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Conserved domains on  [gi|849253135|ref|YP_009149766|]
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helicase DnaB-like [Bacillus phage BCP8-2]

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
 5-407 3.06e-18

41 helicase; Provisional


The actual alignment was detected with superfamily member PHA02542:

Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 87.04  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135   5 IMTQILRKAIENPIFAKEVLAVAPLTVFEgSPAYTEIAGIVKRYYQTNNKPLTEDALltltEDKLDRMKkdaLTQQDYFG 84
Cdd:PHA02542   1 IEETILSNLIFNEDYFRKVWPYLKAEYFE-SGPEKVIFKLIKKHVNEYNAIPTIEAL----SIALENRS---LSEVTFDG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  85 KIHYLYEVRNSG-DNDVIDEKIEEYIRQKMSIDLLTKA---ATN--LKNKEFLEKLPDE--FKKIL--MLNISGKRNEII 154
Cdd:PHA02542  73 AKDLLSSLSDNPeDLDWLVKETEKWCQDRAMYNALSKAieiQDNadKPLEKRNKKLPDVgaIPDIMqeALAISFDSSVGH 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 155 NVLDDAEyKRTSLSTLFQNMIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELEN 234
Cdd:PHA02542 153 DYFEDYE-ERYDSYQSKANKIPFKLEILNKITKGGAERKTLNVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 235 RMILKFEQSLLRQNKSTILTgsvLNQEQFDKRQAFIRQHRQhfGNLFFARYSPQAVTPAKIEQLISDLMIREGIQVDAVV 314
Cdd:PHA02542 232 VIAKRIDANLLDVSLDDIDD---LSKAEYKAKMEKLRSKTQ--GKLIIKQYPTGGAHAGHFRALLNELKLKKNFKPDVII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 315 VDYPELLRNPRATGNeAEDGGRLF----EEMRRIAQDYNVVMWTAAQMNRTAYSA----LVRTAEhmegSHRKKNAAELV 386
Cdd:PHA02542 307 VDYLGICASSRLRVS-SENSYTYVkaiaEELRGLAVEHDVVVWTAAQTTRSGWDSsdvdMSDTAE----SAGLPATADFM 381

                        410       420
                 ....*....|....*....|....*..
gi 849253135 387 LTVNQTPEEYQAGFIRL------YADK 407
Cdd:PHA02542 382 LAVIETEELAQMGQQLVkqlksrYGDK 408
 
Name Accession Description Interval E-value
41 PHA02542
41 helicase; Provisional
 5-407 3.06e-18

41 helicase; Provisional


Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 87.04  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135   5 IMTQILRKAIENPIFAKEVLAVAPLTVFEgSPAYTEIAGIVKRYYQTNNKPLTEDALltltEDKLDRMKkdaLTQQDYFG 84
Cdd:PHA02542   1 IEETILSNLIFNEDYFRKVWPYLKAEYFE-SGPEKVIFKLIKKHVNEYNAIPTIEAL----SIALENRS---LSEVTFDG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  85 KIHYLYEVRNSG-DNDVIDEKIEEYIRQKMSIDLLTKA---ATN--LKNKEFLEKLPDE--FKKIL--MLNISGKRNEII 154
Cdd:PHA02542  73 AKDLLSSLSDNPeDLDWLVKETEKWCQDRAMYNALSKAieiQDNadKPLEKRNKKLPDVgaIPDIMqeALAISFDSSVGH 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 155 NVLDDAEyKRTSLSTLFQNMIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELEN 234
Cdd:PHA02542 153 DYFEDYE-ERYDSYQSKANKIPFKLEILNKITKGGAERKTLNVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 235 RMILKFEQSLLRQNKSTILTgsvLNQEQFDKRQAFIRQHRQhfGNLFFARYSPQAVTPAKIEQLISDLMIREGIQVDAVV 314
Cdd:PHA02542 232 VIAKRIDANLLDVSLDDIDD---LSKAEYKAKMEKLRSKTQ--GKLIIKQYPTGGAHAGHFRALLNELKLKKNFKPDVII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 315 VDYPELLRNPRATGNeAEDGGRLF----EEMRRIAQDYNVVMWTAAQMNRTAYSA----LVRTAEhmegSHRKKNAAELV 386
Cdd:PHA02542 307 VDYLGICASSRLRVS-SENSYTYVkaiaEELRGLAVEHDVVVWTAAQTTRSGWDSsdvdMSDTAE----SAGLPATADFM 381

