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Conserved domains on  [gi|1847896053|ref|XP_034685937|]
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ISWI chromatin-remodeling complex ATPase CHR11 isoform X3 [Vitis riparia]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11477522)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
23-1065 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1995.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   23 EEEQLNDQINDEEDEEELEAVTRTAISEDEDEEAAdggnspateddaAGDSSDGEEDEEDGNAVGGTEISKREKARLKEM 102
Cdd:PLN03142     1 EEEQVNTQANEEEDEEELEAVARSAGSDSDDDEVP------------AEDEDEDEEDDEEAESPAKAEISKREKARLKEL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  103 QKMKKQKIQEILDAQNAAIDADMNNRGKGRLKYLLQQTEIFAHFAKGDQSTSQKKTKGRGRHASKVTEEEEDEECLKEEE 182
Cdd:PLN03142    69 KKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  183 DGLSGTGNTRLVTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPK 262
Cdd:PLN03142   149 DGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  263 STLGNWMNEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENS 342
Cdd:PLN03142   229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  343 LLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKS 422
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  423 DVEKGLPPKKETILKVGMSQLQKQFYRALLQKDLEVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLIT 502
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  503 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 582
Cdd:PLN03142   469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  583 AGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 662
Cdd:PLN03142   549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  663 KTVNKDELLQMVRFGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDD--EKDEN 740
Cdd:PLN03142   629 KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDedDKDEN 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  741 KFDFKKIVSENWIEPPKRERKRNYSESEYFKQTMRQGAPAKQREPRIPRMPQLHDFQFFNTQRLNELYEKEVRYLMQTHQ 820
Cdd:PLN03142   709 KLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQ 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  821 KNQLKDSIDVDEPEDLGDPLTAEEQEEKERLLEEGFSSWSRRDFNTFIRACEKYGRNDVKSIASEMEGKTEEEVERYAKA 900
Cdd:PLN03142   789 KGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKV 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  901 FKERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGN 980
Cdd:PLN03142   869 FWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGN 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  981 WDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLVERENQEFDERERQARKEKKLAKNMTPSKRAMARQATESPTS 1060
Cdd:PLN03142   949 WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSS 1028

                   ....*
gi 1847896053 1061 VKKRK 1065
Cdd:PLN03142  1029 LKKRK 1033
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
23-1065 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1995.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   23 EEEQLNDQINDEEDEEELEAVTRTAISEDEDEEAAdggnspateddaAGDSSDGEEDEEDGNAVGGTEISKREKARLKEM 102
Cdd:PLN03142     1 EEEQVNTQANEEEDEEELEAVARSAGSDSDDDEVP------------AEDEDEDEEDDEEAESPAKAEISKREKARLKEL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  103 QKMKKQKIQEILDAQNAAIDADMNNRGKGRLKYLLQQTEIFAHFAKGDQSTSQKKTKGRGRHASKVTEEEEDEECLKEEE 182
Cdd:PLN03142    69 KKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  183 DGLSGTGNTRLVTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPK 262
Cdd:PLN03142   149 DGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  263 STLGNWMNEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENS 342
Cdd:PLN03142   229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  343 LLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKS 422
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  423 DVEKGLPPKKETILKVGMSQLQKQFYRALLQKDLEVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLIT 502
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  503 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 582
Cdd:PLN03142   469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  583 AGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 662
Cdd:PLN03142   549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  663 KTVNKDELLQMVRFGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDD--EKDEN 740
Cdd:PLN03142   629 KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDedDKDEN 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  741 KFDFKKIVSENWIEPPKRERKRNYSESEYFKQTMRQGAPAKQREPRIPRMPQLHDFQFFNTQRLNELYEKEVRYLMQTHQ 820
Cdd:PLN03142   709 KLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQ 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  821 KNQLKDSIDVDEPEDLGDPLTAEEQEEKERLLEEGFSSWSRRDFNTFIRACEKYGRNDVKSIASEMEGKTEEEVERYAKA 900
Cdd:PLN03142   789 KGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKV 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  901 FKERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGN 980
Cdd:PLN03142   869 FWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGN 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  981 WDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLVERENQEFDERERQARKEKKLAKNMTPSKRAMARQATESPTS 1060
Cdd:PLN03142   949 WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSS 1028

                   ....*
gi 1847896053 1061 VKKRK 1065
Cdd:PLN03142  1029 LKKRK 1033
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
190-655 1.85e-146

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 454.30  E-value: 1.85e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  190 NTRLVTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWM 269
Cdd:COG0553    228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  270 NEIRRFCPVLRAVKFLGNPDERRHIRDnllvAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMR 349
Cdd:COG0553    307 RELAKFAPGLRVLVLDGTRERAKGANP----FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  350 LYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 429
Cdd:COG0553    383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLP 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  430 PKKETILKVGMSQLQKQFYRALLQK-DLEVVNAGGERKRLLNIA--MQLRKCCNHPYLFQGaepgppytTGEHLITNSGK 506
Cdd:COG0553    463 EKTEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRGLILAalTRLRQICSHPALLLE--------EGAELSGRSAK 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  507 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKpGSEKFVFLLSTRAGGL 586
Cdd:COG0553    535 LEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGE 613
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1847896053  587 GINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 655
Cdd:COG0553    614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
201-421 2.71e-136

