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Conserved domains on  [gi|6321275|ref|NP_011352|]
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DNA-dependent ATPase RAD54 [Saccharomyces cerevisiae S288C]

Protein Classification

Rad54_N and DEXHc_RAD54A domain-containing protein( domain architecture ID 13756240)

protein containing domains Rad54_N, DEXHc_RAD54A, and SF2_C_SNF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 271-554 2.67e-150

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A 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: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 442.29  E-value: 2.67e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTGlvmkdyleaeafntssedplksdekaltesqkteQNNRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18067   1 LRPHQREGVKFLYRCVTG----------------------------------RRIRGSHGCIMADEMGLGKTLQCITLMW 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNtLTPLAVDGKKSSMGGGNTTVsqaihaWAQAQGRNIVKPVL 430
Cdd:cd18067  47 TLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKLVQ------WASQQGRRVSTPVL 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:cd18067 120 IISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAA 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6321275  511 EFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18067 200 EFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 271-806 3.52e-121

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 383.04  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCvtglvmkdyleaeafntssedplksdekaltesqkteQNNRGayGCIMADEMGLGKTLQCIALMW 350
Cdd:COG0553 242 LRPYQLEGAAWLLFL-------------------------------------RRLGL--GGLLADDMGLGKTIQALALLL 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGpqgkrLIDKCIIVCPSSLVNNWANELIKWLGpnTLTPLAVDGKKSSMGGGNttvsqaihAWAQAQgrnivkpVL 430
Cdd:COG0553 283 ELKERG-----LARPVLIVAPTSLVGNWQRELAKFAP--GLRVLVLDGTRERAKGAN--------PFEDAD-------LV 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:COG0553 341 ITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK 420

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  511 EFRKNFENPILRGRdadatdkeitkgEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKS- 589
Cdd:COG0553 421 AFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYl 488

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  590 -REVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNfedefddeddlelpddynmpgsKARDVQTKYSAKFSILERFLHKIK 668
Cdd:COG0553 489 rRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------------------EEGAELSGRSAKLEALLELLEELL 546

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  669 tESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQEfIFLLSSKAGGCGINLIGANRLI 748
Cdd:COG0553 547 -AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVI 624

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6321275  749 LMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVD 806
Cdd:COG0553 625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
 29-246 1.14e-61

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


:

Pssm-ID: 430137  Cd Length: 180  Bit Score: 206.73  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     29 VQDSVNRLTKPFRVPYKNTHippaagriatgsdNIVGGRSLRKRSAtVCYSGLDINADEAEYNSQDISfsqltKRRKDAL 108
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATP-------------TRASDRPARKRRK-VSYAGADGDAEDGDSDKPYTN-----VERRLAL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    109 SAQRLAK-DPTRLSHIQYTLRRSFTVPIKGYVQRHS----LPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDgemiv 183
Cdd:pfam08658  62 ATRRVNKfPVFRVKDKETVFRKSFSVPLKNKKQGAYnprrPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVD----- 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275    184 hdtSMDNKEEEskkmikstqEKDNINKEKNSQEERPTQRigrhpalMTNGVRNKPLRELLGDS 246
Cdd:pfam08658 137 ---DRDKPEEE---------EEAEEEEEEEEPEEKARKK-------LDNPLPHKSLAEILGIK 180
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 271-554 2.67e-150

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A 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: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 442.29  E-value: 2.67e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTGlvmkdyleaeafntssedplksdekaltesqkteQNNRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18067   1 LRPHQREGVKFLYRCVTG----------------------------------RRIRGSHGCIMADEMGLGKTLQCITLMW 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNtLTPLAVDGKKSSMGGGNTTVsqaihaWAQAQGRNIVKPVL 430
Cdd:cd18067  47 TLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKLVQ------WASQQGRRVSTPVL 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:cd18067 120 IISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAA 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6321275  511 EFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18067 200 EFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 271-806 3.52e-121

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 383.04  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCvtglvmkdyleaeafntssedplksdekaltesqkteQNNRGayGCIMADEMGLGKTLQCIALMW 350
Cdd:COG0553 242 LRPYQLEGAAWLLFL-------------------------------------RRLGL--GGLLADDMGLGKTIQALALLL 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGpqgkrLIDKCIIVCPSSLVNNWANELIKWLGpnTLTPLAVDGKKSSMGGGNttvsqaihAWAQAQgrnivkpVL 430
Cdd:COG0553 283 ELKERG-----LARPVLIVAPTSLVGNWQRELAKFAP--GLRVLVLDGTRERAKGAN--------PFEDAD-------LV 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:COG0553 341 ITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK 420

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  511 EFRKNFENPILRGRdadatdkeitkgEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKS- 589
Cdd:COG0553 421 AFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYl 488

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  590 -REVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNfedefddeddlelpddynmpgsKARDVQTKYSAKFSILERFLHKIK 668
Cdd:COG0553 489 rRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------------------EEGAELSGRSAKLEALLELLEELL 546

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  669 tESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQEfIFLLSSKAGGCGINLIGANRLI 748
Cdd:COG0553 547 -AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVI 624

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6321275  749 LMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVD 806
Cdd:COG0553 625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 274-621 5.73e-82

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 265.70  E-value: 5.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    274 HQVEGVRFLYRCVTGLVMkdyleaeafntssedplksdekaltesqkteqnnrgayGCIMADEMGLGKTLQCIALMWTLL 353
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGR--------------------------------------GGILADEMGLGKTLQTISLLLYLK 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    354 RQGPQGKRlidKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMgggnttvsqaiHAWAQAQGRNIVKPVLIIS 433
Cdd:pfam00176  43 HVDKNWGG---PTLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQ-----------ERWKNDPNFLADFDVVITT 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    434 YETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFR 513
Cdd:pfam00176 109 YETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFR 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    514 KNFENPILRGrdadatdkeitKGEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKSRE-- 591
Cdd:pfam00176 189 NWFDRPIERG-----------GGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDln 257

                         330       340       350
                  ....*....|....*....|....*....|..
gi 6321275    592 --VKKVVKGVGGSQPLRAIGILKKLCNHPNLL 621
Cdd:pfam00176 258 aiKTGEGGREIKASLLNILMRLRKICNHPGLI 289
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
 29-246 1.14e-61