                        410       420
                 ....*....|....*....|....*..
gi 849253135 387 LTVNQTPEEYQAGFIRL------YADK 407
Cdd:PHA02542 382 LAVIETEELAQMGQQLVkqlksrYGDK 408
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 175-360 6.17e-13

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: 68.69  E-value: 6.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHLNgGGLAKGELgLIVAAS-GTGKTLILTNLATNYTKN-GYNVLFVALE----ELENRMILkfeqSLLRQN 248
Cdd:cd00984    2 LPTGFTDLDKLT-GGLQPGDL-IIIAARpSMGKTAFALNIAENIALDeGLPVLFFSLEmsaeQLAERLLS----SESGVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 249 KSTILTGSvLNQEQFDKRQAFIRQHRQHfgNLFFARYSpqAVTPAKIeQLISDLMIREGIQVDAVVVDYPELLRNPRATG 328
Cdd:cd00984   76 LSKLRTGR-LDDEDWERLTAAMGELSEL--PLYIDDTP--GLTVDEI-RAKARRLKREHGGLGLIVIDYLQLIRGSKRAE 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 849253135 329 NEAEDGGRLFEEMRRIAQDYNVVMWTAAQMNR 360
Cdd:cd00984  150 NRQQEVAEISRSLKALAKELNVPVIALSQLNR 181
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
174-242 2.69e-09

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 57.23  E-value: 2.69e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849253135 174 MIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMILKFEQ 242
Cdd:COG0467    1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAES 69
DnaB_C pfam03796
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ...
 175-332 2.81e-09

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: 57.81  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  175 IPTGFKDIDHLNGGgLAKGELgLIVAA-SGTGKTLILTNLATNYTKN-GYNVLFVALE----ELENRMIlkFEQSLLRQN 248
Cdd:pfam03796   2 LPTGFTDLDRLTGG-LQPGDL-IIIAArPSMGKTAFALNIARNAAVKhKKPVAIFSLEmsaeQLVMRLL--ASEAGVDSQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  249 KstILTGSvLNQEQFDKRQAFIRQHRQHfgNLFFARyspqavTPA-KIEQLISDL--MIREGiQVDAVVVDYPELLRNPR 325
Cdd:pfam03796  78 K--LRTGQ-LTDEDWEKLAKAAGRLSEA--PLYIDD------TPGlSIAEIRAKArrLKREH-GLGLIVIDYLQLMSGGS 145


                  ....*..
gi 849253135  326 ATGNEAE 332
Cdd:pfam03796 146 RGENRQQ 152
circ_KaiC TIGR02655
circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, ...
 175-231 2.75e-04

circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, part of the kaiABC operon that controls circadian rhythm. It may be universal in Cyanobacteria. Each member has two copies of the KaiC domain (pfam06745), which is also found in other proteins. KaiC performs autophosphorylation and acts as its own transcriptional repressor. [Cellular processes, Other]


Pssm-ID: 131703 [Multi-domain]  Cd Length: 484  Bit Score: 43.40  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 849253135  175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEE 231
Cdd:TIGR02655 245 VSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLENACANKERAILFAYEE 301
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 192-274 1.01e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135   192 KGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMILKFEQSLLRQNKSTILTGsvlnqEQFDKRQAFIR 271
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE-----LRLRLALALAR 75


                   ...
gi 849253135   272 QHR 274
Cdd:smart00382  76 KLK 78
 
Name Accession Description Interval E-value
41 PHA02542
41 helicase; Provisional
 5-407 3.06e-18

