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Conserved domains on  [gi|392902167|ref|NP_001255914|]
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DNA repair and recombination protein RAD54-like [Caenorhabditis elegans]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
93-548 8.25e-113

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 356.07  E-value: 8.25e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFdRLRRGSGKngggggAILADDMGLGKSLQTMAAtWALLKgsktAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:COG0553  242 LRPYQLEGAAWLL-FLRRLGLG------GLLADDMGLGKTIQALAL-LLELK----ERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRF-----PAVIALTANDITTYQstiklmpYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLL 247
Cdd:COG0553  310 AKFAPGLRVlvldgTRERAKGANPFEDAD-------LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 248 SLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM--------CSDRPEQLNELIDECMLRRTAADVdLKHL 319
Cdd:COG0553  383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgDEEALERLRRLLRPFLLRRTKEDV-LKDL 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 320 PEKHEYILFCAASPIQKHVHSEICDYM------------TGDALSLIFFARQLANHPKLLLDNLREKTEkskahkhspll 387
Cdd:COG0553  462 PEKTEETLYVELTPEQRALYEAVLEYLrrelegaegirrRGLILAALTRLRQICSHPALLLEEGAELSG----------- 530
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 388 lafdgahmprggvkESGKLTALVDMIKCFRLLQECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFN 467
Cdd:COG0553  531 --------------RSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 468 DHRDPsNIFLLSTKAGGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTG 547
Cdd:COG0553  597 EGPEA-PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675

                 .
gi 392902167 548 L 548
Cdd:COG0553  676 L 676
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
93-548 8.25e-113

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 356.07  E-value: 8.25e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFdRLRRGSGKngggggAILADDMGLGKSLQTMAAtWALLKgsktAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:COG0553  242 LRPYQLEGAAWLL-FLRRLGLG------GLLADDMGLGKTIQALAL-LLELK----ERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRF-----PAVIALTANDITTYQstiklmpYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLL 247
Cdd:COG0553  310 AKFAPGLRVlvldgTRERAKGANPFEDAD-------LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 248 SLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM--------CSDRPEQLNELIDECMLRRTAADVdLKHL 319
Cdd:COG0553  383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgDEEALERLRRLLRPFLLRRTKEDV-LKDL 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 320 PEKHEYILFCAASPIQKHVHSEICDYM------------TGDALSLIFFARQLANHPKLLLDNLREKTEkskahkhspll 387
Cdd:COG0553  462 PEKTEETLYVELTPEQRALYEAVLEYLrrelegaegirrRGLILAALTRLRQICSHPALLLEEGAELSG----------- 530
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 388 lafdgahmprggvkESGKLTALVDMIKCFRLLQECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFN 467
Cdd:COG0553  531 --------------RSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 468 DHRDPsNIFLLSTKAGGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTG 547
Cdd:COG0553  597 EGPEA-PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675

                 .
gi 392902167 548 L 548
Cdd:COG0553  676 L 676
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
93-309 4.98e-98

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: 302.28  E-value: 4.98e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGKNGGGggAILADDMGLGKSLQTMAATWALLKGSKTAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGGGG--AILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRfPAVIALTANDITTYQ-----STIKLMPYLVISYDLAQRHVEKL-KIIRFDVMVCDEGHKLKNLDGKLRKTL 246
Cdd:cd18004   79 DKWLGLRR-IKVVTADGNAKDVKAsldffSSASTYPVLIISYETLRRHAEKLsKKISIDLLICDEGHRLKNSESKTTKAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 247 LSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCS--------------------DRPEQLNELIDECM 306
Cdd:cd18004  158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepilrsrdpdaseedkelgaERSQELSELTSRFI 237

                 ...
gi 392902167 307 LRR 309
Cdd:cd18004  238 LRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
96-367 1.64e-58

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: 199.83  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   96 HQKSGIQFIFDRLRrgsgknGGGGGAILADDMGLGKSLQTMAATWALLKGSKtaqQLANSCLIIVPSSLVNNWKAEFDKW 175
Cdd:pfam00176   1 YQIEGVNWMLSLEN------NLGRGGILADEMGLGKTLQTISLLLYLKHVDK---NWGGPTLIVVPLSLLHNWMNEFERW 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  176 WRLMRFPAVIALTANDITTYQSTIKLMPY----LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI 251
Cdd:pfam00176  72 VSPPALRVVVLHGNKRPQERWKNDPNFLAdfdvVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  252 PRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRK---------MCSDRPEQLNELIDECMLRRTAADVDlKHLPEK 322
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNwfdrpiergGGKKGVSRLHKLLKPFLLRRTKKDVE-KSLPPK 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392902167  323 HEYILFCAASPIQKHVH--------------SEICDYMTGDALSLIFFARQLANHPKLL 367
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqtfllkkdlnaiktGEGGREIKASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
122-548 4.08e-58

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 213.12  E-value: 4.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  122 ILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRfpAVIALTANDITTYQSTIKL 201
Cdd:PLN03142  192 ILADEMGLGKTLQTIS----LLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLR--AVKFHGNPEERAHQREELL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  202 MP----YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVR 277
Cdd:PLN03142  266 VAgkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  278 PSVFGSIVEFRKMCS-----DRPE---QLNELIDECMLRRTAADVDlKHLPEKHEYILFCAASPIQKHVHSEICDY---- 345
Cdd:PLN03142  346 PEIFSSAETFDEWFQisgenDQQEvvqQLHKVLRPFLLRRLKSDVE-KGLPPKKETILKVGMSQMQKQYYKALLQKdldv 424
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  346 --MTGDALSLIFFARQL---ANHPKLLldnlrektekSKAHKHSPLllaFDGAHMprggVKESGKLTALVDMIKCFRLLQ 420
Cdd:PLN03142  425 vnAGGERKRLLNIAMQLrkcCNHPYLF----------QGAEPGPPY---TTGEHL----VENSGKMVLLDKLLPKLKERD 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  421 ECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRDPSNIFLLSTKAGGVGLNLIGASRLVLFDS 500
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 392902167  501 DWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTGL 548
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
DEXDc smart00487
DEAD-like helicases superfamily;
93-279 3.64e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.17  E-value: 3.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167    93 LRPHQKSGIQFIFDRLRRgsgkngggggAILADDMGLGKSLQTMAATWALLKGSKTAQqlansCLIIVP-SSLVNNWKAE 171
Cdd:smart00487   9 LRPYQKEAIEALLSGLRD----------VILAAPTGSGKTLAALLPALEALKRGKGGR-----VLVLVPtRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   172 FDKWWRLMRFPAVIALTANDITTYQSTIKLMPY--LVISYDLAQRHVEK--LKIIRFDVMVCDEGHKLKNLD--GKLRKT 245
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTdiLVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGfgDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 392902167   246 LLSLE-IPRRLILTGTP---MQNDFEEFYSLLDFVRPS 279
Cdd:smart00487 154 LKLLPkNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
93-548 8.25e-113

