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Conserved domains on  [gi|1217756503|ref|WP_089197253|]
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MULTISPECIES: DEAD/DEAH box helicase [Serratia]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11437332)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-530 2.03e-105

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


:

Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 328.91  E-value: 2.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   1 MAFTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKR--ARGRVLVLAHVKELVAQNHAKYCAYgleADI 78
Cdd:COG1061    77 TSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRF---LGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  79 FAAGLQQKESAGKVVFGSVQSVARNLPL--FDGAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLLGLTATPYRL 156
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAHLdeLGDRFGLVIIDEAHHAGAP---SYRRILEAFPAA----YRLGLTATPFRS 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 157 GKGWIYqyhyhgftrgdsASLFRDCIYELPLRYMIKHGFLVPPERLDMPIvqyDFSRLEARSNGLfsEADLNRELKRQNR 236
Cdd:COG1061   227 DGREIL------------LFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRV---DLTDERAEYDAL--SERLREALAADAE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 237 VTPHIISQIV-EYADDRKgVMIFAATVEHAREIHGLL--PNGEAALVSAETPPAERDALIEAFKQQRLRYLVNVAVLTTG 313
Cdd:COG1061   290 RKDKILRELLrEHPDDRK-TLVFCSSVDHAEALAELLneAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 314 FDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPDKKDCLILDYAGNPHDLFTPEVGVSKPHGDSQpvqvfcpacgfanlf 393
Cdd:COG1061   369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYR--------------- 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 394 wgkctengdIIEHYGRRCQGWLEDDDGHREQCDYRFRFKSCPHCGAENDIAARRCHQCQEVLVDPDDMLKAALKLKDALV 473
Cdd:COG1061   434 ---------VEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGK 504
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1217756503 474 LRCGGMELQSGRDEKGEWLKATYYDEDGTSTSERFRLQTPAQRKAFEMLFLRPHQRA 530
Cdd:COG1061   505 AEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELLR 561
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-530 2.03e-105

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 328.91  E-value: 2.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   1 MAFTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKR--ARGRVLVLAHVKELVAQNHAKYCAYgleADI 78
Cdd:COG1061    77 TSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRF---LGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  79 FAAGLQQKESAGKVVFGSVQSVARNLPL--FDGAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLLGLTATPYRL 156
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAHLdeLGDRFGLVIIDEAHHAGAP---SYRRILEAFPAA----YRLGLTATPFRS 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 157 GKGWIYqyhyhgftrgdsASLFRDCIYELPLRYMIKHGFLVPPERLDMPIvqyDFSRLEARSNGLfsEADLNRELKRQNR 236
Cdd:COG1061   227 DGREIL------------LFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRV---DLTDERAEYDAL--SERLREALAADAE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 237 VTPHIISQIV-EYADDRKgVMIFAATVEHAREIHGLL--PNGEAALVSAETPPAERDALIEAFKQQRLRYLVNVAVLTTG 313
Cdd:COG1061   290 RKDKILRELLrEHPDDRK-TLVFCSSVDHAEALAELLneAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 314 FDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPDKKDCLILDYAGNPHDLFTPEVGVSKPHGDSQpvqvfcpacgfanlf 393
Cdd:COG1061   369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYR--------------- 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 394 wgkctengdIIEHYGRRCQGWLEDDDGHREQCDYRFRFKSCPHCGAENDIAARRCHQCQEVLVDPDDMLKAALKLKDALV 473
Cdd:COG1061   434 ---------VEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGK 504
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1217756503 474 LRCGGMELQSGRDEKGEWLKATYYDEDGTSTSERFRLQTPAQRKAFEMLFLRPHQRA 530
Cdd:COG1061   505 AEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELLR 561
ResIII pfam04851
Type III restriction enzyme, res subunit;
3-155 7.21e-35

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 128.94  E-value: 7.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKRARG-----RVLVLAHVKELVAQNHAKYCAYGLEAD 77
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKkgpikKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  78 ---IFAAGLQQKES--AGKVVFGSVQSVARNL-----PLFDGAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLL 147
Cdd:pfam04851  82 eigEIISGDKKDESvdDNKIVVTTIQSLYKALelaslELLPDFFDVIIIDEAHRSGAS---SYRNILEYFKPA----FLL 154

                  ....*...
gi 1217756503 148 GLTATPYR 155
Cdd:pfam04851 155 GLTATPER 162
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
248-356 8.77e-34

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 124.59  E-value: 8.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 248 YADDRKGVMIFAATVEHAREIHGLLPN--GEAALVSAETPPAERD--ALIEAFKQQ-RLRYLVNVAVLTTGFDAPHVDLI 322
Cdd:cd18799     2 YKYVEIKTLIFCVSIEHAEFMAEAFNEagIDAVALNSDYSDRERGdeALILLFFGElKPPILVTVDLLTTGVDIPEVDNV 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1217756503 323 AILRPTESVSLYQQIVGRGLRLAPDKKDCLILDY 356
Cdd:cd18799    82 VFLRPTESRTLFLQMLGRGLRLHEGKDFFTILDF 115
DEXDc smart00487
DEAD-like helicases superfamily;
3-153 1.27e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 1.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503    3 FTLRPYQLEAVEATINHFRRhpepALIVLPTGAGKSLV-----IAELAKRARGRVLVLAHVKELVAQNHAKYCAYGLEAD 77
Cdd:smart00487   7 EPLRPYQKEAIEALLSGLRD----VILAAPTGSGKTLAallpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   78 IFAAGL-----------QQKESAGKVVFGSVQSVARNL---PLFDGAFSLLIVDECHRISDDDdsQYQQIIQHLQKTNPQ 143
Cdd:smart00487  83 LKVVGLyggdskreqlrKLESGKTDILVTTPGRLLDLLendKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPKN 160
                          170
                   ....*....|
gi 1217756503  144 LRLLGLTATP 153
Cdd:smart00487 161 VQLLLLSATP 170
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
3-347 1.54e-16

