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Conserved domains on  [gi|1802031267|gb|QHP23722|]
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DNA helicase (plasmid) [Klebsiella pneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
41 super family cl29348
41 helicase; Provisional
 43-412 6.61e-28

41 helicase; Provisional


The actual alignment was detected with superfamily member PHA02542:

Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 115.54  E-value: 6.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267  43 PNQFSNAANAILVNMVSGYFRMYKSAPSSAAILDMLKRakrdKTIREEMFPDVVAAFKRmLSEKLSDTAYMVDQVATFAK 122
Cdd:PHA02542   25 AEYFESGPEKVIFKLIKKHVNEYNAIPTIEALSIALEN----RSLSEVTFDGAKDLLSS-LSDNPEDLDWLVKETEKWCQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 123 SVAFDDALIKAAEMKEKGDFQ-----------GAM-AIMAKVQQIGSNEATGIyDYYASAAERYKAreYEASDDYVPNSi 190
Cdd:PHA02542  100 DRAMYNALSKAIEIQDNADKPlekrnkklpdvGAIpDIMQEALAISFDSSVGH-DYFEDYEERYDS--YQSKANKIPFK- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 191 ttgLPLLDRMlyQKGWAKREMV-LFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEVHTSILSDRFDARLSETEMSKLV 269
Cdd:PHA02542  176 ---LEILNKI--TKGGAERKTLnVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEEVIAKRIDANLLDVSLDDID 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 E-QRDDVHRKLAEIGAtKGVGNLWVVERPSGSMSPADLDRMLNSMK-ANGMIPDMVVVDYADLMrASYDLRDDRAN---- 343
Cdd:PHA02542  251 DlSKAEYKAKMEKLRS-KTQGKLIIKQYPTGGAHAGHFRALLNELKlKKNFKPDVIIVDYLGIC-ASSRLRVSSENsyty 328

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802031267 344 IRSIYTDLRALYDKHNVAGITASQTNREGGSSEVATMMHAADNIEKVRIADLVITINKTEEEEAKGEAR 412
Cdd:PHA02542  329 VKAIAEELRGLAVEHDVVVWTAAQTTRSGWDSSDVDMSDTAESAGLPATADFMLAVIETEELAQMGQQL 397
 
Name Accession Description Interval E-value
41 PHA02542
41 helicase; Provisional
 43-412 6.61e-28

41 helicase; Provisional


Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 115.54  E-value: 6.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267  43 PNQFSNAANAILVNMVSGYFRMYKSAPSSAAILDMLKRakrdKTIREEMFPDVVAAFKRmLSEKLSDTAYMVDQVATFAK 122
Cdd:PHA02542   25 AEYFESGPEKVIFKLIKKHVNEYNAIPTIEALSIALEN----RSLSEVTFDGAKDLLSS-LSDNPEDLDWLVKETEKWCQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 123 SVAFDDALIKAAEMKEKGDFQ-----------GAM-AIMAKVQQIGSNEATGIyDYYASAAERYKAreYEASDDYVPNSi 190
Cdd:PHA02542  100 DRAMYNALSKAIEIQDNADKPlekrnkklpdvGAIpDIMQEALAISFDSSVGH-DYFEDYEERYDS--YQSKANKIPFK- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 191 ttgLPLLDRMlyQKGWAKREMV-LFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEVHTSILSDRFDARLSETEMSKLV 269
Cdd:PHA02542  176 ---LEILNKI--TKGGAERKTLnVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEEVIAKRIDANLLDVSLDDID 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 E-QRDDVHRKLAEIGAtKGVGNLWVVERPSGSMSPADLDRMLNSMK-ANGMIPDMVVVDYADLMrASYDLRDDRAN---- 343
Cdd:PHA02542  251 DlSKAEYKAKMEKLRS-KTQGKLIIKQYPTGGAHAGHFRALLNELKlKKNFKPDVIIVDYLGIC-ASSRLRVSSENsyty 328

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802031267 344 IRSIYTDLRALYDKHNVAGITASQTNREGGSSEVATMMHAADNIEKVRIADLVITINKTEEEEAKGEAR 412
Cdd:PHA02542  329 VKAIAEELRGLAVEHDVVVWTAAQTTRSGWDSSDVDMSDTAESAGLPATADFMLAVIETEELAQMGQQL 397
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
190-387 3.85e-10

