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Conserved domains on  [gi|1079280793|ref|NP_001333369|]
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DNA excision repair protein ERCC-6 isoform 2 [Homo sapiens]

Protein Classification

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, ...
391-987 1.89e-143

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 455.45  E-value: 1.89e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553    126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553    206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553    285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553    350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553    430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553    494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553    559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1079280793  945 RERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 987
Cdd:COG0553    639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
83-159 2.02e-31

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


:

Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 118.08  E-value: 2.02e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079280793   83 VEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSP 159
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1420-1492 3.09e-31

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: 117.23  E-value: 3.09e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079280793 1420 PTTEHDDLLVEMRNFIAFQAhtDGQASTREILQEFESKLSASQSCVFRELLRNLCTFHRTSGGEGIWKLKPEY 1492
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEF 71
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
391-987 1.89e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 455.45  E-value: 1.89e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553    126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553    206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553    285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553    350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553    430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553    494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553    559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1079280793  945 RERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 987
Cdd:COG0553    639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
507-694 3.62e-120

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: 373.58  E-value: 3.62e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILHETGSYTHKKEK---------LIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAA 657
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1079280793  658 VTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFP 694
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
510-812 2.46e-116

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: 367.01  E-value: 2.46e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFHTW 588
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  589 W--PPFRVAILHETGSYTHKkEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 746
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079280793  747 KSDVkmSLSLPDKNEQVLFCRLTDEQHKVYQNFVDSKEVYRILNGE------MQIFSGLIALRKICNHPDLF 812
Cdd:pfam00176  220 KKDV--EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
462-975 1.34e-89

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 315.59  E-value: 1.34e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  462 KQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQ 541
Cdd:PLN03142   125 KGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQ 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  542 IIAFLAGLsyskirtrgsnYRFEGL-GPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETG-SYTHKKEKLIrdVAHCHG 619
Cdd:PLN03142   205 TISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPeERAHQREELL--VAGKFD 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  620 ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGT 699
Cdd:PLN03142   272 VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSS 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  700 LPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKSDVKMSLslPDKNEQVLFCRLTDEQHKVY--- 776
Cdd:PLN03142   352 AETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQYYkal 417
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  777 -QNFVDS----KEVYRILNGEMQifsgliaLRKICNHPDLFSG---GPKNLKGlpdDELEEDqfgywkrSGKMIVVESLL 848
Cdd:PLN03142   418 lQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG---EHLVEN-------SGKMVLLDKLL 480
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  849 KIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYN-EDTSIFVFLLTTRVGGLGVNLTGAN 927
Cdd:PLN03142   481 PKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAGGLGINLATAD 560
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1079280793  928 RVVIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHR 975
Cdd:PLN03142   561 IVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
83-159 2.02e-31

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 118.08  E-value: 2.02e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079280793   83 VEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSP 159
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1420-1492 3.09e-31

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: 117.23  E-value: 3.09e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079280793 1420 PTTEHDDLLVEMRNFIAFQAhtDGQASTREILQEFESKLSASQSCVFRELLRNLCTFHRTSGGEGIWKLKPEY 1492
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEF 71
DEXDc smart00487
DEAD-like helicases superfamily;
499-707 2.10e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 2.10e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   499 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTV- 577
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPTREl 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   578 MHQWVKEFHTWWPPF--RVAILHETGSYTHKKEKLIRDVAHchgILITSYSYIR--LMQDDISRYDWHYVILDEGHKIRN 653
Cdd:smart00487   67 AEQWAEELKKLGPSLglKVVGLYGGDSKREQLRKLESGKTD---ILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLD 143
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   654 PNAAVTLACKQFRTP---HRIILSGSP---MQNNLRELWSLFDFIFPGKLGTLPVfmEQF 707
Cdd:smart00487  144 GGFGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI--EQF 201
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
391-987 1.89e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 455.45  E-value: 1.89e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553    126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553    206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553    285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553    350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553    430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553    494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553    559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1079280793  945 RERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 987
Cdd:COG0553    639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
507-694 3.62e-120

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: 373.58  E-value: 3.62e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILHETGSYTHKKEK---------LIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAA 657
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1079280793  658 VTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFP 694
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
510-812 2.46e-116

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: 367.01  E-value: 2.46e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFHTW 588
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  589 W--PPFRVAILHETGSYTHKkEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 746
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079280793  747 KSDVkmSLSLPDKNEQVLFCRLTDEQHKVYQNFVDSKEVYRILNGE------MQIFSGLIALRKICNHPDLF 812
Cdd:pfam00176  220 KKDV--EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
462-975 1.34e-89