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 356.07  E-value: 8.25e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFdRLRRGSGKngggggAILADDMGLGKSLQTMAAtWALLKgsktAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:COG0553  242 LRPYQLEGAAWLL-FLRRLGLG------GLLADDMGLGKTIQALAL-LLELK----ERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRF-----PAVIALTANDITTYQstiklmpYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLL 247
Cdd:COG0553  310 AKFAPGLRVlvldgTRERAKGANPFEDAD-------LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 248 SLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM--------CSDRPEQLNELIDECMLRRTAADVdLKHL 319
Cdd:COG0553  383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgDEEALERLRRLLRPFLLRRTKEDV-LKDL 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 320 PEKHEYILFCAASPIQKHVHSEICDYM------------TGDALSLIFFARQLANHPKLLLDNLREKTEkskahkhspll 387
Cdd:COG0553  462 PEKTEETLYVELTPEQRALYEAVLEYLrrelegaegirrRGLILAALTRLRQICSHPALLLEEGAELSG----------- 530
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 388 lafdgahmprggvkESGKLTALVDMIKCFRLLQECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFN 467
Cdd:COG0553  531 --------------RSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 468 DHRDPsNIFLLSTKAGGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTG 547
Cdd:COG0553  597 EGPEA-PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675

                 .
gi 392902167 548 L 548
Cdd:COG0553  676 L 676
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
93-309 4.98e-98

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: 302.28  E-value: 4.98e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGKNGGGggAILADDMGLGKSLQTMAATWALLKGSKTAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGGGG--AILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRfPAVIALTANDITTYQ-----STIKLMPYLVISYDLAQRHVEKL-KIIRFDVMVCDEGHKLKNLDGKLRKTL 246
Cdd:cd18004   79 DKWLGLRR-IKVVTADGNAKDVKAsldffSSASTYPVLIISYETLRRHAEKLsKKISIDLLICDEGHRLKNSESKTTKAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 247 LSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCS--------------------DRPEQLNELIDECM 306
Cdd:cd18004  158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepilrsrdpdaseedkelgaERSQELSELTSRFI 237

                 ...
gi 392902167 307 LRR 309
Cdd:cd18004  238 LRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
96-367 1.64e-58

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: 199.83  E-value: 1.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   96 HQKSGIQFIFDRLRrgsgknGGGGGAILADDMGLGKSLQTMAATWALLKGSKtaqQLANSCLIIVPSSLVNNWKAEFDKW 175
Cdd:pfam00176   1 YQIEGVNWMLSLEN------NLGRGGILADEMGLGKTLQTISLLLYLKHVDK---NWGGPTLIVVPLSLLHNWMNEFERW 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  176 WRLMRFPAVIALTANDITTYQSTIKLMPY----LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI 251
Cdd:pfam00176  72 VSPPALRVVVLHGNKRPQERWKNDPNFLAdfdvVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  252 PRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRK---------MCSDRPEQLNELIDECMLRRTAADVDlKHLPEK 322
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNwfdrpiergGGKKGVSRLHKLLKPFLLRRTKKDVE-KSLPPK 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392902167  323 HEYILFCAASPIQKHVH--------------SEICDYMTGDALSLIFFARQLANHPKLL 367
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqtfllkkdlnaiktGEGGREIKASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
122-548 4.08e-58

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 213.12  E-value: 4.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  122 ILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRfpAVIALTANDITTYQSTIKL 201
Cdd:PLN03142  192 ILADEMGLGKTLQTIS----LLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLR--AVKFHGNPEERAHQREELL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  202 MP----YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVR 277
Cdd:PLN03142  266 VAgkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  278 PSVFGSIVEFRKMCS-----DRPE---QLNELIDECMLRRTAADVDlKHLPEKHEYILFCAASPIQKHVHSEICDY---- 345
Cdd:PLN03142  346 PEIFSSAETFDEWFQisgenDQQEvvqQLHKVLRPFLLRRLKSDVE-KGLPPKKETILKVGMSQMQKQYYKALLQKdldv 424
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  346 --MTGDALSLIFFARQL---ANHPKLLldnlrektekSKAHKHSPLllaFDGAHMprggVKESGKLTALVDMIKCFRLLQ 420
Cdd:PLN03142  425 vnAGGERKRLLNIAMQLrkcCNHPYLF----------QGAEPGPPY---TTGEHL----VENSGKMVLLDKLLPKLKERD 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  421 ECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRDPSNIFLLSTKAGGVGLNLIGASRLVLFDS 500
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 392902167  501 DWNPANDQQAMARIWRDGQVRPCHIYRLITTGTIEEKMLQRQIKKTGL 548
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
93-281 1.01e-53

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: 182.77  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGkngggggAILADDMGLGKSLQTMAATWALLKGSKTAqqlaNSCLIIVPSSLVNNWKAEF 172
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPG-------GILADEMGLGKTLQAIAFLAYLLKEGKER----GPVLVVCPLSVLENWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRfpaVIALTANDITTYQSTIKLMPY----LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLS 248
Cdd:cd17919   70 EKWTPDLR---VVVYHGSQRERAQIRAKEKLDkfdvVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKA 146
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392902167 249 LEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVF 281
Cdd:cd17919  147 LRAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
403-529 1.70e-52

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: 177.67  E-value: 1.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 403 SGKLTALVDMIKCFRLLQECTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRDPsNIFLLSTKA 482
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 392902167 483 GGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQVRPCHIYRLI 529
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
93-290 6.24e-48

