|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-371 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 803.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDGREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 161 DGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEK 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 241 LADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGR 320
Cdd:PRK14939 358 LSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGR 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 66474587 321 NRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPDK 371
Cdd:PRK14939 438 DRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDK 488
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-371 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 615.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDG--REAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:COG0187 356 EKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQ 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 371
Cdd:COG0187 436 GRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIG-DDFDLEK 487
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-371 |
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: 610.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERD--GREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLVY 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:TIGR01059 351 EKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAKQ 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDeYNPDK 371
Cdd:TIGR01059 431 GRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-371 |
6.28e-160 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 461.26 E-value: 6.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYH-LGEPHAPLKQIGDSTGTGTEVRFWPSPTIFS-DTLFHYEILAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 79 SFLNSGVSIRLLDERDGREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKedYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKK--KKKLKEKNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIVS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:smart00433 320 ECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAKS 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 371
Cdd:smart00433 399 GRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEK 450
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
104-261 |
1.97e-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: 248.63 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 104 GGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNSYMDK 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474587 184 EDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLADFLLENPGDAKIVVNKIID 261
Cdd:cd00822 81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
105-261 |
6.58e-69 |
|
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: 214.02 E-value: 6.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 105 GIKAFVEYLNQNKTPIHPKVFHFTTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNSYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474587 183 KEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLADFLLENPGDAKIVVNKIID 261
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-371 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 803.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:PRK14939 118 HGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVAPLKVVGETDKTGTEVRFWPSPEIFENTEFDYDILAKRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDGREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQR 160
Cdd:PRK14939 198 LNSGVRIRLKDERDGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 161 DGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEK 240
Cdd:PRK14939 278 DGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 241 LADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGR 320
Cdd:PRK14939 358 LSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGR 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 66474587 321 NRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPDK 371
Cdd:PRK14939 438 DRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIGRDEFNPDK 488
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-371 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 615.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:COG0187 116 HGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGPLEKIGKTDRTGTTVRFKPDPEIFETTEFDYETLAERLRELAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDG--REAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:COG0187 196 LNKGLTITLTDEREEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNIN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:COG0187 276 TPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:COG0187 356 EKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQ 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 371