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 83.46  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503    3 FTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKS-LVIAEL-----AKRARgRVLVLAHVKELVAQNHAKYCAYGLE- 75
Cdd:PRK11448   412 LGLRYYQEDAIQAVEKAIVEGQREILLAMATGTGKTrTAIALMyrllkAKRFR-RILFLVDRSALGEQAEDAFKDTKIEg 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   76 ----ADIFA-AGLQQK--ESAGKVVFGSVQS-VARNLPLFDGA-------FSLLIVDECHR--------------ISDDD 126
Cdd:PRK11448   491 dqtfASIYDiKGLEDKfpEDETKVHVATVQGmVKRILYSDDPMdkppvdqYDCIIVDEAHRgytldkemsegelqFRDQL 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  127 D--SQYQQIIQHLQKTNpqlrlLGLTATPYR-----LGKGwIYQYHYhgftrgdsaslfRDCI-------YELPLRY--- 189
Cdd:PRK11448   571 DyvSKYRRVLDYFDAVK-----IGLTATPALhtteiFGEP-VYTYSY------------REAVidgylidHEPPIRIetr 632
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  190 MIKHGF-LVPPERLDMpivqYDFSRLEARSNGLfsEADLNRELKRQNR--VTPH----IISQIVEYAD--DRKGVMIFAA 260
Cdd:PRK11448   633 LSQEGIhFEKGEEVEV----INTQTGEIDLATL--EDEVDFEVEDFNRrvITESfnrvVCEELAKYLDptGEGKTLIFAA 706
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  261 TVEHA-----------REIHGLLPNgeaALVSAETPPAERDA-LIEAFKQQRL-RYLVNVAVLTTGFDAPHVDLIAILRP 327
Cdd:PRK11448   707 TDAHAdmvvrllkeafKKKYGQVED---DAVIKITGSIDKPDqLIRRFKNERLpNIVVTVDLLTTGIDVPSICNLVFLRR 783
                          410       420
                   ....*....|....*....|
gi 1217756503  328 TESVSLYQQIVGRGLRLAPD 347
Cdd:PRK11448   784 VRSRILYEQMLGRATRLCPE 803
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
5-56 7.69e-03

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 39.40  E-value: 7.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1217756503   5 LRPYQLEAVEATINHFRrhPEPALIVLPTGAGKSLVIAELAKRARGRVLVLA 56
Cdd:TIGR00603 256 IRPYQEKSLSKMFGNGR--ARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLC 305
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-530 2.03e-105

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 328.91  E-value: 2.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   1 MAFTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKR--ARGRVLVLAHVKELVAQNHAKYCAYgleADI 78
Cdd:COG1061    77 TSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRF---LGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  79 FAAGLQQKESAGKVVFGSVQSVARNLPL--FDGAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLLGLTATPYRL 156
Cdd:COG1061   154 PLAGGGKKDSDAPITVATYQSLARRAHLdeLGDRFGLVIIDEAHHAGAP---SYRRILEAFPAA----YRLGLTATPFRS 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 157 GKGWIYqyhyhgftrgdsASLFRDCIYELPLRYMIKHGFLVPPERLDMPIvqyDFSRLEARSNGLfsEADLNRELKRQNR 236
Cdd:COG1061   227 DGREIL------------LFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRV---DLTDERAEYDAL--SERLREALAADAE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 237 VTPHIISQIV-EYADDRKgVMIFAATVEHAREIHGLL--PNGEAALVSAETPPAERDALIEAFKQQRLRYLVNVAVLTTG 313
Cdd:COG1061   290 RKDKILRELLrEHPDDRK-TLVFCSSVDHAEALAELLneAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 314 FDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPDKKDCLILDYAGNPHDLFTPEVGVSKPHGDSQpvqvfcpacgfanlf 393
Cdd:COG1061   369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDLAGYR--------------- 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 394 wgkctengdIIEHYGRRCQGWLEDDDGHREQCDYRFRFKSCPHCGAENDIAARRCHQCQEVLVDPDDMLKAALKLKDALV 473
Cdd:COG1061   434 ---------VEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGK 504
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1217756503 474 LRCGGMELQSGRDEKGEWLKATYYDEDGTSTSERFRLQTPAQRKAFEMLFLRPHQRA 530
Cdd:COG1061   505 AEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELLR 561
ResIII pfam04851
Type III restriction enzyme, res subunit;
3-155 7.21e-35

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 128.94  E-value: 7.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKRARG-----RVLVLAHVKELVAQNHAKYCAYGLEAD 77
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKkgpikKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  78 ---IFAAGLQQKES--AGKVVFGSVQSVARNL-----PLFDGAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLL 147
Cdd:pfam04851  82 eigEIISGDKKDESvdDNKIVVTTIQSLYKALelaslELLPDFFDVIIIDEAHRSGAS---SYRNILEYFKPA----FLL 154

                  ....*...
gi 1217756503 148 GLTATPYR 155
Cdd:pfam04851 155 GLTATPER 162
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
3-385 1.24e-34

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 139.59  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAEL------AKRARgRVLVLAHVKELVAQNHAKYCAYGLEA 76
Cdd:COG4096   157 IALRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALiyrllkAGRAK-RILFLADRNALVDQAKNAFKPFLPDL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  77 DIFA---AGLQQKESAGKVVFGSVQSVARNLPLFD----------GAFSLLIVDECHR-ISddddSQYQQIIQHLQKTnp 142
Cdd:COG4096   236 DAFTklyNKSKDIDKSARVYFSTYQTMMNRIDGEEeepgyrqfppDFFDLIIIDECHRgIY----SKWRAILDYFDAL-- 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 143 qlrLLGLTATPyrlgKGWIYQyhyhgftrgDSASLF-RDCIYELPLRYMIKHGFLVPPE----RLDMPIVQYDFSRLEAR 217
Cdd:COG4096   310 ---QIGLTATP----KDTIDR---------NTYEYFnGNPVYTYSLEQAVADGFLVPYKviriDTKFDREGIRYDAGEDL 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 218 SN--------------GLFSEADLNREL--KRQNRVtphIISQIVEYAD----DRKG-VMIFAATVEHAREIHGLL---- 272
Cdd:COG4096   374 SDeegeeieleeleedREYEAKDFNRKVvnEDTTRK---VLEELMEYLDkpggDRLGkTIIFAKNDDHADRIVQALrely 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 273 --PNGEAALV---SAETPpaerDALIEAFKQQrlRYLVNVAV----LTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLR 343
Cdd:COG4096   451 peLGGDFVKKitgDDDYG----KSLIDNFKNP--EKYPRIAVtvdmLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTR 524
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1217756503 344 L----APDKKDCLILDYAGNpHDLFTPevgvskphgDSQPVQVFCP 385
Cdd:COG4096   525 LcpdlFPGKTHFTIFDFVGN-TELFAD---------PSFPLRIFEP 560
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
248-356 8.77e-34

