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Conserved domains on  [gi|15224228|ref|NP_179466|]
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chromatin remodeling 8 [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 17572067)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
169-864 4.48e-138

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.04  E-value: 4.48e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  169 RKPSRRDGKKVKVVSFREDTDFDAVFDGASAGFVETERDELVRKGILTPFHKLDGFERRLQQPGPSNSRNLPEGDDENED 248
Cdd:COG0553   25 RLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  249 SSIIDRAVQSMSLAA-KARPTTKLLDAEDLPKLEPPTAPFRRLRKLYKTPNSPDNEAKKRKAGKKSKKTRPLPEKKWRKR 327
Cdd:COG0553  105 ALALLLLALLGLLLSlALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  328 ISREDSSLQGSGDGRRILTTSSCEEEELDDFDDADDNERSSVQLEGGLNIPECIFRKLFDYQRVGVQWLWELHCQRAGGI 407
Cdd:COG0553  185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  408 IGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEILHDSAQdsghgkgqgkasesdyds 487
Cdd:COG0553  265 LADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE------------------ 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  488 essvdsdhepKSKNTKKWDsllnrvlnsESGLLITTYEQLRLQGEKLLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTV 567
Cdd:COG0553  327 ----------RAKGANPFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKAR 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  568 HRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASplqvstayrcavVLRDLIMPYLLRRMKA 647
Cdd:COG0553  388 HRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKE 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  648 DVNAHLTKKTEHVLFCSLTVEQRSTYRAFLAssEVEQIFDGNRNSLYGIDV------MRKICNHPDLLEREHSHQNpdyg 721
Cdd:COG0553  456 DVLKDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAEGIRRRGLIlaaltrLRQICSHPALLLEEGAELS---- 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  722 npERSGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEDMFVFVLT 801
Cdd:COG0553  530 --GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLIS 607
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224228  802 TKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKDVTVYRLITRGTIEEKVYHRQ 864
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1120-1186 1.50e-19

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


:

Pssm-ID: 439329  Cd Length: 72  Bit Score: 83.72  E-value: 1.50e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224228 1120 QPEVLIRKICSFV-QQKGGSADTTSIVNHFRDIVSFNDKQLFKNLLKEIATLEKDQN-RSFWVLKSEYK 1186
Cdd:cd22254    4 EAEELLADIRDFLaFQAGGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGgRGVWVLKPEFR 72
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
169-864 4.48e-138

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.04  E-value: 4.48e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  169 RKPSRRDGKKVKVVSFREDTDFDAVFDGASAGFVETERDELVRKGILTPFHKLDGFERRLQQPGPSNSRNLPEGDDENED 248
Cdd:COG0553   25 RLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  249 SSIIDRAVQSMSLAA-KARPTTKLLDAEDLPKLEPPTAPFRRLRKLYKTPNSPDNEAKKRKAGKKSKKTRPLPEKKWRKR 327
Cdd:COG0553  105 ALALLLLALLGLLLSlALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  328 ISREDSSLQGSGDGRRILTTSSCEEEELDDFDDADDNERSSVQLEGGLNIPECIFRKLFDYQRVGVQWLWELHCQRAGGI 407
Cdd:COG0553  185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  408 IGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEILHDSAQdsghgkgqgkasesdyds 487
Cdd:COG0553  265 LADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE------------------ 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  488 essvdsdhepKSKNTKKWDsllnrvlnsESGLLITTYEQLRLQGEKLLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTV 567
Cdd:COG0553  327 ----------RAKGANPFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKAR 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  568 HRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASplqvstayrcavVLRDLIMPYLLRRMKA 647
Cdd:COG0553  388 HRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKE 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  648 DVNAHLTKKTEHVLFCSLTVEQRSTYRAFLAssEVEQIFDGNRNSLYGIDV------MRKICNHPDLLEREHSHQNpdyg 721
Cdd:COG0553  456 DVLKDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAEGIRRRGLIlaaltrLRQICSHPALLLEEGAELS---- 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  722 npERSGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEDMFVFVLT 801
Cdd:COG0553  530 --GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLIS 607
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224228  802 TKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKDVTVYRLITRGTIEEKVYHRQ 864
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
385-593 1.18e-108

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: 338.14  E-value: 1.18e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKM-YKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSGHGKGQGkasesdydsessvdsdhepksknTKKWDSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18000   81 LHSSGSGTGSEEKLG-----------------------SIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVI 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFP 593
Cdd:cd18000  138 LDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
378-867 5.66e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 296.33  E-value: 5.66e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   378 PECIFRKLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLH-FSKMYKPSIIICPVTLLRQWRREAQKWY 456
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   457 PDFHVEILHDSAQDSGHGKGQGKASEsdydsessvdsdhepkskntkKWDsllnrvlnsesgLLITTYEQLRLQGEKLLN 536
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREELLVAG---------------------KFD------------VCVTSFEMAIKEKTALKR 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   537 IEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVpitvGGYA 616
Cdd:PLN03142  290 FSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI----SGEN 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   617 NasplQVSTAYRCAVVLRdlimPYLLRRMKADVNAHLTKKTEHVLFCSLTVEQRSTYRAFLaSSEVEQIFDG-NRNSLYG 695
Cdd:PLN03142  366 D----QQEVVQQLHKVLR----PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALL-QKDLDVVNAGgERKRLLN 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   696 IdVM--RKICNHPDLLerehshQNPDYGNP--------ERSGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVA 765
Cdd:PLN03142  437 I-AMqlRKCCNHPYLF------QGAEPGPPyttgehlvENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   766 NEYSYRRMDGLTPVKQRMALIDEFN--NSEDmFVFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKK 843
Cdd:PLN03142  510 RGYQYCRIDGNTGGEDRDASIDAFNkpGSEK-FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKK 588
                         490       500
                  ....*....|....*....|....
gi 15224228   844 DVTVYRLITRGTIEEKVYHRQiYK 867
Cdd:PLN03142  589 EVQVFRFCTEYTIEEKVIERA-YK 611
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
388-709 1.75e-83

