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Conserved domains on  [gi|190148862|gb|ACE63406|]
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DNA gyrase B subunit, partial [Pseudonocardia tetrahydrofuranoxydans]

Protein Classification

DNA topoisomerase subunit B( domain architecture ID 1750046)

DNA topoisomerase subunit B relaxes positive DNA supercoils generated during DNA replication; such as Mycoplasma capricolum DNA topoisomerase 4 subunit B and Arabidopsis thaliana mitochondrial DNA gyrase subunit B

EC:  5.6.2.2
PubMed:  11395412

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TOP2c super family cl40739
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
1-409 0e+00

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


The actual alignment was detected with superfamily member PRK05644:

Pssm-ID: 454823 [Multi-domain]  Cd Length: 638  Bit Score: 772.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:PRK05644 107 GGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPvTPLEVIGETDETGTTVTFKPDPEIFETTEFDYD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:PRK05644 187 TLATRLRELAFLNKGLKITLTDEREGE---------------EKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKD 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:PRK05644 252 GIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHP 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:PRK05644 332 EPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLA 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:PRK05644 412 DCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGDDFDISKLR 491
                        410
                 ....*....|
gi 190148862 400 YHKIVLMTDA 409
Cdd:PRK05644 492 YHKIIIMTDA 501
 
Name Accession Description Interval E-value
gyrB PRK05644
DNA gyrase subunit B; Validated
1-409 0e+00

DNA gyrase subunit B; Validated


Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 772.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:PRK05644 107 GGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPvTPLEVIGETDETGTTVTFKPDPEIFETTEFDYD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:PRK05644 187 TLATRLRELAFLNKGLKITLTDEREGE---------------EKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKD 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:PRK05644 252 GIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHP 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:PRK05644 332 EPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLA 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:PRK05644 412 DCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGDDFDISKLR 491
                        410
                 ....*....|
gi 190148862 400 YHKIVLMTDA 409
Cdd:PRK05644 492 YHKIIIMTDA 501
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
1-409 0e+00

DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];


Pssm-ID: 439957 [Multi-domain]  Cd Length: 635  Bit Score: 742.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVPGT-LNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:COG0187  105 DGGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGpLEKIGKTDRTGTTVRFKPDPEIFETTEFDYE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:COG0187  185 TLAERLRELAFLNKGLTITLTDEREEE---------------PKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKD 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:COG0187  250 GIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLP 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:COG0187  330 EPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLA 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:COG0187  410 DCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGDDFDLEKLR 489
                        410
                 ....*....|
gi 190148862 400 YHKIVLMTDA 409
Cdd:COG0187  490 YHKIIIMTDA 499
gyrB TIGR01059
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ...
1-409 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: 643.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:TIGR01059 100 DKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPvGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFD 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   80 TIRRRLQEMAFLNKGLTIVLRDERngdsdeaeepdaegyVAKVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:TIGR01059 180 ILAKRLRELAFLNSGVKISLEDER---------------DGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKE 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:TIGR01059 245 GIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVP 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:TIGR01059 325 DPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLA 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:TIGR01059 405 DCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFDLEKLR 484
                         410
                  ....*....|
gi 190148862  400 YHKIVLMTDA 409
Cdd:TIGR01059 485 YHKIIIMTDA 494
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
1-409 0e+00

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 552.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862     1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTR--SVPGTLNKGAATRRTGTTITFWADPDIFE-TTVYN 77
Cdd:smart00433  71 DDDAYKVSGGLHGVGASVVNALSTEFEVEVARDGKEYKQSFSNngKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDD 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    78 IETIRRRLQEMAFLNKGLTIVLRDERNGdsdeaeepdaegyvakvKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGE 157
Cdd:smart00433 151 FELLKRRLRELAFLNKGVKITLNDERSD-----------------EEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGE 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   158 APGHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDpaLSGDDIREGLAAIVSVK 237
Cdd:smart00433 214 KDNIRVEVAFQYTDGYSENIVSFVNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKEKN--IKGEDVREGLTAFISVK 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   238 VKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELvRRKSAGDIGGLPGK 317
Cdd:smart00433 292 IPEPQFEGQTKEKLGTSEVRFGVEKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKAREL-TRKKKLSSISLPGK 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   318 LADCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAK 397
Cdd:smart00433 371 LADASSAGPKKCELFLVEGDSAGGSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEK 450
                          410
                   ....*....|..
gi 190148862   398 LRYHKIVLMTDA 409
Cdd:smart00433 451 LRYGKIIIMTDA 462
TopoII_Trans_DNA_gyrase cd00822
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ...
131-302 2.77e-91