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 124.59  E-value: 8.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 248 YADDRKGVMIFAATVEHAREIHGLLPN--GEAALVSAETPPAERD--ALIEAFKQQ-RLRYLVNVAVLTTGFDAPHVDLI 322
Cdd:cd18799     2 YKYVEIKTLIFCVSIEHAEFMAEAFNEagIDAVALNSDYSDRERGdeALILLFFGElKPPILVTVDLLTTGVDIPEVDNV 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1217756503 323 AILRPTESVSLYQQIVGRGLRLAPDKKDCLILDY 356
Cdd:cd18799    82 VFLRPTESRTLFLQMLGRGLRLHEGKDFFTILDF 115
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
5-164 1.51e-30

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 117.28  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHFRRHPEPALIVLPTGAGKSLVIAELAKR-----ARGRVLVLAHVKELVAQNHAKYCAYGLEADIF 79
Cdd:cd18032     1 PRYYQQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRlleanRKKRILFLAHREELLEQAERSFKEVLPDGSFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  80 -AAGLQQKESAGKVVFGSVQSVARN--LPLFD-GAFSLLIVDECHRISdddDSQYQQIIQHLQKTnpqlRLLGLTATPYR 155
Cdd:cd18032    81 nLKGGKKKPDDARVVFATVQTLNKRkrLEKFPpDYFDLIIIDEAHHAI---ASSYRKILEYFEPA----FLLGLTATPER 153

                  ....*....
gi 1217756503 156 LGKGWIYQY 164
Cdd:cd18032   154 TDGLDTYEL 162
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
5-153 2.74e-28

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 110.09  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHfrRHPEPALIVLPTGAGKSLVIAEL-AKRARGRVLVLAHVKELVAQNHAKYCAYGLEADI--FAA 81
Cdd:cd17926     1 LRPYQEEALEAWLAH--KNNRRGILVLPTGSGKTLTALALiAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIglIGG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1217756503  82 GLQQKESAGKVVFGSVQSVARNL----PLFDgAFSLLIVDECHRISDDddsQYQQIIQHLQKTnpqlRLLGLTATP 153
Cdd:cd17926    79 GKKKDFDDANVVVATYQSLSNLAeeekDLFD-QFGLLIVDEAHHLPAK---TFSEILKELNAK----YRLGLTATP 146
DEXDc smart00487
DEAD-like helicases superfamily;
3-153 1.27e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 1.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503    3 FTLRPYQLEAVEATINHFRRhpepALIVLPTGAGKSLV-----IAELAKRARGRVLVLAHVKELVAQNHAKYCAYGLEAD 77
Cdd:smart00487   7 EPLRPYQKEAIEALLSGLRD----VILAAPTGSGKTLAallpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   78 IFAAGL-----------QQKESAGKVVFGSVQSVARNL---PLFDGAFSLLIVDECHRISDDDdsQYQQIIQHLQKTNPQ 143
Cdd:smart00487  83 LKVVGLyggdskreqlrKLESGKTDILVTTPGRLLDLLendKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLPKN 160
                          170
                   ....*....|
gi 1217756503  144 LRLLGLTATP 153
Cdd:smart00487 161 VQLLLLSATP 170
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
3-347 1.54e-16

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 83.46  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503    3 FTLRPYQLEAVEATINHFRRHPEPALIVLPTGAGKS-LVIAEL-----AKRARgRVLVLAHVKELVAQNHAKYCAYGLE- 75
Cdd:PRK11448   412 LGLRYYQEDAIQAVEKAIVEGQREILLAMATGTGKTrTAIALMyrllkAKRFR-RILFLVDRSALGEQAEDAFKDTKIEg 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   76 ----ADIFA-AGLQQK--ESAGKVVFGSVQS-VARNLPLFDGA-------FSLLIVDECHR--------------ISDDD 126
Cdd:PRK11448   491 dqtfASIYDiKGLEDKfpEDETKVHVATVQGmVKRILYSDDPMdkppvdqYDCIIVDEAHRgytldkemsegelqFRDQL 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  127 D--SQYQQIIQHLQKTNpqlrlLGLTATPYR-----LGKGwIYQYHYhgftrgdsaslfRDCI-------YELPLRY--- 189
Cdd:PRK11448   571 DyvSKYRRVLDYFDAVK-----IGLTATPALhtteiFGEP-VYTYSY------------REAVidgylidHEPPIRIetr 632
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  190 MIKHGF-LVPPERLDMpivqYDFSRLEARSNGLfsEADLNRELKRQNR--VTPH----IISQIVEYAD--DRKGVMIFAA 260
Cdd:PRK11448   633 LSQEGIhFEKGEEVEV----INTQTGEIDLATL--EDEVDFEVEDFNRrvITESfnrvVCEELAKYLDptGEGKTLIFAA 706
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  261 TVEHA-----------REIHGLLPNgeaALVSAETPPAERDA-LIEAFKQQRL-RYLVNVAVLTTGFDAPHVDLIAILRP 327
Cdd:PRK11448   707 TDAHAdmvvrllkeafKKKYGQVED---DAVIKITGSIDKPDqLIRRFKNERLpNIVVTVDLLTTGIDVPSICNLVFLRR 783
                          410       420
                   ....*....|....*....|
gi 1217756503  328 TESVSLYQQIVGRGLRLAPD 347
Cdd:PRK11448   784 VRSRILYEQMLGRATRLCPE 803
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
28-152 3.46e-16