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: 273.79  E-value: 1.75e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    388 YQRVGVQWLWELHCQRA-GGIIGDEMGLGKTIQVLSFLGSL-HFSKMY-KPSIIICPVTLLRQWRREAQKW--YPDFHVE 462
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLkHVDKNWgGPTLIVVPLSLLHNWMNEFERWvsPPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    463 ILHdsaqdsGHGKGQgkasesdydsessvdsdHEPKSKNTKKWDSllnrvlnsesGLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:pfam00176   81 VLH------GNKRPQ-----------------ERWKNDPNFLADF----------DVVITTYETLRKHKELLKKVHWHRI 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGyanasplq 622
Cdd:pfam00176  128 VLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-------- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    623 vstAYRCAVVLRDLIMPYLLRRMKADVNAHLTKKTEHVLFCSLTVEQRSTYRAFLASSEVEQIFDGN------RNSLYGI 696
Cdd:pfam00176  200 ---GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNIL 276
                          330
                   ....*....|...
gi 15224228    697 DVMRKICNHPDLL 709
Cdd:pfam00176  277 MRLRKICNHPGLI 289
HELICc smart00490
helicase superfamily c-terminal domain;
757-840 7.40e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 7.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228     757 DILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEdmFVFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERA 836
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 15224228     837 WRIG 840
Cdd:smart00490   79 GRAG 82
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1120-1186 1.50e-19

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 83.72  E-value: 1.50e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224228 1120 QPEVLIRKICSFV-QQKGGSADTTSIVNHFRDIVSFNDKQLFKNLLKEIATLEKDQN-RSFWVLKSEYK 1186
Cdd:cd22254    4 EAEELLADIRDFLaFQAGGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGgRGVWVLKPEFR 72
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
169-864 4.48e-138

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.04  E-value: 4.48e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  169 RKPSRRDGKKVKVVSFREDTDFDAVFDGASAGFVETERDELVRKGILTPFHKLDGFERRLQQPGPSNSRNLPEGDDENED 248
Cdd:COG0553   25 RLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  249 SSIIDRAVQSMSLAA-KARPTTKLLDAEDLPKLEPPTAPFRRLRKLYKTPNSPDNEAKKRKAGKKSKKTRPLPEKKWRKR 327
Cdd:COG0553  105 ALALLLLALLGLLLSlALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  328 ISREDSSLQGSGDGRRILTTSSCEEEELDDFDDADDNERSSVQLEGGLNIPECIFRKLFDYQRVGVQWLWELHCQRAGGI 407
Cdd:COG0553  185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  408 IGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEILHDSAQdsghgkgqgkasesdyds 487
Cdd:COG0553  265 LADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE------------------ 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  488 essvdsdhepKSKNTKKWDsllnrvlnsESGLLITTYEQLRLQGEKLLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTV 567
Cdd:COG0553  327 ----------RAKGANPFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKAR 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  568 HRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASplqvstayrcavVLRDLIMPYLLRRMKA 647
Cdd:COG0553  388 HRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKE 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  648 DVNAHLTKKTEHVLFCSLTVEQRSTYRAFLAssEVEQIFDGNRNSLYGIDV------MRKICNHPDLLEREHSHQNpdyg 721
Cdd:COG0553  456 DVLKDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAEGIRRRGLIlaaltrLRQICSHPALLLEEGAELS---- 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  722 npERSGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEDMFVFVLT 801
Cdd:COG0553  530 --GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLIS 607
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224228  802 TKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKDVTVYRLITRGTIEEKVYHRQ 864
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
385-593 1.18e-108

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: 338.14  E-value: 1.18e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKM-YKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSGHGKGQGkasesdydsessvdsdhepksknTKKWDSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18000   81 LHSSGSGTGSEEKLG-----------------------SIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVI 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFP 593
Cdd:cd18000  138 LDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
378-867 5.66e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 296.33  E-value: 5.66e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   378 PECIFRKLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLH-FSKMYKPSIIICPVTLLRQWRREAQKWY 456
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   457 PDFHVEILHDSAQDSGHGKGQGKASEsdydsessvdsdhepkskntkKWDsllnrvlnsesgLLITTYEQLRLQGEKLLN 536
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREELLVAG---------------------KFD------------VCVTSFEMAIKEKTALKR 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   537 IEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVpitvGGYA 616
Cdd:PLN03142  290 FSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI----SGEN 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   617 NasplQVSTAYRCAVVLRdlimPYLLRRMKADVNAHLTKKTEHVLFCSLTVEQRSTYRAFLaSSEVEQIFDG-NRNSLYG 695
Cdd:PLN03142  366 D----QQEVVQQLHKVLR----PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALL-QKDLDVVNAGgERKRLLN 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   696 IdVM--RKICNHPDLLerehshQNPDYGNP--------ERSGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVA 765
Cdd:PLN03142  437 I-AMqlRKCCNHPYLF------QGAEPGPPyttgehlvENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228   766 NEYSYRRMDGLTPVKQRMALIDEFN--NSEDmFVFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKK 843
Cdd:PLN03142  510 RGYQYCRIDGNTGGEDRDASIDAFNkpGSEK-FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKK 588
                         490       500
                  ....*....|....*....|....
gi 15224228   844 DVTVYRLITRGTIEEKVYHRQiYK 867
Cdd:PLN03142  589 EVQVFRFCTEYTIEEKVIERA-YK 611
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
388-709 1.75e-83