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: 272.51  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 131 NGLEDFVAHLNKTKDPIYKKLVAFTGEAPGHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARD 210
Cdd:cd00822    1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 211 KKLLKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSA 290
Cdd:cd00822   81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAILAA 160
                        170
                 ....*....|..
gi 190148862 291 QARLAARKAREL 302
Cdd:cd00822  161 KAREAARKAREL 172
DNA_gyraseB pfam00204
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ...
132-302 4.15e-79

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: 241.37  E-value: 4.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  132 GLEDFVAHLNKTKDPIYKKLVAFTGEAP--GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYAR 209
Cdd:pfam00204   1 GLKDFVEELNKDKKPLHKEIIYFEGESPdnRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  210 DKKLLKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQS 289
Cdd:pfam00204  81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQA 160
                         170
                  ....*....|...
gi 190148862  290 AQARLAARKAREL 302
Cdd:pfam00204 161 AKARLAARKAREA 173
 
Name Accession Description Interval E-value
gyrB PRK05644
DNA gyrase subunit B; Validated
1-409 0e+00

DNA gyrase subunit B; Validated


Pssm-ID: 235542 [Multi-domain]  Cd Length: 638  Bit Score: 772.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:PRK05644 107 GGGGYKVSGGLHGVGVSVVNALSTWLEVEVKRDGKIYYQEYERGVPvTPLEVIGETDETGTTVTFKPDPEIFETTEFDYD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:PRK05644 187 TLATRLRELAFLNKGLKITLTDEREGE---------------EKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKD 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:PRK05644 252 GIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALTRVINDYARKNKLLKEKDDNLTGEDVREGLTAVISVKHP 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:PRK05644 332 EPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAKKIVEKAILAARAREAARKARELTRRKSALESSSLPGKLA 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:PRK05644 412 DCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGDDFDISKLR 491
                        410
                 ....*....|
gi 190148862 400 YHKIVLMTDA 409
Cdd:PRK05644 492 YHKIIIMTDA 501
GyrB COG0187
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
1-409 0e+00

DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];


Pssm-ID: 439957 [Multi-domain]  Cd Length: 635  Bit Score: 742.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVPGT-LNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:COG0187  105 DGGSYKVSGGLHGVGASVVNALSERLEVEVKRDGKIYRQRFERGKPVGpLEKIGKTDRTGTTVRFKPDPEIFETTEFDYE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:COG0187  185 TLAERLRELAFLNKGLTITLTDEREEE---------------PKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKD 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:COG0187  250 GIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRTALTRVINDYARKNGLLKEKDKNLTGDDVREGLTAVISVKLP 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:COG0187  330 EPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPAEAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLA 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:COG0187  410 DCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPLRGKILNVEKARLDKILKNEEIRDLITALGTGIGDDFDLEKLR 489
                        410
                 ....*....|
gi 190148862 400 YHKIVLMTDA 409
Cdd:COG0187  490 YHKIIIMTDA 499
gyrB TIGR01059
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ...
1-409 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: 643.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:TIGR01059 100 DKDSYKVSGGLHGVGVSVVNALSEWLEVTVFRDGKIYRQEFERGIPvGPLEVVGETKKTGTTVRFWPDPEIFETTEFDFD 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   80 TIRRRLQEMAFLNKGLTIVLRDERngdsdeaeepdaegyVAKVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:TIGR01059 180 ILAKRLRELAFLNSGVKISLEDER---------------DGKGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKE 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:TIGR01059 245 GIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRSALTRVINSYAKNNKLLKESKPNLTGEDIREGLTAVISVKVP 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:TIGR01059 325 DPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQEAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLA 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLR 399
Cdd:TIGR01059 405 DCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILSNQEIGAIITALGCGIGKDFDLEKLR 484
                         410
                  ....*....|
gi 190148862  400 YHKIVLMTDA 409
Cdd:TIGR01059 485 YHKIIIMTDA 494
gyrB PRK14939
DNA gyrase subunit B; Provisional
1-409 0e+00