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 75.90  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  28 LIVLPTGAGKSLV----IAELAKRARGRVLVLAHVKELVAQNHAKYCAY---GLEADIFAAGLQQKESAG------KVVF 94
Cdd:cd00046     5 LITAPTGSGKTLAallaALLLLLKKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEEREKnklgdaDIII 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1217756503  95 GSVQSVARNL----PLFDGAFSLLIVDECHRISDDDDSQYQQIIQHLQKTNPQLRLLGLTAT 152
Cdd:cd00046    85 ATPDMLLNLLlredRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
6-153 7.90e-15

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 77.85  E-value: 7.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   6 RPYQLEAVEATINhfrrhpEPALIVLPTGAGKS----LVIAELAKRARGRVLVLAHVKELVAQnHAKYCAYGLEAD---- 77
Cdd:COG1111     5 RLYQLNLAASALR------KNTLVVLPTGLGKTavalLVIAERLHKKGGKVLFLAPTKPLVEQ-HAEFFKEALNIPedei 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  78 -IFAAGLQQKESA-----GKVVFGSVQSV-----ARNLPLFDgaFSLLIVDECHRISDDDDsqYQQIIQHLQKTNPQLRL 146
Cdd:COG1111    78 vVFTGEVSPEKRKelwekARIIVATPQVIendliAGRIDLDD--VSLLIFDEAHRAVGNYA--YVYIAERYHEDAKDPLI 153

                  ....*..
gi 1217756503 147 LGLTATP 153
Cdd:COG1111   154 LGMTASP 160
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
3-153 1.29e-14

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 72.85  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLVIAELAK--------RARGRVLVLAHVKELVAQNHAKYCAYGL 74
Cdd:cd17927     1 FKPRNYQLELAQPALKG-----KNTIICLPTGSGKTFVAVLICEhhlkkfpaGRKGKVVFLANKVPLVEQQKEVFRKHFE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  75 EADIFAAGL----QQKESAGK------VVFGSVQSVARNlpLFDGA------FSLLIVDECHRISddDDSQYQQII---- 134
Cdd:cd17927    76 RPGYKVTGLsgdtSENVSVEQivessdVIIVTPQILVND--LKSGTivslsdFSLLVFDECHNTT--KNHPYNEIMfryl 151
                         170       180
                  ....*....|....*....|
gi 1217756503 135 -QHLQKTNPQLRLLGLTATP 153
Cdd:cd17927   152 dQKLGSSGPLPQILGLTASP 171
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
6-153 3.30e-14

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 70.73  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   6 RPYQLEAVEATINhfrrhPEPALIVLPTGAGKSLV-----IAELAKRARG-RVLVLAHVKELVAQNHAKYCAYGLEADIF 79
Cdd:pfam00270   1 TPIQAEAIPAILE-----GRDVLVQAPTGSGKTLAfllpaLEALDKLDNGpQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  80 AA----GLQQKESAGK-----VVF---GSVQSVARNLPLFDGaFSLLIVDECHRISDDDdsQYQQIIQHLQKTNPQLRLL 147
Cdd:pfam00270  76 VAsllgGDSRKEQLEKlkgpdILVgtpGRLLDLLQERKLLKN-LKLLVLDEAHRLLDMG--FGPDLEEILRRLPKKRQIL 152

                  ....*.
gi 1217756503 148 GLTATP 153
Cdd:pfam00270 153 LLSATL 158
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
3-153 1.09e-13

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 70.20  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLV---IAE--LAKR----ARGRVLVLAHVKELVAQN---HAKYC 70
Cdd:cd18036     1 LELRNYQLELVLPALRG-----KNTIICAPTGSGKTRVavyICRhhLEKRrsagEKGRVVVLVNKVPLVEQQlekFFKYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  71 AYGLEADIFAAGLQQKESAGKVVFGS-------------VQSVARNLPLFDGAFSLLIVDECHRISddDDSQYQQIIQHL 137
Cdd:cd18036    76 RKGYKVTGLSGDSSHKVSFGQIVKASdviictpqilinnLLSGREEERVYLSDFSLLIFDECHHTQ--KEHPYNKIMRMY 153
                         170       180
                  ....*....|....*....|.
gi 1217756503 138 QK-----TNPQLRLLGLTATP 153
Cdd:cd18036   154 LDkklssQGPLPQILGLTASP 174
RPL40A COG1552
Ribosomal protein L40E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ...
417-466 2.03e-13

Ribosomal protein L40E [Translation, ribosomal structure and biogenesis]; Ribosomal protein L40E is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 441161 [Multi-domain]  Cd Length: 50  Bit Score: 64.57  E-value: 2.03e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1217756503 417 DDDGHREQCDYRFRFKSCPHCGAENDIAARRCHQCQEVLVDPDDMLKAAL 466
Cdd:COG1552     1 DMAKFEEAEKRRLNKKICMRCGARNPIRATRCRKCGYKNLRPKKKERRAK 50
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
239-343 7.26e-13

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 64.92  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 239 PHIISQIVEYADDRKgVMIFAATVEHA-REIHGLLPNGEAALVSAETPPAERDALIEAFKQQRLRYLVNVAVLTTGFDAP 317
Cdd:pfam00271   3 LEALLELLKKERGGK-VLIFSQTKKTLeAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
                          90       100
                  ....*....|....*....|....*.
gi 1217756503 318 HVDLIAILRPTESVSLYQQIVGRGLR 343
Cdd:pfam00271  82 DVDLVINYDLPWNPASYIQRIGRAGR 107
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
3-153 1.23e-12