Cdd:COG0187 436 GRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIG-DDFDLEK 487
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-371 |
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: 610.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:TIGR01059 111 HGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPVGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFDILAKRLRELAF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERD--GREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:TIGR01059 191 LNSGVKISLEDERDgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNIN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:TIGR01059 271 TREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLVY 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:TIGR01059 351 EKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAKQ 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDeYNPDK 371
Cdd:TIGR01059 431 GRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKD-FDLEK 482
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
1-371 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 609.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:PRK05644 118 HGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPVTPLEVIGETDETGTTVTFKPDPEIFETTEFDYDTLATRLRELAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDGREAH--FCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:PRK05644 198 LNKGLKITLTDEREGEEKEetFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNIN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:PRK05644 278 THEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:PRK05644 358 EALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQ 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 371
Cdd:PRK05644 438 GRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIG-DDFDISK 489
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-371 |
6.28e-160 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 461.26 E-value: 6.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYH-LGEPHAPLKQIGDSTGTGTEVRFWPSPTIFS-DTLFHYEILAKRLREL 78
Cdd:smart00433 82 HGVGASVVNALSTEFEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDDFELLKRRLREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 79 SFLNSGVSIRLLDERDGREAHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIP 158
Cdd:smart00433 162 AFLNKGVKITLNDERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 159 QRDGGTHLVGFRTALTRTLNSYMDKedYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMG 238
Cdd:smart00433 242 TTEGGTHENGFKDALTRVINEYAKK--KKKLKEKNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIVS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 239 EKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQ 318
Cdd:smart00433 320 ECLLSFLEENPVEASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAKS 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 66474587 319 GRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGrDEYNPDK 371
Cdd:smart00433 399 GRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIG-KDFDIEK 450
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
1-366 |
4.45e-156 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 452.63 E-value: 4.45e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTG--TGTEVRFWPSPTIFSDTLFHYEILAKRLREL 78
Cdd:PRK05559 118 HGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPVGPLEVVGTAGKrkTGTRVRFWPDPKIFDSPKFSPERLKERLRSK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 79 SFLNSGVSIRLLDERDgrEAHFCYEGGIKAFVEYLNQNKTPIHP-KVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNI 157
Cdd:PRK05559 198 AFLLPGLTITLNDERE--RQTFHYENGLKDYLAELNEGKETLPEeFVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 158 PQRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKsAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAM 237
Cdd:PRK05559 276 PTPQGGTHENGFREGLLKAVREFAEKRNLLPKGK-KLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 238 GEKLADFLLENPGDAKIVVNKIIDAARAREAARKARelTRRKGALDIAgLPGKLADCQEKDPALSELYIVEGDSAGGSAK 317
Cdd:PRK05559 355 KDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAKKV--KRKKKTSGPA-LPGKLADCTSQDPERTELFLVEGDSAGGSAK 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66474587 318 QGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDE 366
Cdd:PRK05559 432 QARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDSF 480
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
104-261 |
1.97e-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: 248.63 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 104 GGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNSYMDK 183
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474587 184 EDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLADFLLENPGDAKIVVNKIID 261