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 315.59  E-value: 1.34e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  462 KQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQ 541
Cdd:PLN03142   125 KGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQ 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  542 IIAFLAGLsyskirtrgsnYRFEGL-GPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETG-SYTHKKEKLIrdVAHCHG 619
Cdd:PLN03142   205 TISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPeERAHQREELL--VAGKFD 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  620 ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGT 699
Cdd:PLN03142   272 VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSS 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  700 LPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKSDVKMSLslPDKNEQVLFCRLTDEQHKVY--- 776
Cdd:PLN03142   352 AETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQYYkal 417
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  777 -QNFVDS----KEVYRILNGEMQifsgliaLRKICNHPDLFSG---GPKNLKGlpdDELEEDqfgywkrSGKMIVVESLL 848
Cdd:PLN03142   418 lQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG---EHLVEN-------SGKMVLLDKLL 480
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  849 KIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYN-EDTSIFVFLLTTRVGGLGVNLTGAN 927
Cdd:PLN03142   481 PKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAGGLGINLATAD 560
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1079280793  928 RVVIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHR 975
Cdd:PLN03142   561 IVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
507-694 8.95e-73

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: 240.55  E-value: 8.95e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfegLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE----------RGPVLVVCPLSVLENWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILHetGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17919     71 KWTPDLRVVVYH--GSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFP 694
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
507-745 4.58e-71

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: 237.65  E-value: 4.58e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRgsnyrfeglgpTVIVCPTTVMHQWVKEFH 586
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS-----------VLVVMPTSLIPHWVKEFA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILHetGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYD-----WHYVILDEGHKIRNPNAAVTLA 661
Cdd:cd18001     70 KWTPGLRVKVFH--GTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  662 CKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGK-LGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINP 740
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                   ....*
gi 1079280793  741 YLLRR 745
Cdd:cd18001    228 YFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
510-747 6.97e-66

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: 222.06  E-value: 6.97e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd18012      8 YQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLL-----------SRKEEGRKGPSLVVAPTSLIYNWEEEAAKFA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  590 PPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPH 669
Cdd:cd18012     77 PELKVLVIHGTK----RKREKLRALED-YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADH 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079280793  670 RIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPvqvktaykcacVLRDTINPYLLRRMK 747
Cdd:cd18012    152 RLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALE-----------ELKKLISPFILRRLK 218
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
507-745 3.92e-62

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: 212.21  E-value: 3.92e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsySKIRTRGSNYRFEGLgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILA----SDHHKRANSFNSENL-PSLVVCPPTLVGHWVAEIK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILHETGSYThkKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17999     76 KYFPNAFLKPLAYVGPPQ--ERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRR 745
Cdd:cd17999    154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
838-963 1.00e-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: 203.86  E-value: 1.00e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  838 SGKMIVVESLLKIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVG 917
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1079280793  918 GLGVNLTGANRVVIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLL 963
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
510-745 9.74e-59

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: 202.61  E-value: 9.74e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGSNYRF----------EGLGPTV-IVCPTTVM 578
Cdd:cd18005      4 YQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAV-LGKTGTRRDRENNrprfkkkppaSSAKKPVlIVAPLSVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  579 HQWVKEFHTW-WppFRVAILHETGsythKKEKLIRDV-AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd18005     83 YNWKDELDTWgH--FEVGVYHGSR----KDDELEGRLkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRD 736
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                   ....*....
gi 1079280793  737 TINPYLLRR 745
Cdd:cd18005    237 KLSKFFLRR 245
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
507-745 1.74e-48

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: 172.54  E-value: 1.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK----------GNWGPHLIVVPTSVMLNWEMEFK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRvaILHETGSytHKKEKLIR------DVAHchgILITSYSYIrlMQDDIS--RYDWHYVILDEGHKIRNPNAAV 658
Cdd:cd18003     71 RWCPGFK--ILTYYGS--AKERKLKRqgwmkpNSFH---VCITSYQLV--VQDHQVfkRKKWKYLILDEAHNIKNFKSQR 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  659 TLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITmggysnaSPVQVKTAYKCACV--LRD 736
Cdd:cd18003    142 WQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT-------AMSEGSQEENEELVrrLHK 214

                   ....*....
gi 1079280793  737 TINPYLLRR 745
Cdd:cd18003    215 VLRPFLLRR 223
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
511-729 7.52e-48

