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Conserved domains on  [gi|357380337|pdb|2XX4|A]
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Chain A, ATP-DEPENDENT MOLECULAR CHAPERONE HSP82

Protein Classification

ATP-binding protein; sensor histidine kinase( domain architecture ID 13014549)

ATP-binding protein containing histidine kinase-like ATPase domain, similar to Streptomyces subrutilus DNA gyrase an an essential bacterial enzyme that catalyzes the ATP-dependent negative super-coiling of double-stranded closed-circular DNA; sensor histidine kinase, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals; contains a RisS-like periplasmic domain and may contain a HAMP domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HATPase_Hsp90-like cd16927
Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including ...
14-201 2.24e-109

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: 311.38  E-value: 2.24e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       14 QLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNL 93
Cdd:cd16927   2 QLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGIGMTKEELINNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       94 GTIAKSGTKAFMEALSAGA-DVSMIGQFGVGFYSLFLVADRVQVISKSN-DDEQYIWESNAGGSFTVTldEVNERIGRGT 171
Cdd:cd16927  82 GTIARSGTKAFLEALQEGAkDSDLIGQFGVGFYSAFMVADKVTVTTKSAgDDEGYRWESDGGGSYTIE--EAEGELGRGT 159
                       170       180       190
                ....*....|....*....|....*....|
2XX4_A      172 ILRLFLKDDQLEYLEEKRIKEVIKRHSEFV 201
Cdd:cd16927 160 KITLHLKEDAKEFLEEARIKELVKKYSDFI 189
 
Name Accession Description Interval E-value
HATPase_Hsp90-like cd16927
Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including ...
14-201 2.24e-109

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: 311.38  E-value: 2.24e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       14 QLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNL 93
Cdd:cd16927   2 QLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGIGMTKEELINNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       94 GTIAKSGTKAFMEALSAGA-DVSMIGQFGVGFYSLFLVADRVQVISKSN-DDEQYIWESNAGGSFTVTldEVNERIGRGT 171
Cdd:cd16927  82 GTIARSGTKAFLEALQEGAkDSDLIGQFGVGFYSAFMVADKVTVTTKSAgDDEGYRWESDGGGSYTIE--EAEGELGRGT 159
                       170       180       190
                ....*....|....*....|....*....|
2XX4_A      172 ILRLFLKDDQLEYLEEKRIKEVIKRHSEFV 201
Cdd:cd16927 160 KITLHLKEDAKEFLEEARIKELVKKYSDFI 189
PTZ00272 PTZ00272
heat shock protein 83 kDa (Hsp83); Provisional
3-214 5.87e-104

heat shock protein 83 kDa (Hsp83); Provisional


Pssm-ID: 240341  Cd Length: 701  Bit Score: 314.69  E-value: 5.87e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         3 SETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGI 82
Cdd:PTZ00272   2 TETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKENKTLTVEDNGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        83 GMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTlDE 162
Cdd:PTZ00272  82 GMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNNSDESYVWESSAGGTFTIT-ST 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
2XX4_A       163 VNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:PTZ00272 161 PESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKTTE 212
HtpG COG0326
Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, ...
1-214 3.71e-97

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


Pssm-ID: 440095 [Multi-domain]  Cd Length: 616  Bit Score: 294.72  E-value: 3.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        1 MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDS 80
Cdd:COG0326   1 MAKETGEFQAEVKQLLDLMIHSLYSNKEIFLRELISNASDAIDKLRFLALTDPELKEEDGDLKIRIEVDKEAKTLTISDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       81 GIGMTKAELINNLGTIAKSGTKAFMEALS--AGADVSMIGQFGVGFYSLFLVADRVQVISKS--NDDEQYIWESNAGGSF 156
Cdd:COG0326  81 GIGMTREEVIENLGTIAKSGTREFLEKLKgdQKKDSDLIGQFGVGFYSAFMVADKVEVVTRSagEDAEAVRWESDGDGEY 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
2XX4_A      157 TVtldEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:COG0326 161 TI---EEAEKAERGTEITLHLKEDAEEFLEEWRLREIIKKYSDFIPVPIKMEGEEEET 215
HSP90 pfam00183
Hsp90 protein;
183-214 7.24e-11

Hsp90 protein;


Pssm-ID: 459703  Cd Length: 516  Bit Score: 60.65  E-value: 7.24e-11
                          10        20        30
                  ....*....|....*....|....*....|..
2XX4_A        183 EYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:pfam00183   1 EYLEEKKIKELVKKYSEFINFPIYLWVEKEEE 32
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
26-161 2.06e-09

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 53.42  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A          26 NKEIFLRELISNASDALdkIRYKslsdpkqlETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELinnlgtiaksgTKAFM 105
Cdd:smart00387   1 GDPDRLRQVLSNLLDNA--IKYT--------PEGGRITVTLERDGDHVEITVEDNGPGIPPEDL-----------EKIFE 59
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
2XX4_A         106 EALSAGADVSMIGQFGVGFYSLFLVADRVQV-ISKSNDDEQyiwesnaGGSFTVTLD 161
Cdd:smart00387  60 PFFRTDKRSRKIGGTGLGLSIVKKLVELHGGeISVESEPGG-------GTTFTITLP 109
 