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: 169.26  E-value: 6.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLrrGSGKNGGGGGAILADDMGLGKSLQTMAATWALLK-GSKTAQQLANSCLIIVPSSLVNNWKAE 171
Cdd:cd18066    1 LRPHQREGIEFLYECV--MGMRVNERFGAILADEMGLGKTLQCISLIWTLLRqGPYGGKPVIKRALIVTPGSLVKNWKKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 172 FDKWWRLMRFPAVIALTANDITTYQSTIkLMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI 251
Cdd:cd18066   79 FQKWLGSERIKVFTVDQDHKVEEFIASP-LYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392902167 252 PRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM 290
Cdd:cd18066  158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKV 196
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
93-309 1.15e-46

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: 165.72  E-value: 1.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFD----RLRRGSGKngggggAILADDMGLGKSLQTMAATWALLKGSKTAQQLANSCLIIVPSSLVNNW 168
Cdd:cd18067    1 LRPHQREGVKFLYRcvtgRRIRGSHG------CIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 169 KAEFDKWWRlmrfPAVIALTANDITTYQSTIKLM------------PYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLK 236
Cdd:cd18067   75 ANELGKWLG----GRLQPLAIDGGSKKEIDRKLVqwasqqgrrvstPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 237 NLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMC--------------SDRP---EQLN 299
Cdd:cd18067  151 NSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadaseKERQlgeEKLQ 230
                        250
                 ....*....|...
gi 392902167 300 ELI---DECMLRR 309
Cdd:cd18067  231 ELIsivNRCIIRR 243
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
93-290 4.84e-44

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: 158.61  E-value: 4.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGKNGGGGGAILADDMGLGKSLQTMAATWALLKGSKTaqqlANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18007    1 LKPHQVEGVRFLWSNLVGTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPR----RSRPLVLCPASTLYNWEDEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRFPAVIALTANDITTYQSTIKLMP-------YLVISYD----LAQRH----VEKLKIIRF------DVMVCDE 231
Cdd:cd18007   77 KKWLPPDLRPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYElfrnLASNAttdpRLKQEFIAAlldpgpDLLVLDE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392902167 232 GHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM 290
Cdd:cd18007  157 GHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKK 215
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
93-310 1.81e-38

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: 141.93  E-value: 1.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIfDRLRRGSGKngggggAILADDMGLGKSLQTMAatwaLLKGSKTaQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18012    5 LRPYQKEGFNWL-SFLRHYGLG------GILADDMGLGKTLQTLA----LLLSRKE-EGRKGPSLVVAPTSLIYNWEEEA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKW---WRLM-------RFPAVIALTANDIttyqstiklmpyLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKL 242
Cdd:cd18012   73 AKFapeLKVLvihgtkrKREKLRALEDYDL------------VITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKT 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392902167 243 RKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKM---------CSDRPEQLNELIDECMLRRT 310
Cdd:cd18012  141 AKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRfakpiekdgDEEALEELKKLISPFILRRL 217
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
93-293 8.27e-37

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: 138.28  E-value: 8.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLrrgsgknGGGGGAILADDMGLGKSLQTMAATWALLKGSKTAQQLANS----------------C 156
Cdd:cd18005    1 LRDYQREGVEFMYDLY-------KNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNrprfkkkppassakkpV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 157 LIIVPSSLVNNWKAEFDKWwrlMRFPAVIALTANDITTYQSTIKLMPY--LVISYDLAQRHVEKLKIIRFDVMVCDEGHK 234
Cdd:cd18005   74 LIVAPLSVLYNWKDELDTW---GHFEVGVYHGSRKDDELEGRLKAGRLevVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392902167 235 LKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSD 293
Cdd:cd18005  151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSE 209
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
93-309 2.24e-32

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: 125.18  E-value: 2.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQF---IFDRLRrgsgknggggGAILADDMGLGKSLQTMAATWALLKGSktaqqLANSCLIIVPSSLVNNWK 169
Cdd:cd18001    1 LYPHQREGVAWlwsLHDGGK----------GGILADDMGLGKTVQICAFLSGMFDSG-----LIKSVLVVMPTSLIPHWV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 170 AEFDKWWRLMRF-----PAVIALTAND----------ITTYQSTIKLMPYLviSYDLAQRHVeklkiirFDVMVCDEGHK 234
Cdd:cd18001   66 KEFAKWTPGLRVkvfhgTSKKERERNLeriqrgggvlLTTYGMVLSNTEQL--SADDHDEFK-------WDYVILDEGHK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 235 LKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRP-SVFGSIVEF--------------------RKMCSD 293
Cdd:cd18001  137 IKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFkmefenpitrgrdkdatqgeKALGSE 216
                        250
                 ....*....|....*.
gi 392902167 294 RPEQLNELIDECMLRR 309
Cdd:cd18001  217 VAENLRQIIKPYFLRR 232
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
122-309 1.01e-31

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: 123.13  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRL-------------------MRFP 182
Cdd:cd17995   23 ILADEMGLGKTIQSIA----FLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMnvvvyhgsgesrqiiqqyeMYFK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 183 AVIALTANDIttYQSTIklmpyLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPM 262
Cdd:cd17995   99 DAQGRKKKGV--YKFDV-----LITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392902167 263 QNDFEEFYSLLDFVRPSVFGSIVEF-RKMCS----DRPEQLNELIDECMLRR 309
Cdd:cd17995  172 QNNTEELWSLLNFLEPEKFPSSEEFlEEFGDlktaEQVEKLQALLKPYMLRR 223
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
93-309 5.49e-31

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: 120.77  E-value: 5.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRgsgkngggggAILADDMGLGKSLQTMAatwallkgskTAQQLANSC--LIIVPSSLVNNWKA 170
Cdd:cd18010    1 LLPFQREGVCFALRRGGR----------VLIADEMGLGKTVQAIA----------IAAYYREEWplLIVCPSSLRLTWAD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 171 EFDKWWRLMRFPAVIALTANDITTYQSTIKLmpyLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSL- 249
Cdd:cd18010   61 EIERWLPSLPPDDIQVIVKSKDGLRDGDAKV---VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLl 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392902167 250 -EIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSDRP---------------EQLNELIDECMLRR 309
Cdd:cd18010  138 kRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKqggfgwdysgssnleELHLLLLATIMIRR 213
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
93-288 1.14e-30