Cdd:cd00822 81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
1-365 |
3.15e-75 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 249.80 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVY-------EQTYHLGEPHAPLKQigdstgTGTEVRFWPS-PTIFSDTLFHY---- 68
Cdd:PTZ00109 250 HGVGLSVVNALSSFLKVDVFKGGKIYsielskgKVTKPLSVFSCPLKK------RGTTIHFLPDyKHIFKTHHQHTetee 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 69 ----------EILAKRLRELSFLNSGVSIRLLDERDGREAHFC------YEGGIKAFVEYLNQNKTPIHP--KVFHFTTE 130
Cdd:PTZ00109 324 eegckngfnlDLIKNRIHELSYLNPGLTFYLVDERIANENNFYpyetikHEGGTREFLEELIKDKTPLYKdiNIISIRGV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 131 QDGIGVEVAMQWN-DAYQEGVYCFTNNIpQRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAKSAASGDDVREGLIAVISV 209
Cdd:PTZ00109 404 IKNVNVEVSLSWSlESYTALIKSFANNV-STTAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIPGEFIREGMTAIISV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 210 KVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLADFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIA-GLP 288
Cdd:PTZ00109 483 KLNGAEFDGQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYStILP 562
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474587 289 GKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMI-SSQEVGTLITALGCGIGRD 365
Cdd:PTZ00109 563 GKLVDCISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNKKVfENSEIKLLITSIGLSVNPV 640
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
1-361 |
1.67e-73 |
|
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: 239.82 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTG--TGTEVRFWPSPTIFSDTLFHYEILAKRLREL 78
Cdd:TIGR01055 111 HGVGISVVNALSKRVKIKVYRQGKLYSIAFENGAKVTDLISAGTCGKrlTGTSVHFTPDPEIFDSLHFSVSRLYHILRAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 79 SFLNSGVSIRLLDERDGREAHFCYEGGIKAFV-EYLNQNKTPIhPKVFHFTTEQDGIGVEVAMQWNDAYQEGV---YCft 154
Cdd:TIGR01055 191 AVLCRGVEIEFEDEVNNTKALWNYPDGLKDYLsEAVNGDNTLP-PKPFSGNFEGDDEAVEWALLWLPEGGELFmesYV-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 155 NNIPQRDGGTHLVGFRTALTRTLNSYMDKEDYRKKAkSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVE 234
Cdd:TIGR01055 268 NLIPTPQGGTHVNGLRQGLLDALREFCEMRNNLPRG-VKLTAEDIWDRCSYVLSIKMQDPQFAGQTKERLSSRQVAKFVS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 235 QAMGEKLADFLLENPGDAKIVVNKIIDAARAREAARKAREltrRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGG 314
Cdd:TIGR01055 347 GVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRKRAAKKVV---RKKLTSGPALPGKLADCTRQDLEGTELFLVEGDSAGG 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66474587 315 SAKQGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCG 361
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 ... |
105-261 |
6.58e-69 |
|
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: 214.02 E-value: 6.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 105 GIKAFVEYLNQNKTPIHPKVFHFTTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNSYMD 182
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66474587 183 KEDYRKKAKSAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLADFLLENPGDAKIVVNKIID 261
Cdd:pfam00204 81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
1-100 |
5.99e-46 |
|
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: 155.39 E-value: 5.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIRRNGHVYEQTYHLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFHYEILAKRLRELSF 80
Cdd:cd16928 81 HGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKKTGTTVRFWPDPEIFEKTEFDFDTLKRRLRELAF 160
|
90 100
....*....|....*....|
gi 66474587 81 LNSGVSIRLLDERDGREAHF 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 ... |
106-224 |
1.26e-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: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 106 IKAFVEYLNQNKTpiHPKVFHFTTEQDGIGVEVAMQWND---AYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNsymd 182
Cdd:cd00329 1 LKDRLAEILGDKV--ADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 66474587 183 kedyrkkaksaasGDDVREGLIAVISVKVPD--PKFS-SQTKDKL 224
Cdd:cd00329 75 -------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1-370 |
2.51e-18 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 87.02 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIR--RNGHVYEQTY--HLGEPHAPlkQIGDSTGTG--TEVRFWPSPTIFSDTLF---HYEIL 71
Cdd:PTZ00108 143 NGFGAKLTNIFSTKFTVECVdsKSGKKFKMTWtdNMSKKSEP--RITSYDGKKdyTKVTFYPDYAKFGMTEFdddMLRLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 72 AKRLRELSFLNSGVSIRLLDERDGreahfcyeggIKAFVEYLN---QNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQE 148
Cdd:PTZ00108 221 KKRVYDLAGCFGKLKVYLNGERIA----------IKSFKDYVDlylPDGEEGKKPPYPFVYTSVNGRWEVVVSLSDGQFQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 149 GVyCFTNNIPQRDGGTHLvgfrTALTRTLNSYMDKEDYRKKAKSAA-SGDDVREGLIAVISVKVPDPKFSSQTKDKLVSS 227