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: 410.17  E-value: 2.71e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  201 QGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLR 280
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  281 AVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLIT 360
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896053  361 GTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQI-SGDNDQQEVVQQLHKVLRPFLLRRLK 421
Cdd:cd17997    161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
207-485 5.72e-117

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: 362.39  E-value: 5.72e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLIRLYEN-GINGILADEMGLGKTLQTISLLGYLHEFRGITG-PHMVVAPKSTLGNWMNEIRRFC--PVLRAV 282
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  283 KFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGT 362
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  363 PLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDN-DQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMS 441
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1847896053  442 QLQKQFY-RALLQKDLEVVNAGGE----RKRLLNIAMQLRKCCNHPYLF 485
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGgreiKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
203-395 1.37e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.82  E-value: 1.37e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   203 KMRDYQLAGLNWLIRLYENGIngiLADEMGLGKTLQ-TISLLGYLHEFRGitGPHMVVAP-KSTLGNWMNEIRRFCP--V 278
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPtRELAEQWAEELKKLGPslG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   279 LRAVKFLGNPDERRHIRDnlLVAGKFDVCVTSFEMAIK--EKTTLRRFSWRYIIIDEAHRIKNEN---SLLSKTMRLYST 353
Cdd:smart00487   83 LKVVGLYGGDSKREQLRK--LESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGfgdQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 1847896053   354 NYRLLITGTPLQNNLHELWSLLNflLPEIFSSAETFDEWFQI 395
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPIEQ 200
DpdE NF041062
protein DpdE;
227-389 3.68e-04

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 44.58  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  227 LADEMGLGKTLQT-ISLLGYLHEFRGITGphMVVAPKSTLGNWMNEIRrfcpvlravkflgnpdERRHIRDnLLVAgkfD 305
Cdd:NF041062   175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELR----------------DKFFLDD-FPGA---R 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  306 VCVTSFEMAIKEKTTLRRFSwrYIIIDEAHRI-KNENSLLSKTMRLY--------STNYRLLITGTPLQNNLHELWSLLN 376
Cdd:NF041062   233 VRVLSHEEPERWEPLLDAPD--LLVVDEAHQLaRLAWSGDPPERARYrelaalahAAPRLLLLSATPVLGNEETFLALLH 310
                          170
                   ....*....|....*
gi 1847896053  377 FLLPEIF--SSAETF 389
Cdd:NF041062   311 LLDPDLYplDDLEAF 325
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
23-1065 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1995.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   23 EEEQLNDQINDEEDEEELEAVTRTAISEDEDEEAAdggnspateddaAGDSSDGEEDEEDGNAVGGTEISKREKARLKEM 102
Cdd:PLN03142     1 EEEQVNTQANEEEDEEELEAVARSAGSDSDDDEVP------------AEDEDEDEEDDEEAESPAKAEISKREKARLKEL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  103 QKMKKQKIQEILDAQNAAIDADMNNRGKGRLKYLLQQTEIFAHFAKGDQSTSQKKTKGRGRHASKVTEEEEDEECLKEEE 182
Cdd:PLN03142    69 KKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  183 DGLSGTGNTRLVTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPK 262
Cdd:PLN03142   149 DGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  263 STLGNWMNEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENS 342
Cdd:PLN03142   229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  343 LLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKS 422
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  423 DVEKGLPPKKETILKVGMSQLQKQFYRALLQKDLEVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLIT 502
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  503 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 582
Cdd:PLN03142   469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  583 AGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 662
Cdd:PLN03142   549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQ 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  663 KTVNKDELLQMVRFGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDD--EKDEN 740
Cdd:PLN03142   629 KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDedDKDEN 708
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  741 KFDFKKIVSENWIEPPKRERKRNYSESEYFKQTMRQGAPAKQREPRIPRMPQLHDFQFFNTQRLNELYEKEVRYLMQTHQ 820
Cdd:PLN03142   709 KLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQ 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  821 KNQLKDSIDVDEPEDLGDPLTAEEQEEKERLLEEGFSSWSRRDFNTFIRACEKYGRNDVKSIASEMEGKTEEEVERYAKA 900
Cdd:PLN03142   789 KGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKV 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  901 FKERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGN 980
Cdd:PLN03142   869 FWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGN 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  981 WDELKAAFRTSPLFRFDWFVKSRTTQELARRCDTLIRLVERENQEFDERERQARKEKKLAKNMTPSKRAMARQATESPTS 1060
Cdd:PLN03142   949 WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSS 1028

                   ....*
gi 1847896053 1061 VKKRK 1065
Cdd:PLN03142  1029 LKKRK 1033
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
190-655 1.85e-146

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 454.30  E-value: 1.85e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  190 NTRLVTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWM 269
Cdd:COG0553    228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  270 NEIRRFCPVLRAVKFLGNPDERRHIRDnllvAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMR 349
Cdd:COG0553    307 RELAKFAPGLRVLVLDGTRERAKGANP----FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  350 LYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 429
Cdd:COG0553    383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLP 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  430 PKKETILKVGMSQLQKQFYRALLQK-DLEVVNAGGERKRLLNIA--MQLRKCCNHPYLFQGaepgppytTGEHLITNSGK 506
Cdd:COG0553    463 EKTEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRGLILAalTRLRQICSHPALLLE--------EGAELSGRSAK 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  507 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKpGSEKFVFLLSTRAGGL 586
Cdd:COG0553    535 LEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGE 613
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1847896053  587 GINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 655
Cdd:COG0553    614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
201-421 2.71e-136