41 helicase; Provisional


Pssm-ID: 222864 [Multi-domain]  Cd Length: 473  Bit Score: 87.04  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135   5 IMTQILRKAIENPIFAKEVLAVAPLTVFEgSPAYTEIAGIVKRYYQTNNKPLTEDALltltEDKLDRMKkdaLTQQDYFG 84
Cdd:PHA02542   1 IEETILSNLIFNEDYFRKVWPYLKAEYFE-SGPEKVIFKLIKKHVNEYNAIPTIEAL----SIALENRS---LSEVTFDG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  85 KIHYLYEVRNSG-DNDVIDEKIEEYIRQKMSIDLLTKA---ATN--LKNKEFLEKLPDE--FKKIL--MLNISGKRNEII 154
Cdd:PHA02542  73 AKDLLSSLSDNPeDLDWLVKETEKWCQDRAMYNALSKAieiQDNadKPLEKRNKKLPDVgaIPDIMqeALAISFDSSVGH 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 155 NVLDDAEyKRTSLSTLFQNMIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELEN 234
Cdd:PHA02542 153 DYFEDYE-ERYDSYQSKANKIPFKLEILNKITKGGAERKTLNVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEMAEE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 235 RMILKFEQSLLRQNKSTILTgsvLNQEQFDKRQAFIRQHRQhfGNLFFARYSPQAVTPAKIEQLISDLMIREGIQVDAVV 314
Cdd:PHA02542 232 VIAKRIDANLLDVSLDDIDD---LSKAEYKAKMEKLRSKTQ--GKLIIKQYPTGGAHAGHFRALLNELKLKKNFKPDVII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 315 VDYPELLRNPRATGNeAEDGGRLF----EEMRRIAQDYNVVMWTAAQMNRTAYSA----LVRTAEhmegSHRKKNAAELV 386
Cdd:PHA02542 307 VDYLGICASSRLRVS-SENSYTYVkaiaEELRGLAVEHDVVVWTAAQTTRSGWDSsdvdMSDTAE----SAGLPATADFM 381

                        410       420
                 ....*....|....*....|....*..
gi 849253135 387 LTVNQTPEEYQAGFIRL------YADK 407
Cdd:PHA02542 382 LAVIETEELAQMGQQLVkqlksrYGDK 408
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
 175-360 6.17e-13

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: 68.69  E-value: 6.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHLNgGGLAKGELgLIVAAS-GTGKTLILTNLATNYTKN-GYNVLFVALE----ELENRMILkfeqSLLRQN 248
Cdd:cd00984    2 LPTGFTDLDKLT-GGLQPGDL-IIIAARpSMGKTAFALNIAENIALDeGLPVLFFSLEmsaeQLAERLLS----SESGVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 249 KSTILTGSvLNQEQFDKRQAFIRQHRQHfgNLFFARYSpqAVTPAKIeQLISDLMIREGIQVDAVVVDYPELLRNPRATG 328
Cdd:cd00984   76 LSKLRTGR-LDDEDWERLTAAMGELSEL--PLYIDDTP--GLTVDEI-RAKARRLKREHGGLGLIVIDYLQLIRGSKRAE 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 849253135 329 NEAEDGGRLFEEMRRIAQDYNVVMWTAAQMNR 360
Cdd:cd00984  150 NRQQEVAEISRSLKALAKELNVPVIALSQLNR 181
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
174-242 2.69e-09

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 57.23  E-value: 2.69e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849253135 174 MIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMILKFEQ 242
Cdd:COG0467    1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAES 69
DnaB_C pfam03796
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ...
 175-332 2.81e-09

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: 57.81  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  175 IPTGFKDIDHLNGGgLAKGELgLIVAA-SGTGKTLILTNLATNYTKN-GYNVLFVALE----ELENRMIlkFEQSLLRQN 248
Cdd:pfam03796   2 LPTGFTDLDRLTGG-LQPGDL-IIIAArPSMGKTAFALNIARNAAVKhKKPVAIFSLEmsaeQLVMRLL--ASEAGVDSQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  249 KstILTGSvLNQEQFDKRQAFIRQHRQHfgNLFFARyspqavTPA-KIEQLISDL--MIREGiQVDAVVVDYPELLRNPR 325
Cdd:pfam03796  78 K--LRTGQ-LTDEDWEKLAKAAGRLSEA--PLYIDD------TPGlSIAEIRAKArrLKREH-GLGLIVIDYLQLMSGGS 145


                  ....*..
gi 849253135  326 ATGNEAE 332
Cdd:pfam03796 146 RGENRQQ 152
DnaB COG0305
Replicative DNA helicase [Replication, recombination and repair];
175-329 2.89e-08

Replicative DNA helicase [Replication, recombination and repair];