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: 171.32  E-value: 7.52e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  511 QQTGVRWLWE-----LHCQQAGG--ILGDEMGLGKTIQIIAFL-AGLSYSKIRTRgsnyrfeglgpTVIVCPTTVMHQWV 582
Cdd:cd18007      5 QVEGVRFLWSnlvgtDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSR-----------PLVLCPASTLYNWE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  583 KEFHTWWPPFRVAILHETGSYTHKKEKL-IRDVAHCH---GILITSY-SYIRLMQDDISRYDWH-------------YVI 644
Cdd:cd18007     74 DEFKKWLPPDLRPLLVLVSLSASKRADArLRKINKWHkegGVLLIGYeLFRNLASNATTDPRLKqefiaalldpgpdLLV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  645 LDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQV 724
Cdd:cd18007    154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDV 233

                   ....*
gi 1079280793  725 KTAYK 729
Cdd:cd18007    234 RLMLK 238
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
510-747 7.45e-47

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: 168.33  E-value: 7.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSnyrfegLGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd18009      7 YQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL-----RERGV------WGPFLVIAPLSTLPNWVNEFARFT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  590 PPFRVAILHETGSYTHKKEKLIR---DVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd18009     76 PSVPVLLYHGTKEERERLRKKIMkreGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRM 746
Cdd:cd18009    156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRL 235

                   .
gi 1079280793  747 K 747
Cdd:cd18009    236 K 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
506-747 2.01e-44

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: 161.38  E-value: 2.01e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGSNyrfeglGPTVIVCPTTVMHQWVKEF 585
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYL----MEKKKNN------GPYLVIVPLSTLSNWVSEF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  586 HTWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIrlMQDD--ISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd17996     73 EKWAP--SVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYI--IKDKplLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  664 Q-FRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPV----QVKTAYKCACVLRdti 738
Cdd:cd17996    149 TyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELneeeTLLIIRRLHKVLR--- 225

                   ....*....
gi 1079280793  739 nPYLLRRMK 747
Cdd:cd17996    226 -PFLLRRLK 233
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
506-747 4.91e-44

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: 159.79  E-value: 4.91e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLS-YSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKE 584
Cdd:cd17997      3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKhYKNIN-----------GPHLIIVPKSTLDNWMRE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  585 FHTWWPPFRVAILHetgsyTHKKE--KLIRDVAhCHG---ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVT 659
Cdd:cd17997     72 FKRWCPSLRVVVLI-----GDKEEraDIIRDVL-LPGkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  660 LACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNAspvqVKTAYKcacVLRdtin 739
Cdd:cd17997    146 QIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEV----VQRLHK---VLR---- 214

                   ....*...
gi 1079280793  740 PYLLRRMK 747
Cdd:cd17997    215 PFLLRRIK 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
511-745 2.40e-43

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: 158.22  E-value: 2.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  511 QQTGVRWLWE-LHCQQAGG----ILGDEMGLGKTIQIIAflagLSYSKIRTRgsnyrfEGLGPT----VIVCPTTVMHQW 581
Cdd:cd18004      5 QREGVQFLYDcLTGRRGYGgggaILADEMGLGKTLQAIA----LVWTLLKQG------PYGKPTakkaLIVCPSSLVGNW 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  582 VKEFHTWWPPFRVAILHETGSytHKKEKLIRD---VAHCHGILITSYSYIRLMQDDI---SRYDwhYVILDEGHKIRNPN 655
Cdd:cd18004     75 KAEFDKWLGLRRIKVVTADGN--AKDVKASLDffsSASTYPVLIISYETLRRHAEKLskkISID--LLICDEGHRLKNSE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  656 AAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLR 735
Cdd:cd18004    151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELS 230
                          250
                   ....*....|
gi 1079280793  736 DTINPYLLRR 745
Cdd:cd18004    231 ELTSRFILRR 240
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
510-745 1.54e-42

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: 155.48  E-value: 1.54e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGsNYRfeglGPTVIVCPTTVMHQWVKEFHTWw 589
Cdd:cd17995      4 YQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFL-----EHLYQVE-GIR----GPFLVIAPLSTIPNWQREFETW- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  590 PPFRVAILHETGS----------YTHKKEKL-IRDVAHCHgILITSYSYIrlMQD--DISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd17995     73 TDMNVVVYHGSGEsrqiiqqyemYFKDAQGRkKKGVYKFD-VLITTYEMV--IADaeELRKIPWRVVVVDEAHRLKNRNS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacVLRD 736
Cdd:cd17995    150 KLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTAEQVE---------KLQA 214