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 206.73  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     29 VQDSVNRLTKPFRVPYKNTHippaagriatgsdNIVGGRSLRKRSAtVCYSGLDINADEAEYNSQDISfsqltKRRKDAL 108
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATP-------------TRASDRPARKRRK-VSYAGADGDAEDGDSDKPYTN-----VERRLAL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    109 SAQRLAK-DPTRLSHIQYTLRRSFTVPIKGYVQRHS----LPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDgemiv 183
Cdd:pfam08658  62 ATRRVNKfPVFRVKDKETVFRKSFSVPLKNKKQGAYnprrPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVD----- 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275    184 hdtSMDNKEEEskkmikstqEKDNINKEKNSQEERPTQRigrhpalMTNGVRNKPLRELLGDS 246
Cdd:pfam08658 137 ---DRDKPEEE---------EEAEEEEEEEEPEEKARKK-------LDNPLPHKSLAEILGIK 180
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 332-805 2.85e-59

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 219.67  E-value: 2.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    332 IMADEMGLGKTLQCIALMWTLLR----QGPQgkrlidkcIIVCPSSLVNNWANELIKWlgpntlTPLAVDGKKSsmggGN 407
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVVAPKSTLGNWMNEIRRF------CPVLRAVKFH----GN 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    408 TTVSQAIHAWAQAQGRNivkPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPI 487
Cdd:PLN03142  254 PEERAHQREELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    488 QNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrDADATDKEItkgeaqLQKLSTIVSKFIIRRTNDILAKYLPCKY 567
Cdd:PLN03142  331 QNNLHELWALLNFLLPEIFSSAETFDEWFQI------SGENDQQEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKK 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    568 EHVIFVNLKPLQNELYNKLIKsREVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNFEDefddeddlelpddynmPGSK-- 645
Cdd:PLN03142  399 ETILKVGMSQMQKQYYKALLQ-KDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAE----------------PGPPyt 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    646 ARDVQTKYSAKFSILERFLHKIKtESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQE 725
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLK-ERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    726 FIFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVV 805
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 653-781 1.02e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.15  E-value: 1.02e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  653 YSAKFSILERFLHKIKtESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGqEFIFLLSS 732
Cdd:cd18793   9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6321275  733 KAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFI 781
Cdd:cd18793  87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 655-770 1.02e-24

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: 99.59  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    655 AKFSILERFLhkiKTESDDKIVLISNYTQTLDlIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEgqeFIFLLSSKA 734
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK---IDVLVATDV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6321275    735 GGCGINLIGANRLILMDPDWNPAADQQALARVWRDG 770
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
686-770 4.02e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.34  E-value: 4.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     686 DLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQefiFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALAR 765
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 6321275     766 VWRDG 770
Cdd:smart00490  78 AGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
330-504 2.00e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 87.55  E-value: 2.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     330 GCIMADEMGLGKTLQCIALMWTLLRQGPQGkrlidKCIIVCP-SSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGNT 408
Cdd:smart00487  26 DVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     409 TVSQAIHawaqaqgrnivkpVLIISYETLRRNVDQ--LKNCNVGLMLADEGHRLKN---GDSLTFTALDSISCPRRVILS 483
Cdd:smart00487 101 LESGKTD-------------ILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDggfGDQLEKLLKLLPKNVQLLLLS 167

                          170       180
                   ....*....|....*....|....
gi 6321275     484 GTP---IQNDLSEYFALLSFSNPG 504
Cdd:smart00487 168 ATPpeeIENLLELFLNDPVFIDVG 191
DpdE NF041062
protein DpdE;
334-530 2.02e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 54.98  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    334 ADEMGLGKTLQciALMwtLLRQgpqgkRLIDKC----IIVCPSSLVNNWANELIkwlgpntlTPLAVDgkkSSMGGGntt 409
Cdd:NF041062  176 ADEVGLGKTIE--AGL--VIRQ-----HLLDNPdarvLVLVPDALVRQWRRELR--------DKFFLD---DFPGAR--- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    410 vsqaihawaqaqgrnivkpVLIISYETLRRNVDQLKNCnvGLMLADEGHRL-------KNGDSLTFTALDSI--SCPRRV 480
Cdd:NF041062  233 -------------------VRVLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLL 291

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6321275    481 ILSGTPIQNDLSEYFALLSFSNPGL--LGSRAEFRKNFEN-----PILRGRDADATD 530
Cdd:NF041062  292 LLSATPVLGNEETFLALLHLLDPDLypLDDLEAFRERLEEreelgRLVLGLDPDNPN 348
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 271-554 2.67e-150

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A 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: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 442.29  E-value: 2.67e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTGlvmkdyleaeafntssedplksdekaltesqkteQNNRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18067   1 LRPHQREGVKFLYRCVTG----------------------------------RRIRGSHGCIMADEMGLGKTLQCITLMW 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNtLTPLAVDGKKSSMGGGNTTVsqaihaWAQAQGRNIVKPVL 430
Cdd:cd18067  47 TLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKLVQ------WASQQGRRVSTPVL 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:cd18067 120 IISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAA 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6321275  511 EFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18067 200 EFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 271-806 3.52e-121

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 383.04  E-value: 3.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCvtglvmkdyleaeafntssedplksdekaltesqkteQNNRGayGCIMADEMGLGKTLQCIALMW 350
Cdd:COG0553 242 LRPYQLEGAAWLLFL-------------------------------------RRLGL--GGLLADDMGLGKTIQALALLL 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGpqgkrLIDKCIIVCPSSLVNNWANELIKWLGpnTLTPLAVDGKKSSMGGGNttvsqaihAWAQAQgrnivkpVL 430
Cdd:COG0553 283 ELKERG-----LARPVLIVAPTSLVGNWQRELAKFAP--GLRVLVLDGTRERAKGAN--------PFEDAD-------LV 340

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRA 510
Cdd:COG0553 341 ITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK 420

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  511 EFRKNFENPILRGRdadatdkeitkgEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKS- 589
Cdd:COG0553 421 AFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYl 488

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  590 -REVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNfedefddeddlelpddynmpgsKARDVQTKYSAKFSILERFLHKIK 668
Cdd:COG0553 489 rRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------------------EEGAELSGRSAKLEALLELLEELL 546

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  669 tESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQEfIFLLSSKAGGCGINLIGANRLI 748
Cdd:COG0553 547 -AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVI 624

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6321275  749 LMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVD 806
Cdd:COG0553 625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 271-554 1.16e-109

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They 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: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 336.95  E-value: 1.16e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTGlvmkdyleaeafntssedplksdekaltesqkteQNNRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18004   1 LRPHQREGVQFLYDCLTG----------------------------------RRGYGGGGAILADEMGLGKTLQAIALVW 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGkkssmgggNTTVSQAIHAWAQAQGRnivKPVL 430
Cdd:cd18004  47 TLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDKWLGLRRIKVVTADG--------NAKDVKASLDFFSSAST---YPVL 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNC-NVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSR 509
Cdd:cd18004 116 IISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSL 195