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: 410.17  E-value: 2.71e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  201 QGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLR 280
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  281 AVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLIT 360
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896053  361 GTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQI-SGDNDQQEVVQQLHKVLRPFLLRRLK 421
Cdd:cd17997    161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
207-485 5.72e-117

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: 362.39  E-value: 5.72e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLIRLYEN-GINGILADEMGLGKTLQTISLLGYLHEFRGITG-PHMVVAPKSTLGNWMNEIRRFC--PVLRAV 282
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  283 KFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGT 362
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  363 PLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDN-DQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMS 441
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1847896053  442 QLQKQFY-RALLQKDLEVVNAGGE----RKRLLNIAMQLRKCCNHPYLF 485
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGgreiKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
191-432 3.85e-105

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: 329.32  E-value: 3.85e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  191 TRLVTQPSCIQ-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWM 269
Cdd:cd18064      2 TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  270 NEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMR 349
Cdd:cd18064     82 AEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  350 LYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 429
Cdd:cd18064    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLP 241

                   ...
gi 1847896053  430 PKK 432
Cdd:cd18064    242 PKK 244
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
202-421 1.06e-99

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: 314.32  E-value: 1.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  202 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 281
Cdd:cd18009      2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  282 VKFLGNPDERRHIRDNLL----VAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRL 357
Cdd:cd18009     81 LLYHGTKEERERLRKKIMkregTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896053  358 LITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDND------------QQEVVQQLHKVLRPFLLRRLK 421
Cdd:cd18009    161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDnaadisnlseerEQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
202-421 9.96e-98

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: 308.91  E-value: 9.96e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  202 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 281
Cdd:cd17996      2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  282 VKFLGNPDERRHIRDNlLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTM-RLYSTNYRLLIT 360
Cdd:cd17996     82 IVYKGTPDVRKKLQSQ-IRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLLT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  361 GTPLQNNLHELWSLLNFLLPEIFSSAETFDEWF----QISGDNDQQE--------VVQQLHKVLRPFLLRRLK 421
Cdd:cd17996    161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFntpfANTGEQVKIElneeetllIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
192-421 4.77e-96

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: 304.63  E-value: 4.77e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  192 RLVTQPSCIQG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMN 270
Cdd:cd18065      3 RFEESPSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  271 EIRRFCPVLRAVKFLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRL 350
Cdd:cd18065     83 EFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847896053  351 YSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLHKVLRPFLLRRLK 421
Cdd:cd18065    163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
204-419 1.25e-86

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: 278.47  E-value: 1.25e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTP 363
Cdd:cd18003     81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  364 LQNNLHELWSLLNFLLPEIFSSAETFDEWFQ-------ISGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18003    161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
204-380 5.40e-84

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: 269.82  E-value: 5.40e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLLVaGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTP 363
Cdd:cd17919     81 YHGSQRERAQIRAKEKL-DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                          170
                   ....*....|....*..
gi 1847896053  364 LQNNLHELWSLLNFLLP 380
Cdd:cd17919    160 LQNNLEELWALLDFLDP 176
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
204-419 2.19e-77

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: 253.32  E-value: 2.19e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 283
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLLV-----------AGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYS 352
Cdd:cd17995     80 YHGSGESRQIIQQYEMYfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd17995    160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---GDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
203-419 3.89e-77

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: 252.28  E-value: 3.89e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  203 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 282
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  283 KFLGNPDERRHIRDNLLVAG-----KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRL 357
Cdd:cd17993     81 VYLGDIKSRDTIREYEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896053  358 LITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEwfqiSGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd17993    161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE----EHDEEQEKGIADLHKELEPFILRR 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
204-419 7.85e-72

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: 238.17  E-value: 7.85e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNL------LVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRL 357
Cdd:cd18002     81 YWGNPKDRKVLRKFWdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1847896053  358 LITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQ---------ISGDNDQQevVQQLHKVLRPFLLRR 419
Cdd:cd18002    161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkdieshaenKTGLNEHQ--LKRLHMILKPFMLRR 229
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
204-419 4.98e-70

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: 232.71  E-value: 4.98e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTP 363
Cdd:cd18006     81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  364 LQNNLHELWSLLNFLLPEIFSSaETFDEWFQISGD-NDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18006    161 IQNSLQELYALLSFIEPNVFPK-DKLDDFIKAYSEtDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
200-421 1.02e-68

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: 230.70  E-value: 1.02e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  200 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 279
Cdd:cd18062     20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  280 RAVKFLGNPDERRHIRDnLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRL-YSTNYRLL 358
Cdd:cd18062    100 VKVSYKGSPAARRAFVP-QLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  359 ITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQ----ISG---DNDQQE---VVQQLHKVLRPFLLRRLK 421
Cdd:cd18062    179 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGekvDLNEEEtilIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
200-421 5.17e-68

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: 228.41  E-value: 5.17e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  200 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 279
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  280 RAVKFLGNPDERRHIRDNLLvAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRL-YSTNYRLL 358
Cdd:cd18063    100 VKISYKGTPAMRRSLVPQLR-SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  359 ITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQ----ISG---DNDQQE---VVQQLHKVLRPFLLRRLK 421
Cdd:cd18063    179 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGervDLNEEEtilIIRRLHKVLRPFLLRRLK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
200-421 8.98e-68