                   ....*....
gi 1079280793  737 TINPYLLRR 745
Cdd:cd17995    215 LLKPYMLRR 223
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
507-745 1.09e-41

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: 153.60  E-value: 1.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLweLHCqqaGGILGDEMGLGKTIQIIAFLAG-------LSYSKIRTRGSNYRFEGLGPTVIVCPTTVMH 579
Cdd:cd18008      1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALALILAtrpqdpkIPEELEENSSDPKKLYLSKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  580 QWVKEF--HTWWPPFRVAILHetGSythKKEKLIRDVAHCHgILITSYSyiRLMQDD------------------ISRYD 639
Cdd:cd18008     76 QWKDEIekHTKPGSLKVYVYH--GS---KRIKSIEELSDYD-IVITTYG--TLASEFpknkkgggrdskekeaspLHRIR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  640 WHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNA 719
Cdd:cd18008    148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKAL 227
                          250       260
                   ....*....|....*....|....*.
gi 1079280793  720 SPVQVktaykcacvlrdTINPYLLRR 745
Cdd:cd18008    228 ERLQA------------LLKPILLRR 241
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
506-745 7.98e-39

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: 144.42  E-value: 7.98e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQ----------QQYGPFLVVVPLSTMPAWQREF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  586 HTWWPPFRVAIL------------HETGSYTHKKEKLirdvahchGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRN 653
Cdd:cd17993     71 AKWAPDMNVIVYlgdiksrdtireYEFYFSQTKKLKF--------NVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKN 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  654 PNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQfsvpitmggYSNASPVQVKTaykcacv 733
Cdd:cd17993    143 DESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE---------HDEEQEKGIAD------- 206
                          250
                   ....*....|..
gi 1079280793  734 LRDTINPYLLRR 745
Cdd:cd17993    207 LHKELEPFILRR 218
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
510-725 1.79e-38

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: 143.80  E-value: 1.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQA---------GGILGDEMGLGKTIQIIAFLAGLsyskirtrgsnYRFEGLGPTVIVCPTTVMHQ 580
Cdd:cd18069      4 HQIGGIRFLYDNIIESLerykgssgfGCILAHSMGLGKTLQVISFLDVL-----------LRHTGAKTVLAIVPVNTLQN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  581 WVKEFHTWWPP-----------FRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQD-DIsrydwhyVILDEG 648
Cdd:cd18069     73 WLSEFNKWLPPpealpnvrprpFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGpDV-------VICDEG 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079280793  649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVK 725
Cdd:cd18069    146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
510-745 2.93e-38

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: 142.96  E-value: 2.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWE-LHCQQaGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRFEGLGPTVIVCPTTVMHQWVKEFHTW 588
Cdd:cd18006      4 YQLEGVNWLLQcRAEQH-GCILGDEMGLGKTCQTISLLWYLAG----------RLKLLGPFLVLCPLSVLDNWKEELNRF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  589 WPPFRVAilhetgSYTHKKEKL------IRDVAHCHgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd18006     73 APDLSVI------TYMGDKEKRldlqqdIKSTNRFH-VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  663 KQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLG--TLPVFMEQFSvpitmggysnaspvQVKTAYKCACVLRDTINP 740
Cdd:cd18006    146 SEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYS--------------ETDDESETVEELHLLLQP 211

                   ....*
gi 1079280793  741 YLLRR 745
Cdd:cd18006    212 FLLRR 216
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
510-694 7.04e-38

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: 140.60  E-value: 7.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd17998      4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIP-----------GPHLVVVPSSTLDNWLREFKRWC 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  590 PPFRVAILHetGSYTHKKEklIRDVAHC----HGILITSYSYIRLMQDDIS---RYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd17998     73 PSLKVEPYY--GSQEERKH--LRYDILKgledFDVIVTTYNLATSNPDDRSffkRLKLNYVVYDEGHMLKNMTSERYRHL 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1079280793  663 KQFRTPHRIILSGSPMQNNLRELWSLFDFIFP 694
Cdd:cd17998    149 MTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
506-754 1.18e-36

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: 139.42  E-value: 1.18e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnYRfEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd18064     15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKH---------YR-NIPGPHMVLVPKSTLHNWMAEF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  586 HTWWPPFRVAILheTGSyTHKKEKLIRDV--AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd18064     85 KRWVPTLRAVCL--IGD-KDQRAAFVRDVllPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  664 QFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGgysnaspvQVKTAYKCACVLRdtinPYLL 743
Cdd:cd18064    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG--------DQKLVERLHMVLR----PFLL 229
                          250
                   ....*....|.
gi 1079280793  744 RRMKSDVKMSL 754
Cdd:cd18064    230 RRIKADVEKSL 240
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
510-745 2.09e-34