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 59.54  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLYQkGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEVHTSILSDRfdARLSETEMSKLV 269
Cdd:COG0467     2 VPTGIPGLDELLGG-GLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRR--AESLGLDLEEYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 EQrddvhrklaeigatkgvGNLWVVERPSGSM--SPADL-DRMLNSMKANGmiPDMVVVD-YADLMRASYDLRDDRANIR 345
Cdd:COG0467    79 ES-----------------GLLRIIDLSPEELglDLEELlARLREAVEEFG--AKRVVIDsLSGLLLALPDPERLREFLH 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1802031267 346 SIYTDLRalydKHNVAGITASQTNREGGSSEVATMMHAADNI 387
Cdd:COG0467   140 RLLRYLK----KRGVTTLLTSETGGLEDEATEGGLSYLADGV 177
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 190-440 7.58e-09

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 56.37  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLyqKGWAKREMVLFMGFAKSGKSTAMGEFSINATL-AGYNVLYLSLEVHTSILSDRFDARLSETEMSKL 268
Cdd:cd00984     2 LPTGFTDLDKLT--GGLQPGDLIIIAARPSMGKTAFALNIAENIALdEGLPVLFFSLEMSAEQLAERLLSSESGVSLSKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 269 ---VEQRDDVHR------KLAEIgatkgvgNLWVVERPSgsMSPADLDRMLNSMKANGMIPDMVVVDYADLMRASyDLRD 339
Cdd:cd00984    80 rtgRLDDEDWERltaamgELSEL-------PLYIDDTPG--LTVDEIRAKARRLKREHGGLGLIVIDYLQLIRGS-KRAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 340 DRAN-IRSIYTDLRALYDKHNVAGITASQTNR--EGGSSEVATMmhaADNIEKVRI---ADLVITINKTE----EEEAKG 409
Cdd:cd00984   150 NRQQeVAEISRSLKALAKELNVPVIALSQLNRgvESRTDKRPML---SDLRESGSIeqdADVVIFLYRDEyydkDSEDKG 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1802031267 410 EARLYFAGSRNQKGGvSIRVKQNLEQMRFIE 440
Cdd:cd00984   227 IAEIIIAKNRNGPTG-TVYLAFNPEYTRFTD 256
DnaB_C pfam03796
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ...
 190-371 5.76e-05

DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 427509 [Multi-domain]  Cd Length: 254  Bit Score: 44.33  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLYqkGWAKREMVLFMGFAKSGKSTamgeFSIN-----ATLAGYNVLYLSLE------------VHTSIL 252
Cdd:pfam03796   2 LPTGFTDLDRLTG--GLQPGDLIIIAARPSMGKTA----FALNiarnaAVKHKKPVAIFSLEmsaeqlvmrllaSEAGVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 253 SDRF-DARLSETEMSKLVEQRDDVHRKlaeigatkgvgNLWVVERPSgsMSPADLDRMLNSMKANGMIpDMVVVDYADLM 331
Cdd:pfam03796  76 SQKLrTGQLTDEDWEKLAKAAGRLSEA-----------PLYIDDTPG--LSIAEIRAKARRLKREHGL-GLIVIDYLQLM 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1802031267 332 RASYDlRDDRAN-IRSIYTDLRALYDKHNVAGITASQTNRE 371
Cdd:pfam03796 142 SGGSR-GENRQQeISEISRSLKALAKELNVPVIALSQLSRA 181
 
Name Accession Description Interval E-value
41 PHA02542
41 helicase; Provisional
 43-412 6.61e-28

41 helicase; Provisional


Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 115.54  E-value: 6.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267  43 PNQFSNAANAILVNMVSGYFRMYKSAPSSAAILDMLKRakrdKTIREEMFPDVVAAFKRmLSEKLSDTAYMVDQVATFAK 122
Cdd:PHA02542   25 AEYFESGPEKVIFKLIKKHVNEYNAIPTIEALSIALEN----RSLSEVTFDGAKDLLSS-LSDNPEDLDWLVKETEKWCQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 123 SVAFDDALIKAAEMKEKGDFQ-----------GAM-AIMAKVQQIGSNEATGIyDYYASAAERYKAreYEASDDYVPNSi 190
Cdd:PHA02542  100 DRAMYNALSKAIEIQDNADKPlekrnkklpdvGAIpDIMQEALAISFDSSVGH-DYFEDYEERYDS--YQSKANKIPFK- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 191 ttgLPLLDRMlyQKGWAKREMV-LFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEVHTSILSDRFDARLSETEMSKLV 269
Cdd:PHA02542  176 ---LEILNKI--TKGGAERKTLnVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEEVIAKRIDANLLDVSLDDID 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 E-QRDDVHRKLAEIGAtKGVGNLWVVERPSGSMSPADLDRMLNSMK-ANGMIPDMVVVDYADLMrASYDLRDDRAN---- 343
Cdd:PHA02542  251 DlSKAEYKAKMEKLRS-KTQGKLIIKQYPTGGAHAGHFRALLNELKlKKNFKPDVIIVDYLGIC-ASSRLRVSSENsyty 328

