 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 116 LSAFVAFLNQNKTPiNKVLHFhSQREDGIAVEVALQWND---SFQESIFCYTNNIPQRDGGTHLAGFRAALTRGLNsyie 192
Cdd:cd00329 1 LKDRLAEILGDKVA-DKLIYV-EGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 83017277 193 reglgkkdkvnttGDDAREGLTAIISVKVPD--PKFS-SQTKDKL 234
Cdd:cd00329 75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
1-389 |
9.95e-17 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 81.72 E-value: 9.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSE---------ELKLTIRRAGRIYEQTYHQGvpqaplgvvgESDSTGTTVHFKPSANTF 71
Cdd:PHA02569 120 DDTNRVTGGMNGVGSSLTNFFSVlfigetcdgKNEVTVNCSNGAENISWSTK----------PGKGKGTSVTFIPDFSHF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 72 SNIEF---HFDVLAKRLRELSFLNSGVRIVLKDER-SGKEEVYEYEGGLSAFVaflnqnktpinkvlhfhsQREDGIAVE 147
Cdd:PHA02569 190 EVNGLdqqYLDIILDRLQTLAVVFPDIKFTFNGKKvSGKFKKYAKQFGDDTIV------------------QENDNVSIA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 148 VALQwNDSFQEsiFCYTNNIPQRDGGTHLAGFRAALTRGLNSYIEReglgkKDKVNTTGDDAREGLTAIISVK-VPDPKF 226
Cdd:PHA02569 252 LAPS-PDGFRQ--LSFVNGLHTKNGGHHVDCVMDDICEELIPMIKK-----KHKIEVTKARVKECLTIVLFVRnMSNPRF 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 227 SSQTKDKLVSS--EVKPaveqemgqHFN-DY------LLENPqeakSVVTKMIDAAKAREAARKAREMTR-RKGALDI-- 294
Cdd:PHA02569 324 DSQTKERLTSPfgEIRN--------HIDlDYkkiakqILKTE----AIIMPIIEAALARKLAAEKAAETKaAKKAKKAkv 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 295 -----AGLPGKLADcqqkdpalSEIYLVEGDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALG 369
Cdd:PHA02569 392 akhikANLIGKDAE--------TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITG 463
|
410 420
....*....|....*....|
gi 83017277 370 CGIGKSEFNPdklRYHSIII 389
Cdd:PHA02569 464 LVLGEKAENM---NYKNIAI 480
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
316-389 |
4.49e-12 |
|
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: 62.70 E-value: 4.49e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83017277 316 LVEGDSAGGSAKQGR---DRRTQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSEF-NPDKLRYHSIII 389
Cdd:cd03365 5 LTEGDSAKALAVAGLsvvGRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYeSTKSLRYGRLMI 82
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
1-389 |
2.13e-10 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 62.57 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 1 DNTYKVSGGLHGVGVSVVNALSEELKLTI---RRAGRiYEQTYHQGVPQAPLGVVGESDSTG--TTVHFKPSANTFSNIE 75
Cdd:PLN03237 150 DNEKKTTGGRNGYGAKLTNIFSTEFVIETadgKRQKK-YKQVFSNNMGKKSEPVITKCKKSEnwTKVTFKPDLAKFNMTH 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 76 FHFDVLA---KRLRELS-FLNSGVRIVLKDER----SGKEEVYEYEGGlsafvaflnQNKTPINKVLHFHSQREDGIAVE 147
Cdd:PLN03237 229 LEDDVVAlmkKRVVDIAgCLGKTVKVELNGKRipvkSFSDYVDLYLES---------ANKSRPENLPRIYEKVNDRWEVC 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 148 VALQwNDSFQESIFcyTNNIPQRDGGTHLAgfraALTRGLNSYIeREGLGKKDK-VNTTGDDAREGLTAIISVKVPDPKF 226
Cdd:PLN03237 300 VSLS-EGQFQQVSF--VNSIATIKGGTHVD----YVTNQIANHV-MEAVNKKNKnANIKAHNVKNHLWVFVNALIDNPAF 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 227 SSQTKDKLVSSEVKPAVEQEMGQHFNDyllenpQEAKSVVtkmIDAAKAREAARKAREMTRRKGA--LDIAGLPgKLADC 304
Cdd:PLN03237 372 DSQTKETLTLRQSSFGSKCELSEDFLK------KVMKSGI---VENLLSWADFKQSKELKKTDGAktTRVTGIP-KLEDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83017277 305 QQ---KDPALSEIYLVEGDSA-----GGSAKQGRDRrtQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGKSE 376
Cdd:PLN03237 442 NEaggKNSEKCTLILTEGDSAkalavAGLSVVGRNY--YGVFPLRGKLLNVREASHKQIMNNAEIENIKQILGLQHGKQY 519
|
410
....*....|...
gi 83017277 377 FNPDKLRYHSIII 389
Cdd:PLN03237 520 ESVKSLRYGHLMI 532
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
313-389 |
1.99e-06 |
|
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: 45.81 E-value: 1.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83017277 313 EIYLVEGDSAGGSAKQGRDRRTQAILPLKGKILNVEKARFDKMLssaevgtlitalgcgigkSEFNPDKLRYHSIII 389
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKAL------------------KALKELALKAKEVIL 59
|
|
| |