Pssm-ID: 440074 [Multi-domain]  Cd Length: 429  Bit Score: 55.85  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHLNgGGLAKGELgLIVAA-SGTGKTLILTNLATNY-TKNGYNVLFVALE----ELENRMIlkFEQSLLRQN 248
Cdd:COG0305  174 VPTGFTDLDKLT-GGLQPGDL-IILAArPSMGKTAFALNIARNAaIKEGKPVAIFSLEmsaeQLVMRLL--SSEARIDSS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 249 KstILTGSvLNQEQFDKrqafIRQHRQHFGNL-FFARYSPqAVTPAKIEQLISDLMIREGIqvDAVVVDYPELLRNPRAT 327
Cdd:COG0305  250 K--LRTGK-LSDEDWER----LSSAAGELSEApIYIDDTP-GLTIAEIRAKARRLKREHGL--GLIVIDYLQLMSGSGRS 319


                 ..
gi 849253135 328 GN 329
Cdd:COG0305  320 EN 321
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 175-237 4.89e-08

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: 53.42  E-value: 4.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMI 237
Cdd:cd01124    1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLL 63
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
 182-350 2.27e-07

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: 51.23  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  182 IDHLNGGGLAKGELGLIVAASGTGKTLILTNLA------------TNYTKNGyNVLFVALEELENRMILKFEQSLLRQNk 249
Cdd:pfam13481  22 RRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlggPRVPEQG-KVLYVSAEGPADELRRRLRAAGADLD- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  250 stiltgsvlnqeqFDKRQAFIrqHRQHFGNLFFARYSPQAVTPAkIEQLISDLMIREGIQVdaVVVDypellrnP--RAT 327
Cdd:pfam13481 100 -------------LPARLLFL--SLVESLPLFFLDRGGPLLDAD-VDALEAALEEVEDPDL--VVID-------PlaRAL 154

                         170       180
                  ....*....|....*....|....*.
gi 849253135  328 G---NEAEDGGRLFEEMRRIAQDYNV 350
Cdd:pfam13481 155 GgdeNSNSDVGRLVKALDRLARRTGA 180
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
190-434 2.75e-07

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 52.21  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 190 LAKGELGLIVAASGTGKTLILTNLATNYTKNGY---------NVLFVALE----ELENRMIlkfeqsllrqnkstiltgs 256
Cdd:COG3598   10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGPwlgrrvppgKVLYLAAEddrgELRRRLK------------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 257 vlnqeqfDKRQAFIRQHRQHFGNLFFARYSPQAVTPAKIEQLIsDLMIREGiqVDAVVVDypellrnP--RATG---NEA 331
Cdd:COG3598   71 -------ALGADLGLPFADLDGRLRLLSLAGDLDDTDDLEALE-RAIEEEG--PDLVVID-------PlaRVFGgdeNDA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 332 EDGGRLFEEMRRIAQDYNV-VMWT-----AAQMNRTAYSALvrtaehmeGSHRKKNAAELVLTVNQTPEEyqaGFIRLYA 405
Cdd:COG3598  134 EEMRAFLNPLDRLAERTGAaVLLVhhtgkGGAGKDSGDRAR--------GSSALRGAARSVLVLSREKGE---DLRVLTR 202

                        250       260
                 ....*....|....*....|....*....
gi 849253135 406 DKVRNPPEGQYNRMLGFKVIGSAQTVRDF 434
Cdd:COG3598  203 AKSNYGPEIALRWDNGGRLALEEVAALTA 231
PRK09302 PRK09302
circadian clock protein KaiC; Reviewed
 175-253 6.22e-07

circadian clock protein KaiC; Reviewed


Pssm-ID: 236461 [Multi-domain]  Cd Length: 509  Bit Score: 51.80  E-value: 6.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLI-LTNLATNYTKNGYNVLFVALEE-----LENRMILKFE-QSLLRQ 247
Cdd:PRK09302  13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFaLQFLVNGIKRFDEPGVFVTFEEspediIRNVASFGWDlQKLIDE 92