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: 273.79  E-value: 1.75e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    388 YQRVGVQWLWELHCQRA-GGIIGDEMGLGKTIQVLSFLGSL-HFSKMY-KPSIIICPVTLLRQWRREAQKW--YPDFHVE 462
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLkHVDKNWgGPTLIVVPLSLLHNWMNEFERWvsPPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    463 ILHdsaqdsGHGKGQgkasesdydsessvdsdHEPKSKNTKKWDSllnrvlnsesGLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:pfam00176   81 VLH------GNKRPQ-----------------ERWKNDPNFLADF----------DVVITTYETLRKHKELLKKVHWHRI 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGyanasplq 622
Cdd:pfam00176  128 VLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-------- 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    623 vstAYRCAVVLRDLIMPYLLRRMKADVNAHLTKKTEHVLFCSLTVEQRSTYRAFLASSEVEQIFDGN------RNSLYGI 696
Cdd:pfam00176  200 ---GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNIL 276
                          330
                   ....*....|...
gi 15224228    697 DVMRKICNHPDLL 709
Cdd:pfam00176  277 MRLRKICNHPGLI 289
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
385-644 8.51e-65

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: 219.17  E-value: 8.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEIL 464
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HdsaqdsghgkgqgkasesdydsessvdsdhepkSKNTKKWDSLLNRVLNsESGLLITTYEQLR-----LQGEKLLNIEW 539
Cdd:cd18001   81 H---------------------------------GTSKKERERNLERIQR-GGGVLLTTYGMVLsnteqLSADDHDEFKW 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  540 GYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGK-LGVLPVFEAEFSVPITVGGYANA 618
Cdd:cd18001  127 DYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDA 206
                        250       260
                 ....*....|....*....|....*.
gi 15224228  619 SPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18001  207 TQGEKALGSEVAENLRQIIKPYFLRR 232
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
385-593 3.45e-63

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: 212.43  E-value: 3.45e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFS-KMYKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEgKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSghgkgqgkasesdydsessvdsdhepKSKNTKKWDsllnrvlnSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd17919   81 YHGSQRER--------------------------AQIRAKEKL--------DKFDVVLTTYETLRRDKASLRKFRWDLVV 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFP 593
Cdd:cd17919  127 VDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
726-851 3.70e-60

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: 201.94  E-value: 3.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  726 SGKMKVVAEVLKVWKQQGHRVLLFSQTQQMLDILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEDMFVFVLTTKVG 805
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15224228  806 GLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKDVTVYRLI 851
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
385-646 4.76e-59

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: 202.41  E-value: 4.76e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEIL 464
Cdd:cd18012    5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSaqdsghgkgqgkasesdydsessvdSDHEPKSKNTKKWDsllnrvlnsesgLLITTYEQLRLQGEKLLNIEWGYAVL 544
Cdd:cd18012   85 HGT-------------------------KRKREKLRALEDYD------------LVITSYGLLRRDIELLKEVKFHYLVL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  545 DEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASplqvs 624
Cdd:cd18012  128 DEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEAL----- 202
                        250       260
                 ....*....|....*....|..
gi 15224228  625 tayrcaVVLRDLIMPYLLRRMK 646
Cdd:cd18012  203 ------EELKKLISPFILRRLK 218
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
385-644 7.06e-53

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: 185.66  E-value: 7.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL---------------------HFSKMYKPSIIICPVT 443
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprfkkkpPASSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  444 LLRQWRREAQKWyPDFHVEILHdsaqdsghgkGQGKAsesdydsessvdsdhepkskntkkwDSLLNRVLNSESGLLITT 523
Cdd:cd18005   81 VLYNWKDELDTW-GHFEVGVYH----------GSRKD-------------------------DELEGRLKAGRLEVVVTT 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  524 YEQLRLQGEKLLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFE 603
Cdd:cd18005  125 YDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFK 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15224228  604 AEFSVPITVGGYANASPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18005  205 KHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR 245
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
385-644 4.84e-51

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: 179.85  E-value: 4.84e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSK------MYKPSIIICPVTLLRQWRREAQKWYPD 458
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  459 FHVEILHDsaqdsgHGKGQGKASESdydsessvdsdHEPKSKNtkkwdsllnrvlnsesgLLITTYEQLRLQGEKLLNIE 538
Cdd:cd17999   81 AFLKPLAY------VGPPQERRRLR-----------EQGEKHN-----------------VIVASYDVLRNDIEVLTKIE 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  539 WGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANA 618
Cdd:cd17999  127 WNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKA 206
                        250       260
                 ....*....|....*....|....*.
gi 15224228  619 SPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd17999  207 SAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
385-644 3.11e-43

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: 157.02  E-value: 3.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWyPDFHVEI 463
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLyQVEGIRGPFLVIAPLSTIPNWQREFETW-TDMNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSGhgkgqgkasesdydsessVDSDHEPKSK-NTKKWDSllnRVLNSEsgLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:cd17995   80 YHGSGESRQ------------------IIQQYEMYFKdAQGRKKK---GVYKFD--VLITTYEMVIADAEELRKIPWRVV 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFsvpitvGGYANASplQ 622
Cdd:cd17995  137 VVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTAE--Q 208
                        250       260
                 ....*....|....*....|..
gi 15224228  623 VSTayrcavvLRDLIMPYLLRR 644
Cdd:cd17995  209 VEK-------LQALLKPYMLRR 223
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
389-644 3.29e-42

