|
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 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDGREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 161 DGGTHLVGFRTALTRTLNTYMDREDYSKKAKISAaSGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGE 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSL-TGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 241 KLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQG 320
Cdd:PRK14939 357 KLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQG 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 66474593 321 RNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDEYNPDK 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: 607.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDG--REVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKaKISAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKE-KDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:COG0187 355 SEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAK 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGrDEYNPDK 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: 601.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERD--GREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKiSAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESK-PNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:TIGR01059 350 YEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAK 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDeYNPDK 372
Cdd:TIGR01059 430 QGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-372 |
1.20e-156 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 453.17 E-value: 1.20e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYH-MGEPQAPLKQIGDSNGTGTEVRFWPSATIF-TDTLYHYDILAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFgMTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 79 SFLNSGVSIRLEDERDGREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKIsaaSGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI---KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:smart00433 319 SECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAK 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGrDEYNPDK 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 |
1.21e-78 |
|
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: 239.00 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 104 GGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDR 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474593 184 EDYSKKAKISaASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 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 |
1.29e-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: 203.23 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 105 GIKAFVEYLNQNKTPIHQNVFHFSTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 183 REDYSKKAKIsAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 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 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDGREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 161 DGGTHLVGFRTALTRTLNTYMDREDYSKKAKISAaSGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGE 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSL-TGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 241 KLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQG 320
Cdd:PRK14939 357 KLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQG 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 66474593 321 RNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDEYNPDK 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: 607.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDG--REVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKaKISAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKE-KDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:COG0187 355 SEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAK 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGrDEYNPDK 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: 601.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERD--GREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKiSAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESK-PNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:TIGR01059 350 YEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAK 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDeYNPDK 372
Cdd:TIGR01059 430 QGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| 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: 598.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:PRK05644 118 HGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDTLATRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDG--REVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:PRK05644 198 LNKGLKITLTDEREGeeKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNIN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKISAaSGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:PRK05644 278 THEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNL-TGEDVREGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:PRK05644 357 SEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAK 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:PRK05644 437 QGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIG-DDFDISK 489
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-372 |
1.20e-156 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 453.17 E-value: 1.20e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYH-MGEPQAPLKQIGDSNGTGTEVRFWPSATIF-TDTLYHYDILAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFgMTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 79 SFLNSGVSIRLEDERDGREVHFCYEGGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 159 QRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKIsaaSGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKKKKKLKEKNI---KGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 239 GEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAK 318