                 ....*.
gi 849253135 248 NKSTIL 253
Cdd:PRK09302  93 GKLFIL 98
PRK08840 PRK08840
replicative DNA helicase; Provisional
 175-418 1.84e-06

replicative DNA helicase; Provisional


Pssm-ID: 181562 [Multi-domain]  Cd Length: 464  Bit Score: 50.37  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHlNGGGLAKGELGLIVAASGTGKTLILTNLATNYT-KNGYNVLFVALEELENRMILKFEQSLLRQNKSTIL 253
Cdd:PRK08840 200 VDTGFTDLNK-KTAGLQGSDLIIVAARPSMGKTTFAMNLCENAAmDQDKPVLIFSLEMPAEQLMMRMLASLSRVDQTKIR 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 254 TGSVLNQE--QFDKRQAFIRQHRqhfgNLFFARYSpqAVTPAKIEQLiSDLMIREGIQVDAVVVDYPELLRNPRATGNEA 331
Cdd:PRK08840 279 TGQLDDEDwaRISSTMGILMEKK----NMYIDDSS--GLTPTEVRSR-ARRIAREHGGLSMIMVDYLQLMRVPALSDNRT 351

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 332 EDGGRLFEEMRRIAQDYNVVMWTAAQMNRT----AYSALVRTAEHMEGSHRKKnaAELVLTVNQ----TPEEYQAGFIRL 403
Cdd:PRK08840 352 LEIAEISRSLKALAKELNVPVVALSQLNRSleqrADKRPVNSDLRESGSIEQD--ADLIMFIYRdevyNPDSPLKGTAEI 429

                        250       260
                 ....*....|....*....|...
gi 849253135 404 YADKVRNPP--------EGQYNR 418
Cdd:PRK08840 430 IIGKQRNGPigsvrltfQGQYSR 452
radB PRK09361
DNA repair and recombination protein RadB; Provisional
 173-227 2.81e-06

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 48.32  E-value: 2.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 849253135 173 NMIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFV 227
Cdd:PRK09361   3 ERLPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYI 57
RecA-like_Gp4D_helicase cd19483
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ...
 197-352 3.44e-06

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: 47.95  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 197 LIVAASGTGKTLILTNLATN-YTKNGYNVLFVALEELENRMILKFEQSLLRQNKSTILTGSVLNQEQFDKRQAF-IRQHR 274
Cdd:cd19483    2 TIGAGSGIGKSTIVRELAYHlITEHGEKVGIISLEESVEETAKGLAGKHLGKPEPLELPRDDITEEEEDDAFDNeLGSGR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 849253135 275 QHFGNLFfaryspQAVTPAKIEQLISDLMIREGIQVdaVVVDYPELLRNPRATGNEAEDGGRLFEEMRRIAQDYNVVM 352
Cdd:cd19483   82 FFLYDHF------GSLDWDNLKEKIRYMVKVLGCKV--IVLDHLTILVSGLDSSDERKELDEIMTELAALVKELGVTI 151
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 175-242 4.99e-06

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 47.63  E-value: 4.99e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 849253135  175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLI-LTNLATNYTKNGYNVLFVALEELENRMILKFEQ 242
Cdd:pfam06745   1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFgLQFLYNGALKYGEPGVFVTLEEPPEDLRENARS 69
KaiC_C cd19484
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ...
 175-237 5.70e-06

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: 47.32  E-value: 5.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 849253135 175 IPTGFKDIDH-LNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMI 237
Cdd:cd19484    1 ISTGIPRLDAmLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLI 64
PRK09302 PRK09302
circadian clock protein KaiC; Reviewed
 175-231 1.91e-05

circadian clock protein KaiC; Reviewed


Pssm-ID: 236461 [Multi-domain]  Cd Length: 509  Bit Score: 47.18  E-value: 1.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEE 231
Cdd:PRK09302 255 ISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEE 311
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 175-231 2.70e-05

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 45.60  E-value: 2.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEE 231
Cdd:cd01121   64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEE 120
KaiC-N cd19485
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ...
 175-231 2.78e-05

N-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: 410893 [Multi-domain]  Cd Length: 226  Bit Score: 45.44  E-value: 2.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLI-LTNLATNYTKNGYNVLFVALEE 231
Cdd:cd19485    1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFaAQFLVNGIKEFGEPGVFVTFEE 58
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 175-232 1.28e-04

archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 43.07  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEEL 232
Cdd:cd01394    1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGL 58
PRK07004 PRK07004
replicative DNA helicase; Provisional
 109-361 1.36e-04