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: 154.75  E-value: 3.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  389 QRVGVQWLWE-LHCQRAGGIIG----DEMGLGKTIQVLSFLGSLHFSKMYKPS-----IIICPVTLLRQWRREAQKWYPD 458
Cdd:cd18004    5 QREGVQFLYDcLTGRRGYGGGGailaDEMGLGKTLQAIALVWTLLKQGPYGKPtakkaLIVCPSSLVGNWKAEFDKWLGL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  459 fhvEILHDSAQDSGHGKGQgkasesdydsessvdsdhepkskntkkwDSLLNRVLNSESGLLITTYEQLRLQGEKLLN-I 537
Cdd:cd18004   85 ---RRIKVVTADGNAKDVK----------------------------ASLDFFSSASTYPVLIISYETLRRHAEKLSKkI 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  538 EWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYAN 617
Cdd:cd18004  134 SIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPD 213
                        250       260
                 ....*....|....*....|....*..
gi 15224228  618 ASPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18004  214 ASEEDKELGAERSQELSELTSRFILRR 240
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
384-646 1.88e-39

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: 146.75  E-value: 1.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVE 462
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLmEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  463 ILhdsaqdsghgKGqgkasesdydsessvdsdhepkSKNTKKwdSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:cd17996   83 VY----------KG----------------------TPDVRK--KLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYM 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQ-LQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASPL 621
Cdd:cd17996  129 IIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIEL 208
                        250       260
                 ....*....|....*....|....*....
gi 15224228  622 ----QVSTAYRCAVVLRdlimPYLLRRMK 646
Cdd:cd17996  209 neeeTLLIIRRLHKVLR----PFLLRRLK 233
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
385-644 1.66e-38

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: 143.65  E-value: 1.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSK-MYKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKgNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSgHGKGQGKASEsdydsessvDSDHepkskntkkwdsllnrvlnsesgLLITTYeQLRLQGEKLLN-IEWGYA 542
Cdd:cd18003   81 YYGSAKER-KLKRQGWMKP---------NSFH-----------------------VCITSY-QLVVQDHQVFKrKKWKYL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVggyanasPLQ 622
Cdd:cd18003  127 ILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTA-------MSE 199
                        250       260
                 ....*....|....*....|....
gi 15224228  623 VSTAYRCAVV--LRDLIMPYLLRR 644
Cdd:cd18003  200 GSQEENEELVrrLHKVLRPFLLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
384-646 2.75e-38

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: 142.85  E-value: 2.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVE 462
Cdd:cd17997    3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLkHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  463 ILHdsaqdsGHGKGQGKASESDYDsessvdsdhepksknTKKWDsllnrvlnsesgLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:cd17997   83 VLI------GDKEERADIIRDVLL---------------PGKFD------------VCITSYEMVIKEKTVLKKFNWRYI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVpitvggyANASPLQ 622
Cdd:cd17997  130 IIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV-------NNCDDDN 202
                        250       260
                 ....*....|....*....|....
gi 15224228  623 VSTAYRCAVVLRdlimPYLLRRMK 646
Cdd:cd17997  203 QEVVQRLHKVLR----PFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
388-646 8.88e-38

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: 141.75  E-value: 8.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEILHDS 467
Cdd:cd18009    7 YQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLLYHGT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  468 AQDSghgkgqgkasesdydsessvdsDHEPKSKNTKKWDSLLNRVLnsesgllITTYEQLRLQGEKLLNIEWGYAVLDEG 547
Cdd:cd18009   87 KEER----------------------ERLRKKIMKREGTLQDFPVV-------VTSYEIAMRDRKALQHYAWKYLIVDEG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  548 HRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASPLQVSTAY 627
Cdd:cd18009  138 HRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQ 217
                        250
                 ....*....|....*....
gi 15224228  628 RCAVVLRDLIMPYLLRRMK 646
Cdd:cd18009  218 NIVHMLHAILKPFLLRRLK 236
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
385-644 2.98e-36

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: 137.80  E-value: 2.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLweLHCqraGGIIGDEMGLGKTIQVLS----------------FLGSLHFSKMYKPS--IIICPVTLLR 446
Cdd:cd18008    1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeelEENSSDPKKLYLSKttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  447 QWRREAQK--WYPDFHVEILHDSaqdsghgkgqgkasesdydsessvdsdhePKSKNTKKWdsllnrvlnSESGLLITTY 524
Cdd:cd18008   76 QWKDEIEKhtKPGSLKVYVYHGS-----------------------------KRIKSIEEL---------SDYDIVITTY 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  525 EQLR----------------LQGEKLLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLF 588
Cdd:cd18008  118 GTLAsefpknkkgggrdskeKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLL 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15224228  589 DFVFPGKLGVLPVFEAEFSVPITVGGYANASPLQVstayrcavvlrdLIMPYLLRR 644
Cdd:cd18008  198 RFLRVEPFGDYPWFNSDISKPFSKNDRKALERLQA------------LLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
389-623 4.34e-36

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: 137.04  E-value: 4.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  389 QRVGVQWLWElHC-------QRAGG-IIGDEMGLGKTIQVLSFLGSL--HFSKMYKPsIIICPVTLLRQWRREAQKWYPD 458
Cdd:cd18007    5 QVEGVRFLWS-NLvgtdvgsDEGGGcILAHTMGLGKTLQVITFLHTYlaAAPRRSRP-LVLCPASTLYNWEDEFKKWLPP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  459 FHVeILHDSAQDSGHGKGQGKAsesdydsessvdsdhepksKNTKKWdsllnrvlNSESGLLITTYEQLR---LQGEKLL 535
Cdd:cd18007   83 DLR-PLLVLVSLSASKRADARL-------------------RKINKW--------HKEGGVLLIGYELFRnlaSNATTDP 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  536 NIEW-----------GYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEA 604
Cdd:cd18007  135 RLKQefiaalldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKK 214
                        250
                 ....*....|....*....
gi 15224228  605 EFSVPITVGGYANASPLQV 623
Cdd:cd18007  215 KFVKPIEAGQCVDSTEEDV 233
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
384-605 8.16e-36