DNA gyrase subunit B; Provisional


Pssm-ID: 237860 [Multi-domain]  Cd Length: 756  Bit Score: 642.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVPGT-LNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:PRK14939 107 DQNSYKVSGGLHGVGVSVVNALSEWLELTIRRDGKIHEQEFEHGVPVApLKVVGETDKTGTEVRFWPSPEIFENTEFDYD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGdsdeaeepdaegyvakvKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGEAP 159
Cdd:PRK14939 187 ILAKRLRELAFLNSGVRIRLKDERDG-----------------KEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKD 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 160 GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVK 239
Cdd:PRK14939 250 GIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAALTRTINNYIEKEGLAKKAKVSLTGDDAREGLTAVLSVKVP 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 240 EPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELVRRKSAGDIGGLPGKLA 319
Cdd:PRK14939 330 DPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEAKIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLA 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 320 DCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGI-HDEFDLAKL 398
Cdd:PRK14939 410 DCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKGKILNVEKARFDKMLSSQEIGTLITALGCGIgRDEFNPDKL 489
                        410
                 ....*....|.
gi 190148862 399 RYHKIVLMTDA 409
Cdd:PRK14939 490 RYHKIIIMTDA 500
TOP2c smart00433
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
1-409 0e+00

TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE


Pssm-ID: 214659 [Multi-domain]  Cd Length: 594  Bit Score: 552.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862     1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTR--SVPGTLNKGAATRRTGTTITFWADPDIFE-TTVYN 77
Cdd:smart00433  71 DDDAYKVSGGLHGVGASVVNALSTEFEVEVARDGKEYKQSFSNngKPLSEPKIIGDTKKDGTKVTFKPDLEIFGmTTDDD 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    78 IETIRRRLQEMAFLNKGLTIVLRDERNGdsdeaeepdaegyvakvKEHVFCYPNGLEDFVAHLNKTKDPIYKKLVAFTGE 157
Cdd:smart00433 151 FELLKRRLRELAFLNKGVKITLNDERSD-----------------EEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGE 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   158 APGHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDpaLSGDDIREGLAAIVSVK 237
Cdd:smart00433 214 KDNIRVEVAFQYTDGYSENIVSFVNNIATTEGGTHENGFKDALTRVINEYAKKKKKLKEKN--IKGEDVREGLTAFISVK 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   238 VKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKARELvRRKSAGDIGGLPGK 317
Cdd:smart00433 292 IPEPQFEGQTKEKLGTSEVRFGVEKIVSECLLSFLEENPVEASKIVEKVLLAAKARAAAKKAREL-TRKKKLSSISLPGK 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   318 LADCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAK 397
Cdd:smart00433 371 LADASSAGPKKCELFLVEGDSAGGSAKSGRDRDFQAILPLRGKILNVEKASLDKILKNEEIQALITALGLGIGKDFDIEK 450
                          410
                   ....*....|..
gi 190148862   398 LRYHKIVLMTDA 409
Cdd:smart00433 451 LRYGKIIIMTDA 462
PRK05559 PRK05559
DNA topoisomerase IV subunit B; Reviewed
1-409 0e+00

DNA topoisomerase IV subunit B; Reviewed


Pssm-ID: 235501 [Multi-domain]  Cd Length: 631  Bit Score: 535.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVP-GTLNKGAAT--RRTGTTITFWADPDIFETTVYN 77
Cdd:PRK05559 107 SNKAYKFSGGLHGVGVSVVNALSSRLEVEVKRDGKVYRQRFEGGDPvGPLEVVGTAgkRKTGTRVRFWPDPKIFDSPKFS 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  78 IETIRRRLQEMAFLNKGLTIVLRDERngdsdeaeepdaegyvakvKEHVFCYPNGLEDFVAHLNKTKDPIYKKLV-AFTG 156
Cdd:PRK05559 187 PERLKERLRSKAFLLPGLTITLNDER-------------------ERQTFHYENGLKDYLAELNEGKETLPEEFVgSFEG 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 157 EAPGHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKeKDPALSGDDIREGLAAIVSV 236
Cdd:PRK05559 248 EAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLLKAVREFAEKRNLLP-KGKKLEGEDVREGLAAVLSV 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 237 KVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLAARKarELVRRKSAgDIGGLPG 316
Cdd:PRK05559 327 KIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAEKLAEKAIKAAQARLRAAK--KVKRKKKT-SGPALPG 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 317 KLADCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLA 396
Cdd:PRK05559 404 KLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGKILNTWEASLDDVLANEEIHDIIVAIGIGPGDSFDLE 483
                        410
                 ....*....|...
gi 190148862 397 KLRYHKIVLMTDA 409
Cdd:PRK05559 484 DLRYGKIIIMTDA 496
PTZ00109 PTZ00109
DNA gyrase subunit b; Provisional
2-409 1.26e-95