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6321275  510 AEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18004 196 ASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 274-621 5.73e-82

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 265.70  E-value: 5.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    274 HQVEGVRFLYRCVTGLVMkdyleaeafntssedplksdekaltesqkteqnnrgayGCIMADEMGLGKTLQCIALMWTLL 353
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGR--------------------------------------GGILADEMGLGKTLQTISLLLYLK 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    354 RQGPQGKRlidKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMgggnttvsqaiHAWAQAQGRNIVKPVLIIS 433
Cdd:pfam00176  43 HVDKNWGG---PTLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQ-----------ERWKNDPNFLADFDVVITT 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    434 YETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFR 513
Cdd:pfam00176 109 YETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFR 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    514 KNFENPILRGrdadatdkeitKGEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKSRE-- 591
Cdd:pfam00176 189 NWFDRPIERG-----------GGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDln 257

                         330       340       350
                  ....*....|....*....|....*....|..
gi 6321275    592 --VKKVVKGVGGSQPLRAIGILKKLCNHPNLL 621
Cdd:pfam00176 258 aiKTGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 271-554 6.23e-78

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B 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: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 252.84  E-value: 6.23e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTGLVMKdyleaeafntssedplksdekaltesqkteqnnrGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18066   1 LRPHQREGIEFLYECVMGMRVN----------------------------------ERFGAILADEMGLGKTLQCISLIW 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQG-KRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSsmgggnttVSQAIHAwaqaqgrnIVKPV 429
Cdd:cd18066  47 TLLRQGPYGgKPVIKRALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHK--------VEEFIAS--------PLYSV 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  430 LIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSR 509
Cdd:cd18066 111 LIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSL 190

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6321275  510 AEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18066 191 STYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
 29-246 1.14e-61

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 206.73  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     29 VQDSVNRLTKPFRVPYKNTHippaagriatgsdNIVGGRSLRKRSAtVCYSGLDINADEAEYNSQDISfsqltKRRKDAL 108
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATP-------------TRASDRPARKRRK-VSYAGADGDAEDGDSDKPYTN-----VERRLAL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    109 SAQRLAK-DPTRLSHIQYTLRRSFTVPIKGYVQRHS----LPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDgemiv 183
Cdd:pfam08658  62 ATRRVNKfPVFRVKDKETVFRKSFSVPLKNKKQGAYnprrPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVD----- 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275    184 hdtSMDNKEEEskkmikstqEKDNINKEKNSQEERPTQRigrhpalMTNGVRNKPLRELLGDS 246
Cdd:pfam08658 137 ---DRDKPEEE---------EEAEEEEEEEEPEEKARKK-------LDNPLPHKSLAEILGIK 180
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 332-805 2.85e-59

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 219.67  E-value: 2.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    332 IMADEMGLGKTLQCIALMWTLLR----QGPQgkrlidkcIIVCPSSLVNNWANELIKWlgpntlTPLAVDGKKSsmggGN 407
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVVAPKSTLGNWMNEIRRF------CPVLRAVKFH----GN 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    408 TTVSQAIHAWAQAQGRNivkPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPI 487
Cdd:PLN03142  254 PEERAHQREELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    488 QNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrDADATDKEItkgeaqLQKLSTIVSKFIIRRTNDILAKYLPCKY 567
Cdd:PLN03142  331 QNNLHELWALLNFLLPEIFSSAETFDEWFQI------SGENDQQEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKK 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    568 EHVIFVNLKPLQNELYNKLIKsREVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNFEDefddeddlelpddynmPGSK-- 645
Cdd:PLN03142  399 ETILKVGMSQMQKQYYKALLQ-KDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAE----------------PGPPyt 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    646 ARDVQTKYSAKFSILERFLHKIKtESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQE 725
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLK-ERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    726 FIFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVV 805
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 271-533 1.30e-57

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They 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: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 197.51  E-value: 1.30e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCvtgLVMKDYLEAEAFntssedplksdekaltesqkteqnnrgayGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18007   1 LKPHQVEGVRFLWSN---LVGTDVGSDEGG-----------------------------GCILAHTMGLGKTLQVITFLH 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKRlidkCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSmgggnTTVSQ---AIHAWAQAQGrnivk 427
Cdd:cd18007  49 TYLAAAPRRSR----PLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSAS-----KRADArlrKINKWHKEGG----- 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  428 pVLIISYETLRR---NVDQLKNC-----------NVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSE 493
Cdd:cd18007 115 -VLLIGYELFRNlasNATTDPRLkqefiaalldpGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKE 193

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 6321275  494 YFALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEI 533
Cdd:cd18007 194 YWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDV 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 653-781 1.02e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.15  E-value: 1.02e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  653 YSAKFSILERFLHKIKtESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGqEFIFLLSS 732
Cdd:cd18793   9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6321275  733 KAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFI 781
Cdd:cd18793  87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 271-503 3.19e-54

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: 186.23  E-value: 3.19e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCvtglvmkdyleaeafntssedplksdekaltesqkteqnNRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd17919   1 LRPYQLEGLNFLLEL---------------------------------------YENGPGGILADEMGLGKTLQAIAFLA 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQgkrlIDKCIIVCPSSLVNNWANELIKWLGpnTLTPLAVDGKKSSMgggnttVSQAIHAWAQAQGrnivkpVL 430
Cdd:cd17919  42 YLLKEGKE----RGPVLVVCPLSVLENWEREFEKWTP--DLRVVVYHGSQRER------AQIRAKEKLDKFD------VV 103

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275  431 IISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNP 503
Cdd:cd17919 104 LTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 271-554 9.20e-54

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 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: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 187.20  E-value: 9.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVtglvmkdyleaeafntssedplksdekaltesqkteQNNRGaygCIMADEMGLGKTLQCIALMW 350
Cdd:cd18005   1 LRDYQREGVEFMYDLY------------------------------------KNGRG---GILGDDMGLGKTVQVIAFLA 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLL----------RQGPQGKRLIDKCI------IVCPSSLVNNWANELIKWlGPNTLTPLAvdgkkssmGGGNTTVSQAi 414
Cdd:cd18005  42 AVLgktgtrrdreNNRPRFKKKPPASSakkpvlIVAPLSVLYNWKDELDTW-GHFEVGVYH--------GSRKDDELEG- 111

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  415 hawAQAQGRnivKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEY 494
Cdd:cd18005 112 ---RLKAGR---LEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKEL 185

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  495 FALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18005 186 WCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR 245
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 267-555 4.90e-48