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: 226.68  E-value: 8.98e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  200 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 279
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  280 RAVKFLGNPDERRHIRDnllvAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLI 359
Cdd:cd18012     80 KVLVIHGTKRKREKLRA----LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  360 TGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQ-QEVVQQLHKVLRPFLLRRLK 421
Cdd:cd18012    156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
193-419 7.12e-67

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: 224.88  E-value: 7.12e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  193 LVTQPSCIQGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWM 269
Cdd:cd18054      7 LKKQPSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  270 NEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAG-----KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLL 344
Cdd:cd18054     87 REFEIWAPEINVVVYIGDLMSRNTIREYEWIHSqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896053  345 SKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDqqevVQQLHKVLRPFLLRR 419
Cdd:cd18054    167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
204-383 1.13e-65

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: 219.56  E-value: 1.13e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLLV-AGKFDVCVTSFEMAI---KEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLI 359
Cdd:cd17998     80 YYGSQEERKHLRYDILKgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                          170       180
                   ....*....|....*....|....
gi 1847896053  360 TGTPLQNNLHELWSLLNFLLPEIF 383
Cdd:cd17998    160 TGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
193-419 2.07e-59

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: 203.74  E-value: 2.07e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  193 LVTQPSCIQG----KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNW 268
Cdd:cd18053      6 LKKQPSYIGGheglELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSW 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  269 MNEIRRFCPVLRAVKFLGNPDERRHIRDNLLVAG-----KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSL 343
Cdd:cd18053     86 QREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPqtkrlKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSL 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1847896053  344 LSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEwfqiSGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18053    166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
504-630 2.47e-53

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: 182.29  E-value: 2.47e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  504 SGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKPGSEkFVFLLSTRA 583
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1847896053  584 GGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 630
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
204-419 5.54e-52

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: 182.55  E-value: 5.54e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH-----EFRGITGPHMVVAPKSTLGNWMNEIRRFCP- 277
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHhkranSFNSENLPSLVVCPPTLVGHWVAEIKKYFPn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  278 -VLRAVKFLGNPDERRHIRDNLlvaGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYR 356
Cdd:cd17999     81 aFLKPLAYVGPPQERRRLREQG---EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896053  357 LLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWF------------QISGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd17999    158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrdskaSAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
207-419 9.13e-52

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: 180.33  E-value: 9.13e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 286
Cdd:cd17994      4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  287 npderrhirDNLLVagkfdvcvTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQN 366
Cdd:cd17994     84 ---------DHVLL--------TSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQN 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  367 NLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQqevVQQLHKVLRPFLLRR 419
Cdd:cd17994    147 NLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
204-419 7.28e-51

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: 178.70  E-value: 7.28e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 283
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHI-------RDNL--LVAG--KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYS 352
Cdd:cd18058     79 YHGSQISRQMIqqyemyyRDEQgnPLSGifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF---GDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
206-419 1.51e-50

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: 178.33  E-value: 1.51e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  206 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFL 285
Cdd:cd18001      3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFD-SGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  286 G-NPDERRHIRDNllVAGKFDVCVTSFEMAIKEKTTL-----RRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLI 359
Cdd:cd18001     82 GtSKKERERNLER--IQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1847896053  360 TGTPLQNNLHELWSLLNFLLP-EIFSSAETFDEWFQ--ISGDNDQ----------QEVVQQLHKVLRPFLLRR 419
Cdd:cd18001    160 TGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFEnpITRGRDKdatqgekalgSEVAENLRQIIKPYFLRR 232
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
912-1023 6.80e-50

SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three alpha-helices. It has a role in DNA binding, contacting DNA target sites similar to c-Myb (pfam00249) repeats or homeodomains.


Pssm-ID: 462681 [Multi-domain]  Cd Length: 116  Bit Score: 171.94  E-value: 6.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  912 DRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQY-GQNKGKLYNEECDRFMICMVHKLGYGN---WDELKAA 987
Cdd:pfam09111    1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYpPNNKGKTYTEEEDRFLLCMLYKYGYGNedlYEKIKQE 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1847896053  988 FRTSPLFRFDWFVKSRTTQELARRCDTLIRLVEREN 1023
Cdd:pfam09111   81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
204-419 1.73e-49

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: 174.86  E-value: 1.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFrGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 283
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRD---------NLLVAG--KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYS 352
Cdd:cd18060     79 YHGSLASRQMIQQyemyckdsrGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
204-419 1.89e-48

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: 171.75  E-value: 1.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLgYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 283
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIR---------DNLLVAG--KFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYS 352
Cdd:cd18059     79 YHGSQASRRTIQlyemyfkdpQGRVIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18059    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
206-380 1.16e-47

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: 168.66  E-value: 1.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  206 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV--- 282
Cdd:cd18000      3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVvlh 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  283 ---KFLGNPDERRHIRDNLL----VAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNY 355
Cdd:cd18000     83 ssgSGTGSEEKLGSIERKSQlirkVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
                          170       180
                   ....*....|....*....|....*
gi 1847896053  356 RLLITGTPLQNNLHELWSLLNFLLP 380
Cdd:cd18000    163 RLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
207-419 1.96e-46

