|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-372 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 799.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDGREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 161 DGGTHLVGFRTALTRTLNTYMDKEDYSKKAKMSAaSGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGE 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSL-TGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 241 KMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQG 320
Cdd:PRK14939 357 KLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQG 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 66474597 321 RNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPDK 372
Cdd:PRK14939 437 RDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDK 488
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-372 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 614.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDG--REINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKaKMSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKE-KDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:COG0187 355 SEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAK 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:COG0187 435 QGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIG-DDFDLEK 487
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-372 |
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: 605.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERD--GREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKmSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESK-PNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:TIGR01059 350 YEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAK 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDeYNPDK 372
Cdd:TIGR01059 430 QGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-372 |
1.81e-160 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 462.80 E-value: 1.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTY-KLGEPQAPLKQIGDATTTGTEVRFWPSPTIFS-DTLFHYETLAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFsNNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 79 SFLNSGVSIVLSDERDGREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKMsaaSGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI---KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:smart00433 319 SECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAK 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:smart00433 398 SGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEK 450
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
104-262 |
5.42e-82 |
|
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: 247.47 E-value: 5.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 104 GGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDK 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474597 184 EDYSKKAKMSaASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKMAEFLLENPSDAKIVVNKIID 262
Cdd:cd00822 81 NNLLKKKDVK-LTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
105-262 |
1.36e-67 |
|
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
Pssm-ID: 425522 [Multi-domain] Cd Length: 173 Bit Score: 210.93 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 105 GIKAFVEYLNQSKTPIHPKVFHFSTEH--DGIGVEVAMQWNDGYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGESpdNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 183 KEDYSKKAKMsAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKMAEFLLENPSDAKIVVNKIID 262
Cdd:pfam00204 81 KKGLLKKKDE-KITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-372 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 799.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDGREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 161 DGGTHLVGFRTALTRTLNTYMDKEDYSKKAKMSAaSGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGE 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSL-TGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 241 KMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQG 320
Cdd:PRK14939 357 KLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQG 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 66474597 321 RNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPDK 372
Cdd:PRK14939 437 RDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDK 488
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-372 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 614.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDG--REINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKaKMSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKE-KDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:COG0187 355 SEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAK 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:COG0187 435 QGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIG-DDFDLEK 487
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-372 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 607.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:PRK05644 118 HGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDTLATRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDGREI--NFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:PRK05644 198 LNKGLKITLTDEREGEEKeeTFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNIN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKMSAaSGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:PRK05644 278 THEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNL-TGEDVREGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:PRK05644 357 SEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAK 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:PRK05644 437 QGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIG-DDFDISK 489
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-372 |