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 66.58  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHfrrhpePALIVLPTGAGKSLvIAELAK----R--ARGRVLVLAHVKELVAQNH-AKYCAYGLE 75
Cdd:cd18033     1 VPLRDYQFTIVQKALFQ------NTLVALPTGLGKTF-IAAVVMlnyyRwfPKGKIVFMAPTKPLVSQQIeACYKITGIP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  76 ADIFA--AGLQQKESAGK------VVFGSVQSVARNLPlfDGAF-----SLLIVDECHRISDDddSQYQQIIQHLQKTNP 142
Cdd:cd18033    74 SSQTAelTGSVPPTKRAElwaskrVFFLTPQTLENDLK--EGDCdpksiVCLVIDEAHRATGN--YAYCQVVRELMRYNS 149
                         170
                  ....*....|.
gi 1217756503 143 QLRLLGLTATP 153
Cdd:cd18033   150 HFRILALTATP 160
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
3-153 3.18e-11

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 62.67  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHfrrhpePALIVLPTGAGKSLVIAELAKR----------ARGRVLVLAHVKELVAQNH------ 66
Cdd:cd18034     1 FTPRSYQLELFEAALKR------NTIVVLPTGSGKTLIAVMLIKEmgelnrkeknPKKRAVFLVPTVPLVAQQAeairsh 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  67 -----AKYCAYGLEADIFAAGLQQKESAGKVVFGSVQsVARNLpLFDG-----AFSLLIVDECHRISDDDdsQYQQIIQ- 135
Cdd:cd18034    75 tdlkvGEYSGEMGVDKWTKERWKEELEKYDVLVMTAQ-ILLDA-LRHGflslsDINLLIFDECHHATGDH--PYARIMKe 150
                         170       180
                  ....*....|....*....|
gi 1217756503 136 --HLQKTNPQLRLLGLTATP 153
Cdd:cd18034   151 fyHLEGRTSRPRILGLTASP 170
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
5-153 1.41e-10

DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350788 [Multi-domain]  Cd Length: 208  Bit Score: 61.09  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHFRRHPEPA------LIVLPTGAGKSLVIAELAKRARG-----RVLVLAHVKELVAQNHAKYCAYG 73
Cdd:cd18030    22 ARYYQYYAVEAALERIKTATNKDgdkkggYIWHTQGSGKSLTMFKAAKLLIEdpknpKVVFVVDRKDLDYQTSSTFSRFA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  74 LEADIFA---AGLQQ--KESAGKVVFGSVQSVARN-LPLFDGAFS-----LLIVDECHRisddddSQYQQIIQHLQKTNP 142
Cdd:cd18030   102 AEDVVRAnstKELKEllKNLSGGIIVTTIQKFNNAvKEESKPVLIyrkniVVIVDEAHR------SQFGELAKALKKALP 175
                         170
                  ....*....|.
gi 1217756503 143 QLRLLGLTATP 153
Cdd:cd18030   176 NATFIGFTGTP 186
HELICc smart00490
helicase superfamily c-terminal domain;
276-343 3.00e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.84  E-value: 3.00e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1217756503  276 EAALVSAETPPAERDALIEAFKQQRLRYLVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLR 343
Cdd:smart00490  13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
4-152 4.08e-10

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 59.20  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   4 TLRPYQLEAVEATINHfrrhPEPALIVLPTGAGKSLvIAELA-----KRARGRVLVLAHVKELVAQNHA----KYCAYGL 74
Cdd:cd17921     1 LLNPIQREALRALYLS----GDSVLVSAPTSSGKTL-IAELAilralATSGGKAVYIAPTRALVNQKEAdlreRFGPLGK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  75 EADIF--AAGLQQKESAGKVVFGSVQ----SVARNLP-LFDGAFSLLIVDECHRISDDDDSQ-YQQIIQHLQKTNPQLRL 146
Cdd:cd17921    76 NVGLLtgDPSVNKLLLAEADILVATPekldLLLRNGGeRLIQDVRLVVVDEAHLIGDGERGVvLELLLSRLLRINKNARF 155

                  ....*.
gi 1217756503 147 LGLTAT 152
Cdd:cd17921   156 VGLSAT 161
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
5-363 8.77e-10

Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];


Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 61.81  E-value: 8.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHFRRHPEPA---LIVLPTGAGKSLVIAELAKRARG-------RVLVLahV--KELVAQNHAKYCAY 72
Cdd:COG0610   256 ARYHQYFAVRKAVERVKEAEGDGkggVIWHTQGSGKSLTMVFLAQKLARlpdldnpTVVVV--TdrKDLDDQLFDTFKAF 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  73 GLEADIFA---AGLQQ--KESAGKVVFGSVQ-------SVARNLPLFDGAFsLLIVDECHRisddddSQYQQIIQHLQKT 140
Cdd:COG0610   334 GRESVVQAesrADLREllESDSGGIIVTTIQkfpealdEIKYPELSDRKNI-IVIVDEAHR------SQYGGLAKNMRDA 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 141 NPQLRLLGLTATPyrLGKgwiyqyhyhgfTRGDSASLFRDCIYelplRYMIKH----GFLVPP---ERLdmPIVQYDFSR 213
Cdd:COG0610   407 LPNASFFGFTGTP--IFK-----------EDRTTLEVFGDYIH----TYTITQaiedGATLPLlyeYRL--AKLKLDKEK 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 214 LEARSNGLFSEAD------LNRELKRQNRV--TPHIISQIVEY--------ADDRKG-VMIFAATVEHA----REIHGLL 272
Cdd:COG0610   468 IDEEFDELTEGLDdeekekLKAKWALLEEVlgAPERIEQIAEDivehfeerTRPGKGkAMVVTSSREAAvryyEAFDKLR 547
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 273 P-----NGEAALV----SAETPP--------AERDALIEAFK--QQRLRYLVNVAVLTTGFDAP--H---VDliailRPT 328
Cdd:COG0610   548 PewgykPLKIAVVfsgsANDDPEelkehgnkEYEKDLAKRFKdpDDPLKLLIVVDMLLTGFDAPslHtlyVD-----KPL 622
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1217756503 329 ESVSLYQQIvGRGLRLAPDKKDCLILDYAGNPHDL 363
Cdd:COG0610   623 KGHNLMQAI-SRVNRVFPGKPYGLIVDYRGIFENL 656
uvsW PHA02558
UvsW helicase; Provisional
6-120 2.03e-09