DNA gyrase subunit b; Provisional


Pssm-ID: 240272 [Multi-domain]  Cd Length: 903  Bit Score: 305.65  E-value: 1.26e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   2 SDSYAVSGGLHGVGVSVVNALSTRLDVEIdtdgFHWDQQYTRSvpgtLNKGAAT----------RRTGTTITFWAD-PDI 70
Cdd:PTZ00109 240 SQMYEYSSGLHGVGLSVVNALSSFLKVDV----FKGGKIYSIE----LSKGKVTkplsvfscplKKRGTTIHFLPDyKHI 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  71 FETTV--------------YNIETIRRRLQEMAFLNKGLTIVLRDERNgdSDEAEEPDAEgyvakvkehVFCYPNGLEDF 136
Cdd:PTZ00109 312 FKTHHqhteteeeegckngFNLDLIKNRIHELSYLNPGLTFYLVDERI--ANENNFYPYE---------TIKHEGGTREF 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 137 VAHLNKTKDPIYK--KLVAFTGEAPGHALEVAMQWNSG-YTESVYTFANTINThEGGTHEEGFRAALTSTVNKYARDKKL 213
Cdd:PTZ00109 381 LEELIKDKTPLYKdiNIISIRGVIKNVNVEVSLSWSLEsYTALIKSFANNVST-TAGTHIDGFKYAITRCVNGNIKKNGY 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 214 LKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQAR 293
Cdd:PTZ00109 460 FKGNFVNIPGEFIREGMTAIISVKLNGAEFDGQTKTKLGNHLLKTILESIVFEQLSEILEFEPNLLLAIYNKSLAAKKAF 539
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 294 LAARKARELVRRKSAGDIG-GLPGKLADCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARID-R 371
Cdd:PTZ00109 540 EEAKAAKDLIRQKNNQYYStILPGKLVDCISDDIERNELFIVEGESAAGNAKQARNREFQAVLPLKGKILNIEKIKNNkK 619
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 372 VLKNTEVQAIITALGTGIH-----------------DEF---------------DLAKLRYHKIVLMTDA 409
Cdd:PTZ00109 620 VFENSEIKLLITSIGLSVNpvtwrqydlshgtkaskDESvqnnnstltkkknslFDTPLRYGKIILLTDA 689
TopoII_Trans_DNA_gyrase cd00822
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ...
131-302 2.77e-91

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: 272.51  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 131 NGLEDFVAHLNKTKDPIYKKLVAFTGEAPGHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARD 210
Cdd:cd00822    1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 211 KKLLKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSA 290
Cdd:cd00822   81 NNLLKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAILAA 160
                        170
                 ....*....|..
gi 190148862 291 QARLAARKAREL 302
Cdd:cd00822  161 KAREAARKAREL 172
parE_Gneg TIGR01055
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ...
5-409 3.81e-87

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: 276.80  E-value: 3.81e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    5 YAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTR--SVPGTLNKGAATRR-TGTTITFWADPDIFETTVYNIETI 81
Cdd:TIGR01055 104 YHFSGGLHGVGISVVNALSKRVKIKVYRQGKLYSIAFENgaKVTDLISAGTCGKRlTGTSVHFTPDPEIFDSLHFSVSRL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   82 RRRLQEMAFLNKGLTIVLRDERNgdsdeaeepdaegyvakVKEHVFCYPNGLEDFVAHLNKTKDPIYKKLvaFTGEAPG- 160
Cdd:TIGR01055 184 YHILRAKAVLCRGVEIEFEDEVN-----------------NTKALWNYPDGLKDYLSEAVNGDNTLPPKP--FSGNFEGd 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  161 -HALEVAMQW-NSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKeKDPALSGDDIREGLAAIVSVKV 238
Cdd:TIGR01055 245 dEAVEWALLWlPEGGELFMESYVNLIPTPQGGTHVNGLRQGLLDALREFCEMRNNLP-RGVKLTAEDIWDRCSYVLSIKM 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  239 KEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQSAQARLaaRKARELVRRKSAGDIGgLPGKL 318
Cdd:TIGR01055 324 QDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNVQLAEHLAEHAISSAQRRK--RAAKKVVRKKLTSGPA-LPGKL 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  319 ADCRSTDPSKSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGiHDEFDLAKL 398
Cdd:TIGR01055 401 ADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILPLWGKILNTWEVSLDKVLNSQEIHDIEVALGID-PDSNDLSQL 479
                         410
                  ....*....|.
gi 190148862  399 RYHKIVLMTDA 409
Cdd:TIGR01055 480 RYGKICILADA 490
DNA_gyraseB pfam00204
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ...
132-302 4.15e-79