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: 605.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERD--GREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKmSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESK-PNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:TIGR01059 350 YEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAK 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDeYNPDK 372
Cdd:TIGR01059 430 QGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-372 |
1.81e-160 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 462.80 E-value: 1.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTY-KLGEPQAPLKQIGDATTTGTEVRFWPSPTIFS-DTLFHYETLAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFsNNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 79 SFLNSGVSIVLSDERDGREINFCYEGGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 159 QRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKMsaaSGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI---KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 239 GEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:smart00433 319 SECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAK 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474597 319 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:smart00433 398 SGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEK 450
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-367 |
1.03e-157 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 456.87 E-value: 1.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATT--TGTEVRFWPSPTIFSDTLFHYETLAKRLREL 78
Cdd:PRK05559 118 HGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTAGKrkTGTRVRFWPDPKIFDSPKFSPERLKERLRSK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 79 SFLNSGVSIVLSDERDGREinFCYEGGIKAFVEYLNQSKTPIHP-KVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNI 157
Cdd:PRK05559 198 AFLLPGLTITLNDERERQT--FHYENGLKDYLAELNEGKETLPEeFVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 158 PQRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAKmsAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQA 237
Cdd:PRK05559 276 PTPQGGTHENGFREGLLKAVREFAEKRNLLPKGK--KLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 238 MGEKMAEFLLENPSDAKIVVNKIIDAARAREAARKARemTRRKGALDIAgLPGKLADCQEKDPALSELYIVEGDSAGGSA 317
Cdd:PRK05559 354 VKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKV--KRKKKTSGPA-LPGKLADCTSQDPERTELFLVEGDSAGGSA 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 66474597 318 KQGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDE 367
Cdd:PRK05559 431 KQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDSF 480
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
104-262 |
5.42e-82 |
|
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: 247.47 E-value: 5.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 104 GGIKAFVEYLNQSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDK 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474597 184 EDYSKKAKMSaASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKMAEFLLENPSDAKIVVNKIID 262
Cdd:cd00822 81 NNLLKKKDVK-LTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
1-366 |
1.91e-75 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 250.18 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATT-TGTEVRFWPS-PTIFSDTLFHYET-------- 70
Cdd:PTZ00109 250 HGVGLSVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCPLKkRGTTIHFLPDyKHIFKTHHQHTETeeeegckn 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 71 ------LAKRLRELSFLNSGVSIVLSDERDGREINFC------YEGGIKAFVEYLNQSKTPIHP--KVFHFSTEHDGIGV 136
Cdd:PTZ00109 330 gfnldlIKNRIHELSYLNPGLTFYLVDERIANENNFYpyetikHEGGTREFLEELIKDKTPLYKdiNIISIRGVIKNVNV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 137 EVAMQWNDG-YQEGVYCFTNNIpQRDGGTHLVGFRTALTRTLNTYMDKEDYSKkAKMSAASGDDVREGLIAVISVKVPDP 215
Cdd:PTZ00109 410 EVSLSWSLEsYTALIKSFANNV-STTAGTHIDGFKYAITRCVNGNIKKNGYFK-GNFVNIPGEFIREGMTAIISVKLNGA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 216 KFSSQTKDKLVSSEVKTAVEQAMGEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREMTRRKGALDIA-GLPGKLAD 294
Cdd:PTZ00109 488 EFDGQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYStILPGKLVD 567
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66474597 295 CQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMI-SSQEVGTLITALGCGIGRD 366
Cdd:PTZ00109 568 CISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNKKVfENSEIKLLITSIGLSVNPV 640
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
1-362 |
3.70e-75 |
|
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: 244.44 E-value: 3.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDAT--TTGTEVRFWPSPTIFSDTLFHYETLAKRLREL 78
Cdd:TIGR01055 111 HGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGkrLTGTSVHFTPDPEIFDSLHFSVSRLYHILRAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 79 SFLNSGVSIVLSDERDGREINFCYEGGIKAFV-EYLNQSKTPIhPKVFHFSTEHDGIGVEVAMQW-NDGYQEGVYCFTNN 156
Cdd:TIGR01055 191 AVLCRGVEIEFEDEVNNTKALWNYPDGLKDYLsEAVNGDNTLP-PKPFSGNFEGDDEAVEWALLWlPEGGELFMESYVNL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 157 IPQRDGGTHLVGFRTALTRTLNTYMD-KEDYSKKAKMSAasgDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVE 235
Cdd:TIGR01055 270 IPTPQGGTHVNGLRQGLLDALREFCEmRNNLPRGVKLTA---EDIWDRCSYVLSIKMQDPQFAGQTKERLSSRQVAKFVS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 236 QAMGEKMAEFLLENPSDAKIVVNKIIDAARAREAARKAREmtrRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGG 315
Cdd:TIGR01055 347 GVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKKVV---RKKLTSGPALPGKLADCTRQDLEGTELFLVEGDSAGG 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66474597 316 SAKQGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCG 362
Cdd:TIGR01055 424 SAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGID 470
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
105-262 |
1.36e-67 |
|
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
Pssm-ID: 425522 [Multi-domain] Cd Length: 173 Bit Score: 210.93 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 105 GIKAFVEYLNQSKTPIHPKVFHFSTEH--DGIGVEVAMQWNDGYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGESpdNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 183 KEDYSKKAKMsAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKMAEFLLENPSDAKIVVNKIID 262