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: 120.76  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFD----RLRRGSGKNGGGggAILADDMGLGKSLQTMAATWALLKGSKTAQqlANSCLIIVPSSLVNNW 168
Cdd:cd18068    1 LKPHQVDGVQFMWDccceSLKKTKKSPGSG--CILAHCMGLGKTLQVVTFLHTVLLCEKLEN--FSRVLVVCPLNTVLNW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 169 KAEFDKWWRLMRFPAVIALtaNDITTYQS----TIKLMPY------LVISYDL--------AQRHVEKLKIIRF------ 224
Cdd:cd18068   77 LNEFEKWQEGLKDEEKIEV--NELATYKRpqerSYKLQRWqeeggvMIIGYDMyrilaqerNVKSREKLKEIFNkalvdp 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392902167 225 --DVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFR 288
Cdd:cd18068  155 gpDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFR 220
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
122-287 1.64e-30

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: 120.17  E-value: 1.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWwrlmrFPAVIAL----TANDITTYQS 197
Cdd:cd17996   26 ILADEMGLGKTIQTISLITYLME----KKKNNGPYLVIVPLSTLSNWVSEFEKW-----APSVSKIvykgTPDVRKKLQS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 198 TIKLMPY--LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI-PRRLILTGTPMQNDFEEFYSLLD 274
Cdd:cd17996   97 QIRAGKFnvLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHaRYRLLLTGTPLQNNLPELWALLN 176
                        170
                 ....*....|...
gi 392902167 275 FVRPSVFGSIVEF 287
Cdd:cd17996  177 FLLPKIFKSCKTF 189
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
122-304 2.38e-30

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: 119.80  E-value: 2.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAaTWALLKGSKTAQQLanscLIIVPSSLVNNWKAEFDKWwrlmrFPAVIAL----TAND------ 191
Cdd:cd18009   26 ILADEMGLGKTIQTIA-LLAHLRERGVWGPF----LVIAPLSTLPNWVNEFARF-----TPSVPVLlyhgTKEErerlrk 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 192 -ITTYQSTIKLMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFY 270
Cdd:cd18009   96 kIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELW 175
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392902167 271 SLLDFVRPSVFGSIVEFRKM-----CSDRPEQLNELIDE 304
Cdd:cd18009  176 SLLNFLLPDVFDDLSSFESWfdfssLSDNAADISNLSEE 214
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
93-316 7.53e-30

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: 117.99  E-value: 7.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGKNGGGGG--AILADDMGLGKSLQTMAATWALLKGSKtaqqlANSCLIIVPSSLVNNWKA 170
Cdd:cd18069    1 LKPHQIGGIRFLYDNIIESLERYKGSSGfgCILAHSMGLGKTLQVISFLDVLLRHTG-----AKTVLAIVPVNTLQNWLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 171 EFDKWW-RLMRFPAV------IALTANDITTYQSTIKLMP-------YLVISYDLAQRHVEKlkiirfDVMVCDEGHKLK 236
Cdd:cd18069   76 EFNKWLpPPEALPNVrprpfkVFILNDEHKTTAARAKVIEdwvkdggVLLMGYEMFRLRPGP------DVVICDEGHRIK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 237 NLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMcSDRPEQLNELIDEcmlrrTAADVDL 316
Cdd:cd18069  150 NCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNM-FERPILNGQCVDS-----TPQDVKL 223
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
93-288 8.41e-30

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: 117.84  E-value: 8.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIfDRLRRGSGKngggggAILADDMGLGKSLQTMAATWALLKGSKTAQQLANSC-LIIVPSSLVNNWKAE 171
Cdd:cd17999    1 LRPYQQEGINWL-AFLNKYNLH------GILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPsLVVCPPTLVGHWVAE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 172 FDKwwrlmRFP-AVIALTANDiTTYQSTIKLMPY------LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRK 244
Cdd:cd17999   74 IKK-----YFPnAFLKPLAYV-GPPQERRRLREQgekhnvIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSK 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392902167 245 TLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFR 288
Cdd:cd17999  148 AVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQ 191
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
122-310 1.03e-29

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: 117.42  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTANDITTYQSTIKL 201
Cdd:cd17997   26 ILADEMGLGKTLQTIS----LLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLIGDKEERADIIRDVLLP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 202 MPYLVI--SYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPS 279
Cdd:cd17997  102 GKFDVCitSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPD 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392902167 280 VFGSIVEF-----RKMCSD----RPEQLNELIDECMLRRT 310
Cdd:cd17997  182 VFTSSEDFdewfnVNNCDDdnqeVVQRLHKVLRPFLLRRI 221
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
93-278 2.71e-29

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: 115.11  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGkngggggAILADDMGLGKSLQTmAATWALLKGSKtaqQLANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVG-------GILGDEMGLGKTIQI-IAFLAALHHSK---LGLGPSLIVCPATVLKQWVKEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWWRLMRfpaVIALTANDITTYQSTIKLMPY---------------LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKN 237
Cdd:cd18000   70 HRWWPPFR---VVVLHSSGSGTGSEEKLGSIErksqlirkvvgdggiLITTYEGFRKHKDLLLNHNWQYVILDEGHKIRN 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392902167 238 LDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRP 278
Cdd:cd18000  147 PDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
93-293 3.01e-28

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: 113.22  E-value: 3.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGkngggggAILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEF 172
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLN-------GILADEMGLGKTIQTIA----LLAHLACEKGNWGPHLIVVPTSVMLNWEMEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 DKWwrlmrFPAVIALT---------------AND------ITTYQSTIKlmpylvisydlaQRHVEKLKiiRFDVMVCDE 231
Cdd:cd18003   70 KRW-----CPGFKILTyygsakerklkrqgwMKPnsfhvcITSYQLVVQ------------DHQVFKRK--KWKYLILDE 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392902167 232 GHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSD 293
Cdd:cd18003  131 AHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSN 192
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
122-309 3.70e-28

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: 112.83  E-value: 3.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTA--NDITTY---Q 196
Cdd:cd17993   24 ILADEMGLGKTVQTISFLSYLFH----SQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIVYLGDIKsrDTIREYefyF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 197 STIKLMPY--LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLD 274
Cdd:cd17993  100 SQTKKLKFnvLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLH 179
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392902167 275 FVRPSVFGSIVEFRKMCSDRPE----QLNELIDECMLRR 309
Cdd:cd17993  180 FLMPGKFDIWEEFEEEHDEEQEkgiaDLHKELEPFILRR 218
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
93-309 9.69e-28