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 60.02  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   6 RPYQLEAVEATINHFRRhpepaLIVLPTGAGKSLVIAELAK----RARGRVLVLAHVKELVAQNHAKYCAYGLEADIFAA 81
Cdd:PHA02558  116 HWYQYDAVYEGLKNNRR-----LLNLPTSAGKSLIQYLLSRyyleNYEGKVLIIVPTTSLVTQMIDDFVDYRLFPREAMH 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1217756503  82 GL---QQKESAGKVVFGSVQSvARNLP--LFDgAFSLLIVDECH 120
Cdd:PHA02558  191 KIysgTAKDTDAPIVVSTWQS-AVKQPkeWFD-QFGMVIVDECH 232
PRK13766 PRK13766
Hef nuclease; Provisional
28-153 3.16e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 59.89  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  28 LIVLPTGAGKS----LVIAELAKRARGRVLVLAHVKELVAQnHAKYCAYGLEAD-----IFAAGLQQKESA-----GKVV 93
Cdd:PRK13766   33 LVVLPTGLGKTaialLVIAERLHKKGGKVLILAPTKPLVEQ-HAEFFRKFLNIPeekivVFTGEVSPEKRAelwekAKVI 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1217756503  94 FGSVQSV-----ARNLPLFDgaFSLLIVDECHRISddDDSQYQQIIQ--HLQKTNPqlRLLGLTATP 153
Cdd:PRK13766  112 VATPQVIendliAGRISLED--VSLLIFDEAHRAV--GNYAYVYIAEryHEDAKNP--LVLGLTASP 172
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
4-152 7.53e-09

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 55.42  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   4 TLRPYQLEAVEATINHFRRhpepALIVLPTGAGKSLvIAELAKRAR----GRVLVLAHVKELVAQNH---AKYCAYGLEA 76
Cdd:cd18028     1 ELYPPQAEAVRAGLLKGEN----LLISIPTASGKTL-IAEMAMVNTllegGKALYLVPLRALASEKYeefKKLEEIGLKV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  77 -------DIFAAGLQQKEsagkVVFGS---VQSVARNLPLFDGAFSLLIVDECHRISDDDDSQYQQ-IIQHLQKTNPQLR 145
Cdd:cd18028    76 gistgdyDEDDEWLGDYD----IIVATyekFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLEsIVARLRRLNPNTQ 151

                  ....*..
gi 1217756503 146 LLGLTAT 152
Cdd:cd18028   152 IIGLSAT 158
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
5-153 8.85e-09

DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350833 [Multi-domain]  Cd Length: 200  Bit Score: 55.63  E-value: 8.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATInhfrrHPEPALIVLPTGAGKSLVIAELAKR-----ARGRVLVLAHVKELVAQNHA--------KYCA 71
Cdd:cd18075     3 LHGYQWEVVAPAL-----RGKNSIIWLPTGAGKTRAAVYVARRhletkRGAKVAVLVNKVHLVDQHLEkefhvlldKYTV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  72 YGLEADI-FAAGLQQKESAGKVVFGSVQSVARNLPLFD-------GAFSLLIVDECHRIsdDDDSQYQQII-----QHLQ 138
Cdd:cd18075    78 TAISGDSsHKCFFGQLARGSDVVICTAQILQNALLSGEeeahvelTDFSLLVIDECHHT--HKEAVYNKIMlsyleKKLS 155
                         170
                  ....*....|....*
gi 1217756503 139 KTNPQLRLLGLTATP 153
Cdd:cd18075   156 RQGDLPQILGLTASP 170
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
304-355 1.85e-08

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 51.55  E-value: 1.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1217756503 304 LVNVAVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPDKKDCLILD 355
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
3-152 2.80e-08

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 54.18  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   3 FTLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLV--IAELAKRARGRVLVLAhVKELVA----QNHAkycaygLEA 76
Cdd:cd18018    11 PSFRPGQEEAIARLLSG-----RSTLVVLPTGAGKSLCyqLPALLLRRRGPGLTLV-VSPLIAlmkdQVDA------LPR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  77 DIFAAGL-------QQKESAGKVVFGSVQ----SVARnlpLFDGAF----------SLLIVDECHRISD---DDDSQYQQ 132
Cdd:cd18018    79 AIKAAALnssltreERRRILEKLRAGEVKilyvSPER---LVNESFrellrqtppiSLLVVDEAHCISEwshNFRPDYLR 155
                         170       180
                  ....*....|....*....|
gi 1217756503 133 IIQHLQKTNPQLRLLGLTAT 152
Cdd:cd18018   156 LCRVLRELLGAPPVLALTAT 175
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
28-153 5.27e-08

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 52.90  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  28 LIVLPTGAGKS----LVIAELAKRARGRVLVLAHVKELVAQNHAKYCAYGLEADIFAA--GLQQKES------AGKVVFG 95
Cdd:cd18035    20 LIVLPTGLGKTiiaiLVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSltGEVKPEEraerwdASKIIVA 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1217756503  96 SVQSVARNL-----PLFDgaFSLLIVDECHRISddDDSQYQQIIQHLQKTNPQLRLLGLTATP 153
Cdd:cd18035   100 TPQVIENDLlagriTLDD--VSLLIFDEAHHAV--GNYAYVYIAHRYKREANNPLILGLTASP 158
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
4-152 7.82e-08