Cdd:pfam00204 81 KKGLLKKKDE-KITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
1-100 |
3.29e-47 |
|
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: 158.47 E-value: 3.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIRRQGHVYEQTYKLGEPQAPLKQIGDATTTGTEVRFWPSPTIFSDTLFHYETLAKRLRELSF 80
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIFEKTEFDFDTLKRRLRELAF 160
|
90 100
....*....|....*....|
gi 66474597 81 LNSGVSIVLSDERDGREINF 100
Cdd:cd16928 161 LNKGLKIVLEDERTGKEEVF 180
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
106-225 |
1.54e-22 |
|
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: 91.17 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 106 IKAFVEYLNQSKTpiHPKVFHFSTEHDGIGVEVAMQWND---GYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNtymd 182
Cdd:cd00329 1 LKDRLAEILGDKV--ADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66474597 183 kedyskkakmsaasGDDVREGLIAVISVKVPD--PKFS-SQTKDKL 225
Cdd:cd00329 75 --------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1-371 |
6.88e-18 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 85.48 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 1 HGVGVSVVNALSDTLKLTIR--RQGHVYEQTYK--LGEPQAP-LKQIGDATTTgTEVRFWPSPTIFSDTLF---HYETLA 72
Cdd:PTZ00108 143 NGFGAKLTNIFSTKFTVECVdsKSGKKFKMTWTdnMSKKSEPrITSYDGKKDY-TKVTFYPDYAKFGMTEFdddMLRLLK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 73 KRLRELSFLNSGVSIVLSDERdgreInfcyegGIKAFVEYLN---QSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEG 149
Cdd:PTZ00108 222 KRVYDLAGCFGKLKVYLNGER----I------AIKSFKDYVDlylPDGEEGKKPPYPFVYTSVNGRWEVVVSLSDGQFQQ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 150 VyCFTNNIPQRDGGTHLvgfrTALTRTLNTYMDKEDYSKKAKMSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSE 229
Cdd:PTZ00108 292 V-SFVNSICTTKGGTHV----NYILDQLISKLQEKAKKKKKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTKP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 230 VKTAVEQAMGEKMAEFLLENPsdakiVVNKIIDAARAREAARKAREM--TRRKGaldIAGLPgKLADCQEKDPALSE--- 304
Cdd:PTZ00108 367 SKFGSTCELSEKLIKYVLKSP-----ILENIVEWAQAKLAAELNKKMkaGKKSR---ILGIP-KLDDANDAGGKNSEect 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 305 LYIVEGDSAGGSAKQG---RNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPD 371
Cdd:PTZ00108 438 LILTEGDSAKALALAGlsvVGRDYYGVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEDPK 507
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
153-370 |
1.06e-11 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 66.32 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 153 FTNNIPQRDGGTHLVGFRTALTRTLNTyMDKEDYskKAKMSAASgddVREGLIAVISVK-VPDPKFSSQTKDKLVSS--E 229
Cdd:PHA02569 264 FVNGLHTKNGGHHVDCVMDDICEELIP-MIKKKH--KIEVTKAR---VKECLTIVLFVRnMSNPRFDSQTKERLTSPfgE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 230 VKTAVeQAMGEKMAEFLLENPSdakiVVNKIIDAARAREAARKAREMTR-RKGALDI-------AGLPGKLADcqekdpa 301
Cdd:PHA02569 338 IRNHI-DLDYKKIAKQILKTEA----IIMPIIEAALARKLAAEKAAETKaAKKAKKAkvakhikANLIGKDAE------- 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474597 302 lSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNP 370
Cdd:PHA02569 406 -TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKAENM 473
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
44-371 |
2.18e-11 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 65.50 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 44 DATTTGTEVRFWPSPTIFSDTLFHYET---LAKRLRELS-FLNSGVSIVLSDERDGreinfcyeggIKAFVEYLN----- 114
Cdd:PLN03128 182 KASENWTKITFKPDLAKFNMTRLDEDVvalMSKRVYDIAgCLGKKLKVELNGKKLP----------VKSFQDYVGlylgp 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 115 QSKTPIHPKVFHFSTEhdgiGVEVAMQWNDGYQEGVyCFTNNIPQRDGGTHLvgfrTALTRTLNTYMdKEDYSKKAKMSA 194
Cdd:PLN03128 252 NSREDPLPRIYEKVND----RWEVCVSLSDGSFQQV-SFVNSIATIKGGTHV----DYVADQIVKHI-QEKVKKKNKNAT 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 195 A-SGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEqamGEKMAEFL--LENPSdakiVVNKIIDAARAREAAR 271
Cdd:PLN03128 322 HvKPFQIKNHLWVFVNCLIENPTFDSQTKETLTTRPSSFGSK---CELSEEFLkkVEKCG----VVENILSWAQFKQQKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 272 KAREMTRRKGALdiAGLPgKLADCQEKDPALSE---LYIVEGDSAGGSAKQGR---NRKNQAILPLKGKILNVEKARFDK 345
Cdd:PLN03128 395 LKKKDGAKRQRL--TGIP-KLDDANDAGGKKSKdctLILTEGDSAKALAMSGLsvvGRDHYGVFPLRGKLLNVREASHKQ 471
|
330 340
....*....|....*....|....*.
gi 66474597 346 MISSQEVGTLITALGCGIGRdEYNPD 371
Cdd:PLN03128 472 IMKNAEITNIKQILGLQFGK-TYDEE 496
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
305-369 |
1.80e-09 |
|
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: 55.00 E-value: 1.80e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474597 305 LYIVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYN 369
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYE 70
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
106-360 |
1.03e-07 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 54.10 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 106 IKAFVEYLN---QSKTPIHPKVFHFSTEHDGIGVEVAMQWNDGYQEGVyCFTNNIPQRDGGTHLvgfrTALTRTLNTYMd 182
Cdd:PLN03237 263 VKSFSDYVDlylESANKSRPENLPRIYEKVNDRWEVCVSLSEGQFQQV-SFVNSIATIKGGTHV----DYVTNQIANHV- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 183 KEDYSKKAKMSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLvssevkTAVEQAMGEKmaeFLLENPSDAKIVVNKIID 262
Cdd:PLN03237 337 MEAVNKKNKNANIKAHNVKNHLWVFVNALIDNPAFDSQTKETL------TLRQSSFGSK---CELSEDFLKKVMKSGIVE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474597 263 AARAREAARKAREMTRRKGA--LDIAGLPgKLADCQE---KDPALSELYIVEGDSAGGSAKQGRN---RKNQAILPLKGK 334
Cdd:PLN03237 408 NLLSWADFKQSKELKKTDGAktTRVTGIP-KLEDANEaggKNSEKCTLILTEGDSAKALAVAGLSvvgRNYYGVFPLRGK 486
|
250 260
....*....|....*....|....*.
gi 66474597 335 ILNVEKARFDKMISSQEVGTLITALG 360
Cdd:PLN03237 487 LLNVREASHKQIMNNAEIENIKQILG 512
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
304-348 |
5.07e-07 |
|
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: 47.35 E-value: 5.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66474597 304 ELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMIS 348
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALK 45
|
|
|