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: 112.38  E-value: 9.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRlrrgsgknggggGAILADDMGLGKSLQT---MAAT--------WALLKGSKTAQQLANSC--LII 159
Cdd:cd18008    1 LLPYQKQGLAWMLPR------------GGILADEMGLGKTIQAlalILATrpqdpkipEELEENSSDPKKLYLSKttLIV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 160 VPSSLVNNWKAEFDKWWRLMRFPAVIALTANDITtyqSTIKLMPYLVI--SY----------------DLAQRHVEKLKI 221
Cdd:cd18008   69 VPLSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIK---SIEELSDYDIVitTYgtlasefpknkkgggrDSKEKEASPLHR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 222 IRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSDRP------ 295
Cdd:cd18008  146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFskndrk 225
                        250
                 ....*....|....*.
gi 392902167 296 --EQLNELIDECMLRR 309
Cdd:cd18008  226 alERLQALLKPILLRR 241
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
93-309 1.08e-27

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: 111.38  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLrrgsgknGGGGGAILADDMGLGKSLQTMAATWaLLKGSktaQQLANSCLIIVPSSLVNNWKAEf 172
Cdd:cd18006    1 LRPYQLEGVNWLLQCR-------AEQHGCILGDEMGLGKTCQTISLLW-YLAGR---LKLLGPFLVLCPLSVLDNWKEE- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 173 dkwwrLMRF-PAVIALT-ANDI---TTYQSTIKLMP---YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRK 244
Cdd:cd18006   69 -----LNRFaPDLSVITyMGDKekrLDLQQDIKSTNrfhVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHK 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392902167 245 TLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFG-----SIVEFRKMCSDRPEQLNEL---IDECMLRR 309
Cdd:cd18006  144 TLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdkldDFIKAYSETDDESETVEELhllLQPFLLRR 216
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
121-281 5.05e-27

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: 108.63  E-value: 5.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAATWALLKGSKTAQQLansclIIVPSSLVNNWKAEFDKWW---------------RLMRFPAVI 185
Cdd:cd17998   22 GILADEMGLGKTIQVIAFLAYLKEIGIPGPHL-----VVVPSSTLDNWLREFKRWCpslkvepyygsqeerKHLRYDILK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 186 ALTANDI--TTYQstiklmpyLVISYDLAQRHvekLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQ 263
Cdd:cd17998   97 GLEDFDVivTTYN--------LATSNPDDRSF---FKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQ 165
                        170
                 ....*....|....*...
gi 392902167 264 NDFEEFYSLLDFVRPSVF 281
Cdd:cd17998  166 NNLLELMSLLNFIMPKPF 183
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
93-309 1.20e-25

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: 105.06  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRrgsgkngggGGAILADDMGLGKSLQtMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAE- 171
Cdd:cd18011    1 PLPHQIDAVLRALRKPP---------VRLLLADEVGLGKTIE-AGLIIKELL----LRGDAKRVLILCPASLVEQWQDEl 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 172 FDKWWRlmRFPAVIALTANDITTYQSTIKLMPYLVI-SYDLAQRHVE---KLKIIRFDVMVCDEGHKLKNLDGKLRKTLL 247
Cdd:cd18011   67 QDKFGL--PFLILDRETAAQLRRLIGNPFEEFPIVIvSLDLLKRSEErrgLLLSEEWDLVVVDEAHKLRNSGGGKETKRY 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392902167 248 SL--EI----PRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSDRPEQLNElidecMLRR 309
Cdd:cd18011  145 KLgrLLakraRHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRLDGLREVLAKV-----LLRR 207
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
122-309 3.70e-25

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: 104.70  E-value: 3.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIA--LTANDITTYQ--- 196
Cdd:cd18054   43 ILADEMGLGKTIQTISFLSYLFH----QHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVVYIGdlMSRNTIREYEwih 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 197 STIKLMPY--LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLD 274
Cdd:cd18054  119 SQTKRLKFnaLITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLH 198
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392902167 275 FVRPSVFGSIVEFR----KMCSDRPEQLNELIDECMLRR 309
Cdd:cd18054  199 FIMPEKFEFWEDFEedhgKGRENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
121-322 3.79e-25

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: 104.75  E-value: 3.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTANDITTYQSTik 200
Cdd:cd18064   37 GILADEMGLGKTLQTIS----LLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDV-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 201 LMP----YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFV 276
Cdd:cd18064  111 LLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFL 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392902167 277 RPSVFGSIVEF------RKMCSDRP--EQLNELIDECMLRRTAADVDlKHLPEK 322
Cdd:cd18064  191 LPDVFNSAEDFdswfdtNNCLGDQKlvERLHMVLRPFLLRRIKADVE-KSLPPK 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
121-289 4.00e-25

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: 105.14  E-value: 4.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWwrlmrFPAVIALTANDITTYQSTik 200
Cdd:cd18063   45 GILADEMGLGKTIQTIALITYLME----HKRLNGPYLIIVPLSTLSNWTYEFDKW-----APSVVKISYKGTPAMRRS-- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 201 LMP--------YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI-PRRLILTGTPMQNDFEEFYS 271
Cdd:cd18063  114 LVPqlrsgkfnVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRILLTGTPLQNKLPELWA 193
                        170
                 ....*....|....*...
gi 392902167 272 LLDFVRPSVFGSIVEFRK 289
Cdd:cd18063  194 LLNFLLPTIFKSCSTFEQ 211
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
93-309 1.78e-24

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: 102.44  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFI-FDRLRRGSgkngggggAILADDMGLGKSLQTMAATWALLKGSktaqqLANSCLIIVPSSLVNNWKAE 171
Cdd:cd18060    1 LREYQLEGVNWLlFNWYNRQN--------CILADEMGLGKTIQSIAFLQEVYNVG-----IHGPFLVIAPLSTITNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 172 FDKWWRLMRFPAVIALTAND-ITTYQSTIK-----LMP------YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLD 239
Cdd:cd18060   68 FNTWTEMNTIVYHGSLASRQmIQQYEMYCKdsrgrLIPgaykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRN 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392902167 240 GKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSD-----RPEQLNELIDECMLRR 309
Cdd:cd18060  148 CKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDlkteeQVQKLQAILKPMMLRR 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
121-309 1.87e-24