Cdd:smart00433 319 SECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAK 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66474593 319 QGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGrDEYNPDK 372
Cdd:smart00433 398 SGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEK 450
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-367 |
5.56e-152 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 442.23 E-value: 5.56e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGD--SNGTGTEVRFWPSATIFTDTLYHYDILAKRLREL 78
Cdd:PRK05559 118 HGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTagKRKTGTRVRFWPDPKIFDSPKFSPERLKERLRSK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 79 SFLNSGVSIRLEDERDGREvhFCYEGGIKAFVEYLNQNKTPIH-QNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNI 157
Cdd:PRK05559 198 AFLLPGLTITLNDERERQT--FHYENGLKDYLAELNEGKETLPeEFVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 158 PQRDGGTHLVGFRTALTRTLNTYMDREDYSKKAKisAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQA 237
Cdd:PRK05559 276 PTPQGGTHENGFREGLLKAVREFAEKRNLLPKGK--KLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 238 MGEKLGEFLLENPGDAKIVVNKIIDAARAREAARKARemTRRKGALDIAgLPGKLADCQEKDPALSELYIVEGDSAGGSA 317
Cdd:PRK05559 354 VKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKV--KRKKKTSGPA-LPGKLADCTSQDPERTELFLVEGDSAGGSA 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 66474593 318 KQGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDE 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 |
1.21e-78 |
|
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: 239.00 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 104 GGIKAFVEYLNQNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDR 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474593 184 EDYSKKAKISaASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 262
Cdd:cd00822 81 NNLLKKKDVK-LTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
1-366 |
9.22e-74 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 245.95 E-value: 9.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDS-NGTGTEVRFWPSA-TIFTDTLYHY---------- 68
Cdd:PTZ00109 250 HGVGLSVVNALSSFLKVDVFKGGKIYSIELSKGKVTKPLSVFSCPlKKRGTTIHFLPDYkHIFKTHHQHTeteeeegckn 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 69 ----DILAKRLRELSFLNSGVSIRLEDERDGREVHFC------YEGGIKAFVEYLNQNKTPIHQ--NVFHFSTEQDGIGV 136
Cdd:PTZ00109 330 gfnlDLIKNRIHELSYLNPGLTFYLVDERIANENNFYpyetikHEGGTREFLEELIKDKTPLYKdiNIISIRGVIKNVNV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 137 EVAMQWN-DAYQEGVYCFTNNIpQRDGGTHLVGFRTALTRTLNTYMDREDYSKkAKISAASGDDVREDLIAVISVKVPDP 215
Cdd:PTZ00109 410 EVSLSWSlESYTALIKSFANNV-STTAGTHIDGFKYAITRCVNGNIKKNGYFK-GNFVNIPGEFIREGMTAIISVKLNGA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 216 KFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREMTRRKGALDIA-GLPGKLAD 294
Cdd:PTZ00109 488 EFDGQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYStILPGKLVD 567
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66474593 295 CQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVERARFD-RMISSQEVGTLITALGCGIGRD 366
Cdd:PTZ00109 568 CISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkKVFENSEIKLLITSIGLSVNPV 640
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
1-362 |
6.96e-71 |
|
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: 232.89 E-value: 6.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNG--TGTEVRFWPSATIFTDTLYHYDILAKRLREL 78
Cdd:TIGR01055 111 HGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKrlTGTSVHFTPDPEIFDSLHFSVSRLYHILRAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 79 SFLNSGVSIRLEDERDGREVHFCYEGGIKAFV-EYLNQNKTPIhQNVFHFSTEQDGIGVEVAMQWNDAYQEGV---YCft 154
Cdd:TIGR01055 191 AVLCRGVEIEFEDEVNNTKALWNYPDGLKDYLsEAVNGDNTLP-PKPFSGNFEGDDEAVEWALLWLPEGGELFmesYV-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 155 NNIPQRDGGTHLVGFRTALTRTLNTYMD-REDYSKKAKISAasgDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTA 233
Cdd:TIGR01055 268 NLIPTPQGGTHVNGLRQGLLDALREFCEmRNNLPRGVKLTA---EDIWDRCSYVLSIKMQDPQFAGQTKERLSSRQVAKF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 234 VEQAMGEKLGEFLLENPGDAKIVVNKIIDAARAREAARKAREmtrRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSA 313
Cdd:TIGR01055 345 VSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKKVV---RKKLTSGPALPGKLADCTRQDLEGTELFLVEGDSA 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66474593 314 GGSAKQGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCG 362
Cdd:TIGR01055 422 GGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGID 470
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
105-262 |
1.29e-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: 203.23 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 105 GIKAFVEYLNQNKTPIHQNVFHFSTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 183 REDYSKKAKIsAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 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 |
8.98e-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: 157.31 E-value: 8.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIRRNGHVYEQTYHMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILAKRLRELSF 80
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIFEKTEFDFDTLKRRLRELAF 160
|
90 100
....*....|....*....|
gi 66474593 81 LNSGVSIRLEDERDGREVHF 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 |
1.56e-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: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 106 IKAFVEYLNQNKTpiHQNVFHFSTEQDGIGVEVAMQWND---AYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNtymd 182