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: 135.56  E-value: 8.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVe 462
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLfHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  463 ILHDSAQDSghgkgqgkasesdydseSSVDSDHE---PKSKNTKkwdslLNrvlnsesgLLITTYEQLRLQGEKLLNIEW 539
Cdd:cd17993   80 IVYLGDIKS-----------------RDTIREYEfyfSQTKKLK-----FN--------VLLTTYEIILKDKAFLGSIKW 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224228  540 GYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAE 605
Cdd:cd17993  130 QYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE 195
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
384-644 1.42e-34

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: 132.82  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVE 462
Cdd:cd18054   20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLfHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  463 ILHDSAQdsghgkgqgkasesdydsessvdsdhepkSKNT-KKWDSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGY 541
Cdd:cd18054  100 VYIGDLM-----------------------------SRNTiREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  542 AVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSvpitvGGYANaspl 621
Cdd:cd18054  151 LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-----KGREN---- 221
                        250       260
                 ....*....|....*....|...
gi 15224228  622 qvstAYRCavvLRDLIMPYLLRR 644
Cdd:cd18054  222 ----GYQS---LHKVLEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
388-644 7.07e-34

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: 129.87  E-value: 7.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWE-LHCQRaGGIIGDEMGLGKTIQVLSFLGSLHFS-KMYKPSIIICPVTLLRQWRREAQKWYPDFHV---- 461
Cdd:cd18006    4 YQLEGVNWLLQcRAEQH-GCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVitym 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  462 ---EILHDSAQDSghgkgqgkasesdydsessvdsdhepksKNTKKWDSLLnrvlnsesglliTTYEQLRLQGEKLLNIE 538
Cdd:cd18006   83 gdkEKRLDLQQDI----------------------------KSTNRFHVLL------------TTYEICLKDASFLKSFP 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  539 WGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGvlpvfeaefsvPITVGGYANA 618
Cdd:cd18006  123 WASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP-----------KDKLDDFIKA 191
                        250       260
                 ....*....|....*....|....*.
gi 15224228  619 SPlQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18006  192 YS-ETDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
384-656 3.05e-33

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: 129.02  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFH-V 461
Cdd:cd18064   15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRaV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  462 EILHDSAQDSGHGKgqgkasesdydsessvdsdhepkskntkkwdsllNRVLNSESGLLITTYEQLRLQGEKLLNIEWGY 541
Cdd:cd18064   95 CLIGDKDQRAAFVR----------------------------------DVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRY 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  542 AVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGgyanaspl 621
Cdd:cd18064  141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG-------- 212
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15224228  622 QVSTAYRCAVVLRdlimPYLLRRMKADVNAHLTKK 656
Cdd:cd18064  213 DQKLVERLHMVLR----PFLLRRIKADVEKSLPPK 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
388-644 1.11e-32

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: 127.27  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWEL-----HCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMY--KP----SIIICPVTLLRQWRREAQKWY 456
Cdd:cd18066    4 HQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYggKPvikrALIVTPGSLVKNWKKEFQKWL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  457 PDFHVEILhdsaqdsghgkgqgkasesdydsesSVDSDHepkskntkKWDSLLNRVLNSesgLLITTYEQLRLQGEKLLN 536
Cdd:cd18066   84 GSERIKVF-------------------------TVDQDH--------KVEEFIASPLYS---VLIISYEMLLRSLDQISK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  537 IEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYA 616
Cdd:cd18066  128 LNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREP 207
                        250       260
                 ....*....|....*....|....*...
gi 15224228  617 NASPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18066  208 TATPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
385-593 3.17e-32

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: 124.03  E-value: 3.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEIL 464
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSAQDSGHGKGQGKasesdydsessvdsdhepksKNTKKWDsllnrvlnsesgLLITTYEQLRLQGE--KLL-NIEWGY 541
Cdd:cd17998   81 YGSQEERKHLRYDIL--------------------KGLEDFD------------VIVTTYNLATSNPDdrSFFkRLKLNY 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15224228  542 AVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFP 593
Cdd:cd17998  129 VVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
384-605 4.70e-30

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: 119.77  E-value: 4.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  384 KLFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVE 462
Cdd:cd18053   20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLfHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  463 I-LHDsaqdsghgkgqgkasesdyDSESSVDSDHEPKSKNTKKWdsllnrvlnsESGLLITTYEQLRLQGEKLLNIEWGY 541
Cdd:cd18053  100 VyLGD-------------------INSRNMIRTHEWMHPQTKRL----------KFNILLTTYEILLKDKSFLGGLNWAF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224228  542 AVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAE 605
Cdd:cd18053  151 IGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEE 214
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
388-646 5.16e-29

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: 117.09  E-value: 5.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFhVEILHd 466
Cdd:cd18063   27 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLmEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV-VKISY- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  467 saqdsghgKGQgkasesdydsessvdsdhePKSKNtkkwdSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAVLDE 546
Cdd:cd18063  105 --------KGT-------------------PAMRR-----SLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  547 GHRIRNPNSDITLVCKQLQTV-HRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGyaNASPLQVST 625
Cdd:cd18063  153 GHRMKNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG--ERVDLNEEE 230
                        250       260
                 ....*....|....*....|.
gi 15224228  626 AYRCAVVLRDLIMPYLLRRMK 646
Cdd:cd18063  231 TILIIRRLHKVLRPFLLRRLK 251
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
405-628 9.76e-29

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: 115.68  E-value: 9.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  405 GGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYP-----------DFHVEILHDSAQDSgh 473
Cdd:cd18069   30 GCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPppealpnvrprPFKVFILNDEHKTT-- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  474 gkgqgkasesdydsessvdsdhEPKSKNTKKWDSllnrvlnsESGLLITTYEQLRLQ-GEKLLniewgyaVLDEGHRIRN 552
Cdd:cd18069  108 ----------------------AARAKVIEDWVK--------DGGVLLMGYEMFRLRpGPDVV-------ICDEGHRIKN 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224228  553 PNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASPLQVSTA-YR 628
Cdd:cd18069  151 CHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMrYR 227
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
385-646 1.07e-28