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 170.05  E-value: 4.90e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  267 LAKILRPHQVEGVRFLYRcvtglvmkdyleaeafntssedplksdekaLTESQkteqnnrgaYGCIMADEMGLGKTLQCI 346
Cdd:cd18012   1 LKATLRPYQKEGFNWLSF------------------------------LRHYG---------LGGILADDMGLGKTLQTL 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  347 ALmwtLLRQGPQGKRLidKCIIVCPSSLVNNWANELIKWlGPnTLTPLAVDGKKSSmgggnttvSQAIHAWAQAQgrniv 426
Cdd:cd18012  42 AL---LLSRKEEGRKG--PSLVVAPTSLIYNWEEEAAKF-AP-ELKVLVIHGTKRK--------REKLRALEDYD----- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  427 kpVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLL 506
Cdd:cd18012 102 --LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLL 179

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 6321275  507 GSRAEFRKNFENPILRGRDADAtdkeitkgeaqLQKLSTIVSKFIIRRT 555
Cdd:cd18012 180 GSYKRFKKRFAKPIEKDGDEEA-----------LEELKKLISPFILRRL 217
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 271-554 2.60e-46

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L 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: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 165.62  E-value: 2.60e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRcvtglvmkdyleaeafntssedplksdekaLTESQKteqnnrgayGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18001   1 LYPHQREGVAWLWS------------------------------LHDGGK---------GGILADDMGLGKTVQICAFLS 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGpqgkrLIDKCIIVCPSSLVNNWANELIKWlGPNTLTplavdgkKSSMGGGNTTVSQAIHAWAQAQGrnivkpVL 430
Cdd:cd18001  42 GMFDSG-----LIKSVLVVMPTSLIPHWVKEFAKW-TPGLRV-------KVFHGTSKKERERNLERIQRGGG------VL 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  431 IISYETLRRNVDQLKNCNVG-----LMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPG- 504
Cdd:cd18001 103 LTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGs 182

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6321275  505 LLGSRAEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18001 183 LLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 324-554 4.37e-43

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 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: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 156.36  E-value: 4.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  324 NNRGAYGcIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIDKC-IIVCPSSLVNNWANELIKWLGPNTLTPLAVDGkkss 402
Cdd:cd17999  16 NKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPsLVVCPPTLVGHWVAEIKKYFPNAFLKPLAYVG---- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  403 mgggnttvSQAIHAWAQAQGRNivKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVIL 482
Cdd:cd17999  91 --------PPQERRRLREQGEK--HNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLIL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd17999 161 SGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 271-533 6.88e-41

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a 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: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 150.81  E-value: 6.88e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVTglvmkdyleaeafntssedplksdeKALTESQKTEQNnrgayGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18068   1 LKPHQVDGVQFMWDCCC-------------------------ESLKKTKKSPGS-----GCILAHCMGLGKTLQVVTFLH 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLLRQGPQGKrlIDKCIIVCPSSLVNNWANELIKWL----GPNTLTPLAVDGKKSSmgggnTTVSQAIHAWAQAQGrniv 426
Cdd:cd18068  51 TVLLCEKLEN--FSRVLVVCPLNTVLNWLNEFEKWQeglkDEEKIEVNELATYKRP-----QERSYKLQRWQEEGG---- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  427 kpVLIISYETLR-----RNVDQ-----------LKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQND 490
Cdd:cd18068 120 --VMIIGYDMYRilaqeRNVKSreklkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNN 197

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 6321275  491 LSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEI 533
Cdd:cd18068 198 LIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 271-533 3.62e-39

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 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: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 144.96  E-value: 3.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYrcvtglvmKDYLEA-EAFNTSSedplksdekaltesqkteqnnrgAYGCIMADEMGLGKTLQCIALM 349
Cdd:cd18069   1 LKPHQIGGIRFLY--------DNIIESlERYKGSS-----------------------GFGCILAHSMGLGKTLQVISFL 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  350 WTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWLGPNTLTPLAVDG--KKSSMGGGNTTVSQ---AIHAWAQAQGrn 424
Cdd:cd18069  50 DVLLRHTGAKTVLA-----IVPVNTLQNWLSEFNKWLPPPEALPNVRPRpfKVFILNDEHKTTAArakVIEDWVKDGG-- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  425 ivkpVLIISYET--LRRNVDqlkncnvgLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSN 502
Cdd:cd18069 123 ----VLLMGYEMfrLRPGPD--------VVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190

                       250       260       270
                ....*....|....*....|....*....|.
gi 6321275  503 PGLLGSRAEFRKNFENPILRGRDADATDKEI 533
Cdd:cd18069 191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDV 221
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 271-554 4.40e-32

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L 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: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 124.47  E-value: 4.40e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVtglvmkdyleaeafntssedplksdekaltesqkteqnnRGAYGCIMADEMGLGKTLQCIALMW 350
Cdd:cd18006   1 LRPYQLEGVNWLLQCR---------------------------------------AEQHGCILGDEMGLGKTCQTISLLW 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TL-LRQGPQGKRLIdkciiVCPSSLVNNWANELiKWLGPNtLTPLAVDGKKSSmgggNTTVSQAIHAWAQAQgrnivkpV 429
Cdd:cd18006  42 YLaGRLKLLGPFLV-----LCPLSVLDNWKEEL-NRFAPD-LSVITYMGDKEK----RLDLQQDIKSTNRFH-------V 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  430 LIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSR 509
Cdd:cd18006 104 LLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKD 183

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 6321275  510 A--EFRKNFenpilrgrdadatdKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18006 184 KldDFIKAY--------------SETDDESETVEELHLLLQPFLLRR 216
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 332-554 1.79e-31

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS 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: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 123.27  E-value: 1.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWLgPnTLTPLAVDGKKSSMgggNTTVS 411
Cdd:cd18009  26 ILADEMGLGKTIQTIALLAHLRERGVWGPFLV-----IAPLSTLPNWVNEFARFT-P-SVPVLLYHGTKEER---ERLRK 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 QAIhawaQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDL 491
Cdd:cd18009  96 KIM----KREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNL 171

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321275  492 SEYFALLSFSNPGLLGSRAEFRKNFEnpiLRGRDADATDKEITKGEAQ---LQKLSTIVSKFIIRR 554
Cdd:cd18009 172 SELWSLLNFLLPDVFDDLSSFESWFD---FSSLSDNAADISNLSEEREqniVHMLHAILKPFLLRR 234
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 330-506 2.66e-30

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 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: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 118.58  E-value: 2.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  330 GCIMADEMGLGKTLQCIALmwtlLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLavdgkKSSMGGGNTT 409
Cdd:cd18000  21 GGILGDEMGLGKTIQIIAF----LAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVL-----HSSGSGTGSE 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  410 VSQAIHAWAQAQGRNIVKP--VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPI 487
Cdd:cd18000  92 EKLGSIERKSQLIRKVVGDggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPI 171