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 52.92  E-value: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   4 TLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLV--IAELAkrARGRVLV----LAHVKELV---AQNHAKYCAYGL 74
Cdd:cd17920    12 EFRPGQLEAINAVLAG-----RDVLVVMPTGGGKSLCyqLPALL--LDGVTLVvsplISLMQDQVdrlQQLGIRAAALNS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  75 EADIF---AAGLQQKESAGKVVF--------GSVQSVARNLPLFdGAFSLLIVDECHRISDD-DD--SQYQQIIQHLQKT 140
Cdd:cd17920    85 TLSPEekrEVLLRIKNGQYKLLYvtperllsPDFLELLQRLPER-KRLALIVVDEAHCVSQWgHDfrPDYLRLGRLRRAL 163
                         170
                  ....*....|..
gi 1217756503 141 nPQLRLLGLTAT 152
Cdd:cd17920   164 -PGVPILALTAT 174
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
5-152 3.41e-07

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 50.38  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHfrRHPEPALIVLPTGAGKSLVIAELAKRARGRVLVLAHVKELVAQNHAKYCAYGLEAD----IFA 80
Cdd:cd18029     9 LRPYQEKALSKMFGN--GRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDeqigRFT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  81 AGLQQKESAGKVVFGSVQSVA---RNLPLFDG--------AFSLLIVDECHRISddddSQYQQIIQHLQKTNpqlRLLGL 149
Cdd:cd18029    87 SDKKEIFPEAGVTVSTYSMLAntrKRSPESEKfmefiterEWGLIILDEVHVVP----APMFRRVLTLQKAH---CKLGL 159

                  ...
gi 1217756503 150 TAT 152
Cdd:cd18029   160 TAT 162
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
5-153 5.95e-07

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 49.87  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVEATINHFRRHPePALIVLPTGAGKSL-VIAELA-----KRARGRVLV------LAH-VKELvaQNHAKYCA 71
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLqAIAFLAyllkeGKERGPVLVvcplsvLENwEREF--EKWTPDLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  72 ----YGLEADIFAAGLQQKESAGKVV---FGSVQSVARNLPLFDgaFSLLIVDECHRISDDDdsqyQQIIQHLQKTNPQL 144
Cdd:cd17919    78 vvvyHGSQRERAQIRAKEKLDKFDVVlttYETLRRDKASLRKFR--WDLVVVDEAHRLKNPK----SQLSKALKALRAKR 151

                  ....*....
gi 1217756503 145 RLLgLTATP 153
Cdd:cd17919   152 RLL-LTGTP 159
COG4889 COG4889
Predicted helicase [General function prediction only];
3-153 8.11e-07

Predicted helicase [General function prediction only];


Pssm-ID: 443917 [Multi-domain]  Cd Length: 1571  Bit Score: 52.27  E-value: 8.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503    3 FTLRPYQLEAVEATINHFRRHPEPALIVLPtGAGK---SLVIAELAKRARGRVLVLAHVKELVAQ------NHAKY---- 69
Cdd:COG4889    168 KTLRPHQQEAIEAVLAGFKTHDRGKLIMAC-GTGKtftSLRIAEELAGKGGRVLFLVPSISLLSQtlrewtAESEVplrs 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   70 ---C--------AYGLEADIF---------------AAGLQQKESAGK--VVFGSVQS---VAR----NLPLFDgafsLL 114
Cdd:COG4889    247 favCsdskvgkrRKKDDEDTSahdlaypattdaeklAAAAQKRHDADRmtVVFSTYQSidvVADaqklGLPEFD----LI 322
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1217756503  115 IVDECHR-----ISDDDDSQYQQIiqHLQKTNPQLRLLGLTATP 153
Cdd:COG4889    323 ICDEAHRttgatLAGEDESAFVRV--HDNDYIKAKKRLYMTATP 364
DEXHc_UvsW cd18031
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system ...
8-164 9.73e-07

DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system that repairs DNA damage by a process that involves homologous recombination. UvsW is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350789 [Multi-domain]  Cd Length: 161  Bit Score: 48.97  E-value: 9.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   8 YQLEAVEATINHFRRhpepaLIVLPTGAGKSLVIAELAK----RARGRVLVLAHVKELVAQNHAKYCAY------GLEAD 77
Cdd:cd18031     4 YQKDAVFEGLVNRRR-----ILNLPTSAGRSLIQALLARyyleNYEGKILIIVPTTALTTQMADDFVDYrlfshaMIKKI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  78 IFAAGLQQKESAGKVVFGSV-QSVARNLPLFDGAFSLLIVDECHRISDDDDSQYQQIIQHLQKTnpqlrlLGLTATPyRL 156
Cdd:cd18031    79 GGGASKDDKYKNDAPVVVGTwQTVVKQPKEWFSQFGMMMNDECHLATGKSISSIISGLNNCMFK------FGLSGSL-RD 151

                  ....*...
gi 1217756503 157 GKGWIYQY 164
Cdd:cd18031   152 GKANIMQY 159
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
5-153 1.13e-06

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 49.59  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   5 LRPYQLEAVeatiNHFRRHPEPALI----VlptGAGKS----LVIAELAKRARG-RVLVLAhVKELVAQ-NHAKYCAYGL 74
Cdd:cd18011     1 PLPHQIDAV----LRALRKPPVRLLladeV---GLGKTieagLIIKELLLRGDAkRVLILC-PASLVEQwQDELQDKFGL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  75 EADIF-AAGLQQKESAGKVVFG-------SVQSVARN----LPLFDGAFSLLIVDECHRIS---DDDDSQYQQIIQHLQK 139
Cdd:cd18011    73 PFLILdRETAAQLRRLIGNPFEefpivivSLDLLKRSeerrGLLLSEEWDLVVVDEAHKLRnsgGGKETKRYKLGRLLAK 152
                         170
                  ....*....|....
gi 1217756503 140 TNPqlRLLGLTATP 153
Cdd:cd18011   153 RAR--HVLLLTATP 164
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
8-153 4.34e-05

SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 45.11  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   8 YQLEAVEATINHFRRHPEP--ALIVLPTGAGKSLVIAELAKRARG-----RVLVLAHVKELVAQNHAKYCAYGLEADIFA 80
Cdd:pfam18766   1 QQYFAVNKAVERVLEDGDRrgGVIWHTQGSGKSLTMVFLARKLRRelknpTVVVVTDRNDLDDQLTKTFAACGREVPVQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  81 ---AGLQQK-ESAGKVVFGSVQSVARNLplfDGAFSLL--------IVDECHRisddddSQYQQIIQHLQKTNPQLRLLG 148
Cdd:pfam18766  81 esrKDLRELlRGSGGIIFTTIQKFGETP---DEGFPVLsdrrniivLVDEAHR------SQYGGLAANMRDALPNAAFIG 151

