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Conserved domains on  [gi|308388149]
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Chain B, Heat shock protein 83

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSP90 super family cl46693
Hsp90 protein;
19-231 1.75e-162

Hsp90 protein;


The actual alignment was detected with superfamily member PTZ00272:

Pssm-ID: 481033  Cd Length: 701  Bit Score: 465.69  E-value: 1.75e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:PTZ00272   1 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKENKTLTVEDNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDDAYTWESSAGGTFTVTST 178
Cdd:PTZ00272  81 IGMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNNSDESYVWESSAGGTFTITST 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308388149 179 PDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:PTZ00272 161 PESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKTTEK 213
 
Name Accession Description Interval E-value
PTZ00272 PTZ00272
heat shock protein 83 kDa (Hsp83); Provisional
19-231 1.75e-162

heat shock protein 83 kDa (Hsp83); Provisional


Pssm-ID: 240341  Cd Length: 701  Bit Score: 465.69  E-value: 1.75e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:PTZ00272   1 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKENKTLTVEDNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDDAYTWESSAGGTFTVTST 178
Cdd:PTZ00272  81 IGMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNNSDESYVWESSAGGTFTITST 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308388149 179 PDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:PTZ00272 161 PESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKTTEK 213
HATPase_Hsp90-like cd16927
Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including ...
30-217 6.52e-117

Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including Escherichia coli HtpG, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of 90 kilodalton heat-shock protein (Hsp90) eukaryotic homologs including cytosolic Hsp90, mitochondrial TRAP1 (tumor necrosis factor receptor-associated protein 1), GRP94 (94 kDa glucose-regulated protein) of the endoplasmic reticulum (ER), and chloroplast Hsp90C. It also includes the bacterial homologs of Hsp90, known as HtpG (High temperature protein G). Hsp90 family of chaperones assist other proteins to fold correctly, stabilizes them against heat stress, and aids in protein degradation.


Pssm-ID: 340404 [Multi-domain]  Cd Length: 189  Bit Score: 331.02  E-value: 6.52e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  30 NQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSGIGMTKADLVNN 109
Cdd:cd16927    1 NQLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGIGMTKEELINN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149 110 LGTIARSGTKSFMEAL-EAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDD-AYTWESSAGGTFTVTSTPDcDLKRGT 187
Cdd:cd16927   81 LGTIARSGTKAFLEALqEGAKDSDLIGQFGVGFYSAFMVADKVTVTTKSAGDDeGYRWESDGGGSYTIEEAEG-ELGRGT 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 308388149 188 RIVLHLKEDQQEYLEERRLKDLIKKHSEFI 217
Cdd:cd16927  160 KITLHLKEDAKEFLEEARIKELVKKYSDFI 189
HtpG COG0326
Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, ...
19-231 3.26e-103

Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440095 [Multi-domain]  Cd Length: 616  Bit Score: 310.90  E-value: 3.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:COG0326    2 AKETGEFQAEVKQLLDLMIHSLYSNKEIFLRELISNASDAIDKLRFLALTDPELKEEDGDLKIRIEVDKEAKTLTISDNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEAL--EAGGDMSMIGQFGVGFYSAYLVADRVTVVSK--NNEDDAYTWESSAGGTFT 174
Cdd:COG0326   82 IGMTREEVIENLGTIAKSGTREFLEKLkgDQKKDSDLIGQFGVGFYSAFMVADKVEVVTRsaGEDAEAVRWESDGDGEYT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308388149 175 VTSTPdcDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:COG0326  162 IEEAE--KAERGTEITLHLKEDAEEFLEEWRLREIIKKYSDFIPVPIKMEGEEEETE 216
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
43-194 2.71e-12

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 61.13  E-value: 2.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149    43 NKEIFLRELISNSSDACDKIRyqsltnqsvlGDEPHLRIRVIPDRVNKTLTVEDSGIGMTKADLvnnlgtiarsgTKSFM 122
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYT----------PEGGRITVTLERDGDHVEITVEDNGPGIPPEDL-----------EKIFE 59
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308388149   123 EALEAGGDMSMIGQFGVGFYSAYLVADRVtvvsknneddaytwessaGGTFTVTSTPdcdlKRGTRIVLHLK 194
Cdd:smart00387  60 PFFRTDKRSRKIGGTGLGLSIVKKLVELH------------------GGEISVESEP----GGGTTFTITLP 109
HSP90 pfam00183
Hsp90 protein;
199-231 2.01e-11

Hsp90 protein;


Pssm-ID: 459703  Cd Length: 516  Bit Score: 62.96  E-value: 2.01e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 308388149  199 EYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:pfam00183   1 EYLEEKKIKELVKKYSEFINFPIYLWVEKEEEV 33
 