replicative DNA helicase; Provisional


Pssm-ID: 235907 [Multi-domain]  Cd Length: 460  Bit Score: 44.13  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 109 IRQKMSI-DLLTKAATNLKNKEFLEKLPDEFKKILMLNISGKRN-----EIINVLD------DAEYKRTSLSTLfqNMIP 176
Cdd:PRK07004 120 LRRLVSVaDEISADAFNPQGKEVRQLLDEAESKVFSIAEEGARGtqgflEIGPLLTqvveriDTLYHTANPSDV--TGTP 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 177 TGFKDIDHLNgGGLAKGELGLIVAASGTGKTLILTNLATNYT-KNGYNVLFVALEELENRMILKFEQSLLRQNKSTILTG 255
Cdd:PRK07004 198 TGFVDLDRMT-SGMHGGELIIVAGRPSMGKTAFSMNIGEYVAvEYGLPVAVFSMEMPGTQLAMRMLGSVGRLDQHRMRTG 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 256 SVLNQEQFDKRQAFIRQHRQHfgnlFFARYSPqAVTPAKIEQLiSDLMIREGIQVDAVVVDYPELLRNPRATGNEAEDGG 335
Cdd:PRK07004 277 RLTDEDWPKLTHAVQKMSEAQ----LFIDETG-GLNPMELRSR-ARRLARQCGKLGLIIIDYLQLMSGSSQGENRATEIS 350

                        250       260
                 ....*....|....*....|....*.
gi 849253135 336 RLFEEMRRIAQDYNVVMWTAAQMNRT 361
Cdd:PRK07004 351 EISRSLKSLAKELDVPVIALSQLNRG 376
circ_KaiC TIGR02655
circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, ...
 175-231 2.75e-04

circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, part of the kaiABC operon that controls circadian rhythm. It may be universal in Cyanobacteria. Each member has two copies of the KaiC domain (pfam06745), which is also found in other proteins. KaiC performs autophosphorylation and acts as its own transcriptional repressor. [Cellular processes, Other]


Pssm-ID: 131703 [Multi-domain]  Cd Length: 484  Bit Score: 43.40  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 849253135  175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEE 231
Cdd:TIGR02655 245 VSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLENACANKERAILFAYEE 301
ResIII pfam04851
Type III restriction enzyme, res subunit;
196-228 4.81e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.73  E-value: 4.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 849253135  196 GLIVAASGTGKTLILTNLATNYTKNGY--NVLFVA 228
Cdd:pfam04851  26 GLIVMATGSGKTLTAAKLIARLFKKGPikKVLFLV 60
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
 175-233 8.34e-04

C-terminal domain of KaiC family protein; uncharacterized subfamily; 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: 410895 [Multi-domain]  Cd Length: 219  Bit Score: 40.75  E-value: 8.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 IPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNG-YNVLFVALEELE 233
Cdd:cd19487    1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGeRSVLFSFDESIG 60
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 192-274 1.01e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135   192 KGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEELENRMILKFEQSLLRQNKSTILTGsvlnqEQFDKRQAFIR 271
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE-----LRLRLALALAR 75


                   ...
gi 849253135   272 QHR 274
Cdd:smart00382  76 KLK 78
PRK05595 PRK05595
replicative DNA helicase; Provisional
 61-230 1.75e-03

replicative DNA helicase; Provisional


Pssm-ID: 235525 [Multi-domain]  Cd Length: 444  Bit Score: 40.58  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  61 LLTLTE-----DKLDRMkkdaltqqdyfGKIHYLYEVRNSGDNDVideKIEEYIR---QKMSIDLLTKAATNL-----KN 127
Cdd:PRK05595  65 MLTLTEnlkstDKLEAA-----------GGVTYITELSNSIVSTA---NIQSYIKivkDKSTLRRLIKSSTEIiensyNN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 128 KEFLEKLPDEFKKILmLNISGKRN----EIINVLddAEYKRTSLSTLFQNM-----IPTGFKDIDHLNGGgLAKGELGLI 198
Cdd:PRK05595 131 QDDVEKVIDSAEKKI-FDISEKRTtsdfEPLSNV--LERGFEQIENLFNNKgettgVASGFRELDAKTSG-FQKGDMILI 206

