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Conserved domains on  [gi|4557565|ref|NP_000115|]
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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 4557565   391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553  126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553  206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553  285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553  350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553  430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553  494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|...
gi 4557565   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 4557565    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 4557565  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 4557565   391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553  126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553  206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553  285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553  350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553  430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553  494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILHETGSYTHKKEK---------LIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAA 657
Cdd:cd18000   71 RWWPPFRVVVLHSSGSGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4557565   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 4557565     510 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFHTW 588
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565     589 W--PPFRVAILHETGSYTHKkEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565     667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 746
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557565     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 4557565    462 KQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQ 541
Cdd:PLN03142  125 KGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQ 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    542 IIAFLAGLsyskirtrgsnYRFEGL-GPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETG-SYTHKKEKLIrdVAHCHG 619
Cdd:PLN03142  205 TISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPeERAHQREELL--VAGKFD 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    620 ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGT 699
Cdd:PLN03142  272 VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSS 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    700 LPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKSDVKMSLslPDKNEQVLFCRLTDEQHKVY--- 776
Cdd:PLN03142  352 AETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQYYkal 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    777 -QNFVDS----KEVYRILNGEMQifsgliaLRKICNHPDLFSG---GPKNLKGlpdDELEEDqfgywkrSGKMIVVESLL 848
Cdd:PLN03142  418 lQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG---EHLVEN-------SGKMVLLDKLL 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    849 KIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYN-EDTSIFVFLLTTRVGGLGVNLTGAN 927
Cdd:PLN03142  481 PKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAGGLGINLATAD 560
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 4557565    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 4557565    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 4557565  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 4557565      499 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTV- 577
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPTREl 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565      578 MHQWVKEFHTWWPPF--RVAILHETGSYTHKKEKLIRDVAHchgILITSYSYIR--LMQDDISRYDWHYVILDEGHKIRN 653
Cdd:smart00487   67 AEQWAEELKKLGPSLglKVVGLYGGDSKREQLRKLESGKTD---ILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLD 143
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565      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 4557565   391 AEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLRRWNK 470
Cdd:COG0553  126 LLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   471 LRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLs 550
Cdd:COG0553  206 ELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL- 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   551 yskiRTRGSNyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRL 630
Cdd:COG0553  285 ----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR----ERAKGANPFED-ADLVITSYGLLRR 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   631 MQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVP 710
Cdd:COG0553  350 DIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   711 ITMGGYSNASpvqvktaykcacVLRDTINPYLLRRMKSDVKmsLSLPDKNEQVLFCRLTDEQHKVYQNFVDskEVYRILN 790
Cdd:COG0553  430 IEKGDEEALE------------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELE 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   791 GE------MQIFSGLIALRKICNHPDLFSGGPKNLKGlpddeleedqfgywkRSGKMIVVESLLKIWHKQGQRVLLFSQS 864
Cdd:COG0553  494 GAegirrrGLILAALTRLRQICSHPALLLEEGAELSG---------------RSAKLEALLELLEELLAEGEKVLVFSQF 558
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   865 RQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQA 944