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: 241.37  E-value: 4.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  132 GLEDFVAHLNKTKDPIYKKLVAFTGEAP--GHALEVAMQWNSGYTESVYTFANTINTHEGGTHEEGFRAALTSTVNKYAR 209
Cdd:pfam00204   1 GLKDFVEELNKDKKPLHKEIIYFEGESPdnRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  210 DKKLLKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLGNTEVKSFVQRISNEWLADWFERNPTEARTIVNKAVQS 289
Cdd:pfam00204  81 KKGLLKKKDEKITGEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQA 160
                         170
                  ....*....|...
gi 190148862  290 AQARLAARKAREL 302
Cdd:pfam00204 161 AKARLAARKAREA 173
TOPRIM_TopoIIA_GyrB cd03366
TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
329-409 4.51e-52

TOPRIM_TopoIIA_GyrB: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to the Escherichia coli GyrB subunit. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. DNA gyrase is more effective at relaxing supercoils than decatentating DNA. DNA gyrase in addition inserts negative supercoils in the presence of ATP. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173786 [Multi-domain]  Cd Length: 114  Bit Score: 169.76  E-value: 4.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 329 SEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAKLRYHKIVLMTD 408
Cdd:cd03366    1 SELYIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKARLDKILKNEEIRALITALGTGIGEDFDLEKLRYHKIIIMTD 80

                 .
gi 190148862 409 A 409
Cdd:cd03366   81 A 81
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
1-109 1.47e-48

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: 163.09  E-value: 1.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDGFHWDQQYTRSVPGT-LNKGAATRRTGTTITFWADPDIFETTVYNIE 79
Cdd:cd16928   70 DGGSYKVSGGLHGVGVSVVNALSERLEVEVKRDGKIYRQEFSRGGPLTpLEVIGETKKTGTTVRFWPDPEIFEKTEFDFD 149
                         90       100       110
                 ....*....|....*....|....*....|
gi 190148862  80 TIRRRLQEMAFLNKGLTIVLRDERNGDSDE 109
Cdd:cd16928  150 TLKRRLRELAFLNKGLKIVLEDERTGKEEV 179
TOPRIM_TopoIIA_like cd01030
TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
329-409 9.91e-43

TOPRIM_TopoIIA_like: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173780 [Multi-domain]  Cd Length: 115  Bit Score: 145.73  E-value: 9.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 329 SEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIH-DEFDLAKLRYHKIVLMT 407
Cdd:cd01030    1 CELILVEGDSAGGSAKQGRDRVFQAVFPLRGKILNVEKASLKKILKNEEIQNIIKALGLGIGkDDFDLDKLRYGKIIIMT 80

                 ..
gi 190148862 408 DA 409
Cdd:cd01030   81 DA 82
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1-408 1.61e-27