                  ....*
gi 1217756503 149 LTATP 153
Cdd:pfam18766 152 FTGTP 156
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1-153 1.96e-04

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 44.45  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   1 MAFTLRPYQLEAVEATINHFRRHP------EPalivlptGAGKSL----VIAELAKRAR-GRVLVLA--HVKELVAQNHA 67
Cdd:COG0553   238 LKATLRPYQLEGAAWLLFLRRLGLgglladDM-------GLGKTIqalaLLLELKERGLaRPVLIVAptSLVGNWQRELA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  68 KYcAYGLEADIFAAGLQQKESAGK-----VVFGSVQSVARNLPLF-DGAFSLLIVDECHRISDDDDSQYqQIIQHLQKTN 141
Cdd:COG0553   311 KF-APGLRVLVLDGTRERAKGANPfedadLVITSYGLLRRDIELLaAVDWDLVILDEAQHIKNPATKRA-KAVRALKARH 388
                         170
                  ....*....|..
gi 1217756503 142 pqlRLLgLTATP 153
Cdd:COG0553   389 ---RLA-LTGTP 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
255-322 2.56e-04

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 41.34  E-value: 2.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1217756503 255 VMIFAATVEHAREIHGLLPNG--EAALVSAETPPAERDALIEAFKQQRLRYLVnvavlTT-----GFDAPHVDLI 322
Cdd:cd18787    30 AIIFVNTKKRVDRLAELLEELgiKVAALHGDLSQEERERALKKFRSGKVRVLV-----ATdvaarGLDIPGVDHV 99
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
4-40 9.55e-04

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 42.05  E-value: 9.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1217756503   4 TLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLV 40
Cdd:COG0514    17 SFRPGQEEIIEAVLAG-----RDALVVMPTGGGKSLC 48
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
6-152 1.60e-03

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 40.20  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   6 RPYQLEAVEATInhfrrHPEPALIVLPTGAGKSLVIAELAKRARGRVLVLAHVKELVAQNHAKY-----CAYGLEADIFA 80
Cdd:cd18016    19 RTNQLEAINAAL-----LGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLtsldiPATYLTGDKTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  81 AG-------LQQKESAGKVVFGSVQSVARNLPLFDGAFSL--------LIVDECHRISD---DDDSQYQQiIQHLQKTNP 142
Cdd:cd18016    94 AEatkiylqLSKKDPIIKLLYVTPEKISASNRLISTLENLyerkllarFVIDEAHCVSQwghDFRPDYKR-LNMLRQKFP 172
                         170
                  ....*....|
gi 1217756503 143 QLRLLGLTAT 152
Cdd:cd18016   173 SVPMMALTAT 182
Cas3_I cd09696
CRISPR/Cas system-associated protein Cas3; Distinct Cas3 family with HD domain fused to ...
232-353 2.01e-03

CRISPR/Cas system-associated protein Cas3; Distinct Cas3 family with HD domain fused to C-termus of Helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DNA helicase Cas3; This protein includes both DEAH and HD motifs; signature gene for Type I


Pssm-ID: 187827 [Multi-domain]  Cd Length: 843  Bit Score: 41.16  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503 232 KRQNRVTPHIISQIVEYADDRKGVMIFAATVEHAREIHGLLPNGEAALVSAETPPAERDALIE----------------A 295
Cdd:cd09696   251 SDEKFLSTMVKELNLLMKDSGGAILVFCRTVKHVRKVFAKLPKEKFELLTGTLRGAERDDLVKkeifnrflpqmlsgsrA 330
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1217756503 296 FKQQRLRYLVNVAVLTTGFDAPHVDLIAILRPTESVslyQQIVGRGLRLApDKKDCLI 353
Cdd:cd09696   331 RPQQGTVYLVCTSAGEVGVNISADHLVCDLAPFESM---QQRFGRVNRFG-ELQACQI 384
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
4-152 2.32e-03

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 39.66  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   4 TLRPYQLEAVEATINHfrrhpEPALIVLPTGAGKSLVIAELAKRARGRVLVLAHVKELVaQNHAKYC-AYGLEADIFAA- 81
Cdd:cd18015    18 KFRPLQLETINATMAG-----RDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLM-EDQLMALkKLGISATMLNAs 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503  82 -----------GLQQKESAGKVVFGSVQSVARNLPLFD--------GAFSLLIVDECHRISD---DDDSQYQQiIQHLQK 139
Cdd:cd18015    92 sskehvkwvhaALTDKNSELKLLYVTPEKIAKSKRFMSklekaynaGRLARIAIDEVHCCSQwghDFRPDYKK-LGILKR 170
                         170
                  ....*....|...
gi 1217756503 140 TNPQLRLLGLTAT 152
Cdd:cd18015   171 QFPNVPILGLTAT 183
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
23-150 5.12e-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: 37.74  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1217756503   23 HPEPALIVLPTGAGKSLVIAELAKRARGRVlvlAHVKELVAQNHAKYCAYGLEADIFaaGLQQKESAGKVVFGSVQSVAR 102
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPG---GGVIYIDGEDILEEVLDQLLLIIV--GGKKASGSGELRLRLALALAR 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1217756503  103 NLPlfdgaFSLLIVDECHRISDDDDSQYQQIIQHLQKTNPQLRLLGLT 150
Cdd:smart00382  76 KLK-----PDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
5-56 7.69e-03

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 39.40  E-value: 7.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1217756503   5 LRPYQLEAVEATINHFRrhPEPALIVLPTGAGKSLVIAELAKRARGRVLVLA 56
Cdd:TIGR00603 256 IRPYQEKSLSKMFGNGR--ARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLC 305
 
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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