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILHETGSYTHKKEK---------LIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAA 657
Cdd:cd18000   71 RWWPPFRVVVLHSSGSGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4557565   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 4557565     510 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFHTW 588
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565     589 W--PPFRVAILHETGSYTHKkEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565     667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 746
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557565     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 4557565    462 KQRLRRWNKLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQ 541
Cdd:PLN03142  125 KGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQ 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    542 IIAFLAGLsyskirtrgsnYRFEGL-GPTVIVCPTTVMHQWVKEFHTWWPPFRVAILHETG-SYTHKKEKLIrdVAHCHG 619
Cdd:PLN03142  205 TISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPeERAHQREELL--VAGKFD 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    620 ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGT 699
Cdd:PLN03142  272 VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSS 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    700 LPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKSDVKMSLslPDKNEQVLFCRLTDEQHKVY--- 776
Cdd:PLN03142  352 AETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQYYkal 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    777 -QNFVDS----KEVYRILNGEMQifsgliaLRKICNHPDLFSG---GPKNLKGlpdDELEEDqfgywkrSGKMIVVESLL 848
Cdd:PLN03142  418 lQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG---EHLVEN-------SGKMVLLDKLL 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565    849 KIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYN-EDTSIFVFLLTTRVGGLGVNLTGAN 927
Cdd:PLN03142  481 PKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAGGLGINLATAD 560
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 4557565    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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfegLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE----------RGPVLVVCPLSVLENWEREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILHetGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17919   71 KWTPDLRVVVYH--GSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                        170       180
                 ....*....|....*....|....*...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRgsnyrfeglgpTVIVCPTTVMHQWVKEFH 586
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS-----------VLVVMPTSLIPHWVKEFA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILHetGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYD-----WHYVILDEGHKIRNPNAAVTLA 661
Cdd:cd18001   70 KWTPGLRVKVFH--GTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   662 CKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGK-LGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINP 740
Cdd:cd18001  148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                 ....*
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd18012    8 YQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLL-----------SRKEEGRKGPSLVVAPTSLIYNWEEEAAKFA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   590 PPFRVAILHETGsythKKEKLIRDVAHcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPH 669
Cdd:cd18012   77 PELKVLVIHGTK----RKREKLRALED-YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADH 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsySKIRTRGSNYRFEGLgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILA----SDHHKRANSFNSENL-PSLVVCPPTLVGHWVAEIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILHETGSYThkKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17999   76 KYFPNAFLKPLAYVGPPQ--ERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557565   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 4557565   838 SGKMIVVESLLKIWHKQGQRVLLFSQSRQMLDILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSIFVFLLTTRVG 917
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGSNYRF----------EGLGPTV-IVCPTTVM 578
Cdd:cd18005    4 YQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAV-LGKTGTRRDRENNrprfkkkppaSSAKKPVlIVAPLSVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   579 HQWVKEFHTW-WppFRVAILHETGsythKKEKLIRDV-AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd18005   83 YNWKDELDTWgH--FEVGVYHGSR----KDDELEGRLkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRD 736
Cdd:cd18005  157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                 ....*....
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK----------GNWGPHLIVVPTSVMLNWEMEFK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRvaILHETGSytHKKEKLIR------DVAHchgILITSYSYIrlMQDDIS--RYDWHYVILDEGHKIRNPNAAV 658
Cdd:cd18003   71 RWCPGFK--ILTYYGS--AKERKLKRqgwmkpNSFH---VCITSYQLV--VQDHQVfkRKKWKYLILDEAHNIKNFKSQR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   659 TLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITmggysnaSPVQVKTAYKCACV--LRD 736
Cdd:cd18003  142 WQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT-------AMSEGSQEENEELVrrLHK 214