                       170
                ....*....|....*....
gi 6321275  488 QNDLSEYFALLSFSNPGLL 506
Cdd:cd18000 172 QNNLKELWSLFDFVFPPYL 190
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 329-554 2.51e-29

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to 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: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 117.39  E-value: 2.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  329 YGCIMADEMGLGKTLQCIALMWTLLRQGPQG----------KRLIDKC---IIVCPSSLVNNWANELIKWLGPNTLTPLA 395
Cdd:cd18008  15 RGGILADEMGLGKTIQALALILATRPQDPKIpeeleenssdPKKLYLSkttLIVVPLSLLSQWKDEIEKHTKPGSLKVYV 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  396 VDGKKSsmgggNTTVSQAIHAwaqaqgrNIVkpvlIISYETLRR---------NVDQLKNCNVGLM-------LADEGHR 459
Cdd:cd18008  95 YHGSKR-----IKSIEELSDY-------DIV----ITTYGTLASefpknkkggGRDSKEKEASPLHrirwyrvILDEAHN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  460 LKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADatdkeitkgeaq 539
Cdd:cd18008 159 IKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKA------------ 226

                       250
                ....*....|....*
gi 6321275  540 LQKLSTIVSKFIIRR 554
Cdd:cd18008 227 LERLQALLKPILLRR 241
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 271-554 5.26e-29

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the 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: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 115.81  E-value: 5.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  271 LRPHQVEGVRFLYRCVtglvmkdyleaeafntssedplksdekaltesqkteQNNRGaygCIMADEMGLGKTLQCIALMW 350
Cdd:cd17995   1 LRDYQLEGVNWLLFNW------------------------------------YNRRN---CILADEMGLGKTIQSIAFLE 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  351 TLL-RQGPQGKRLIdkciiVCPSSLVNNWANELIKWlgpntlTPLAVDGKKSSMGGGNTT-VSQAIHAWAQAQ-GRNIVK 427
Cdd:cd17995  42 HLYqVEGIRGPFLV-----IAPLSTIPNWQREFETW------TDMNVVVYHGSGESRQIIqQYEMYFKDAQGRkKKGVYK 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  428 -PVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLL 506
Cdd:cd17995 111 fDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKF 190

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6321275  507 GSRAEFRKNFenpilrGRdadatdkeiTKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd17995 191 PSSEEFLEEF------GD---------LKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 331-554 5.95e-29

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both 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: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 115.53  E-value: 5.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQ----GPQgkrlidkcIIVCPSSLVNNWANELIKWL-GPNTLTPLavdgkkssmgg 405
Cdd:cd17993  23 GILADEMGLGKTVQTISFLSYLFHSqqqyGPF--------LVVVPLSTMPAWQREFAKWApDMNVIVYL----------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  406 GNTTVSQAI--HAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILS 483
Cdd:cd17993  84 GDIKSRDTIreYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLIT 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321275  484 GTPIQNDLSEYFALLSFSNPGllgsRAEFRKNFEnpilrgrdaDATDKEITKGEAQLQKlstIVSKFIIRR 554
Cdd:cd17993 164 GTPLQNSLKELWALLHFLMPG----KFDIWEEFE---------EEHDEEQEKGIADLHK---ELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 332-555 1.08e-27

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) 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: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 112.03  E-value: 1.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMwTLLRQ-----GPQgkrlidkcIIVCPSSLVNNWANELIKWLgPNTltplavdgkkssmggg 406
Cdd:cd17997  26 ILADEMGLGKTLQTISLL-GYLKHykninGPH--------LIIVPKSTLDNWMREFKRWC-PSL---------------- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  407 NTTVSQAIHAWAQAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVIL 482
Cdd:cd17997  80 RVVVLIGDKEERADIIRDVLLPgkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFEnpilrgrdadaTDKEITKGEAQLQKLSTIVSKFIIRRT 555
Cdd:cd17997 160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-----------VNNCDDDNQEVVQRLHKVLRPFLLRRI 221
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 331-554 3.98e-27

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 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: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 109.99  E-value: 3.98e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALM------WTLLrqgpqgkrlidkciIVCPSSLVNNWANELIKWLGpnTLTPLAVdgkkSSMG 404
Cdd:cd18010  19 VLIADEMGLGKTVQAIAIAayyreeWPLL--------------IVCPSSLRLTWADEIERWLP--SLPPDDI----QVIV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  405 GGNTTVSqaiHAWAQaqgrnivkpVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSI--SCPRRVIL 482
Cdd:cd18010  79 KSKDGLR---DGDAK---------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILL 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADatdkeiTKGEAQLQKLSTIVSK-FIIRR 554
Cdd:cd18010 147 SGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWD------YSGSSNLEELHLLLLAtIMIRR 213
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 332-554 5.93e-26

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 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: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 107.40  E-value: 5.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQgpqgKRLIDKCIIVCPSSLVNNWANELIKWlGPNTLTPLAVdgkkSSMGGGNTTVS 411
Cdd:cd18054  43 ILADEMGLGKTIQTISFLSYLFHQ----HQLYGPFLLVVPLSTLTSWQREFEIW-APEINVVVYI----GDLMSRNTIRE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 qaiHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDL 491
Cdd:cd18054 114 ---YEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSL 190

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275  492 SEYFALLSFSNPgllgSRAEFRKNFENPILRGRDADatdkeitkgeaqLQKLSTIVSKFIIRR 554
Cdd:cd18054 191 KELWSLLHFIMP----EKFEFWEDFEEDHGKGRENG------------YQSLHKVLEPFLLRR 237
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 331-554 7.41e-26

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 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: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 106.68  E-value: 7.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWLGPNTLtplavdgkkssMGGGNTTV 410
Cdd:cd18060  22 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLV-----IAPLSTITNWEREFNTWTEMNTI-----------VYHGSLAS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAIHAW----AQAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVIL 482
Cdd:cd18060  86 RQMIQQYemycKDSRGRLIPGAykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLL 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdkeiTKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18060 166 TGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---------------LKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 332-563 1.62e-25

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) 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: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 105.91  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLrqgpQGKRLIDKCIIVCPSSLVNNWANELIKWLgPnTLTPLAVDGKKssmgggnttvs 411
Cdd:cd17996  26 ILADEMGLGKTIQTISLITYLM----EKKKNNGPYLVIVPLSTLSNWVSEFEKWA-P-SVSKIVYKGTP----------- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 qAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDS-LTFTALDSISCPRRVILSGTPIQND 490
Cdd:cd17996  89 -DVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSkLTQTLNTYYHARYRLLLTGTPLQNN 167