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: 116.30  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFhvei 463
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLmEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 lhdsaqdsghgkgqgkasesdydseSSVDSDHEPKSKNtkkwdSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18062  100 -------------------------VKVSYKGSPAARR-----AFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCK-QLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGyaNASPLQ 622
Cdd:cd18062  150 VDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG--EKVDLN 227
                        250       260
                 ....*....|....*....|....
gi 15224228  623 VSTAYRCAVVLRDLIMPYLLRRMK 646
Cdd:cd18062  228 EEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
388-644 1.82e-28

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: 115.26  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWELHCQRA-----GGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSI----IICPVTLLRQWRREAQKWyp 457
Cdd:cd18067    4 HQREGVKFLYRCVTGRRirgshGCIMADEMGLGKTLQCITLMWTLlRQSPQCKPEIdkaiVVSPSSLVKNWANELGKW-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  458 dfhveiLHDSAQDSGHGKGQGKASESdydsessvdsdhepkskNTKKWDSLLNRVLNSEsgLLITTYEQLRLQGEKLLNI 537
Cdd:cd18067   82 ------LGGRLQPLAIDGGSKKEIDR-----------------KLVQWASQQGRRVSTP--VLIISYETFRLHVEVLQKG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  538 EWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYAN 617
Cdd:cd18067  137 EVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDAD 216
                        250       260
                 ....*....|....*....|....*..
gi 15224228  618 ASPLQVSTAYRCAVVLRDLIMPYLLRR 644
Cdd:cd18067  217 ASEKERQLGEEKLQELISIVNRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
727-840 5.58e-28

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: 109.22  E-value: 5.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228    727 GKMKVVAEVLKvwKQQGHRVLLFSQTQQMLDIlESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEdmFVFVLTTKVGG 806
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 15224228    807 LGTNLTGANRVIIFDPDWNPSNDMQARERAWRIG 840
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
385-646 2.48e-27

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: 111.65  E-value: 2.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSL-HFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd18065   16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHdsaqdsghGKGQGKASEsdydsessvdsdhepkskntkkwdsLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18065   96 LI--------GDKDARAAF-------------------------IRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGgyanasplQV 623
Cdd:cd18065  143 IDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG--------DQ 214
                        250       260
                 ....*....|....*....|...
gi 15224228  624 STAYRCAVVLRdlimPYLLRRMK 646
Cdd:cd18065  215 KLVERLHAVLK----PFLLRRIK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
385-644 3.28e-27

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: 110.22  E-value: 3.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYK-PSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHdsaqdsghgkgqgkasesdydsessvdSDHepkskntkkwdsllnrvlnsesgLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd17994   81 YV---------------------------GDH-----------------------VLLTSYELISIDQAILGSIDWAVLV 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPitvggyanASPLQV 623
Cdd:cd17994  111 VDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADI--------SKEDQI 182
                        250       260
                 ....*....|....*....|.
gi 15224228  624 STayrcavvLRDLIMPYLLRR 644
Cdd:cd17994  183 KK-------LHDLLGPHMLRR 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
385-644 7.57e-27

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: 110.29  E-value: 7.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSK-MYKPSIIICPVTLLRQWRREAQKWYPDFHVEI 463
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHnIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDsghgkgqgkasesdydsessvdsdhepKSKNTKKWDSLLNRVLNSESGLLITTYeQLRLQGEKLLN-IEWGYA 542
Cdd:cd18002   81 YWGNPKD---------------------------RKVLRKFWDRKNLYTRDAPFHVVITSY-QLVVQDEKYFQrVKWQYM 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPIT--VGGYANASP 620
Cdd:cd18002  133 VLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshAENKTGLNE 212
                        250       260
                 ....*....|....*....|....
gi 15224228  621 LQVStayRCAVVLRdlimPYLLRR 644
Cdd:cd18002  213 HQLK---RLHMILK----PFMLRR 229
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
388-644 1.20e-24

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: 103.94  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYK-PSIIICPVTLLRQWRREAQKWYPDFHVeILHD 466
Cdd:cd18055    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKgPFLVSAPLSTIINWEREFQMWAPDFYV-VTYT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  467 SAQDSghgkgqgkaSESDYDSESSVDSDHEPKSKNTKKwdslLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAVLDE 546
Cdd:cd18055   83 GDKDS---------RAIIRENEFSFDDNAVKGGKKAFK----MKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  547 GHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSvpitvggyanasplQVSTA 626
Cdd:cd18055  150 AHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------------DISKE 215
                        250
                 ....*....|....*...
gi 15224228  627 YRCAvVLRDLIMPYLLRR 644
Cdd:cd18055  216 DQIK-KLHDLLGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
385-606 1.43e-24

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 103.20  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWyPDFHVEIL 464
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTW-TEMNAIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSaqdsghgkgQGKASESDYDSESSVDSDHEPKSKNTKkwdsllnrvlnseSGLLITTYEQLRLQGEKLLNIEWGYAVL 544
Cdd:cd18058   80 HGS---------QISRQMIQQYEMYYRDEQGNPLSGIFK-------------FQVVITTFEMILADCPELKKINWSCVII 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224228  545 DEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEF 606
Cdd:cd18058  138 DEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
385-606 2.81e-24

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 102.44  E-value: 2.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWyPDFHVEIL 464
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTW-TEMNTIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSaqdsghgkgqgkasesdyDSESSVDSDHEPKSKNTK--------KWDSLlnrvlnsesgllITTYEQLRLQGEKLLN 536
Cdd:cd18060   80 HGS------------------LASRQMIQQYEMYCKDSRgrlipgayKFDAL------------ITTFEMILSDCPELRE 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  537 IEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVlpvfEAEF 606
Cdd:cd18060  130 IEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPS----ESEF 195
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
385-606 3.42e-24