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: 132.28  E-value: 2.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWEL-----HCQQAGGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYrfeGLGP----TVIVCPTTVMHQ 580
Cdd:cd18066      4 HQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTL------LRQGPY---GGKPvikrALIVTPGSLVKN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  581 WVKEFHTWWPPFRVAILheTGSYTHKKEKLIRdvAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTL 660
Cdd:cd18066     75 WKKEFQKWLGSERIKVF--TVDQDHKVEEFIA--SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  661 ACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINP 740
Cdd:cd18066    151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230

                   ....*
gi 1079280793  741 YLLRR 745
Cdd:cd18066    231 FILRR 235
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
506-745 1.95e-33

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: 129.74  E-value: 1.95e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRFEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFH----------QHQLYGPFLLVVPLSTLTSWQREF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  586 HTWWPPFRVAI-LHETGS--------YTHKKEKLIRdvahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd18054     90 EIWAPEINVVVyIGDLMSrntireyeWIHSQTKRLK-----FNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmGGYSNaspvqvktAYKCacvLRD 736
Cdd:cd18054    165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-----KGREN--------GYQS---LHK 228

                   ....*....
gi 1079280793  737 TINPYLLRR 745
Cdd:cd18054    229 VLEPFLLRR 237
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
507-747 6.10e-33

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: 128.62  E-value: 6.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyRFEGlgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18062     24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK--------RING--PFLIIVPLSTLSNWVYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK-QF 665
Cdd:cd18062     94 KWAP--SVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  666 RTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYLL 743
Cdd:cd18062    172 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----EKVDLNEEETILIIrrLHKVLRPFLL 247

                   ....
gi 1079280793  744 RRMK 747
Cdd:cd18062    248 RRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
507-747 7.76e-33

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: 127.83  E-value: 7.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnYRfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKH---------YR-NIPGPHMVLVPKSTLHNWMNEFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAILheTGSyTHKKEKLIRDVAHCH--GILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQ 664
Cdd:cd18065     86 RWVPSLRAVCL--IGD-KDARAAFIRDVMMPGewDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  665 FRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktaYKCACVLRDTINPYLLR 744
Cdd:cd18065    163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD------------QKLVERLHAVLKPFLLR 230

                   ...
gi 1079280793  745 RMK 747
Cdd:cd18065    231 RIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
507-747 9.64e-33

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: 128.26  E-value: 9.64e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyRFEGlgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK--------RLNG--PYLIIVPLSTLSNWTYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK-QF 665
Cdd:cd18063     94 KWAP--SVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  666 RTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYLL 743
Cdd:cd18063    172 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----ERVDLNEEETILIIrrLHKVLRPFLL 247

                   ....
gi 1079280793  744 RRMK 747
Cdd:cd18063    248 RRLK 251
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
507-745 6.84e-32

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: 124.92  E-value: 6.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEH----------NIWGPFLVIAPASTLHNWQQEIS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVaiLHETGSYTHKK--------EKLIRDVAHCHgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAV 658
Cdd:cd18002     71 RFVPQFKV--LPYWGNPKDRKvlrkfwdrKNLYTRDAPFH-VVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  659 TLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPIT--MGGYSNASPVQVKTaykcacvLRD 736
Cdd:cd18002    148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshAENKTGLNEHQLKR-------LHM 220

                   ....*....
gi 1079280793  737 TINPYLLRR 745
Cdd:cd18002    221 ILKPFMLRR 229
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
83-159 2.02e-31

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 118.08  E-value: 2.02e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079280793   83 VEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSP 159
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1420-1492 3.09e-31

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: 117.23  E-value: 3.09e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079280793 1420 PTTEHDDLLVEMRNFIAFQAhtDGQASTREILQEFESKLSASQSCVFRELLRNLCTFHRTSGGEGIWKLKPEY 1492
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEF 71
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
507-745 7.53e-30

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: 117.93  E-value: 7.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAilhetgSYTHKKeklirdvahchgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17994     71 MWAPDFYVV------TYVGDH------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1079280793  667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPitmggysnASPVQVKTaykcacvLRDTINPYLLRR 745
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADI--------SKEDQIKK-------LHDLLGPHMLRR 196
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
510-725 2.88e-29