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321275  491 LSEYFALLSFSNPGLLGSRAEFRKNFENPIlrgrdadatdkeITKGEAQLQKLSTIVSKFIIRRTNDILAKYL 563
Cdd:cd17996 168 LPELWALLNFLLPKIFKSCKTFEQWFNTPF------------ANTGEQVKIELNEEETLLIIRRLHKVLRPFL 228
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 332-554 1.69e-25

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP 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: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 105.51  E-value: 1.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQ----GPQgkrlidkcIIVCPSSLVNNWANELIKWL-GPNTLTPL--AVDGKKSSMG 404
Cdd:cd18003  23 ILADEMGLGKTIQTIALLAHLACEkgnwGPH--------LIVVPTSVMLNWEMEFKRWCpGFKILTYYgsAKERKLKRQG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  405 ggnttvsqaihaWAQAQGRNivkpVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSG 484
Cdd:cd18003  95 ------------WMKPNSFH----VCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTG 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  485 TPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPIlrgRDADATDKEITKGeaQLQKLSTIVSKFIIRR 554
Cdd:cd18003 159 TPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL---TAMSEGSQEENEE--LVRRLHKVLRPFLLRR 223
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 655-770 1.02e-24

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: 99.59  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    655 AKFSILERFLhkiKTESDDKIVLISNYTQTLDlIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEgqeFIFLLSSKA 734
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK---IDVLVATDV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6321275    735 GGCGINLIGANRLILMDPDWNPAADQQALARVWRDG 770
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 331-554 2.67e-24

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 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: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 102.04  E-value: 2.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWLGPNTLtplavdgkkssMGGGNTTV 410
Cdd:cd18058  22 CILADEMGLGKTIQSITFLSEIFLMGIRGPFLI-----IAPLSTITNWEREFRTWTEMNAI-----------VYHGSQIS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAIHAWA----QAQGRNIVK----PVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVIL 482
Cdd:cd18058  86 RQMIQQYEmyyrDEQGNPLSGifkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLL 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdkeiTKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18058 166 TGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---------------LKTEEQVKKLQSILKPMMLRR 222
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 332-554 3.09e-24

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 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: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 102.20  E-value: 3.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQgpqgKRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLavdgkkssmgGGNTTVS 411
Cdd:cd18002  23 ILADEMGLGKTVQSIAVLAHLAEE----HNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPY----------WGNPKDR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 QAIHA-WAQAQ--GRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQ 488
Cdd:cd18002  89 KVLRKfWDRKNlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQ 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321275  489 NDLSEYFALLSFSNPGLLGSRAEFRKNFEnpilrgRDADATDKEITK-GEAQLQKLSTIVSKFIIRR 554
Cdd:cd18002 169 NSMAELWALLHFIMPTLFDSHDEFNEWFS------KDIESHAENKTGlNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 331-554 2.30e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 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: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 99.34  E-value: 2.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWlgpNTLTPLAVDGKKSSmgggNTTV 410
Cdd:cd18059  22 CILADEMGLGKTIQSITFLYEIYLKGIHGPFLV-----IAPLSTIPNWEREFRTW---TELNVVVYHGSQAS----RRTI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAIHAWAQAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTP 486
Cdd:cd18059  90 QLYEMYFKDPQGRVIKGSykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTP 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321275  487 IQNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdkeiTKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18059 170 LQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---------------LKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 331-506 1.25e-22

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 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: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 96.30  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQGPQGKRLidkciIVCPSSLVNNWANELIKWLgPNtLTPLAVDGkkssmgggnttv 410
Cdd:cd17998  22 GILADEMGLGKTIQVIAFLAYLKEIGIPGPHL-----VVVPSSTLDNWLREFKRWC-PS-LKVEPYYG------------ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAihawAQAQGRNIVKP------VLIISYETLRRNVDQ---LKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVI 481
Cdd:cd17998  83 SQE----ERKHLRYDILKgledfdVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158

                       170       180
                ....*....|....*....|....*..
gi 6321275  482 LSGTPIQNDLSEYFALLSF--SNPGLL 506
Cdd:cd17998 159 LTGTPLQNNLLELMSLLNFimPKPFIL 185
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 332-554 1.33e-22

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 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: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 98.21  E-value: 1.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQgpqgKRLIDKCIIVCPSSLVNNWANELIKWlGPNTLtplavdgkKSSMGGgnttvS 411
Cdd:cd18063  46 ILADEMGLGKTIQTIALITYLMEH----KRLNGPYLIIVPLSTLSNWTYEFDKW-APSVV--------KISYKG-----T 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 QAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDS-ISCPRRVILSGTPIQND 490
Cdd:cd18063 108 PAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILLTGTPLQNK 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321275  491 LSEYFALLSFSNPGLLGSRAEFRKNFENPI-LRGRDADATDKEITkgeAQLQKLSTIVSKFIIRR 554
Cdd:cd18063 188 LPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETI---LIIRRLHKVLRPFLLRR 249
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 332-554 1.42e-22

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 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: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 97.81  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLrqgpQGKRLIDKCIIVCPSSLVNNWANELIKWlGPNTLtplavdgkKSSMGGgnttvS 411
Cdd:cd18062  46 ILADEMGLGKTIQTIALITYLM----EHKRINGPFLIIVPLSTLSNWVYEFDKW-APSVV--------KVSYKG-----S 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 QAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDS-ISCPRRVILSGTPIQND 490
Cdd:cd18062 108 PAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNK 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321275  491 LSEYFALLSFSNPGLLGSRAEFRKNFENPI-LRGRDADATDKEITkgeAQLQKLSTIVSKFIIRR 554
Cdd:cd18062 188 LPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETI---LIIRRLHKVLRPFLLRR 249
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 330-515 1.53e-21

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: 93.51  E-value: 1.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  330 GCIMADEMGLGKTLQCIALMWTLLRQGpqgkrLIDKCIIVCPSSLVNNWANELIKWLGpntLTPLAVDGKkssmgGGNTT 409
Cdd:cd18011  19 RLLLADEVGLGKTIEAGLIIKELLLRG-----DAKRVLILCPASLVEQWQDELQDKFG---LPFLILDRE-----TAAQL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  410 VSQAIHAWAQAqgrnivkPVLIISYETLRRN---VDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSI------SCPRRV 480
Cdd:cd18011  86 RRLIGNPFEEF-------PIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRARHVL 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6321275  481 ILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKN 515
Cdd:cd18011 159 LLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL 193
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 331-554 2.74e-21