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 115.53  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEIDTDG----FH--WDQQYTRSVPGTL--NKGAATRrtgTTITFWADPDIFE 72
Cdd:PTZ00108  132 DDTEKRVTGGRNGFGAKLTNIFSTKFTVECVDSKsgkkFKmtWTDNMSKKSEPRItsYDGKKDY---TKVTFYPDYAKFG 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   73 TTVYNIETIR---RRLQEMAFLNKGLTIVLRDERNGDSDeaeepdaegyvakVKEHVFCYPngledfvahlnKTKDPIYK 149
Cdd:PTZ00108  209 MTEFDDDMLRllkKRVYDLAGCFGKLKVYLNGERIAIKS-------------FKDYVDLYL-----------PDGEEGKK 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  150 KLVAFTGEAPGHALEVAMqwnsGYTESVYT---FANTINTHEGGTHEEGFRAALTSTVNKYAR-DKKLLKEKDPALsgdd 225
Cdd:PTZ00108  265 PPYPFVYTSVNGRWEVVV----SLSDGQFQqvsFVNSICTTKGGTHVNYILDQLISKLQEKAKkKKKKGKEIKPNQ---- 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  226 IREGLAAIVSVKVKEPQFEGQTKTKLgNTEVKSFVQ-RISNEWLADWFERNPteartIVNKAVQSAQARLAArkarELVR 304
Cdd:PTZ00108  337 IKNHLWVFVNCLIVNPSFDSQTKETL-TTKPSKFGStCELSEKLIKYVLKSP-----ILENIVEWAQAKLAA----ELNK 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  305 RKSAGDIGGLPG--KLADCRS--TDPSKSEVYIV-EGDSAGGSAKSG-----RDSMtqAILPIRGKIINVEKARIDRVLK 374
Cdd:PTZ00108  407 KMKAGKKSRILGipKLDDANDagGKNSEECTLILtEGDSAKALALAGlsvvgRDYY--GVFPLRGKLLNVRDASLKQLMN 484
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 190148862  375 NTEVQAIITALGTGIHDEFDLAK-LRYHKIVLMTD 408
Cdd:PTZ00108  485 NKEIQNLFKILGLDIGKKYEDPKgLRYGSLMIMTD 519
PLN03128 PLN03128
DNA topoisomerase 2; Provisional
1-408 6.83e-21

DNA topoisomerase 2; Provisional


Pssm-ID: 215593 [Multi-domain]  Cd Length: 1135  Bit Score: 95.16  E-value: 6.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862    1 DSDSYAVSGGLHGVGVSVVNALSTRLDVEI--DTDGFHWDQQYTR--SVPGT-LNKGAATRRTGTTITFWADPDIFETTV 75
Cdd:PLN03128  124 DDNEKKTTGGRNGYGAKLANIFSTEFTVETadGNRGKKYKQVFTNnmSVKSEpKITSCKASENWTKITFKPDLAKFNMTR 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   76 YNIETI---RRRLQEMA-FLNKGLTIVLRDER---NGDSDeaeepdaegYVakvkehvfcypnGLEDFVAHLNKTKDPIY 148
Cdd:PLN03128  204 LDEDVValmSKRVYDIAgCLGKKLKVELNGKKlpvKSFQD---------YV------------GLYLGPNSREDPLPRIY 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  149 KKLvaftgeapGHALEVAMQWNSGYTESVyTFANTINTHEGGTHEEgfraALTSTVNKYARDKKLLKEKDPA-LSGDDIR 227
Cdd:PLN03128  263 EKV--------NDRWEVCVSLSDGSFQQV-SFVNSIATIKGGTHVD----YVADQIVKHIQEKVKKKNKNAThVKPFQIK 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  228 EGLAAIVSVKVKEPQFEGQTKTKLgNTEVKSFVQR--ISNEWLadwfernpteaRTIVNKAVQSAQARLAARKARELVRR 305
Cdd:PLN03128  330 NHLWVFVNCLIENPTFDSQTKETL-TTRPSSFGSKceLSEEFL-----------KKVEKCGVVENILSWAQFKQQKELKK 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  306 KSAGDIGGLPG--KLADCRSTDPSKSE---VYIVEGDSAGGSAKSG-----RDSMtqAILPIRGKIINVEKARIDRVLKN 375
Cdd:PLN03128  398 KDGAKRQRLTGipKLDDANDAGGKKSKdctLILTEGDSAKALAMSGlsvvgRDHY--GVFPLRGKLLNVREASHKQIMKN 475
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 190148862  376 TEVQAIITALG---TGIHDEFDLAKLRYHKIVLMTD 408
Cdd:PLN03128  476 AEITNIKQILGlqfGKTYDEENTKSLRYGHLMIMTD 511
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
133-252 9.18e-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: 86.55  E-value: 9.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 133 LEDFVAHLNKTKDPiyKKLVAFTGEAPGHALEVAMQWNS---GYTESVYTFANTINTHEGGTHEEGFRAALTSTVNkyar 209
Cdd:cd00329    1 LKDRLAEILGDKVA--DKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 190148862 210 dkkllkekdpalsGDDIREGLAAIVSVKV--KEPQFE-GQTKTKLG 252
Cdd:cd00329   75 -------------GDDVRRYPVAVLSLKIppSLVDVNvHPTKEEVR 107
39 PHA02569
DNA topoisomerase II large subunit; Provisional
3-409 2.66e-16