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: 118.07  E-value: 2.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWELHCQQ---------AGGILGDEMGLGKTIQIIAFLaglsyskiRTRGSNYRFEGLGPTVIVCPTTVMHQ 580
Cdd:cd18068      4 HQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFL--------HTVLLCEKLENFSRVLVVCPLNTVLN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  581 WVKEFHTWWPPFRVAILHETGSYTHKKEKLIRDVAHCH-----GILITSYSYIRLM------------QDDISRY----- 638
Cdd:cd18068     76 WLNEFEKWQEGLKDEEKIEVNELATYKRPQERSYKLQRwqeegGVMIIGYDMYRILaqernvksreklKEIFNKAlvdpg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  639 -DwhYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYS 717
Cdd:cd18068    156 pD--FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCA 233

                   ....*...
gi 1079280793  718 NASPVQVK 725
Cdd:cd18068    234 DSTLVDVR 241
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
510-745 4.66e-29

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: 117.19  E-value: 4.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  510 YQQTGVRWLWElhCQQA-------GGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYRFEGLGPTVIVCPTTVMHQWV 582
Cdd:cd18067      4 HQREGVKFLYR--CVTGrrirgshGCIMADEMGLGKTLQCITLMWTL------LRQSPQCKPEIDKAIVVSPSSLVKNWA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  583 KEFHTWWPPFRVAILHETGSythKKEKLIRDV--AHCHG------ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18067     76 NELGKWLGGRLQPLAIDGGS---KKEIDRKLVqwASQQGrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  655 NAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVL 734
Cdd:cd18067    153 DNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQEL 232
                          250
                   ....*....|.
gi 1079280793  735 RDTINPYLLRR 745
Cdd:cd18067    233 ISIVNRCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
499-707 2.10e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 2.10e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   499 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTV- 577
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPTREl 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   578 MHQWVKEFHTWWPPF--RVAILHETGSYTHKKEKLIRDVAHchgILITSYSYIR--LMQDDISRYDWHYVILDEGHKIRN 653
Cdd:smart00487   67 AEQWAEELKKLGPSLglKVVGLYGGDSKREQLRKLESGKTD---ILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLD 143
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   654 PNAAVTLACKQFRTP---HRIILSGSP---MQNNLRELWSLFDFIFPGKLGTLPVfmEQF 707
Cdd:smart00487  144 GGFGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI--EQF 201
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
507-735 2.11e-28

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 114.22  E-value: 2.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRW-LwelhcqQAGG--ILGDEMGLGKTIQIIAFLAglsyskirtrgsNYRFEGlgPTVIVCPTTVMHQWVK 583
Cdd:cd18010      1 LLPFQREGVCFaL------RRGGrvLIADEMGLGKTVQAIAIAA------------YYREEW--PLLIVCPSSLRLTWAD 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  584 EFHTWwppFRVAILHETGSYTHKKEKLIRDVahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd18010     61 EIERW---LPSLPPDDIQVIVKSKDGLRDGD---AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAAL 134
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079280793  664 QF--RTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGY----SNASPVQVKTAYKCACVLR 735
Cdd:cd18010    135 PLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGwdysGSSNLEELHLLLLATIMIR 212
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
506-706 2.62e-28

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: 114.76  E-value: 2.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsyskirtrgsNYRF---EGLGPTVIVCPTTVMHQWV 582
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL-------------NYLFhehQLYGPFLLVVPLSTLTSWQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  583 KEFHTWWPPFRVAI---------LHETGSYTHKKEKLIRdvahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRN 653
Cdd:cd18053     87 REIQTWAPQMNAVVylgdinsrnMIRTHEWMHPQTKRLK-----FNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1079280793  654 PNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQ 706
Cdd:cd18053    162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEE 214
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
507-745 7.01e-28

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: 113.57  E-value: 7.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHTKG---------PFLVSAPLSTIINWEREFQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRV----------AILHETG-SYT-------HKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18055     71 MWAPDFYVvtytgdkdsrAIIRENEfSFDdnavkggKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18055    151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1079280793  729 kcacvLRDTINPYLLRR 745
Cdd:cd18055    221 -----LHDLLGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
507-745 9.07e-27