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: 102.42  E-value: 3.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWyPDFHVEIL 464
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-TELNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSaqdsghgkgqgKASESDYDSESSVDSDHEPKS-KNTKKWDSLlnrvlnsesgllITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18059   80 HGS-----------QASRRTIQLYEMYFKDPQGRViKGSYKFHAI------------ITTFEMILTDCPELRNIPWRCVV 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEF 606
Cdd:cd18059  137 IDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
385-644 8.40e-24

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: 101.29  E-value: 8.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYK-PSIIICPVTLLRQWRREAQKWYPDFHVeI 463
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEMWAPDFYV-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSghgkgqgkasesdYDSESSVDSDHEPKSKNTKKWDSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18057   80 TYTGDKES-------------RSVIRENEFSFEDNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSvpitvggyanasplQV 623
Cdd:cd18057  147 VDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------------DI 212
                        250       260
                 ....*....|....*....|.
gi 15224228  624 STAYRCAvVLRDLIMPYLLRR 644
Cdd:cd18057  213 SKEDQIK-KLHDLLGPHMLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
388-624 3.79e-23

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: 99.96  E-value: 3.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  388 YQRVGVQWLWELHCQR---------AGGIIGDEMGLGKTIQVLSFLGSLHFSKM---YKPSIIICPVTLLRQWRREAQKW 455
Cdd:cd18068    4 HQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFLHTVLLCEKlenFSRVLVVCPLNTVLNWLNEFEKW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  456 YPDfhveilhdsaqdsghgkgqgkASESDYDSESSVDSDHEPKSKNTKKWDSllnrvlNSESGLLITTYEQLR-LQGEK- 533
Cdd:cd18068   84 QEG---------------------LKDEEKIEVNELATYKRPQERSYKLQRW------QEEGGVMIIGYDMYRiLAQERn 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  534 --------------LLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVL 599
Cdd:cd18068  137 vksreklkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTI 216
                        250       260
                 ....*....|....*....|....*
gi 15224228  600 PVFEAEFSVPITVGGYANASPLQVS 624
Cdd:cd18068  217 KEFRNRFVNPIQNGQCADSTLVDVR 241
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
385-644 4.52e-23

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: 99.37  E-value: 4.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYK-PSIIICPVTLLRQWRREAQKWYPDFHVeI 463
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMWAPDMYV-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSghgkgqgkasesdYDSESSVDSDHEPKSKNTKKWDSLLNRVLNSESGLLITTYEQLRLQGEKLLNIEWGYAV 543
Cdd:cd18056   80 TYVGDKDS-------------RAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  544 LDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSvpitvggyANASPLQV 623
Cdd:cd18056  147 VDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA--------DIAKEDQI 218
                        250       260
                 ....*....|....*....|.
gi 15224228  624 STayrcavvLRDLIMPYLLRR 644
Cdd:cd18056  219 KK-------LHDMLGPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
757-840 7.40e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 7.40e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228     757 DILESFLVANEYSYRRMDGLTPVKQRMALIDEFNNSEdmFVFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERA 836
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 15224228     837 WRIG 840
Cdd:smart00490   79 GRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
377-601 8.48e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.48  E-value: 8.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228     377 IPECIFRKLFDYQRVGVQWLWELHCqraGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICP-VTLLRQWRREAQKW 455
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228     456 YPDFHVEILhdsaqdsghgkgqgkasesdydsesSVDSDHEPKSKntkkwdslLNRVLNSESGLLITTYEQLR--LQGEK 533
Cdd:smart00487   78 GPSLGLKVV-------------------------GLYGGDSKREQ--------LRKLESGKTDILVTTPGRLLdlLENDK 124
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224228     534 LLNIEWGYAVLDEGHRIRNPN--SDITLVCKQL-QTVHRIIMTGAP---IQNKLTELWSLFDFVFPGKLGVLPV 601
Cdd:smart00487  125 LSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
405-623 1.48e-21

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: 95.23  E-value: 1.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  405 GGIIGDEMGLGKTIQVLSFLgslhfskMYKPSIIICPVTLLRQWRREAQKWYPDFHVEILhdsaqdSGHGKGQGKasesd 484
Cdd:cd18071   50 GGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKPGQLKVY------TYHGGERNR----- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  485 ydsessvdsdhEPKskntkkwdsllnrvLNSESGLLITTYEQLRLQ-----GEKLLNIEWGYAVLDEGHRIRNPNSDITL 559
Cdd:cd18071  112 -----------DPK--------------LLSKYDIVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTK 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224228  560 VCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEFSVPITVGGYANASPLQV 623
Cdd:cd18071  167 AVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQV 230
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
385-606 1.52e-21

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 94.69  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWyPDFHVEIL 464
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTW-TDLNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 HDSAqdsghgkgqgkasesdydSESSVDSDHEPKSKNTKkwdsllNRVLNSESGL--LITTYEQLRLQGEKLLNIEWGYA 542
Cdd:cd18061   80 HGSL------------------ISRQMIQQYEMYFRDSQ------GRIIRGAYRFqaIITTFEMILGGCPELNAIDWRCV 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLGVLPVFEAEF 606
Cdd:cd18061  136 IIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1120-1186 1.50e-19

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 83.72  E-value: 1.50e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15224228 1120 QPEVLIRKICSFV-QQKGGSADTTSIVNHFRDIVSFNDKQLFKNLLKEIATLEKDQN-RSFWVLKSEYK 1186
Cdd:cd22254    4 EAEELLADIRDFLaFQAGGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGgRGVWVLKPEFR 72
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
385-597 1.83e-18