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: 166.34  E-value: 1.96e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 286
Cdd:cd18055      4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  287 NPDERRHIR-------DNLLVAGK------------FDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKT 347
Cdd:cd18055     84 DKDSRAIIRenefsfdDNAVKGGKkafkmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1847896053  348 MRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18055    164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---ADISKEDQIKKLHDLLGPHMLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
205-419 2.63e-46

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: 166.31  E-value: 2.63e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  205 RDYQLAGLNWLIrlyENGinGILADEMGLGKTLQTISL-LGYLHEFRGITGPHM----------------VVAPKSTLGN 267
Cdd:cd18008      2 LPYQKQGLAWML---PRG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLSQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  268 WMNEIRRFC--PVLRAVKFLGNpdeRRHIRDNLLVagKFDVCVTSFEM----------------AIKEKTTLRRFSWRYI 329
Cdd:cd18008     77 WKDEIEKHTkpGSLKVYVYHGS---KRIKSIEELS--DYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  330 IIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQQEVVQQLH 409
Cdd:cd18008    152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERLQ 231
                          250
                   ....*....|
gi 1847896053  410 KVLRPFLLRR 419
Cdd:cd18008    232 ALLKPILLRR 241
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
204-419 4.64e-46

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: 165.62  E-value: 4.64e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIR-------DNLLVAGK------------FDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLL 344
Cdd:cd18057     81 YTGDKESRSVIRenefsfeDNAIRSGKkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896053  345 SKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---ADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
204-419 9.75e-45

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: 161.33  E-value: 9.75e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 283
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEIL-LTGIRGPFLIIAPLSTIANWEREFRTWTD-LNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHI-------RDN----LLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYS 352
Cdd:cd18061     79 YHGSLISRQMIqqyemyfRDSqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisGDNDQQEVVQQLHKVLRPFLLRR 419
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
204-419 1.57e-44

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: 161.00  E-value: 1.57e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 283
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIR-------DNLLVAGK------------FDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLL 344
Cdd:cd18056     81 YVGDKDSRAIIRenefsfeDNAIRGGKkasrmkkeasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1847896053  345 SKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQqevVQQLHKVLRPFLLRR 419
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ---IKKLHDMLGPHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
204-419 3.58e-40

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: 149.07  E-value: 3.58e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLG------------YLHEFRGITGPH--------MVVAPKS 263
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrENNRPRFKKKPPassakkpvLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  264 TLGNWMNEIRRFCPvLRAVKFLGNPDERrhIRDNLLVAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSL 343
Cdd:cd18005     81 VLYNWKDELDTWGH-FEVGVYHGSRKDD--ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  344 LSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWF--------QISGDNDQ----QEVVQQLHKV 411
Cdd:cd18005    158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFsepikrgqRHTATARElrlgRKRKQELAVK 237

                   ....*...
gi 1847896053  412 LRPFLLRR 419
Cdd:cd18005    238 LSKFFLRR 245
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
204-419 4.93e-37

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: 139.73  E-value: 4.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWL----IRLYENGING-ILADEMGLGKTLQTISLLGYLHEFRGITGPH----MVVAPKSTLGNWMNEIRR 274
Cdd:cd18004      1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  275 FCPvLRAVKFL---GNPDERRHIRDNLLVAGKFDVCVTSFEmaikektTLRRFSWRYI--------IIDEAHRIKNENSL 343
Cdd:cd18004     81 WLG-LRRIKVVtadGNAKDVKASLDFFSSASTYPVLIISYE-------TLRRHAEKLSkkisidllICDEGHRLKNSESK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  344 LSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQI----SGDNDQ--------QEVVQQLHKV 411
Cdd:cd18004    153 TTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrSRDPDAseedkelgAERSQELSEL 232

                   ....*...
gi 1847896053  412 LRPFLLRR 419
Cdd:cd18004    233 TSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
226-393 5.19e-33

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: 128.18  E-value: 5.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  226 ILADEMGLGKTLQTISLL-GYLHEFRGITGPhMVVAPKSTLGNWMNEIRRFCPvlravkflgnPDERR-HIRDNLLVAGK 303
Cdd:cd18007     30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKWLP----------PDLRPlLVLVSLSASKR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  304 FDVCV-----------------TSFEMAIKEKTTLRRFSWRY-----------IIIDEAHRIKNENSLLSKTMRLYSTNY 355
Cdd:cd18007     99 ADARLrkinkwhkeggvlligyELFRNLASNATTDPRLKQEFiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKR 178
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1847896053  356 RLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWF 393
Cdd:cd18007    179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
203-395 1.37e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.82  E-value: 1.37e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   203 KMRDYQLAGLNWLIRLYENGIngiLADEMGLGKTLQ-TISLLGYLHEFRGitGPHMVVAP-KSTLGNWMNEIRRFCP--V 278
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPtRELAEQWAEELKKLGPslG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   279 LRAVKFLGNPDERRHIRDnlLVAGKFDVCVTSFEMAIK--EKTTLRRFSWRYIIIDEAHRIKNEN---SLLSKTMRLYST 353
Cdd:smart00487   83 LKVVGLYGGDSKREQLRK--LESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGfgdQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 1847896053   354 NYRLLITGTPLQNNLHELWSLLNflLPEIFSSAETFDEWFQI 395
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPIEQ 200
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
206-389 2.76e-28