Cdd:cd00329 1 LKDRLAEILGDKV--ADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66474593 183 redyskkakisaasGDDVREDLIAVISVKVPD--PKFS-SQTKDKL 225
Cdd:cd00329 75 --------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1-371 |
1.44e-19 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 90.49 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIR--RNGHVYEQTY--HMGEPQAPlkQIGDSNGTG--TEVRFWPSATIFTDTLY---HYDIL 71
Cdd:PTZ00108 143 NGFGAKLTNIFSTKFTVECVdsKSGKKFKMTWtdNMSKKSEP--RITSYDGKKdyTKVTFYPDYAKFGMTEFdddMLRLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 72 AKRLRELSFLNSGVSIRLEDERDGrevhfcyeggIKAFVEYLN---QNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQE 148
Cdd:PTZ00108 221 KKRVYDLAGCFGKLKVYLNGERIA----------IKSFKDYVDlylPDGEEGKKPPYPFVYTSVNGRWEVVVSLSDGQFQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 149 GVyCFTNNIPQRDGGTHLvgfrTALTRTLNTYMDREDYSKKAKISAASGDDVREDLIAVISVKVPDPKFSSQTKDKLVSS 228
Cdd:PTZ00108 291 QV-SFVNSICTTKGGTHV----NYILDQLISKLQEKAKKKKKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 229 EVKTAVEQAMGEKLGEFLLENPgdakiVVNKIIDAARAREAARKAREM--TRRKGaldIAGLPgKLADCQEKDPALSE-- 304
Cdd:PTZ00108 366 PSKFGSTCELSEKLIKYVLKSP-----ILENIVEWAQAKLAAELNKKMkaGKKSR---ILGIP-KLDDANDAGGKNSEec 436
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66474593 305 -LYIVEGDSAGGSAKQG---RNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDEYNPD 371
Cdd:PTZ00108 437 tLILTEGDSAKALALAGlsvVGRDYYGVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEDPK 507
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
1-371 |
3.62e-11 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 64.73 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 1 HGVGVSVVNALSEKLLLTIR--RNGHVYEQTY--HMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDI---LAK 73
Cdd:PLN03128 135 NGYGAKLANIFSTEFTVETAdgNRGKKYKQVFtnNMSVKSEPKITSCKASENWTKITFKPDLAKFNMTRLDEDVvalMSK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 74 RLRELS-FLNSGVSIRLEDERDGrevhfcyeggIKAFVEYLN-----QNKTPIHQNVFHFSTEQDGIGVEVAmqwNDAYQ 147
Cdd:PLN03128 215 RVYDIAgCLGKKLKVELNGKKLP----------VKSFQDYVGlylgpNSREDPLPRIYEKVNDRWEVCVSLS---DGSFQ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 148 EgvYCFTNNIPQRDGGTHLvgfrTALTRTLNTYMdREDYSKKAKISAA-SGDDVREDLIAVISVKVPDPKFSSQTKDKLV 226
Cdd:PLN03128 282 Q--VSFVNSIATIKGGTHV----DYVADQIVKHI-QEKVKKKNKNATHvKPFQIKNHLWVFVNCLIENPTFDSQTKETLT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 227 SSEVKTAVEQAMGEklgEFL--LENPGdakiVVNKIIDAARAREAARKAREMTRRKGALdiAGLPgKLADCQEKDPALSE 304
Cdd:PLN03128 355 TRPSSFGSKCELSE---EFLkkVEKCG----VVENILSWAQFKQQKELKKKDGAKRQRL--TGIP-KLDDANDAGGKKSK 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66474593 305 ---LYIVEGDSAGGSAKQGR---NRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRdEYNPD 371
Cdd:PLN03128 425 dctLILTEGDSAKALAMSGLsvvGRDHYGVFPLRGKLLNVREASHKQIMKNAEITNIKQILGLQFGK-TYDEE 496
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
153-370 |
5.11e-11 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 64.00 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 153 FTNNIPQRDGGTHLVGFRTALTRTLNTYMDREdysKKAKISAASgddVREDLIAVISVK-VPDPKFSSQTKDKLVSS--E 229
Cdd:PHA02569 264 FVNGLHTKNGGHHVDCVMDDICEELIPMIKKK---HKIEVTKAR---VKECLTIVLFVRnMSNPRFDSQTKERLTSPfgE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 230 VKTAVeQAMGEKLGEFLLENPGdakiVVNKIIDAARAREAARKAREMTR-RKGALDI-------AGLPGKLADcqekdpa 301
Cdd:PHA02569 338 IRNHI-DLDYKKIAKQILKTEA----IIMPIIEAALARKLAAEKAAETKaAKKAKKAkvakhikANLIGKDAE------- 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474593 302 lSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDEYNP 370
Cdd:PHA02569 406 -TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKAENM 473
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
305-369 |
1.74e-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: 1.74e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474593 305 LYIVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVERARFDRMISSQEVGTLITALGCGIGRDEYN 369
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYE 70
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| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
26-360 |
2.19e-06 |
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DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 49.86 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 26 YEQTY--HMGEPQAPLKQIGDSNGTGTEVRFWPSATIFTDTLYHYDILA---KRLRELSFlNSGVSIRLEdeRDGREVHf 100
Cdd:PLN03237 187 YKQVFsnNMGKKSEPVITKCKKSENWTKVTFKPDLAKFNMTHLEDDVVAlmkKRVVDIAG-CLGKTVKVE--LNGKRIP- 262
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 101 cyeggIKAFVEYLN---QNKTPIHQNVFHFSTEQDGIGVEVAMQWNDAYQEGVyCFTNNIPQRDGGTHLvgfrTALTRTL 177
Cdd:PLN03237 263 -----VKSFSDYVDlylESANKSRPENLPRIYEKVNDRWEVCVSLSEGQFQQV-SFVNSIATIKGGTHV----DYVTNQI 332
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 178 NTYMdREDYSKKAKISAASGDDVREDLIAVISVKVPDPKFSSQTKDKLvssevkTAVEQAMGEK--LGEFLLEnpgdaKI 255
Cdd:PLN03237 333 ANHV-MEAVNKKNKNANIKAHNVKNHLWVFVNALIDNPAFDSQTKETL------TLRQSSFGSKceLSEDFLK-----KV 400
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474593 256 VVNKIIDAARAREAARKAREMTRRKGA--LDIAGLPgKLADCQE---KDPALSELYIVEGDSAGGSAKQGRN---RKNQA 327
Cdd:PLN03237 401 MKSGIVENLLSWADFKQSKELKKTDGAktTRVTGIP-KLEDANEaggKNSEKCTLILTEGDSAKALAVAGLSvvgRNYYG 479
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330 340 350
....*....|....*....|....*....|...
gi 66474593 328 ILPLKGKILNVERARFDRMISSQEVGTLITALG 360
Cdd:PLN03237 480 VFPLRGKLLNVREASHKQIMNNAEIENIKQILG 512
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| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
304-339 |
3.12e-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: 45.04 E-value: 3.12e-06
10 20 30
....*....|....*....|....*....|....*.
gi 66474593 304 ELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVE 339
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLE 36
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