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: 110.13  E-value: 9.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIR-----------GPFLIIAPLSTITNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWwPPFRVAILHETG---SYTHKKEKLIRD--------VAHCHGIlITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPN 655
Cdd:cd18058     70 TW-TEMNAIVYHGSQisrQMIQQYEMYYRDeqgnplsgIFKFQVV-ITTFEMILADCPELKKINWSCVIIDEAHRLKNRN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  656 AAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTaykcacvLR 735
Cdd:cd18058    148 CKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG--------DLKTEEQVKK-------LQ 212
                          250
                   ....*....|
gi 1079280793  736 DTINPYLLRR 745
Cdd:cd18058    213 SILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
507-745 1.06e-26

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: 110.15  E-value: 1.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSL-YKEGHSKG---------PYLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRVAIL---HETGSYTHKKEKLIRDVAHCHG---------------ILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18057     71 MWAPDFYVVTYtgdKESRSVIRENEFSFEDNAIRSGkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLVVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18057    151 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1079280793  729 kcacvLRDTINPYLLRR 745
Cdd:cd18057    221 -----LHDLLGPHMLRR 232
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
839-952 7.20e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 103.44  E-value: 7.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  839 GKMIVVESLLKiwHKQGQRVLLFSQSRQMLDIlEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTsiFVFLLTTRVGG 918
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1079280793  919 LGVNLTGANRVVIYDPDWNPSTDTQARERAWRIG 952
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
507-745 1.76e-25

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: 106.69  E-value: 1.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWWPPFRV----------AILHETG-SYT-------HKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18056     71 MWAPDMYVvtyvgdkdsrAIIRENEfSFEdnairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18056    151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA--------DIAKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1079280793  729 kcacvLRDTINPYLLRR 745
Cdd:cd18056    221 -----LHDMLGPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
507-707 2.45e-25

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: 105.88  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIH-----------GPFLVIAPLSTIPNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWwPPFRVAILHETGS-----------YTHKKEKLIRDVAHCHGIlITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPN 655
Cdd:cd18059     70 TW-TELNVVVYHGSQAsrrtiqlyemyFKDPQGRVIKGSYKFHAI-ITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1079280793  656 AAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQF 707
Cdd:cd18059    148 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
507-692 3.72e-25

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: 106.03  E-value: 3.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWL-WELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRG-------------SNYRFEGLGpTVIV 572
Cdd:cd18072      1 LLLHQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEekekalteweskkDSTLVPSAG-TLVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  573 CPTTVMHQWVKEF--HTWWPPFRVAILHetGSYTHKKEKLIRDvahcHGILITSYSyirLMQDDISRYD----------- 639
Cdd:cd18072     80 CPASLVHQWKNEVesRVASNKLRVCLYH--GPNRERIGEVLRD----YDIVITTYS---LVAKEIPTYKeesrssplfri 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1079280793  640 -WHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFI 692
Cdd:cd18072    151 aWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
527-724 5.00e-25

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: 105.63  E-value: 5.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  527 GGILGDEMGLGKTIQIIAFLAGlsyskirtrgsnyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAIlhetgsYTHK 606
Cdd:cd18071     50 GGILADDMGLGKTLTTISLILA------------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKV------YTYH 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  607 KEKLIRDVAHCHG--ILITSYSYirLMQDD-------ISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSP 677
Cdd:cd18071    106 GGERNRDPKLLSKydIVLTTYNT--LASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTP 183
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1079280793  678 MQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQV 724
Cdd:cd18071    184 IQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQV 230
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
507-707 8.05e-25

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: 104.32  E-value: 8.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIR-----------GPFLIIAPLSTIANWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWwPPFRVAILHetGSYTHKK-----EKLIRDV-------AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18061     70 TW-TDLNVVVYH--GSLISRQmiqqyEMYFRDSqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNK 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1079280793  655 NAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQF 707
Cdd:cd18061    147 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
507-745 7.84e-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: 101.67  E-value: 7.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIH-----------GPFLVIAPLSTITNWEREFN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  587 TWwPPFRVAILHetGSYTHKK-----EKLIRDV-------AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18060     70 TW-TEMNTIVYH--GSLASRQmiqqyEMYCKDSrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  655 NAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacVL 734
Cdd:cd18060    147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF------GDLKTEEQVQ---------KL 211
                          250
                   ....*....|.
gi 1079280793  735 RDTINPYLLRR 745
Cdd:cd18060    212 QAILKPMMLRR 222
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
507-692 1.16e-21