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: 113.45  E-value: 2.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  206 DYQLAGLNWLIRlyeNGINGILADEMGLGKTLQTISLLGYLHEfrgiTGPHMVVAPKSTLGNWMNEIRRFCPVL--RAVK 283
Cdd:cd18010      3 PFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPSLppDDIQ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  284 FLGNPDERRHIRDNLlvagkfdVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSK-TMRLY-STNYRLLITG 361
Cdd:cd18010     76 VIVKSKDGLRDGDAK-------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKaALPLLkRAKRVILLSG 148
                          170       180
                   ....*....|....*....|....*...
gi 1847896053  362 TPLQNNLHELWSLLNFLLPEIFSSAETF 389
Cdd:cd18010    149 TPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
220-419 5.84e-27

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: 110.64  E-value: 5.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  220 ENGINGILADEMGLGKTLQTISLLgylhefrgITGPHMVVAPKSTLGNWMNEIRRFC-PVlrAVKFLGNPDERRHIRDNL 298
Cdd:cd18071     46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVkPG--QLKVYTYHGGERNRDPKL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  299 LvaGKFDVCVTSF-----EMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWS 373
Cdd:cd18071    116 L--SKYDIVLTTYntlasDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1847896053  374 LLNFLLPEIFSSAETFDEWFQ---ISGDNDQQEVVQQLHKVLrpfLLRR 419
Cdd:cd18071    194 LLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQI---TLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
519-619 3.77e-26

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: 103.83  E-value: 3.77e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  519 ERDSRVLIFSQMTRLLDilEDYLMFR-GYLYCRIDGNTGGEDRDASIDAFNKpgsEKFVFLLSTRAGGLGINLATADVVI 597
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDVAERGLDLPDVDLVI 87
                           90       100
                   ....*....|....*....|..
gi 1847896053  598 LYDSDWNPQVDLQAQDRAHRIG 619
Cdd:pfam00271   88 NYDLPWNPASYIQRIGRAGRAG 109
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
207-419 1.88e-23

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: 100.63  E-value: 1.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISLL--------------------GYLHEFRGITGPH--MVVAPKS 263
Cdd:cd18072      4 HQKQALAWLLwRERQKPRGGILADDMGLGKTLTMIALIlaqkntqnrkeeekekalteWESKKDSTLVPSAgtLVVCPAS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  264 TLGNWMNEIRRFCP--VLRAVKFLGNPDERrhirdNLLVAGKFDVCVTSFEMAIKE---------KTTLRRFSWRYIIID 332
Cdd:cd18072     84 LVHQWKNEVESRVAsnKLRVCLYHGPNRER-----IGEVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  333 EAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFqisgDNDQQEVVQQLHKVL 412
Cdd:cd18072    159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV----DNKSRKGGERLNILT 234

                   ....*..
gi 1847896053  413 RPFLLRR 419
Cdd:cd18072    235 KSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
535-619 5.57e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.82  E-value: 5.57e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053   535 DILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNKPgseKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDR 614
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1847896053   615 AHRIG 619
Cdd:smart00490   78 AGRAG 82
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
204-419 2.56e-22

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: 97.16  E-value: 2.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYEN----GING-ILADEMGLGKTLQTISLLGYLHEFRGITGPH----MVVAPKSTLGNWMNEI-- 272
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGrrirGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELgk 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  273 ---RRFCPV----------LRAVKFLGNPDERRHIRDNLLVagkfdvcvtSFEMAIKEKTTLRRFSWRYIIIDEAHRIKN 339
Cdd:cd18067     81 wlgGRLQPLaidggskkeiDRKLVQWASQQGRRVSTPVLII---------SYETFRLHVEVLQKGEVGLVICDEGHRLKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  340 ENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQI------SGDNDQQEV------VQQ 407
Cdd:cd18067    152 SDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpilkgrDADASEKERqlgeekLQE 231
                          250
                   ....*....|..
gi 1847896053  408 LHKVLRPFLLRR 419
Cdd:cd18067    232 LISIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
226-394 4.72e-22

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: 96.07  E-value: 4.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  226 ILADEMGLGKTLQTISLLGYLHEfRGITGPH------MVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPDerrHIRDNLL 299
Cdd:cd18066     28 ILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQD---HKVEEFI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  300 VAGKFDVCVTSFEMAIKEKTTLRRFSWRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLL 379
Cdd:cd18066    104 ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVN 183
                          170
                   ....*....|....*
gi 1847896053  380 PEIFSSAETFDEWFQ 394
Cdd:cd18066    184 PGILGSLSTYRKVYE 198
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
222-393 7.42e-22

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: 96.11  E-value: 7.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  222 GINGILADEMGLGKTLQTISLLG--YLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFL--------GNPDER 291
Cdd:cd18068     28 GSGCILAHCMGLGKTLQVVTFLHtvLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDEEKIevnelatyKRPQER 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  292 RHIRDNLLVAGkfDVCVTSFEM--------AIKEKTTLRRFSWRY--------IIIDEAHRIKNENSLLSKTMRLYSTNY 355
Cdd:cd18068    108 SYKLQRWQEEG--GVMIIGYDMyrilaqerNVKSREKLKEIFNKAlvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKR 185
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1847896053  356 RLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWF 393
Cdd:cd18068    186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
204-391 5.44e-21