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 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: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 93.53  E-value: 2.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIdkciiVCPSSLVNNWANELIKWLGPNTLtplavdgkkssMGGGNTTV 410
Cdd:cd18061  22 CILADEMGLGKTIQSITFLYEILLTGIRGPFLI-----IAPLSTIANWEREFRTWTDLNVV-----------VYHGSLIS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAIHAWA----QAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVIL 482
Cdd:cd18061  86 RQMIQQYEmyfrDSQGRIIRGAyrfqAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLL 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321275  483 SGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdkeiTKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18061 166 TGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 331-525 3.79e-21

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. 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: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 93.58  E-value: 3.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  331 CIMADEMGLGKTLQCIALMWTLLRQgpqgKRLIDKCIIVCPSSLVNNWANELIKWlgpntlTPLAvdGKKSSMGGGNTTV 410
Cdd:cd18053  42 CILADEMGLGKTIQTISFLNYLFHE----HQLYGPFLLVVPLSTLTSWQREIQTW------APQM--NAVVYLGDINSRN 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 SQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQND 490
Cdd:cd18053 110 MIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNS 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6321275  491 LSEYFALLSFSNPGLLGSraefRKNFENPILRGRD 525
Cdd:cd18053 190 LKELWSLLHFIMPEKFSS----WEDFEEEHGKGRE 220
HELICc smart00490
helicase superfamily c-terminal domain;
686-770 4.02e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.34  E-value: 4.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     686 DLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQefiFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALAR 765
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 6321275     766 VWRDG 770
Cdd:smart00490  78 AGRAG 82
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 320-554 9.96e-20

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 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: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 89.45  E-value: 9.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  320 KTEQNNRGA--YGCIMADEMGLGKTLQCIALMwtllrqgpqgkrLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVD 397
Cdd:cd18071  38 NFSQKKRPElvRGGILADDMGLGKTLTTISLI------------LANFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYH 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  398 GkkssmGGGNTTVSQAihawaqaQGRNIVkpvlIISYETLRR---NVDQ--LKNCNVGLMLADEGHRLKNGDSLTFTALD 472
Cdd:cd18071 106 G-----GERNRDPKLL-------SKYDIV----LTTYNTLASdfgAKGDspLHTINWLRVVLDEGHQIRNPNAQQTKAVL 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  473 SISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDadatdkeitKGEAQLQKLstiVSKFII 552
Cdd:cd18071 170 NLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDP---------TGLKRLQVL---MKQITL 237


                ..
gi 6321275  553 RR 554
Cdd:cd18071 238 RR 239
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 332-554 1.53e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 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: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 88.53  E-value: 1.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQG-PQGKRLIDkciivCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGN--- 407
Cdd:cd18055  23 ILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVS-----APLSTIINWEREFQMWAPDFYVVTYTGDKDSRAIIRENefs 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  408 ---TTVSQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSG 484
Cdd:cd18055  98 fddNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTG 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  485 TPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFenpilrgrdadatdKEITKgEAQLQKLSTIVSKFIIRR 554
Cdd:cd18055 178 TPLQNNLEELFHLLNFLTPERFNNLEGFLEEF--------------ADISK-EDQIKKLHDLLGPHMLRR 232
DEXDc smart00487
DEAD-like helicases superfamily;
330-504 2.00e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 87.55  E-value: 2.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     330 GCIMADEMGLGKTLQCIALMWTLLRQGPQGkrlidKCIIVCP-SSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGNT 408
Cdd:smart00487  26 DVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275     409 TVSQAIHawaqaqgrnivkpVLIISYETLRRNVDQ--LKNCNVGLMLADEGHRLKN---GDSLTFTALDSISCPRRVILS 483
Cdd:smart00487 101 LESGKTD-------------ILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDggfGDQLEKLLKLLPKNVQLLLLS 167

                          170       180
                   ....*....|....*....|....
gi 6321275     484 GTP---IQNDLSEYFALLSFSNPG 504
Cdd:smart00487 168 ATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 332-554 3.22e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 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: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 86.72  E-value: 3.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQG-PQGKRLIDkciivCPSSLVNNWANELIKWlgpntltplAVDGKKSSMGGGNttv 410
Cdd:cd17994  23 ILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVS-----APLSTIINWEREFEMW---------APDFYVVTYVGDH--- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  411 sqaihawaqaqgrnivkpVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQND 490
Cdd:cd17994  86 ------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNN 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321275  491 LSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdkeITKgEAQLQKLSTIVSKFIIRR 554
Cdd:cd17994 148 LEELFHLLNFLTPERFNNLQGFLEEFAD--------------ISK-EDQIKKLHDLLGPHMLRR 196
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 332-554 4.59e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 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: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 87.04  E-value: 4.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQG-PQGKRLIDkciivCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGN--- 407
Cdd:cd18057  23 ILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVS-----APLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENefs 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  408 ---TTVSQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSG 484
Cdd:cd18057  98 fedNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTG 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  485 TPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFenpilrgrdadatdKEITKgEAQLQKLSTIVSKFIIRR 554
Cdd:cd18057 178 TPLQNNLEELFHLLNFLTPERFNNLEGFLEEF--------------ADISK-EDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 332-554 2.06e-18

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 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: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 85.50  E-value: 2.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLLRQG-PQGKRLIDkciivCPSSLVNNWANELIKWlGPNTLTPLAVDGKKS-------SM 403
Cdd:cd18056  23 ILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVS-----APLSTIINWEREFEMW-APDMYVVTYVGDKDSraiirenEF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  404 GGGNTTVSQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILS 483
Cdd:cd18056  97 SFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLT 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321275  484 GTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFenpilrgrdadatdKEITKgEAQLQKLSTIVSKFIIRR 554
Cdd:cd18056 177 GTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF--------------ADIAK-EDQIKKLHDMLGPHMLRR 232
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 332-566 2.41e-18

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 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: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 85.49  E-value: 2.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLlrqgPQGKRLIDKCIIVCPSSLVNNWANELIKWLgpNTLTPLAVDGKKSSMGggnttvs 411
Cdd:cd18064  38 ILADEMGLGKTLQTISLLGYM----KHYRNIPGPHMVLVPKSTLHNWMAEFKRWV--PTLRAVCLIGDKDQRA------- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 qaihawaqAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPI 487
Cdd:cd18064 105 --------AFVRDVLLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPL 176

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321275  488 QNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGrdadatDKEItkgeaqLQKLSTIVSKFIIRRTNDILAKYLPCK 566
Cdd:cd18064 177 QNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG------DQKL------VERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 332-554 2.96e-17