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802031267 344 IRSIYTDLRALYDKHNVAGITASQTNREGGSSEVATMMHAADNIEKVRIADLVITINKTEEEEAKGEAR 412
Cdd:PHA02542  329 VKAIAEELRGLAVEHDVVVWTAAQTTRSGWDSSDVDMSDTAESAGLPATADFMLAVIETEELAQMGQQL 397
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
190-387 3.85e-10

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 59.54  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLYQkGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEVHTSILSDRfdARLSETEMSKLV 269
Cdd:COG0467     2 VPTGIPGLDELLGG-GLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRR--AESLGLDLEEYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 EQrddvhrklaeigatkgvGNLWVVERPSGSM--SPADL-DRMLNSMKANGmiPDMVVVD-YADLMRASYDLRDDRANIR 345
Cdd:COG0467    79 ES-----------------GLLRIIDLSPEELglDLEELlARLREAVEEFG--AKRVVIDsLSGLLLALPDPERLREFLH 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1802031267 346 SIYTDLRalydKHNVAGITASQTNREGGSSEVATMMHAADNI 387
Cdd:COG0467   140 RLLRYLK----KRGVTTLLTSETGGLEDEATEGGLSYLADGV 177
PRK06904 PRK06904
replicative DNA helicase; Validated
 190-438 2.74e-09

replicative DNA helicase; Validated


Pssm-ID: 136106 [Multi-domain]  Cd Length: 472  Bit Score: 58.85  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMlyQKGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYN-VLYLSLEVHTSILSDRFDARLSETEMSKL 268
Cdd:PRK06904  204 VTTGFTDLDKK--TAGLQPSDLIIVAARPSMGKTTFAMNLCENAAMASEKpVLVFSLEMPAEQIMMRMLASLSRVDQTKI 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 269 VEQRDDVHRKLAEIGATKGV----GNLWVVErpSGSMSPADL-DRMLNSMKANGMIpDMVVVDYADLMRASyDLRDDRA- 342
Cdd:PRK06904  282 RTGQNLDQQDWAKISSTVGMfkqkPNLYIDD--SSGLTPTELrSRARRVYRENGGL-SLIMVDYLQLMRAP-GFEDNRTl 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 343 NIRSIYTDLRALYDKHNVAGITASQTNR----EGGSSEVATMMHAADNIEKvrIADLVITINKTE-----EEEAKGEARL 413
Cdd:PRK06904  358 EIAEISRSLKALAKELKVPVVALSQLNRtlenRGDKRPVNSDLRESGSIEQ--DADLIMFIYRDEvynetTEDNKGVAEI 435

                         250       260
                  ....*....|....*....|....*
gi 1802031267 414 YFAGSRNQKGGvSIRVKQNLEQMRF 438
Cdd:PRK06904  436 IIGKQRNGPIG-RVRLAFQGQYSRF 459
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 190-440 7.58e-09

C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 410864 [Multi-domain]  Cd Length: 256  Bit Score: 56.37  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLyqKGWAKREMVLFMGFAKSGKSTAMGEFSINATL-AGYNVLYLSLEVHTSILSDRFDARLSETEMSKL 268
Cdd:cd00984     2 LPTGFTDLDKLT--GGLQPGDLIIIAARPSMGKTAFALNIAENIALdEGLPVLFFSLEMSAEQLAERLLSSESGVSLSKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 269 ---VEQRDDVHR------KLAEIgatkgvgNLWVVERPSgsMSPADLDRMLNSMKANGMIPDMVVVDYADLMRASyDLRD 339
Cdd:cd00984    80 rtgRLDDEDWERltaamgELSEL-------PLYIDDTPG--LTVDEIRAKARRLKREHGGLGLIVIDYLQLIRGS-KRAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 340 DRAN-IRSIYTDLRALYDKHNVAGITASQTNR--EGGSSEVATMmhaADNIEKVRI---ADLVITINKTE----EEEAKG 409
Cdd:cd00984   150 NRQQeVAEISRSLKALAKELNVPVIALSQLNRgvESRTDKRPML---SDLRESGSIeqdADVVIFLYRDEyydkDSEDKG 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1802031267 410 EARLYFAGSRNQKGGvSIRVKQNLEQMRFIE 440
Cdd:cd00984   227 IAEIIIAKNRNGPTG-TVYLAFNPEYTRFTD 256
PRK08840 PRK08840
replicative DNA helicase; Provisional
 179-438 2.78e-06