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 92.35  E-value: 5.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLYENGIngILADEMGLGKTLQTISLLGYLhEFRGITGPHMVVAPKSTLGNWMNEIRRF--CPVLRA 281
Cdd:cd18011      1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQDKfgLPFLIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  282 VKFLGNPDERRHIRdnllVAGKFDVCVTSFEMA---IKEKTTLRRFSWRYIIIDEAHRIKNEN----SLLSKTMRLYS-- 352
Cdd:cd18011     78 DRETAAQLRRLIGN----PFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLAkr 153
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1847896053  353 TNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDE 391
Cdd:cd18011    154 ARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
207-401 7.39e-19

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: 86.79  E-value: 7.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  207 YQLAGLNWLirlYEN------------GINGILADEMGLGKTLQTISLLGYLheFRGITGPH-MVVAPKSTLGNWMNEIR 273
Cdd:cd18069      4 HQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLSEFN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  274 RFCPVLRA----------VKFLGNPDERRHIRDNLLV--AGKFDVCVTSFEMaikekttlrrFSWR----YIIIDEAHRI 337
Cdd:cd18069     79 KWLPPPEAlpnvrprpfkVFILNDEHKTTAARAKVIEdwVKDGGVLLMGYEM----------FRLRpgpdVVICDEGHRI 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1847896053  338 KNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDEWFQISGDNDQ 401
Cdd:cd18069    149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQ 212
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
204-418 1.88e-18

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: 86.24  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIRLyengiNGILADEMGLGKTLQTISLL------------GYLHEFRGITGPHM-------------V 258
Cdd:cd18070      1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDClvaetpvsskatlI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  259 VAPKSTLGNWMNEIRRFCPV-LRAVKFLGNPDE---RRHIRDNLLVAgkfDVCVTSFE---------MAIKEKTTLRRFS 325
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDgalASPAPEILAEY---DIVVTTYDvlrtelhyaEANRSNRRRRRQK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  326 -------------WRYIIIDEAHRIKNENSLLSKTMRLYSTNYRLLITGTPLQNNLHELWSLLNFLLPEIFSSAETFDE- 391
Cdd:cd18070    153 ryeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARv 232
                          250       260
                   ....*....|....*....|....*..
gi 1847896053  392 WFQISGDNDQQEvvqQLHKVLRPFLLR 418
Cdd:cd18070    233 LIRPQGRNKARE---PLAALLKELLWR 256
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
769-855 1.78e-16

HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of which (H2, H3, H4) form an L-like configuration. Helix H2 runs antiparallel to helices H3 and H4, packing closely against helix H4, whilst helix H1 reposes in the concave surface formed by these three helices and runs perpendicular to them. The domain confers DNA and nucleosome binding properties to the protein.


Pssm-ID: 430414  Cd Length: 110  Bit Score: 76.06  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  769 YFKQTMRQGAPAKQREPRIPRMP---QLHDFQFFNTqRLNELYEKEvryLMQTHQKNQLK---DSIDVDEPEDLGD---- 838
Cdd:pfam09110    5 YYKDVLGTGGKKSTTKPKAPRAPkqiNIQDHQFFPP-RLKELQEKE---QLYYKKKIGYKvtlDDGKEEDGEEFEEerea 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1847896053  839 -------------PLTAEEQEEKERLLEEG 855
Cdd:pfam09110   81 krkleqeeidnaePLTEEEEAEKEELLSEG 110
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
204-378 6.63e-13

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: 69.30  E-value: 6.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGLNWLIrlyENGINGILADeMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGN-WMNEIRRFcPVLRAV 282
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKW-NHLRNL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  283 KF---LGNPDERRHirdnlLVAGKFDVCVTSFEMA---IKEKttLRRFSWRYIIIDEAHRIKNENSLLSK-TMRLYSTNY 355
Cdd:cd18013     75 TVsvaVGTERQRSK-----AANTPADLYVINRENLkwlVNKS--GDPWPFDMVVIDELSSFKSPRSKRFKaLRKVRPVIK 147
                          170       180
                   ....*....|....*....|....
gi 1847896053  356 RLL-ITGTPLQNNLHELWSLLNFL 378
Cdd:cd18013    148 RLIgLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
202-780 1.22e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 65.43  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  202 GKMRDYQLAGLN-WLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITgphmVVAPKSTLGN-WMNEIRRFcpvL 279
Cdd:COG1061     79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVL----VLVPRRELLEqWAEELRRF---L 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  280 RAVKFLGNPDERRhirdnllvagkFDVCVTSFEMAIKEKTtLRRFS--WRYIIIDEAHRIKNENslLSKTMRLYSTNYRL 357
Cdd:COG1061    152 GDPLAGGGKKDSD-----------APITVATYQSLARRAH-LDELGdrFGLVIIDEAHHAGAPS--YRRILEAFPAAYRL 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  358 LITGTPL-QNNLHELWSLLNFLLPEIfssaetfdewfqisgdnDQQEVVQQlhKVLRPFLLRRLKSDVEKglppkketil 436
Cdd:COG1061    218 GLTATPFrSDGREILLFLFDGIVYEY-----------------SLKEAIED--GYLAPPEYYGIRVDLTD---------- 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  437 kvgmsqlQKQFYRALLQKDLEVVNAGGERKRLlnIAMQLRKccNHPylfqgaepgppyttgehlitnsgkmvlldkllpk 516
Cdd:COG1061    269 -------ERAEYDALSERLREALAADAERKDK--ILRELLR--EHP---------------------------------- 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  517 lkeRDSRVLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLSTRAGGLGINLATADVV 596
Cdd:COG1061    304 ---DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDVA 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  597 ILYDSDWNPQVDLQAQDRAHRIGQKKE-VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVR 675
Cdd:COG1061    378 ILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEV 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  676 FGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDEKDENKFDFKKIVSENWIEP 755
Cdd:COG1061    458 KGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
                          570       580
                   ....*....|....*....|....*
gi 1847896053  756 PKRERKRNYSESEYFKQTMRQGAPA 780
Cdd:COG1061    538 LLELLAALLRLEELAALLLKELLRA 562
ResIII pfam04851
Type III restriction enzyme, res subunit;
203-363 2.96e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 51.13  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  203 KMRDYQLAGL-NWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITgPHMVVAPKSTLGN-WMNEIRRFCPVLR 280
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRKDLLEqALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  281 AVKFLGNPDERRHIRDNllvagkFDVCVTSFEMAIKE-KTTLRRFS---WRYIIIDEAHRiknensLLSKTMR----LYS 352
Cdd:pfam04851   82 EIGEIISGDKKDESVDD------NKIVVTTIQSLYKAlELASLELLpdfFDVIIIDEAHR------SGASSYRnileYFK 149
                          170
                   ....*....|.
gi 1847896053  353 TNYRLLITGTP 363
Cdd:pfam04851  150 PAFLLGLTATP 160
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
858-902 5.74e-07