                 ....*....
gi 4557565   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 4557565   511 QQTGVRWLWE-----LHCQQAGG--ILGDEMGLGKTIQIIAFL-AGLSYSKIRTRgsnyrfeglgpTVIVCPTTVMHQWV 582
Cdd:cd18007    5 QVEGVRFLWSnlvgtDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSR-----------PLVLCPASTLYNWE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   583 KEFHTWWPPFRVAILHETGSYTHKKEKL-IRDVAHCH---GILITSY-SYIRLMQDDISRYDWH-------------YVI 644
Cdd:cd18007   74 DEFKKWLPPDLRPLLVLVSLSASKRADArLRKINKWHkegGVLLIGYeLFRNLASNATTDPRLKqefiaalldpgpdLLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   645 LDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQV 724
Cdd:cd18007  154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDV 233

                 ....*
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSnyrfegLGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd18009    7 YQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL-----RERGV------WGPFLVIAPLSTLPNWVNEFARFT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   590 PPFRVAILHETGSYTHKKEKLIR---DVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd18009   76 PSVPVLLYHGTKEERERLRKKIMkreGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   667 TPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRM 746
Cdd:cd18009  156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRL 235

                 .
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGSNyrfeglGPTVIVCPTTVMHQWVKEF 585
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYL----MEKKKNN------GPYLVIVPLSTLSNWVSEF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   586 HTWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIrlMQDD--ISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd17996   73 EKWAP--SVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYI--IKDKplLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   664 Q-FRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPV----QVKTAYKCACVLRdti 738
Cdd:cd17996  149 TyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELneeeTLLIIRRLHKVLR--- 225

                 ....*....
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLS-YSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKE 584
Cdd:cd17997    3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKhYKNIN-----------GPHLIIVPKSTLDNWMRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   585 FHTWWPPFRVAILHetgsyTHKKE--KLIRDVAhCHG---ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVT 659
Cdd:cd17997   72 FKRWCPSLRVVVLI-----GDKEEraDIIRDVL-LPGkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   660 LACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNAspvqVKTAYKcacVLRdtin 739
Cdd:cd17997  146 QIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEV----VQRLHK---VLR---- 214

                 ....*...
gi 4557565   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 4557565   511 QQTGVRWLWE-LHCQQAGG----ILGDEMGLGKTIQIIAflagLSYSKIRTRgsnyrfEGLGPT----VIVCPTTVMHQW 581
Cdd:cd18004    5 QREGVQFLYDcLTGRRGYGgggaILADEMGLGKTLQAIA----LVWTLLKQG------PYGKPTakkaLIVCPSSLVGNW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   582 VKEFHTWWPPFRVAILHETGSytHKKEKLIRD---VAHCHGILITSYSYIRLMQDDI---SRYDwhYVILDEGHKIRNPN 655
Cdd:cd18004   75 KAEFDKWLGLRRIKVVTADGN--AKDVKASLDffsSASTYPVLIISYETLRRHAEKLskkISID--LLICDEGHRLKNSE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   656 AAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLR 735
Cdd:cd18004  151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELS 230
                        250
                 ....*....|
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGsNYRfeglGPTVIVCPTTVMHQWVKEFHTWw 589
Cdd:cd17995    4 YQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFL-----EHLYQVE-GIR----GPFLVIAPLSTIPNWQREFETW- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   590 PPFRVAILHETGS----------YTHKKEKL-IRDVAHCHgILITSYSYIrlMQD--DISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd17995   73 TDMNVVVYHGSGEsrqiiqqyemYFKDAQGRkKKGVYKFD-VLITTYEMV--IADaeELRKIPWRVVVVDEAHRLKNRNS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacVLRD 736
Cdd:cd17995  150 KLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTAEQVE---------KLQA 214

                 ....*....
gi 4557565   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 4557565   507 LFKYQQTGVRWLweLHCqqaGGILGDEMGLGKTIQIIAFLAG-------LSYSKIRTRGSNYRFEGLGPTVIVCPTTVMH 579
Cdd:cd18008    1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALALILAtrpqdpkIPEELEENSSDPKKLYLSKTTLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   580 QWVKEF--HTWWPPFRVAILHetGSythKKEKLIRDVAHCHgILITSYSyiRLMQDD------------------ISRYD 639
Cdd:cd18008   76 QWKDEIekHTKPGSLKVYVYH--GS---KRIKSIEELSDYD-IVITTYG--TLASEFpknkkgggrdskekeaspLHRIR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   640 WHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNA 719
Cdd:cd18008  148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKAL 227
                        250       260
                 ....*....|....*....|....*.
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQ----------QQYGPFLVVVPLSTMPAWQREF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   586 HTWWPPFRVAIL------------HETGSYTHKKEKLirdvahchGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRN 653
Cdd:cd17993   71 AKWAPDMNVIVYlgdiksrdtireYEFYFSQTKKLKF--------NVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   654 PNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQfsvpitmggYSNASPVQVKTaykcacv 733
Cdd:cd17993  143 DESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE---------HDEEQEKGIAD------- 206
                        250
                 ....*....|..
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQA---------GGILGDEMGLGKTIQIIAFLAGLsyskirtrgsnYRFEGLGPTVIVCPTTVMHQ 580
Cdd:cd18069    4 HQIGGIRFLYDNIIESLerykgssgfGCILAHSMGLGKTLQVISFLDVL-----------LRHTGAKTVLAIVPVNTLQN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   581 WVKEFHTWWPP-----------FRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQD-DIsrydwhyVILDEG 648
Cdd:cd18069   73 WLSEFNKWLPPpealpnvrprpFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGpDV-------VICDEG 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557565   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 4557565   510 YQQTGVRWLWE-LHCQQaGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRFEGLGPTVIVCPTTVMHQWVKEFHTW 588
Cdd:cd18006    4 YQLEGVNWLLQcRAEQH-GCILGDEMGLGKTCQTISLLWYLAG----------RLKLLGPFLVLCPLSVLDNWKEELNRF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   589 WPPFRVAilhetgSYTHKKEKL------IRDVAHCHgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd18006   73 APDLSVI------TYMGDKEKRldlqqdIKSTNRFH-VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   663 KQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLG--TLPVFMEQFSvpitmggysnaspvQVKTAYKCACVLRDTINP 740
Cdd:cd18006  146 SEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYS--------------ETDDESETVEELHLLLQP 211