replicative DNA helicase; Provisional


Pssm-ID: 181562 [Multi-domain]  Cd Length: 464  Bit Score: 49.60  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 179 YEASDDYVpNSITTGLPLLDRMlyQKGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYN-VLYLSLEVHTSILSDRFD 257
Cdd:PRK08840  190 YKTPQDGV-TGVDTGFTDLNKK--TAGLQGSDLIIVAARPSMGKTTFAMNLCENAAMDQDKpVLIFSLEMPAEQLMMRML 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 258 ARLSETEMSKL-VEQRDDvhRKLAEIGATKGV----GNLWVVErpSGSMSPADL-DRMLNSMKANGMIpDMVVVDYADLM 331
Cdd:PRK08840  267 ASLSRVDQTKIrTGQLDD--EDWARISSTMGIlmekKNMYIDD--SSGLTPTEVrSRARRIAREHGGL-SMIMVDYLQLM 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 332 RASyDLRDDRA-NIRSIYTDLRALYDKHNVAGITASQTNR----EGGSSEVATMMHAADNIEKvrIADLVITINKTE--- 403
Cdd:PRK08840  342 RVP-ALSDNRTlEIAEISRSLKALAKELNVPVVALSQLNRsleqRADKRPVNSDLRESGSIEQ--DADLIMFIYRDEvyn 418

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1802031267 404 -EEEAKGEARLYFAGSRNQKGGvSIRVKQNLEQMRF 438
Cdd:PRK08840  419 pDSPLKGTAEIIIGKQRNGPIG-SVRLTFQGQYSRF 453
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 190-405 5.80e-06

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 47.26  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLYQkGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLEvhtsilsdrfdarlsetemsklv 269
Cdd:cd01124     1 VKTGIPGLDELLGG-GIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFE----------------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 270 EQRDDVHRKLAEIG----ATKGVGNLWVVERPSGSMSPADLDRMLNSMKANgmIPDM----VVVDYADLMRASY-DLRDD 340
Cdd:cd01124    57 ESPERLLRNAKSFGwdfdEMEDEGKLIIVDAPPTEAGRFSLDELLSRILSI--IKSFkakrVVIDSLSGLRRAKeDQMRA 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802031267 341 RANIRSIYTDLRAlydkhnvAGITASQTN-REGGSSEVATMMHAADNiekvrIADLVITINKTEEE 405
Cdd:cd01124   135 RRIVIALLNELRA-------AGVTTIFTSeMRSFLSSESAGGGDVSF-----IVDGVILLRYVEIE 188
DnaB_C pfam03796
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ...
 190-371 5.76e-05

DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.


Pssm-ID: 427509 [Multi-domain]  Cd Length: 254  Bit Score: 44.33  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLYqkGWAKREMVLFMGFAKSGKSTamgeFSIN-----ATLAGYNVLYLSLE------------VHTSIL 252
Cdd:pfam03796   2 LPTGFTDLDRLTG--GLQPGDLIIIAARPSMGKTA----FALNiarnaAVKHKKPVAIFSLEmsaeqlvmrllaSEAGVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 253 SDRF-DARLSETEMSKLVEQRDDVHRKlaeigatkgvgNLWVVERPSgsMSPADLDRMLNSMKANGMIpDMVVVDYADLM 331
Cdd:pfam03796  76 SQKLrTGQLTDEDWEKLAKAAGRLSEA-----------PLYIDDTPG--LSIAEIRAKARRLKREHGL-GLIVIDYLQLM 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1802031267 332 RASYDlRDDRAN-IRSIYTDLRALYDKHNVAGITASQTNRE 371
Cdd:pfam03796 142 SGGSR-GENRQQeISEISRSLKALAKELNVPVIALSQLSRA 181
KaiC_C cd19484
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ...
 190-246 1.39e-04