Name Accession Description Interval E-value
HATPase_Hsp90-like cd16927
Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including ...
14-201 2.24e-109

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: 311.38  E-value: 2.24e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       14 QLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNL 93
Cdd:cd16927   2 QLLDLIIHSLYSNKEIFLRELISNASDALDKLRYLSLTDPSLLDDDPELEIRISPDKENRTLTISDTGIGMTKEELINNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       94 GTIAKSGTKAFMEALSAGA-DVSMIGQFGVGFYSLFLVADRVQVISKSN-DDEQYIWESNAGGSFTVTldEVNERIGRGT 171
Cdd:cd16927  82 GTIARSGTKAFLEALQEGAkDSDLIGQFGVGFYSAFMVADKVTVTTKSAgDDEGYRWESDGGGSYTIE--EAEGELGRGT 159
                       170       180       190
                ....*....|....*....|....*....|
2XX4_A      172 ILRLFLKDDQLEYLEEKRIKEVIKRHSEFV 201
Cdd:cd16927 160 KITLHLKEDAKEFLEEARIKELVKKYSDFI 189
PTZ00272 PTZ00272
heat shock protein 83 kDa (Hsp83); Provisional
3-214 5.87e-104

heat shock protein 83 kDa (Hsp83); Provisional


Pssm-ID: 240341  Cd Length: 701  Bit Score: 314.69  E-value: 5.87e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         3 SETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGI 82
Cdd:PTZ00272   2 TETFAFQAEINQLMSLIINTFYSNKEIFLRELISNASDACDKIRYQSLTDPSVLGESPRLCIRVVPDKENKTLTVEDNGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        83 GMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTlDE 162
Cdd:PTZ00272  82 GMTKADLVNNLGTIARSGTKAFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVTSKNNSDESYVWESSAGGTFTIT-ST 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
2XX4_A       163 VNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:PTZ00272 161 PESDMKRGTRITLHLKEDQMEYLEPRRLKELIKKHSEFIGYDIELMVEKTTE 212
PRK05218 PRK05218
heat shock protein 90; Provisional
1-212 8.55e-98

heat shock protein 90; Provisional


Pssm-ID: 235366 [Multi-domain]  Cd Length: 613  Bit Score: 296.25  E-value: 8.55e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         1 MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDS 80
Cdd:PRK05218   1 MAMETGEFQAEVKQLLHLMIHSLYSNKEIFLRELISNASDAIDKLRFEALTDPALYEGDGDLKIRISFDKEARTLTISDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        81 GIGMTKAELINNLGTIAKSGTKAFMEALS--AGADVSMIGQFGVGFYSLFLVADRVQVISKS--NDDEQYIWESNAGGSF 156
Cdd:PRK05218  81 GIGMTREEVIENLGTIAKSGTKEFLEKLKgdQKKDSQLIGQFGVGFYSAFMVADKVTVITRSagPAAEAVRWESDGEGEY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
2XX4_A       157 TVtlDEVnERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKE 212
Cdd:PRK05218 161 TI--EEI-EKEERGTEITLHLKEDEDEFLDEWRIRSIIKKYSDFIPVPIKLEKEEE 213
HtpG COG0326
Molecular chaperone, HSP90 family [Posttranslational modification, protein turnover, ...
1-214 3.71e-97

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


Pssm-ID: 440095 [Multi-domain]  Cd Length: 616  Bit Score: 294.72  E-value: 3.71e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        1 MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDS 80
Cdd:COG0326   1 MAKETGEFQAEVKQLLDLMIHSLYSNKEIFLRELISNASDAIDKLRFLALTDPELKEEDGDLKIRIEVDKEAKTLTISDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       81 GIGMTKAELINNLGTIAKSGTKAFMEALS--AGADVSMIGQFGVGFYSLFLVADRVQVISKS--NDDEQYIWESNAGGSF 156
Cdd:COG0326  81 GIGMTREEVIENLGTIAKSGTREFLEKLKgdQKKDSDLIGQFGVGFYSAFMVADKVEVVTRSagEDAEAVRWESDGDGEY 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
2XX4_A      157 TVtldEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:COG0326 161 TI---EEAEKAERGTEITLHLKEDAEEFLEEWRLREIIKKYSDFIPVPIKMEGEEEET 215
PTZ00130 PTZ00130
heat shock protein 90; Provisional
4-213 1.77e-73