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: 101.36  E-value: 1.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAATWALLKGSKTAQQLanscLIIVPSSLVNNWKAEFDKWwrlmrfpavialtAND---ITTYQS 197
Cdd:cd17994   22 TILADEMGLGKTIQTIVFLYSLYKEGHSKGPF----LVSAPLSTIINWEREFEMW-------------APDfyvVTYVGD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 198 TIKLMPYLVISYDLAQrhvekLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVR 277
Cdd:cd17994   85 HVLLTSYELISIDQAI-----LGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLT 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 392902167 278 PSVFGSIVEFRKMCSD--RPEQ---LNELIDECMLRR 309
Cdd:cd17994  160 PERFNNLQGFLEEFADisKEDQikkLHDLLGPHMLRR 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
121-289 5.27e-24

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: 101.66  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWwrlmrFPAVIALT------ANDITT 194
Cdd:cd18062   45 GILADEMGLGKTIQTIALITYLME----HKRINGPFLIIVPLSTLSNWVYEFDKW-----APSVVKVSykgspaARRAFV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 195 YQSTIKLMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEI-PRRLILTGTPMQNDFEEFYSLL 273
Cdd:cd18062  116 PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRLLLTGTPLQNKLPELWALL 195
                        170
                 ....*....|....*.
gi 392902167 274 DFVRPSVFGSIVEFRK 289
Cdd:cd18062  196 NFLLPTIFKSCSTFEQ 211
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
404-518 4.08e-23

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: 94.58  E-value: 4.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  404 GKLTALVDMIKCFRllQECTVIVSNYIETLDmIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFndhRDPSNIFLLSTKAG 483
Cdd:pfam00271   1 EKLEALLELLKKER--GGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDF---RKGKIDVLVATDVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 392902167  484 GVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDG 518
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
122-309 2.20e-22

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: 96.42  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWwrlmrFPAVIAL----TANDITTYQS 197
Cdd:cd18002   23 ILADEMGLGKTVQSIA----VLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRF-----VPQFKVLpywgNPKDRKVLRK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 198 TI--KLMPY-------LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEE 268
Cdd:cd18002   94 FWdrKNLYTrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAE 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392902167 269 FYSLLDFVRPSVFGSIVEFRKMCSDRPE---QLNELIDECMLRR 309
Cdd:cd18002  174 LWALLHFIMPTLFDSHDEFNEWFSKDIEshaENKTGLNEHQLKR 217
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
121-287 2.36e-22

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: 96.63  E-value: 2.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 121 AILADDMGLGKSLQTMAatwaLLKGSKTAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRfpAVIALTANDITTYQSTIK 200
Cdd:cd18065   37 GILADEMGLGKTLQTIA----LLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR--AVCLIGDKDARAAFIRDV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 201 LMP----YLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFV 276
Cdd:cd18065  111 MMPgewdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFL 190
                        170
                 ....*....|.
gi 392902167 277 RPSVFGSIVEF 287
Cdd:cd18065  191 LPDVFNSADDF 201
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
122-309 1.94e-21

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: 93.57  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWAL-LKGsktaqqLANSCLIIVPSSLVNNWKAEFDKWWRLmrfpAVIALTANDITTYQSTIK 200
Cdd:cd18058   23 ILADEMGLGKTIQSITFLSEIfLMG------IRGPFLIIAPLSTITNWEREFRTWTEM----NAIVYHGSQISRQMIQQY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 201 LMPY----------------LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQN 264
Cdd:cd18058   93 EMYYrdeqgnplsgifkfqvVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQN 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392902167 265 DFEEFYSLLDFVRPSVFGSIVEFRKMCSD-----RPEQLNELIDECMLRR 309
Cdd:cd18058  173 SVEELFSLLNFLEPSQFPSETTFLEEFGDlkteeQVKKLQSILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
122-309 2.86e-21

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: 93.15  E-value: 2.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKGSKTAQQLanscLIIVPSSLVNNWKAEFDKWwrLMRFPAVI---------ALTANDI 192
Cdd:cd18055   23 ILADEMGLGKTIQTIVFLYSLYKEGHTKGPF----LVSAPLSTIINWEREFQMW--APDFYVVTytgdkdsraIIRENEF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 193 TTYQSTIK--------------LMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILT 258
Cdd:cd18055   97 SFDDNAVKggkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLT 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392902167 259 GTPMQNDFEEFYSLLDFVRPSVF----GSIVEFRKMC-SDRPEQLNELIDECMLRR 309
Cdd:cd18055  177 GTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADISkEDQIKKLHDLLGPHMLRR 232
DEXDc smart00487
DEAD-like helicases superfamily;
93-279 3.64e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.17  E-value: 3.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167    93 LRPHQKSGIQFIFDRLRRgsgkngggggAILADDMGLGKSLQTMAATWALLKGSKTAQqlansCLIIVP-SSLVNNWKAE 171
Cdd:smart00487   9 LRPYQKEAIEALLSGLRD----------VILAAPTGSGKTLAALLPALEALKRGKGGR-----VLVLVPtRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   172 FDKWWRLMRFPAVIALTANDITTYQSTIKLMPY--LVISYDLAQRHVEK--LKIIRFDVMVCDEGHKLKNLD--GKLRKT 245
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTdiLVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGfgDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 392902167   246 LLSLE-IPRRLILTGTP---MQNDFEEFYSLLDFVRPS 279
Cdd:smart00487 154 LKLLPkNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
122-309 3.68e-20

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: 90.12  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKGSKTAqqlaNSCLIIVPSSLVNNWKAEFDKWW--------------RLMRFPAVIAL 187
Cdd:cd18057   23 ILADEMGLGKTVQTIVFLYSLYKEGHSK----GPYLVSAPLSTIINWEREFEMWApdfyvvtytgdkesRSVIRENEFSF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 188 TANDITTYQSTIKL-------MPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGT 260
Cdd:cd18057   99 EDNAIRSGKKVFRMkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGT 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392902167 261 PMQNDFEEFYSLLDFVRPSVF----GSIVEFRKMC-SDRPEQLNELIDECMLRR 309
Cdd:cd18057  179 PLQNNLEELFHLLNFLTPERFnnleGFLEEFADISkEDQIKKLHDLLGPHMLRR 232
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
122-309 4.14e-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: 90.22  E-value: 4.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATwallkgsktaqqLANSCLIIVPSSLVNNWKAEFDKWWR------LMRFPAVIALTANDITTY 195
Cdd:cd18071   52 ILADDMGLGKTLTTISLI------------LANFTLIVCPLSVLSNWETQFEEHVKpgqlkvYTYHGGERNRDPKLLSKY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 196 QstIKLMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDF 275
Cdd:cd18071  120 D--IVLTTYNTLASDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392902167 276 VR------PSVFGSIVEfRKMCSDRP---EQLNELIDECMLRR 309
Cdd:cd18071  198 LHlkpfsnPEYWRRLIQ-RPLTMGDPtglKRLQVLMKQITLRR 239
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
122-289 1.79e-19