C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410892 [Multi-domain]  Cd Length: 218  Bit Score: 43.09  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802031267 190 ITTGLPLLDRMLYQKGWAKREMVLFMGFAKSGKSTAMGEFSINATLAGYNVLYLSLE 246
Cdd:cd19484     1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFE 57
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 204-373 3.01e-03

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 38.90  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 204 KGW-AKREMVLFMGFAKSGKST---------AMGE--FSINATLAGYNVLYLSLEVHTSILSDRFDArlsetemskLVEQ 271
Cdd:pfam13481  27 KGLlPAGGLGLLAGAPGTGKTTlaldlaaavATGKpwLGGPRVPEQGKVLYVSAEGPADELRRRLRA---------AGAD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 272 RDDVHRKLaeigATKGVGNLWVVE-RPSGSMSPADLDRMLNSMKANGMiPDMVVVDyaDLMRASYDLRDDRANIRSIYTD 350
Cdd:pfam13481  98 LDLPARLL----FLSLVESLPLFFlDRGGPLLDADVDALEAALEEVED-PDLVVID--PLARALGGDENSNSDVGRLVKA 170

                         170       180
                  ....*....|....*....|...
gi 1802031267 351 LRALYDKHNVAGITASQTNREGG 373
Cdd:pfam13481 171 LDRLARRTGATVLLVHHVGKDGA 193
RecA-like_Gp4D_helicase cd19483
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ...
 212-373 4.64e-03

RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410891 [Multi-domain]  Cd Length: 231  Bit Score: 38.32  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 212 VLFMGFAKSGKSTAMGEFSIN-ATLAGYNVLYLSLEVHTSILSDRFDAR-LSETEMSKLVEQRDDVHRKLAEIGATKGVG 289
Cdd:cd19483     1 VTIGAGSGIGKSTIVRELAYHlITEHGEKVGIISLEESVEETAKGLAGKhLGKPEPLELPRDDITEEEEDDAFDNELGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 290 NLWVVERpSGSMSPADLDRMLNSMKANGMIpDMVVVDYADLMRASYDLRDDRANIRSIYTDLRALYDKHNVAGITASQTN 369
Cdd:cd19483    81 RFFLYDH-FGSLDWDNLKEKIRYMVKVLGC-KVIVLDHLTILVSGLDSSDERKELDEIMTELAALVKELGVTIILVSHLR 158


                  ....
gi 1802031267 370 REGG 373
Cdd:cd19483   159 RPGG 162
DnaB COG0305
Replicative DNA helicase [Replication, recombination and repair];
190-438 7.51e-03

Replicative DNA helicase [Replication, recombination and repair];


Pssm-ID: 440074 [Multi-domain]  Cd Length: 429  Bit Score: 38.52  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 190 ITTGLPLLDRMLyqKGWAKREMVLFMGfaksgkSTAMG--EFSIN-----ATLAGYNVLYLSLEV------------HTS 250
Cdd:COG0305   174 VPTGFTDLDKLT--GGLQPGDLIILAA------RPSMGktAFALNiarnaAIKEGKPVAIFSLEMsaeqlvmrllssEAR 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 251 ILSDRF-DARLSETEMSKLVEQRDDVHRKlaeigatkgvgNLWVVERPSgsMSPADLDRMLNSMKANGMIpDMVVVDYAD 329
Cdd:COG0305   246 IDSSKLrTGKLSDEDWERLSSAAGELSEA-----------PIYIDDTPG--LTIAEIRAKARRLKREHGL-GLIVIDYLQ 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802031267 330 LMRASyDLRDDRAN-IRSIYTDLRALYDKHNVAGITASQTNReggSSEVAT----MMhaAD-----NIEKVriADLVITI 399
Cdd:COG0305   312 LMSGS-GRSENRQQeISEISRSLKALAKELNVPVIALSQLSR---AVEQRTdkrpQL--SDlresgSIEQD--ADVVMFL 383

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1802031267 400 N----KTEEEEAKGEARLYFAGSRNqkGGV-SIRVKQNLEQMRF 438
Cdd:COG0305   384 YrdeyYNPDSEDKGIAEIIIAKQRN--GPTgTVKLAFDGEYTRF 425
 
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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