                 ....*
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFHTWW 589
Cdd:cd17998    4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIP-----------GPHLVVVPSSTLDNWLREFKRWC 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   590 PPFRVAILHetGSYTHKKEklIRDVAHC----HGILITSYSYIRLMQDDIS---RYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd17998   73 PSLKVEPYY--GSQEERKH--LRYDILKgledFDVIVTTYNLATSNPDDRSffkRLKLNYVVYDEGHMLKNMTSERYRHL 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnYRfEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd18064   15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKH---------YR-NIPGPHMVLVPKSTLHNWMAEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   586 HTWWPPFRVAILheTGSyTHKKEKLIRDV--AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd18064   85 KRWVPTLRAVCL--IGD-KDQRAAFVRDVllPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   664 QFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGgysnaspvQVKTAYKCACVLRdtinPYLL 743
Cdd:cd18064  162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG--------DQKLVERLHMVLR----PFLL 229
                        250
                 ....*....|.
gi 4557565   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 4557565   510 YQQTGVRWLWEL-----HCQQAGGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYrfeGLGP----TVIVCPTTVMHQ 580
Cdd:cd18066    4 HQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTL------LRQGPY---GGKPvikrALIVTPGSLVKN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   581 WVKEFHTWWPPFRVAILheTGSYTHKKEKLIRdvAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTL 660
Cdd:cd18066   75 WKKEFQKWLGSERIKVF--TVDQDHKVEEFIA--SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   661 ACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINP 740
Cdd:cd18066  151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230

                 ....*
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRFEGLGPTVIVCPTTVMHQWVKEF 585
Cdd:cd18054   20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFH----------QHQLYGPFLLVVPLSTLTSWQREF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   586 HTWWPPFRVAI-LHETGS--------YTHKKEKLIRdvahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNA 656
Cdd:cd18054   90 EIWAPEINVVVyIGDLMSrntireyeWIHSQTKRLK-----FNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   657 AVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmGGYSNaspvqvktAYKCacvLRD 736
Cdd:cd18054  165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-----KGREN--------GYQS---LHK 228

                 ....*....
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyRFEGlgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK--------RING--PFLIIVPLSTLSNWVYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK-QF 665
Cdd:cd18062   94 KWAP--SVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   666 RTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYLL 743
Cdd:cd18062  172 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----EKVDLNEEETILIIrrLHKVLRPFLL 247

                 ....
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnYRfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18065   16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKH---------YR-NIPGPHMVLVPKSTLHNWMNEFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAILheTGSyTHKKEKLIRDVAHCH--GILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQ 664
Cdd:cd18065   86 RWVPSLRAVCL--IGD-KDARAAFIRDVMMPGewDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   665 FRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktaYKCACVLRDTINPYLLR 744
Cdd:cd18065  163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD------------QKLVERLHAVLKPFLLR 230