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 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: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 81.99  E-value: 2.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  332 IMADEMGLGKTLQCIALMWTLlrqgPQGKRLIDKCIIVCPSSLVNNWANELIKWLgpNTLTPLAVDGKKSSMGggnttvs 411
Cdd:cd18065  38 ILADEMGLGKTLQTIALLGYL----KHYRNIPGPHMVLVPKSTLHNWMNEFKRWV--PSLRAVCLIGDKDARA------- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  412 qaihawaqAQGRNIVKP----VLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPI 487
Cdd:cd18065 105 --------AFIRDVMMPgewdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPL 176

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321275  488 QNDLSEYFALLSFSNPGLLGSRAEFRKNFENpilrgrdadatdKEITKGEAQLQKLSTIVSKFIIRR 554
Cdd:cd18065 177 QNNLHELWALLNFLLPDVFNSADDFDSWFDT------------KNCLGDQKLVERLHAVLKPFLLRR 231
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 330-500 4.52e-12

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH 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: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 67.37  E-value: 4.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  330 GCIMADEMGLGKTLQCIALMwtLLRQGPQGK--------RLIDKC---------------IIVCPSSLVNNWANElIKWL 386
Cdd:cd18070  16 GGILADEMGLGKTVEVLALI--LLHPRPDNDldaadddsDEMVCCpdclvaetpvsskatLIVCPSAILAQWLDE-INRH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  387 GPNTLTPLAVDGKKSSMGggntTVSQAIHAWAQAQgrnivkpVLIISYETLRRNVdqlkncnvglmlaDEGHRLKNGDSL 466
Cdd:cd18070  93 VPSSLKVLTYQGVKKDGA----LASPAPEILAEYD-------IVVTTYDVLRTEL-------------HYAEANRSNRRR 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321275  467 T-FTALDSISCP------RRVIL----------------------------SGTPIQNDLSEYFALLSF 500
Cdd:cd18070 149 RrQKRYEAPPSPlvlvewWRVCLdeaqmvesstskaaemarrlprvnrwcvSGTPIQRGLDDLFGLLSF 217
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 330-500 2.01e-11

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 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: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 64.81  E-value: 2.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  330 GCIMADEMGLGKTLQCIALMWTL-----LRQGPQGKRLI--DKC-----------IIVCPSSLVNNWANELIKWLGPNTL 391
Cdd:cd18072  22 GGILADDMGLGKTLTMIALILAQkntqnRKEEEKEKALTewESKkdstlvpsagtLVVCPASLVHQWKNEVESRVASNKL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  392 TPLAVDGKKSSmgggntTVSQAIHAWaqaqgrNIVkpvlIISYETLRRNVDQLKNCNVGLMLA---------DEGHRLKN 462
Cdd:cd18072 102 RVCLYHGPNRE------RIGEVLRDY------DIV----ITTYSLVAKEIPTYKEESRSSPLFriawariilDEAHNIKN 165

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6321275  463 GDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSF 500
Cdd:cd18072 166 PKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKF 203
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 329-523 1.01e-08

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family 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: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 56.59  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  329 YGCIMADeMGLGKTLQCIALMWTLLRQGPQGKRLidkciIVCPSSLV-NNWANELIKWLGPNTLTPLAVDGKKSSMgggn 407
Cdd:cd18013  17 YCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVL-----VIAPLRVArSTWPDEVEKWNHLRNLTVSVAVGTERQR---- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  408 ttvSQAIHAWAQaqgrnivkpVLIISYETLRRNVDQLKN-CNVGLMLADEGHRLKNGDSLTFTALDSIscpRRVI----- 481
Cdd:cd18013  87 ---SKAANTPAD---------LYVINRENLKWLVNKSGDpWPFDMVVIDELSSFKSPRSKRFKALRKV---RPVIkrlig 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6321275  482 LSGTPIQNDLSEYFALLSFSNPG-LLG-SRAEFRKNFENPILRG 523
Cdd:cd18013 152 LTGTPSPNGLMDLWAQIALLDQGeRLGrSITAYRERWFDPDKRN 195
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 312-486 5.16e-08

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: 52.69  E-value: 5.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  312 EKALTESQKTEQNNRGAygCIMAdeMGLGKTLQCIALMWTLLRqgpqgkrliDKCIIVCPS-SLVNNWANELIKWLGPnt 390
Cdd:cd17926   6 EEALEAWLAHKNNRRGI--LVLP--TGSGKTLTALALIAYLKE---------LRTLIVVPTdALLDQWKERFEDFLGD-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  391 ltplAVDGKkssMGGGNTTVsqaihawaqaqgrNIVKPVLIISYETLRRNV----DQLKNCnvGLMLADEGHRLkngDSL 466
Cdd:cd17926  71 ----SSIGL---IGGGKKKD-------------FDDANVVVATYQSLSNLAeeekDLFDQF--GLLIVDEAHHL---PAK 125

                       170       180
                ....*....|....*....|.
gi 6321275  467 TFTA-LDSISCPRRVILSGTP 486
Cdd:cd17926 126 TFSEiLKELNAKYRLGLTATP 146
DpdE NF041062
protein DpdE;
334-530 2.02e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 54.98  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    334 ADEMGLGKTLQciALMwtLLRQgpqgkRLIDKC----IIVCPSSLVNNWANELIkwlgpntlTPLAVDgkkSSMGGGntt 409
Cdd:NF041062  176 ADEVGLGKTIE--AGL--VIRQ-----HLLDNPdarvLVLVPDALVRQWRRELR--------DKFFLD---DFPGAR--- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275    410 vsqaihawaqaqgrnivkpVLIISYETLRRNVDQLKNCnvGLMLADEGHRL-------KNGDSLTFTALDSI--SCPRRV 480
Cdd:NF041062  233 -------------------VRVLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLL 291

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6321275    481 ILSGTPIQNDLSEYFALLSFSNPGL--LGSRAEFRKNFEN-----PILRGRDADATD 530
Cdd:NF041062  292 LLSATPVLGNEETFLALLHLLDPDLypLDDLEAFRERLEEreelgRLVLGLDPDNPN 348
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 328-460 2.17e-03

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: 39.31  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321275  328 AYGCIMADEMGLGKTLqcIALMWTLLRQGPQGKRLidkCIIVCPSSLVNNWANELIKWLGPNtlTPLAVdgkkssMGGGN 407
Cdd:cd00046   1 GENVLITAPTGSGKTL--AALLAALLLLLKKGKKV---LVLVPTKALALQTAERLRELFGPG--IRVAV------LVGGS 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6321275  408 TTVSQAIHAWAQAqgrnivkPVLIISYETLRRNV---DQLKNCNVGLMLADEGHRL 460
Cdd:cd00046  68 SAEEREKNKLGDA-------DIIIATPDMLLNLLlreDRLFLKDLKLIIVDEAHAL 116
 
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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