Cdd:PTZ00108 291 QV-SFVNSICTTKGGTHV----NYILDQLISKLQEKAKKKKKKGKEiKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 228 EVKTAVEQAMGEKLADFLLENPgdakivvnkIIDAARAREAARKARELTRRKGALD---IAGLPgKLADCQEKDPALSE- 303
Cdd:PTZ00108 366 PSKFGSTCELSEKLIKYVLKSP---------ILENIVEWAQAKLAAELNKKMKAGKksrILGIP-KLDDANDAGGKNSEe 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66474587 304 --LYIVEGDSAGGSAKQG---RNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNPD 370
Cdd:PTZ00108 436 ctLILTEGDSAKALALAGlsvVGRDYYGVFPLRGKLLNVRDASLKQLMNNKEIQNLFKILGLDIGKKYEDPK 507
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
1-370 |
1.39e-12 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 69.35 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 1 HGVGVSVVNALSDKLLLTIR--RNGHVYEQTY--HLGEPHAPLKQIGDSTGTGTEVRFWPSPTIFSDTLFH---YEILAK 73
Cdd:PLN03128 135 NGYGAKLANIFSTEFTVETAdgNRGKKYKQVFtnNMSVKSEPKITSCKASENWTKITFKPDLAKFNMTRLDedvVALMSK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 74 RLRELS-FLNSGVSIRLLDERDGreahfcyeggIKAFVEYLN-----QNKTPIHPKVFHFTTEQDGIGVEVAmqwNDAYQ 147
Cdd:PLN03128 215 RVYDIAgCLGKKLKVELNGKKLP----------VKSFQDYVGlylgpNSREDPLPRIYEKVNDRWEVCVSLS---DGSFQ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 148 EgvYCFTNNIPQRDGGTHLvgfrTALTRTLNSYMdKEDYRKKAKSAAS--GDDVREGLIAVISVKVPDPKFSSQTKDKLV 225
Cdd:PLN03128 282 Q--VSFVNSIATIKGGTHV----DYVADQIVKHI-QEKVKKKNKNATHvkPFQIKNHLWVFVNCLIENPTFDSQTKETLT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 226 SSEVKTAVEQAMGEklaDFL--LENPGdakiVVNKIIDAARAREAARKARELTRRKGALdiAGLPgKLADCQEKDPALSE 303
Cdd:PLN03128 355 TRPSSFGSKCELSE---EFLkkVEKCG----VVENILSWAQFKQQKELKKKDGAKRQRL--TGIP-KLDDANDAGGKKSK 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66474587 304 ---LYIVEGDSAGGSAKQGR---NRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRdEYNPD 370
Cdd:PLN03128 425 dctLILTEGDSAKALAMSGLsvvGRDHYGVFPLRGKLLNVREASHKQIMKNAEITNIKQILGLQFGK-TYDEE 496
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
153-369 |
1.80e-12 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 68.63 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 153 FTNNIPQRDGGTHLVGFRTALTRTLNSYMdkedyRKKAKSAASGDDVREGLIAVISVK-VPDPKFSSQTKDKLVSS--EV 229
Cdd:PHA02569 264 FVNGLHTKNGGHHVDCVMDDICEELIPMI-----KKKHKIEVTKARVKECLTIVLFVRnMSNPRFDSQTKERLTSPfgEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 230 KTAVeQAMGEKLADFLLENPGdakiVVNKIIDAARAREAARKARELTR-RKGALDI-------AGLPGKLADcqekdpal 301
Cdd:PHA02569 339 RNHI-DLDYKKIAKQILKTEA----IIMPIIEAALARKLAAEKAAETKaAKKAKKAkvakhikANLIGKDAE-------- 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474587 302 SELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYNP 369
Cdd:PHA02569 406 TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAITGLVLGEKAENM 473
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
304-368 |
2.38e-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: 54.61 E-value: 2.38e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66474587 304 LYIVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGRDEYN 368
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHGKSDYE 70
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| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
106-359 |
5.58e-07 |
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DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 51.79 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 106 IKAFVEYLN---QNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVyCFTNNIPQRDGGTHLvgfrTALTRTLNSYMd 182
Cdd:PLN03237 263 VKSFSDYVDlylESANKSRPENLPRIYEKVNDRWEVCVSLSEGQFQQV-SFVNSIATIKGGTHV----DYVTNQIANHV- 336
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 183 KEDYRKKAKSA-ASGDDVREGLIAVISVKVPDPKFSSQTKDKLvssevkTAVEQAMGEKLA---DFLlenpgdAKIVVNK 258
Cdd:PLN03237 337 MEAVNKKNKNAnIKAHNVKNHLWVFVNALIDNPAFDSQTKETL------TLRQSSFGSKCElseDFL------KKVMKSG 404
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66474587 259 IIDAARAREAARKARELTRRKGA--LDIAGLPgKLADCQE---KDPALSELYIVEGDSAGGSAKQGRN---RKNQAILPL 330
Cdd:PLN03237 405 IVENLLSWADFKQSKELKKTDGAktTRVTGIP-KLEDANEaggKNSEKCTLILTEGDSAKALAVAGLSvvgRNYYGVFPL 483
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250 260
....*....|....*....|....*....
gi 66474587 331 KGKILNVEKARFDKMISSQEVGTLITALG 359
Cdd:PLN03237 484 RGKLLNVREASHKQIMNNAEIENIKQILG 512
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| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
303-347 |
6.78e-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: 46.97 E-value: 6.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66474587 303 ELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMIS 347
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALK 45
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