DNA topoisomerase II large subunit; Provisional


Pssm-ID: 177398 [Multi-domain]  Cd Length: 602  Bit Score: 80.95  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862   3 DSYAVSGGLHGVGVSVVNALSTRLdVEIDTDGfhwDQQYT-RSVPGTLNKGAATRRT---GTTITFWADPDIFETTVYN- 77
Cdd:PHA02569 121 DTNRVTGGMNGVGSSLTNFFSVLF-IGETCDG---KNEVTvNCSNGAENISWSTKPGkgkGTSVTFIPDFSHFEVNGLDq 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  78 --IETIRRRLQEMAFLNKGLTIVLrderNGdsdeaeepdaEGYVAKVKEHVFCYPnglEDFVAHLNKtkdpiykKLVAFT 155
Cdd:PHA02569 197 qyLDIILDRLQTLAVVFPDIKFTF----NG----------KKVSGKFKKYAKQFG---DDTIVQEND-------NVSIAL 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 156 GEAPghalevamqwnSGYTESvyTFANTINTHEGGTHEEGFRAALTSTVNKYARDKKLLKEKDPAlsgddIREGLAAIVS 235
Cdd:PHA02569 253 APSP-----------DGFRQL--SFVNGLHTKNGGHHVDCVMDDICEELIPMIKKKHKIEVTKAR-----VKECLTIVLF 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 236 VK-VKEPQFEGQTKTKLGNT--EVKSFVQrISNEWLADWFERNPTEARTIVNKAV---QSAQARLAARKARELVRRKSAG 309
Cdd:PHA02569 315 VRnMSNPRFDSQTKERLTSPfgEIRNHID-LDYKKIAKQILKTEAIIMPIIEAALarkLAAEKAAETKAAKKAKKAKVAK 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862 310 DI-GGLPGKLADcrstdpskSEVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKNTEVQAIITAlgTG 388
Cdd:PHA02569 394 HIkANLIGKDAE--------TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKELFDICAI--TG 463
                        410       420
                 ....*....|....*....|.
gi 190148862 389 IHDEFDLAKLRYHKIVLMTDA 409
Cdd:PHA02569 464 LVLGEKAENMNYKNIAIMTDA 484
PLN03237 PLN03237
DNA topoisomerase 2; Provisional
179-408 1.47e-13

DNA topoisomerase 2; Provisional


Pssm-ID: 215641 [Multi-domain]  Cd Length: 1465  Bit Score: 72.59  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  179 TFANTINTHEGGTHEEgfraALTSTVNKYARDKKLLKEKDPALSGDDIREGLAAIVSVKVKEPQFEGQTKTKLgNTEVKS 258
Cdd:PLN03237  311 SFVNSIATIKGGTHVD----YVTNQIANHVMEAVNKKNKNANIKAHNVKNHLWVFVNALIDNPAFDSQTKETL-TLRQSS 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  259 FVQRISnewLADWFERNpTEARTIVNKAVQSAQARlaarKARELVRR--KSAGDIGGLPgKLADCRSTDPSKSE---VYI 333
Cdd:PLN03237  386 FGSKCE---LSEDFLKK-VMKSGIVENLLSWADFK----QSKELKKTdgAKTTRVTGIP-KLEDANEAGGKNSEkctLIL 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190148862  334 VEGDSAGGSAKSGRDSMTQ---AILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDLAK-LRYHKIVLMTD 408
Cdd:PLN03237  457 TEGDSAKALAVAGLSVVGRnyyGVFPLRGKLLNVREASHKQIMNNAEIENIKQILGLQHGKQYESVKsLRYGHLMIMTD 535
TOPRIM_TopoIIA cd03365
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ...
335-408 4.05e-13

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: 65.40  E-value: 4.05e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190148862 335 EGDSAGGSAKSGRDSM---TQAILPIRGKIINVEKARIDRVLKNTEVQAIITALGTGI--HDEFDLAKLRYHKIVLMTD 408
Cdd:cd03365    7 EGDSAKALAVAGLSVVgrdYYGVFPLRGKLLNVREASHKQIMENAEIQNIKKILGLQHgkSDYESTKSLRYGRLMIMTD 85
Toprim pfam01751
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ...
330-409 2.46e-09

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: 53.90  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190148862  330 EVYIVEGDSAGGSAKSGRDSMTQAILPIRGKIINVEKARIDRVLKntevqaiitalgtgihdEFDLAKLRYHKIVLMTDA 409
Cdd:pfam01751   1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALK-----------------ALKELALKAKEVILATDP 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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