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: 88.18  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKgsktAQQLANSCLIIVPSSLVNNWKAEFDKWWRLMRfpAVIAL----TANDITTYQ- 196
Cdd:cd18053   43 ILADEMGLGKTIQTISFLNYLFH----EHQLYGPFLLVVPLSTLTSWQREIQTWAPQMN--AVVYLgdinSRNMIRTHEw 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 197 ---STIKL-MPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSL 272
Cdd:cd18053  117 mhpQTKRLkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSL 196
                        170
                 ....*....|....*..
gi 392902167 273 LDFVRPSVFGSIVEFRK 289
Cdd:cd18053  197 LHFIMPEKFSSWEDFEE 213
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
122-309 6.10e-19

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: 86.66  E-value: 6.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKGSKTAQQLanscLIIVPSSLVNNWKAEFDKWWRLMRFPAVIA-------LTANDITT 194
Cdd:cd18056   23 ILADEMGLGKTVQTAVFLYSLYKEGHSKGPF----LVSAPLSTIINWEREFEMWAPDMYVVTYVGdkdsraiIRENEFSF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 195 YQSTIK--------------LMPYLVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGT 260
Cdd:cd18056   99 EDNAIRggkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGT 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392902167 261 PMQNDFEEFYSLLDFVRPSVF----GSIVEFRKMC-SDRPEQLNELIDECMLRR 309
Cdd:cd18056  179 PLQNNLEELFHLLNFLTPERFhnleGFLEEFADIAkEDQIKKLHDMLGPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
434-518 1.47e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 80.72  E-value: 1.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   434 DMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRdpsNIFLLSTKAGGVGLNLIGASRLVLFDSDWNPANDQQAMAR 513
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK---IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 392902167   514 IWRDG 518
Cdd:smart00490  78 AGRAG 82
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
122-309 2.26e-18

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: 84.70  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWAL-LKGsktaqqLANSCLIIVPSSLVNNWKAEFDKWWRLmrfpAVIALTANDITTYQSTIK 200
Cdd:cd18059   23 ILADEMGLGKTIQSITFLYEIyLKG------IHGPFLVIAPLSTIPNWEREFRTWTEL----NVVVYHGSQASRRTIQLY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 201 LMPY----------------LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQN 264
Cdd:cd18059   93 EMYFkdpqgrvikgsykfhaIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQN 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392902167 265 DFEEFYSLLDFVRPSVFGSIVEFRKMCSD-----RPEQLNELIDECMLRR 309
Cdd:cd18059  173 TVEELFSLLHFLEPSRFPSETTFMQEFGDlkteeQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
122-309 2.51e-16

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: 78.51  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 122 ILADDMGLGKSLQTMAATWALLKGSktaqqLANSCLIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTANDITTY------ 195
Cdd:cd18061   23 ILADEMGLGKTIQSITFLYEILLTG-----IRGPFLIIAPLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQyemyfr 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 196 --QSTIKLMPY----LVISYDLAQRHVEKLKIIRFDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEF 269
Cdd:cd18061   98 dsQGRIIRGAYrfqaIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEEL 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 392902167 270 YSLLDFVRPSVFGSIVEFRKMCSD-----RPEQLNELIDECMLRR 309
Cdd:cd18061  178 FSLLHFLEPLRFPSESTFMQEFGDlkteeQVQKLQAILKPMMLRR 222
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
93-309 5.41e-16

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: 77.91  E-value: 5.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRRGSGKngggggAILADDMGLGKSLQTMAATWALLKG----------------SKTAQQLANSC 156
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRG------GILADDMGLGKTLTMIALILAQKNTqnrkeeekekalteweSKKDSTLVPSA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 157 --LIIVPSSLVNNWKAEFDKWWRLMRFPAVIALTAN--DITTYQSTIKLmpyLVISYDLAQRHVEKLKI---------IR 223
Cdd:cd18072   75 gtLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNreRIGEVLRDYDI---VITTYSLVAKEIPTYKEesrssplfrIA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 224 FDVMVCDEGHKLKNLDGKLRKTLLSLEIPRRLILTGTPMQNDFEEFYSLLDFVRPSVFGSIVEFRKMCSDRP----EQLN 299
Cdd:cd18072  152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSrkggERLN 231
                        250
                 ....*....|
gi 392902167 300 ELIDECMLRR 309
Cdd:cd18072  232 ILTKSLLLRR 241
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
93-274 2.51e-11

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: 63.91  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRLRrgsgknggggGAILADdMGLGKSLQTMAATWALLKGSKTAQqlansCLIIVPSSLV-NNWKAE 171
Cdd:cd18013    1 PHPYQKVAINFIIEHPY----------CGLFLD-MGLGKTVTTLTALSDLQLDDFTRR-----VLVIAPLRVArSTWPDE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 172 FDKWWRLmrfpavialtanDITTYQSTI----KLMPYL-------VISYDLAQRHVEKLKI-IRFDVMVCDEGHKLKNLD 239
Cdd:cd18013   65 VEKWNHL------------RNLTVSVAVgterQRSKAAntpadlyVINRENLKWLVNKSGDpWPFDMVVIDELSSFKSPR 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392902167 240 GKLRKTLLSL--EIPRRLILTGTPMQNDFEEFYS---LLD 274
Cdd:cd18013  133 SKRFKALRKVrpVIKRLIGLTGTPSPNGLMDLWAqiaLLD 172
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
128-261 7.21e-09