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 47.18  E-value: 5.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1847896053  858 SWSRRDFNTFIRACEKYGRNDVKSIASEMEGKTEEEVERYAKAFK 902
Cdd:cd00167      1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
856-904 1.54e-06

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 46.06  E-value: 1.54e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1847896053   856 FSSWSRRDFNTFIRACEKYGRNDVKSIASEMEGKTEEEVERYAKAFKER 904
Cdd:smart00717    1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNLLKP 49
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
572-630 9.91e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.62  E-value: 9.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1847896053  572 SEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQkKEVQVFRFC 630
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
204-363 1.28e-05

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: 46.14  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  204 MRDYQLAGL-NWLIRLYENGinGILADEMGLGKTLQTISLLGYLHEFRGItgphmVVAPKSTLGN-WMNEIRRFCPVlRA 281
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKELRTL-----IVVPTDALLDqWKERFEDFLGD-SS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  282 VKFLGNPDERRHIRDNLLVAgkfdvCVTSFEMAIKE-KTTLRRFSwrYIIIDEAHRIKNENslLSKTMRLYSTNYRLLIT 360
Cdd:cd17926     73 IGLIGGGKKKDFDDANVVVA-----TYQSLSNLAEEeKDLFDQFG--LLIVDEAHHLPAKT--FSEILKELNAKYRLGLT 143

                   ...
gi 1847896053  361 GTP 363
Cdd:cd17926    144 ATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
224-337 9.89e-05

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 43.55  E-value: 9.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  224 NGILADEMGLGKTLqtISLLGYLHEFRGITGPHMVVAPKSTLGN-WMNEIR-RFCPVLRAVKFLG--NPDERRHIRdnll 299
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPTKALALqTAERLReLFGPGIRVAVLVGgsSAEEREKNK---- 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1847896053  300 vAGKFDVCVTSFEMAIKEKTTLRRFS---WRYIIIDEAHRI 337
Cdd:cd00046     77 -LGDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAL 116
DpdE NF041062
protein DpdE;
227-389 3.68e-04

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 44.58  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  227 LADEMGLGKTLQT-ISLLGYLHEFRGITGphMVVAPKSTLGNWMNEIRrfcpvlravkflgnpdERRHIRDnLLVAgkfD 305
Cdd:NF041062   175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELR----------------DKFFLDD-FPGA---R 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  306 VCVTSFEMAIKEKTTLRRFSwrYIIIDEAHRI-KNENSLLSKTMRLY--------STNYRLLITGTPLQNNLHELWSLLN 376
Cdd:NF041062   233 VRVLSHEEPERWEPLLDAPD--LLVVDEAHQLaRLAWSGDPPERARYrelaalahAAPRLLLLSATPVLGNEETFLALLH 310
                          170
                   ....*....|....*
gi 1847896053  377 FLLPEIF--SSAETF 389
Cdd:NF041062   311 LLDPDLYplDDLEAF 325
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
436-605 4.52e-04

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 43.47  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  436 LKVGMSQLQKQFYRALLQ-------KDLEVVNAGGERKRLLNIAMQLRKCC---NHPYLF----------QGAEPgppyt 495
Cdd:pfam11496    8 LPTPMTSYQKELTEQIVSlhysdilKYCETSDSKEDISLIKSMTLCLENLSlvaTHPYLLvdhympksllLKDEP----- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847896053  496 tgEHLITNSGKMVLLDKLLPKLKERDSR----VLIFSQMTRLLDILEDYLMFRGYLYCRIDGNTG-GEDRDASIDAFNKP 570
Cdd:pfam11496   83 --EKLAYTSGKFLVLNDLVNLLIERDRKepinVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLyGENKKVSDSGNKKI 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1847896053  571 GSEKFVFLLSTR-----AGGLGINlaTADVVILYDSDWNP 605
Cdd:pfam11496  161 HSTTCHLLSSTGqltndDSLLENY--KFDLIIAFDSSVDT 198
 
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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