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: 96.26  E-value: 1.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWElhcqqAGGILGDEMGLGKTIQIIAFLA-------GLSYSKIRTRGSNYRFEGL--------GPTVI 571
Cdd:cd18070      1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILlhprpdnDLDAADDDSDEMVCCPDCLvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  572 VCPTTVMHQWVKEFHTWWPPfRVAILHETGSYTHKKEKL--IRDVAHcHGILITSYSYIR--LMQDDI----------SR 637
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPS-SLKVLTYQGVKKDGALASpaPEILAE-YDIVVTTYDVLRteLHYAEAnrsnrrrrrqKR 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079280793  638 Y----------DWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFI 692
Cdd:cd18070    154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFL 218
HELICc smart00490
helicase superfamily c-terminal domain;
869-952 1.98e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 1.98e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793   869 DILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSifVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQARERA 948
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1079280793   949 WRIG 952
Cdd:smart00490   79 GRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
507-695 1.01e-18

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: 86.19  E-value: 1.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWELhcQQAGGILGDEMGLGKTIQiiaflAGL--SYSKIRTRGsnyrfeglGPTVIVCPTTVMHQWVKE 584
Cdd:cd18011      1 PLPHQIDAVLRALRK--PPVRLLLADEVGLGKTIE-----AGLiiKELLLRGDA--------KRVLILCPASLVEQWQDE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  585 -FHTWWPPFRVAilheTGSYTHKKEKLIRDVAHCHGILITSYSYIRLM---QDDISRYDWHYVILDEGHKIRN-PNAAVT 659
Cdd:cd18011     66 lQDKFGLPFLIL----DRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNsGGGKET 141
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1079280793  660 L---ACKQF--RTPHRIILSGSPMQNNLRELWSLFDFIFPG 695
Cdd:cd18011    142 KrykLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPG 182
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
452-677 1.41e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.19  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  452 YRDDGDEDYYKQRLRRWNKLRLQDKEKRLKLEDDSEESDAeFDEGFKVPGFLFKkLFKYQQTGVRWLWELHCQQAG-GIL 530
Cdd:COG1061     28 LSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEA-LEAGDEASGTSFE-LRPYQQEALEALLAALERGGGrGLV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  531 gdEM--GLGKTIqIIAFLAglsyskirtrgsnYRFEGLGPTVIVCPTTV-MHQWVKEFHTWwppfrvaiLHETGSYTHKK 607
Cdd:COG1061    106 --VAptGTGKTV-LALALA-------------AELLRGKRVLVLVPRRElLEQWAEELRRF--------LGDPLAGGGKK 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079280793  608 EKlirdvahCHGILITSYS--YIRLMQDDISRyDWHYVILDEGHKIRNPNAAVTLacKQFRTPHRIILSGSP 677
Cdd:COG1061    162 DS-------DAPITVATYQslARRAHLDELGD-RFGLVIIDEAHHAGAPSYRRIL--EAFPAAYRLGLTATP 223
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
507-717 2.10e-07

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: 53.51  E-value: 2.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  507 LFKYQQTGVRWLWElhcQQAGGILGDeMGLGKTIQIIAFLAGLsyskirtrgsnyRFEGL-GPTVIVCPTTVM-HQWVKE 584
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDL------------QLDDFtRRVLVIAPLRVArSTWPDE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  585 FHTWWPPF--RVAILHETGSythKKEKLIRDVAHCHGILITSYSYIRLMQDDisRYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd18013     65 VEKWNHLRnlTVSVAVGTER---QRSKAANTPADLYVINRENLKWLVNKSGD--PWPFDMVVIDELSSFKSPRSKRFKAL 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1079280793  663 KQFR-TPHRII-LSGSPMQNNLRELWSLFDFIFPGK-LG-TLPVFMEQFSVPITMGGYS 717
Cdd:cd18013    140 RKVRpVIKRLIgLTGTPSPNGLMDLWAQIALLDQGErLGrSITAYRERWFDPDKRNGQQ 198
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
905-955 3.62e-07

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: 48.85  E-value: 3.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1079280793  905 TSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQARERAWRIGQKK 955
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
527-674 9.01e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 50.09  E-value: 9.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079280793  527 GGILGDEMGLGKTIqiIAFLAGLSYskIRTRGsnyrfeglGPTVIVCPT-TVMHQWVKEFHTWW-PPFRVAILHetGSYT 604
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLAALLL--LLKKG--------KKVLVLVPTkALALQTAERLRELFgPGIRVAVLV--GGSS 68
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079280793  605 HK-KEKLIRDVAHchgILITSYSYIR--LMQDD-ISRYDWHYVILDEGHKI----RNPNAAVTLACKQFRTPHRIILS 674
Cdd:cd00046     69 AEeREKNKLGDAD---IIIATPDMLLnlLLREDrLFLKDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILL 143
 
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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