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: 55.00  E-value: 7.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 128 GLGKSLQTMAATWALLKGSktaqqlansCLIIVPS-SLVNNWKAEFDKW---WRLMRFPAVIALTAND----ITTYQSTI 199
Cdd:cd17926   28 GSGKTLTALALIAYLKELR---------TLIVVPTdALLDQWKERFEDFlgdSSIGLIGGGKKKDFDDanvvVATYQSLS 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392902167 200 KLMpylvisydlaqrHVEKLKIIRFDVMVCDEGHklkNLDGK-LRKTLLSLEIPRRLILTGTP 261
Cdd:cd17926   99 NLA------------EEEKDLFDQFGLLIVDEAH---HLPAKtFSEILKELNAKYRLGLTATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
89-576 3.47e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.57  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  89 FARHLRPHQKSGIQFIFDRLRRgsgkngGGGGAILADDMGLGKSLqtMAATWA--LLKGSKTaqqlanscLIIVPS-SLV 165
Cdd:COG1061   77 TSFELRPYQQEALEALLAALER------GGGRGLVVAPTGTGKTV--LALALAaeLLRGKRV--------LVLVPRrELL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 166 NNWKAEFDKWWRLmrfpAVIALTANDITTyqstiklmPYLVISYDLAQRHVEKLKII-RFDVMVCDEGHKLknLDGKLRK 244
Cdd:COG1061  141 EQWAEELRRFLGD----PLAGGGKKDSDA--------PITVATYQSLARRAHLDELGdRFGLVIIDEAHHA--GAPSYRR 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 245 TLLSLEIPRRLILTGTP----MQNDFEEFYslldfvrpsvFGSIVEFRkmcsdrpeqLNELIDECMLRrtaadvdlkhlp 320
Cdd:COG1061  207 ILEAFPAAYRLGLTATPfrsdGREILLFLF----------DGIVYEYS---------LKEAIEDGYLA------------ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 321 eKHEYIlfcaasPIQKHVHSEICDYMTGDAlsliFFARQLANHPKLLLDNLREKTEKSKAHKHsplllafdgahmprggv 400
Cdd:COG1061  256 -PPEYY------GIRVDLTDERAEYDALSE----RLREALAADAERKDKILRELLREHPDDRK----------------- 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 401 kesgkltalvdmikcfrllqecTVIVSNYIETLDMIQQLCEYLNFKVLRLDGKTQVPDRQKLVRTFNDHRDPsniFLLST 480
Cdd:COG1061  308 ----------------------TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR---ILVTV 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 481 KAGGVGLNLIGASRLVLFDSDWNPANDQQAMARIWRDGQV-RPCHIYRLITTGT-IEEKMLQRQIKKTGLGCVIDAIEVG 558
Cdd:COG1061  363 DVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGkEDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEES 442
                        490
                 ....*....|....*...
gi 392902167 559 DTIATFTDEDLKDIFTFT 576
Cdd:COG1061  443 EELALLIAVKPALEVKGE 460
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
93-308 4.47e-05

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: 45.80  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  93 LRPHQKSGIQFIFDRlrrgsgknggggGAILADDMGLGKSLQTMA---ATWAlLKGSKTAQQL----------------- 152
Cdd:cd18070    1 LLPYQRRAVNWMLVP------------GGILADEMGLGKTVEVLAlilLHPR-PDNDLDAADDdsdemvccpdclvaetp 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 153 --ANSCLIIVPSSLVNNWKAEFDKWWRlmrfPAVIALTANDITTYQSTIKLMPYLVISYDLAqrhVEKLKIIRFDVMVCD 230
Cdd:cd18070   68 vsSKATLIVCPSAILAQWLDEINRHVP----SSLKVLTYQGVKKDGALASPAPEILAEYDIV---VTTYDVLRTELHYAE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 231 EGHKLKNLDGKLRKT-----LLSLE-------------------------IPR--RLILTGTPMQNDFEEFYSLLDFVRP 278
Cdd:cd18070  141 ANRSNRRRRRQKRYEappspLVLVEwwrvcldeaqmvesstskaaemarrLPRvnRWCVSGTPIQRGLDDLFGLLSFLGV 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 392902167 279 SVFGSIVEFRKM------CSDRPEQLNELIDECMLR 308
Cdd:cd18070  221 EPFCDSDWWARVlirpqgRNKAREPLAALLKELLWR 256
ResIII pfam04851
Type III restriction enzyme, res subunit;
93-261 7.99e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.73  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167   93 LRPHQKSGIqfifDRLRRGSGKNGGGGGAILAddMGLGKSLQTMAATWALLKgsktaQQLANSCLIIVPS-SLVNNWKAE 171
Cdd:pfam04851   4 LRPYQIEAI----ENLLESIKNGQKRGLIVMA--TGSGKTLTAAKLIARLFK-----KGPIKKVLFLVPRkDLLEQALEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167  172 FDKWwRLMRFPAVIALTANDITTYQSTIKLmpyLVISYDLAQRHV----EKLKIIRFDVMVCDEGHKLknLDGKLRKTLL 247
Cdd:pfam04851  73 FKKF-LPNYVEIGEIISGDKKDESVDDNKI---VVTTIQSLYKALelasLELLPDFFDVIIIDEAHRS--GASSYRNILE 146
                         170
                  ....*....|....
gi 392902167  248 SLEIPRRLILTGTP 261
Cdd:pfam04851 147 YFKPAFLLGLTATP 160
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
123-263 7.41e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 39.82  E-value: 7.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 123 LADDMGLGKslqTMAAtwallkGSKTAQQL----ANSCLIIVPSSLVNNWKAE-----------FDkwwrLMRFPAVIAL 187
Cdd:PRK04914 174 LADEVGLGK---TIEA------GMIIHQQLltgrAERVLILVPETLQHQWLVEmlrrfnlrfslFD----EERYAEAQHD 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392902167 188 TANDITTYQstiklmpyLVI-SYDLAQRH---VEKLKIIRFDVMVCDEGHKL------KNLDGKLRKTlLSLEIPRRLIL 257
Cdd:PRK04914 241 ADNPFETEQ--------LVIcSLDFLRRNkqrLEQALAAEWDLLVVDEAHHLvwseeaPSREYQVVEQ-LAEVIPGVLLL 311

                 ....*.
gi 392902167 258 TGTPMQ 263
Cdd:PRK04914 312 TATPEQ 317
 
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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