Name Accession Description Interval E-value
PTZ00272 PTZ00272
heat shock protein 83 kDa (Hsp83); Provisional
19-231 1.75e-162

heat shock protein 83 kDa (Hsp83); Provisional


Pssm-ID: 240341  Cd Length: 701  Bit Score: 465.69  E-value: 1.75e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:PTZ00272   1 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKENKTLTVEDNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDDAYTWESSAGGTFTVTST 178
Cdd:PTZ00272  81 IGMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNNSDESYVWESSAGGTFTITST 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 308388149 179 PDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:PTZ00272 161 PESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKTTEK 213
HATPase_Hsp90-like cd16927
Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including ...
30-217 6.52e-117

Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including Escherichia coli HtpG, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of 90 kilodalton heat-shock protein (Hsp90) eukaryotic homologs including cytosolic Hsp90, mitochondrial TRAP1 (tumor necrosis factor receptor-associated protein 1), GRP94 (94 kDa glucose-regulated protein) of the endoplasmic reticulum (ER), and chloroplast Hsp90C. It also includes the bacterial homologs of Hsp90, known as HtpG (High temperature protein G). Hsp90 family of chaperones assist other proteins to fold correctly, stabilizes them against heat stress, and aids in protein degradation.


Pssm-ID: 340404 [Multi-domain]  Cd Length: 189  Bit Score: 331.02  E-value: 6.52e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  30 NQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSGIGMTKADLVNN 109
Cdd:cd16927    1 NQLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGIGMTKEELINN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149 110 LGTIARSGTKSFMEAL-EAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDD-AYTWESSAGGTFTVTSTPDcDLKRGT 187
Cdd:cd16927   81 LGTIARSGTKAFLEALqEGAKDSDLIGQFGVGFYSAFMVADKVTVTTKSAGDDeGYRWESDGGGSYTIEEAEG-ELGRGT 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 308388149 188 RIVLHLKEDQQEYLEERRLKDLIKKHSEFI 217
Cdd:cd16927  160 KITLHLKEDAKEFLEEARIKELVKKYSDFI 189
PRK05218 PRK05218
heat shock protein 90; Provisional
19-228 5.15e-105

heat shock protein 90; Provisional


Pssm-ID: 235366 [Multi-domain]  Cd Length: 613  Bit Score: 315.51  E-value: 5.15e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:PRK05218   2 AMETGEFQAEVKQLLHLMIHSLYSNKEIFLRELISNASDAIDKLRFEALTDPALYEGDGDLKIRISFDKEARTLTISDNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEAL--EAGGDMSMIGQFGVGFYSAYLVADRVTVVSK--NNEDDAYTWESSAGGTFT 174
Cdd:PRK05218  82 IGMTREEVIENLGTIAKSGTKEFLEKLkgDQKKDSQLIGQFGVGFYSAFMVADKVTVITRsaGPAAEAVRWESDGEGEYT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308388149 175 VTSTPDCDlkRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENT 228
Cdd:PRK05218 162 IEEIEKEE--RGTEITLHLKEDEDEFLDEWRIRSIIKKYSDFIPVPIKLEKEEE 213
HtpG COG0326
Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, ...
19-231 3.26e-103

Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440095 [Multi-domain]  Cd Length: 616  Bit Score: 310.90  E-value: 3.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  19 MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSG 98
Cdd:COG0326    2 AKETGEFQAEVKQLLDLMIHSLYSNKEIFLRELISNASDAIDKLRFLALTDPELKEEDGDLKIRIEVDKEAKTLTISDNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  99 IGMTKADLVNNLGTIARSGTKSFMEAL--EAGGDMSMIGQFGVGFYSAYLVADRVTVVSK--NNEDDAYTWESSAGGTFT 174
Cdd:COG0326   82 IGMTREEVIENLGTIAKSGTREFLEKLkgDQKKDSDLIGQFGVGFYSAFMVADKVEVVTRsaGEDAEAVRWESDGDGEYT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308388149 175 VTSTPdcDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:COG0326  162 IEEAE--KAERGTEITLHLKEDAEEFLEEWRLREIIKKYSDFIPVPIKMEGEEEETE 216
PTZ00130 PTZ00130
heat shock protein 90; Provisional
21-227 2.21e-78

heat shock protein 90; Provisional


Pssm-ID: 185466 [Multi-domain]  Cd Length: 814  Bit Score: 251.11  E-value: 2.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  21 ETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSGIG 100
Cdd:PTZ00130  66 EQHQYQTEVTRLMDIIVNSLYTQKEVFLRELISNAADALEKIRFLSLSDESVLGEEKKLEIRISANKEKNILSITDTGIG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149 101 MTKADLVNNLGTIARSGTKSFMEAL-EAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDDAYTWESSAGGTFTVTSTP 179
Cdd:PTZ00130 146 MTKEDLINNLGTIAKSGTSNFLEAIsKSGGDMSLIGQFGVGFYSAFLVADKVIVYTKNNNDEQYIWESTADAKFTIYKDP 225
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 308388149 180 -DCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVEN 227
Cdd:PTZ00130 226 rGSTLKRGTRISLHLKEDATNLMNDKKLVDLISKYSQFIQYPIYLLHEN 274
PRK14083 PRK14083
HSP90 family protein; Provisional
24-229 6.27e-33