                        170       180       190
                 ....*....|....*....|....*....|...
gi 849253135 199 VAASGTGKTLILTNLATNYT-KNGYNVLFVALE 230
Cdd:PRK05595 207 AARPSMGKTTFALNIAEYAAlREGKSVAIFSLE 239
PRK05748 PRK05748
replicative DNA helicase; Provisional
 61-237 2.40e-03

replicative DNA helicase; Provisional


Pssm-ID: 180232 [Multi-domain]  Cd Length: 448  Bit Score: 40.32  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135  61 LLTLTEDkLDrmKKDALTQqdyFGKIHYLYEVRNS---GDNdvidekIEEY---IRQKMSIDLLTKAATNLKNKEF---- 130
Cdd:PRK05748  67 VVTVTEI-LD--DQGDLEE---VGGLSYLAELANSvptAAN------IEYYakiVAEKAMLRRLIRTATEIANDAYeped 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 131 -LEKLPDEFKKiLMLNISGKRN-----EIINVLDDAeYKRtsLSTLFQNM-----IPTGFKDIDHLNgGGLAKGELgLIV 199
Cdd:PRK05748 135 dADEILDEAEK-KIFEVSERRNksgfkNIKDVLVKA-YDR--IEMLHNQTgditgIPTGFTDLDKMT-SGLQPNDL-IIV 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 849253135 200 AAS-GTGKTLILTNLATNY-TKNGYNVLFVALE----ELENRMI 237
Cdd:PRK05748 209 AARpSVGKTAFALNIAQNVaTKTDKNVAIFSLEmgaeSLVMRML 252
PRK08533 PRK08533
flagellar accessory protein FlaH; Reviewed
 181-244 7.80e-03

flagellar accessory protein FlaH; Reviewed


Pssm-ID: 181459  Cd Length: 230  Bit Score: 38.13  E-value: 7.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 849253135 181 DIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVAlEELENRMILKFEQSL 244
Cdd:PRK08533  12 ELHKRLGGGIPAGSLILIEGDESTGKSILSQRLAYGFLQNGYSVSYVS-TQLTTTEFIKQMMSL 74
PRK08506 PRK08506
replicative DNA helicase; Provisional
 101-246 7.83e-03

replicative DNA helicase; Provisional


Pssm-ID: 236278 [Multi-domain]  Cd Length: 472  Bit Score: 38.84  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 101 IDEKIEEYIRQKMSIDLLTKAATNLKNKEF---LEKLPDEFKKIlMLNISGKRNEIINVLDDAEYKRT--SLSTLFQNM- 174
Cdd:PRK08506  73 IDEEILLEILATNPIDNIEAYVEEIKEKSIkreLLSLANTIPEQ-AVEEDQKSSDILDEVERELYSITngSNSEDFKDSk 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 175 -----------------------IPTGFKDIDHLNGGgLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALEe 231
Cdd:PRK08506 152 eviestmehikkqkrlgnkdiigLDTGFVELNKMTKG-FNKGDLIIIAARPSMGKTTLCLNMALKALNQDKGVAFFSLE- 229

                        170
                 ....*....|....*
gi 849253135 232 lenrmiLKFEQSLLR 246
Cdd:PRK08506 230 ------MPAEQLMLR 238
Twinkle_C cd01122
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ...
 188-350 8.10e-03

C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.


Pssm-ID: 410867  Cd Length: 266  Bit Score: 37.99  E-value: 8.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 188 GGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALE----ELENRMILKFEQSLLRQnkstiltgsvlNQEQF 263
Cdd:cd01122   38 KGHRRGELTIFTGPTGSGKTTFLSEYSLDLCMQGVNTLWGSFEiknvRLAKTMLTQFAGKNLED-----------NLREF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 849253135 264 DKRQAFirqhrqhFGNL--FFARYSPQavtpAKIEQLIsDLMIR--EGIQVDAVVVDYPELLRNPRATGNEA-EDGGRLF 338
Cdd:cd01122  107 DEWADK-------FELLpmYFMKFHGS----TDIDEVL-DAMEHavYVYDIQHIVIDNLQFMMGTQASGSDRfELQDLII 174

                        170
                 ....*....|..
gi 849253135 339 EEMRRIAQDYNV 350
Cdd:cd01122  175 GKFRRFATNNNV 186
FlaH COG2874
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
174-230 8.25e-03

Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];


Pssm-ID: 442121  Cd Length: 230  Bit Score: 37.89  E-value: 8.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 849253135 174 MIPTGFKDIDHLNGGGLAKGELGLIVAASGTGKTLILTNLATNYTKNGYNVLFVALE 230
Cdd:COG2874    2 IISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTE 58
 
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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