heat shock protein 90; Provisional


Pssm-ID: 185466 [Multi-domain]  Cd Length: 814  Bit Score: 237.25  E-value: 1.77e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         4 ETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIG 83
Cdd:PTZ00130  66 EQHQYQTEVTRLMDIIVNSLYTQKEVFLRELISNAADALEKIRFLSLSDESVLGEEKKLEIRISANKEKNILSITDTGIG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        84 MTKAELINNLGTIAKSGTKAFMEALS-AGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDE 162
Cdd:PTZ00130 146 MTKEDLINNLGTIAKSGTSNFLEAISkSGGDMSLIGQFGVGFYSAFLVADKVIVYTKNNNDEQYIWESTADAKFTIYKDP 225
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
2XX4_A       163 VNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQL----VVTKEV 213
Cdd:PTZ00130 226 RGSTLKRGTRISLHLKEDATNLMNDKKLVDLISKYSQFIQYPIYLlhenVYTEEV 280
PRK14083 PRK14083
HSP90 family protein; Provisional
8-212 2.08e-29

HSP90 family protein; Provisional


Pssm-ID: 237603 [Multi-domain]  Cd Length: 601  Bit Score: 114.27  E-value: 2.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         8 FQAEITQLMSLIINTVYSNKEIFLRELISNASDAldkIRYKSLSDPkqlETEPDlfIRITP-KPEQKVLEIRDSGIGMTK 86
Cdd:PRK14083   5 FQVDLRGVIDLLSRHLYSSPRVYVRELLQNAVDA---ITARRALDP---TAPGR--IRIELtDAGGGTLIVEDNGIGLTE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A        87 AELINNLGTIAKSGTKAfmEALSAGADvSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYI-WESNAGGSFTVTLDEVnE 165
Cdd:PRK14083  77 EEVHEFLATIGRSSKRD--ENLGFARN-DFLGQFGIGLLSCFLVADEIVVVSRSAKDGPAVeWRGKADGTYSVRKLET-E 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2XX4_A       166 RIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKE 212
Cdd:PRK14083 153 RAEPGTTVYLRPRPDAEEWLERETVEELAKKYGSLLPVPIRVEGEKG 199
HSP90 pfam00183
Hsp90 protein;
183-214 7.24e-11

Hsp90 protein;


Pssm-ID: 459703  Cd Length: 516  Bit Score: 60.65  E-value: 7.24e-11
                          10        20        30
                  ....*....|....*....|....*....|..
2XX4_A        183 EYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVE 214
Cdd:pfam00183   1 EYLEEKKIKELVKKYSEFINFPIYLWVEKEEE 32
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
26-161 2.06e-09

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 53.42  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A          26 NKEIFLRELISNASDALdkIRYKslsdpkqlETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELinnlgtiaksgTKAFM 105
Cdd:smart00387   1 GDPDRLRQVLSNLLDNA--IKYT--------PEGGRITVTLERDGDHVEITVEDNGPGIPPEDL-----------EKIFE 59
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
2XX4_A         106 EALSAGADVSMIGQFGVGFYSLFLVADRVQV-ISKSNDDEQyiwesnaGGSFTVTLD 161
Cdd:smart00387  60 PFFRTDKRSRKIGGTGLGLSIVKKLVELHGGeISVESEPGG-------GTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
26-181 2.50e-05

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: 41.97  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         26 NKEIFLRELISNASDALDKIRYKslsdpkqletEPDLFIRITPKpEQKVLEIRDSGIGMTKaELINNLGTiaksgtkAFM 105
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAK----------AGEITVTLSEG-GELTLTVEDNGIGIPP-EDLPRIFE-------PFS 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2XX4_A        106 EalsagADVSMIGQFGVGFYslflvadrvqvISKSnddeqyIWESnAGGSFTVTldevnERIGRGTILRLFLKDDQ 181
Cdd:pfam02518  62 T-----ADKRGGGGTGLGLS-----------IVRK------LVEL-LGGTITVE-----SEPGGGTTVTLTLPLAQ 109
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
68-145 2.52e-03

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: 36.93  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A         68 PKPEQKVLEIR--DSGIGMTKAELINNLGtIAKSGTKAfmealSAGADVsmIGQFGVG--FYSLFLVADrVQVISKSNDD 143
Cdd:pfam13589  25 NKNRGGGTEIVieDDGHGMSPEELINALR-LATSAKEA-----KRGSTD--LGRYGIGlkLASLSLGAK-LTVTSKKEGK 95

                  ..
2XX4_A        144 EQ 145
Cdd:pfam13589  96 SS 97
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
31-126 4.38e-03

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 35.85  E-value: 4.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2XX4_A       31 LRELISNASDALdkirykslsdpkqlETEPDLFI-RITPKPEQKVLEIRDSGIGMTKAELINNLGtiaksgtkaFMEALS 109
Cdd:cd16931  16 VAELVDNARDAD--------------ATRLDIFIdDINLLRGGFMLSFLDDGNGMTPEEAHHMIS---------FGFSDK 72
                        90
                ....*....|....*..
2XX4_A      110 AGADVSMIGQFGVGFYS 126
Cdd:cd16931  73 RSDDHDHIGRYGNGFKS 89
 
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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