HSP90 family protein; Provisional


Pssm-ID: 237603 [Multi-domain]  Cd Length: 601  Bit Score: 125.05  E-value: 6.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  24 AFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNqsvlgdEPHLRIRvIPDRVNKTLTVEDSGIGMTK 103
Cdd:PRK14083   4 RFQVDLRGVIDLLSRHLYSSPRVYVRELLQNAVDAITARRALDPTA------PGRIRIE-LTDAGGGTLIVEDNGIGLTE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149 104 ADLVNNLGTIARSgTKSFMEALEAGGDMsmIGQFGVGFYSAYLVADRVTVVSKNNED-DAYTWESSAGGTFTVTSTPDCD 182
Cdd:PRK14083  77 EEVHEFLATIGRS-SKRDENLGFARNDF--LGQFGIGLLSCFLVADEIVVVSRSAKDgPAVEWRGKADGTYSVRKLETER 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 308388149 183 LKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTT 229
Cdd:PRK14083 154 AEPGTTVYLRPRPDAEEWLERETVEELAKKYGSLLPVPIRVEGEKGG 200
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
43-194 2.71e-12

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 61.13  E-value: 2.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149    43 NKEIFLRELISNSSDACDKIRyqsltnqsvlGDEPHLRIRVIPDRVNKTLTVEDSGIGMTKADLvnnlgtiarsgTKSFM 122
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYT----------PEGGRITVTLERDGDHVEITVEDNGPGIPPEDL-----------EKIFE 59
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308388149   123 EALEAGGDMSMIGQFGVGFYSAYLVADRVtvvsknneddaytwessaGGTFTVTSTPdcdlKRGTRIVLHLK 194
Cdd:smart00387  60 PFFRTDKRSRKIGGTGLGLSIVKKLVELH------------------GGEISVESEP----GGGTTFTITLP 109
HSP90 pfam00183
Hsp90 protein;
199-231 2.01e-11

Hsp90 protein;


Pssm-ID: 459703  Cd Length: 516  Bit Score: 62.96  E-value: 2.01e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 308388149  199 EYLEERRLKDLIKKHSEFIGYDIELMVENTTEK 231
Cdd:pfam00183   1 EYLEEKKIKELVKKYSEFINFPIYLWVEKEEEV 33
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
43-197 6.21e-09

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 51.99  E-value: 6.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149   43 NKEIFLRELISNSSDACDKIRyqsltnqsvlGDEPHLRIRVIPDrVNKTLTVEDSGIGMTKADLvnnlgtiARSGTKsFM 122
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHA----------AKAGEITVTLSEG-GELTLTVEDNGIGIPPEDL-------PRIFEP-FS 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308388149  123 EAleaggDMSMIGQFGVGFYSAYLVADRVtvvsknneddaytwessaGGTFTVTSTPDcdlkRGTRIVLHLKEDQ 197
Cdd:pfam02518  62 TA-----DKRGGGGTGLGLSIVRKLVELL------------------GGTITVESEPG----GGTTVTLTLPLAQ 109
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
45-165 5.07e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 41.93  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149   45 EIFLRELISNSSDAcdkiryqsltnqsvlgDEPHLRIRVIPDRVNKT-LTVEDSGIGMTKADLVNNLGtIARSGTksfme 123
Cdd:pfam13589   2 EGALAELIDNSIDA----------------DATNIKIEVNKNRGGGTeIVIEDDGHGMSPEELINALR-LATSAK----- 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 308388149  124 alEAGGDMSMIGQFGVGFYSAYLVADR-VTVVSKNNED-DAYTW 165
Cdd:pfam13589  60 --EAKRGSTDLGRYGIGLKLASLSLGAkLTVTSKKEGKsSTLTL 101
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
49-227 1.04e-03

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 38.87  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149  49 RELISNSSDACDKIryqsltnqsvlGDEPHLRIRVipDRVNK---TLTVEDSGIGMTKADLVNNLGTIArSGTKSFMEAL 125
Cdd:cd16933   25 RELVENSLDATEEA-----------GILPDIKVEI--EEIGKdhyKVIVEDNGPGIPEEQIPKVFGKVL-YGSKYHNKQS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308388149 126 EaggdmsmiGQFGVGFYSAYLVADR-----VTVVSKNNEDDAYTWE-------SSAGGTFTVTSTPDCDLKRGTRIVLHL 193
Cdd:cd16933   91 R--------GQQGLGISAAVLYSQMttgkpVEIISSTKDSNYAYVVklmidtdKNEPEILEKEEVENRYKWHGTRVELEL 162
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 308388149 194 KED-----QQEYLEERRLKdLIKKHSEFIGYDIELMVEN 227
Cdd:cd16933  163 EGNwvaarSQILEYYKRTA-VIAPYAEIIFIVPDGETEV 200
 
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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