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: 85.33  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWElHCQRAggIIGDEMGLGKTIQVlsfLGSLHFSKMYKPSIIICPVTLLRQWRREAQKWYPDFHVEIL 464
Cdd:cd18010    1 LLPFQREGVCFALR-RGGRV--LIADEMGLGKTVQA---IAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 H--DSAQDSGhgkgqgkasesdydsessvdSDHEPKskntkkwdsllnrvlnsesgLLITTYEQLRLQGEKLLNIEWGYA 542
Cdd:cd18010   75 QviVKSKDGL--------------------RDGDAK--------------------VVIVSYDLLRRLEKQLLARKFKVV 114
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQL--QTVHRIIMTGAPIQNKLTELWSLFDFVFPGKLG 597
Cdd:cd18010  115 ICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFG 171
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
385-591 7.42e-16

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 78.29  E-value: 7.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWL-WELHCQRAGGIIGDEMGLGKTIQVLSFL--------------------GSLHFSKMYKPS---IIIC 440
Cdd:cd18072    1 LLLHQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIALIlaqkntqnrkeeekekalteWESKKDSTLVPSagtLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  441 PVTLLRQWRREAQKWYPDFHVEILhdsaqdSGHGkgqgkasesdydsessvdSDHEPKSKNTKKWDsllnrvlnsesgLL 520
Cdd:cd18072   81 PASLVHQWKNEVESRVASNKLRVC------LYHG------------------PNRERIGEVLRDYD------------IV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  521 ITTY----EQLRLQGEK-----LLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAPIQNKLTELWSLFDFV 591
Cdd:cd18072  125 ITTYslvaKEIPTYKEEsrsspLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
385-601 1.62e-15

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: 77.77  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWElhcqrAGGIIGDEMGLGKTIQVLSFL------------GSLHFSKMY--------------KPSII 438
Cdd:cd18070    1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVccpdclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  439 ICPVTLLRQWRREAQKWYPDfHVEILHDSAQDSghgkgqgkasesdydseSSVDSDHEPKskntkkwdsllnRVLNSEsg 518
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPS-SLKVLTYQGVKK-----------------DGALASPAPE------------ILAEYD-- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  519 LLITTYEQLR--------------LQGEK--------LLNIEWGYAVLDEGHRIRNPNSDITLVCKQLQTVHRIIMTGAP 576
Cdd:cd18070  124 IVVTTYDVLRtelhyaeanrsnrrRRRQKryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTP 203
                        250       260
                 ....*....|....*....|....*
gi 15224228  577 IQNKLTELWSLFDFvfpgkLGVLPV 601
Cdd:cd18070  204 IQRGLDDLFGLLSF-----LGVEPF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
385-587 3.35e-12

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: 66.93  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVqwLWELHCQRAGGIIGDEMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQWRREAQKwypDFHVEIL 464
Cdd:cd18011    1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQD---KFGLPFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  465 hdsaqdsghgkgqgkasesdydsesSVDSDHEPKSKNtkkwdslLNRVLNSESGLLITTYEQLRLQGE---KLLNIEWGY 541
Cdd:cd18011   76 -------------------------ILDRETAAQLRR-------LIGNPFEEFPIVIVSLDLLKRSEErrgLLLSEEWDL 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15224228  542 AVLDEGHRIRN-----PNSDITLvCKQL--QTVHRIIMTGAPIQNKLTELWSL 587
Cdd:cd18011  124 VVVDEAHKLRNsgggkETKRYKL-GRLLakRARHVLLLTATPHNGKEEDFRAL 175
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
385-597 1.55e-11

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 65.06  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  385 LFDYQRVGVQWLWElhcQRAGGIIGDeMGLGKTIQVLSFLGSLHFSKMYKPSIIICPVTLLRQ-WRREAQKWypdfhvEI 463
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW------NH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  464 LHDSAQDSGHGKGqgkasesdydsessvdsdhepkskntkkwdSLLNRVLNSESGLLITTYEQLR-LQGEKLLNIEWGYA 542
Cdd:cd18013   71 LRNLTVSVAVGTE------------------------------RQRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMV 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15224228  543 VLDEGHRIRNPNSDITLVCKQLQ-TVHRII-MTGAPIQNKLTELWSLFDFVFPGK-LG 597
Cdd:cd18013  121 VIDELSSFKSPRSKRFKALRKVRpVIKRLIgLTGTPSPNGLMDLWAQIALLDQGErLG 178
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
728-973 2.72e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 58.20  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  728 KMKVVAEVLK--VWKQQGHRVLLFSQTQQMLDILESFLVANEYSYRRM---------DGLTPvKQRMALIDEFNNSEdmF 796
Cdd:COG1111  336 KLSKLREILKeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegdKGLTQ-KEQIEILERFRAGE--F 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  797 VFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKdvtVYRLITRGTIEEKVYHRQIYKHFLTNKILK 876
Cdd:COG1111  413 NVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR---VVVLIAKGTRDEAYYWSSRRKEKKMKSILK 489
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224228  877 NpqQRRFFKARDMKDLFI-----LKDDGDSNASTETSNIFSQLAEEINIVGVQSDKKPESDTQLALHKTAEGSSEQTDVE 951
Cdd:COG1111  490 K--LKKLLDKQEKEKLKEsaqatLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLELRELG 567
                        250       260
                 ....*....|....*....|..
gi 15224228  952 MTDKTGEAMDEETNILKSLFDA 973
Cdd:COG1111  568 EKVDDEVNLILEIDRVDVVDDG 589
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
786-848 1.18e-05

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: 1.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224228  786 IDEFNNSEDMFVFVLTTKVGGLGTNLTGANRVIIFDPDWNPSNDMQARERAWRIGQKKDVTVY 848
Cdd:cd18785   13 IEHAEEIASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
 
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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