                 ...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyRFEGlgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18063   24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK--------RLNG--PYLIIVPLSTLSNWTYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPpfRVAILHETGSYTHKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK-QF 665
Cdd:cd18063   94 KWAP--SVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   666 RTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYLL 743
Cdd:cd18063  172 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----ERVDLNEEETILIIrrLHKVLRPFLL 247

                 ....
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyrfEGLGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEH----------NIWGPFLVIAPASTLHNWQQEIS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVaiLHETGSYTHKK--------EKLIRDVAHCHgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAV 658
Cdd:cd18002   71 RFVPQFKV--LPYWGNPKDRKvlrkfwdrKNLYTRDAPFH-VVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   659 TLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPIT--MGGYSNASPVQVKTaykcacvLRD 736
Cdd:cd18002  148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshAENKTGLNEHQLKR-------LHM 220

                 ....*....
gi 4557565   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 4557565    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 4557565  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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAilhetgSYTHKKeklirdvahchgILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACKQFR 666
Cdd:cd17994   71 MWAPDFYVV------TYVGDH------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557565   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 4557565   510 YQQTGVRWLWELHCQQ---------AGGILGDEMGLGKTIQIIAFLaglsyskiRTRGSNYRFEGLGPTVIVCPTTVMHQ 580
Cdd:cd18068    4 HQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFL--------HTVLLCEKLENFSRVLVVCPLNTVLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   581 WVKEFHTWWPPFRVAILHETGSYTHKKEKLIRDVAHCH-----GILITSYSYIRLM------------QDDISRY----- 638
Cdd:cd18068   76 WLNEFEKWQEGLKDEEKIEVNELATYKRPQERSYKLQRwqeegGVMIIGYDMYRILaqernvksreklKEIFNKAlvdpg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   639 -DwhYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYS 717
Cdd:cd18068  156 pD--FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCA 233

                 ....*...
gi 4557565   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 4557565   510 YQQTGVRWLWElhCQQA-------GGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYRFEGLGPTVIVCPTTVMHQWV 582
Cdd:cd18067    4 HQREGVKFLYR--CVTGrrirgshGCIMADEMGLGKTLQCITLMWTL------LRQSPQCKPEIDKAIVVSPSSLVKNWA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   583 KEFHTWWPPFRVAILHETGSythKKEKLIRDV--AHCHG------ILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18067   76 NELGKWLGGRLQPLAIDGGS---KKEIDRKLVqwASQQGrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   655 NAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVL 734
Cdd:cd18067  153 DNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQEL 232
                        250
                 ....*....|.
gi 4557565   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 4557565      499 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRFEGLGPTVIVCPTTV- 577
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPTREl 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565      578 MHQWVKEFHTWWPPF--RVAILHETGSYTHKKEKLIRDVAHchgILITSYSYIR--LMQDDISRYDWHYVILDEGHKIRN 653
Cdd:smart00487   67 AEQWAEELKKLGPSLglKVVGLYGGDSKREQLRKLESGKTD---ILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLD 143
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565      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 4557565   507 LFKYQQTGVRW-LwelhcqQAGG--ILGDEMGLGKTIQIIAFLAglsyskirtrgsNYRFEGlgPTVIVCPTTVMHQWVK 583
Cdd:cd18010    1 LLPFQREGVCFaL------RRGGrvLIADEMGLGKTVQAIAIAA------------YYREEW--PLLIVCPSSLRLTWAD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   584 EFHTWwppFRVAILHETGSYTHKKEKLIRDVahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPNAAVTLACK 663
Cdd:cd18010   61 EIERW---LPSLPPDDIQVIVKSKDGLRDGD---AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAAL 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557565   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 4557565   506 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsyskirtrgsNYRF---EGLGPTVIVCPTTVMHQWV 582
Cdd:cd18053   20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL-------------NYLFhehQLYGPFLLVVPLSTLTSWQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   583 KEFHTWWPPFRVAI---------LHETGSYTHKKEKLIRdvahcHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRN 653
Cdd:cd18053   87 REIQTWAPQMNAVVylgdinsrnMIRTHEWMHPQTKRLK-----FNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHTKG---------PFLVSAPLSTIINWEREFQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRV----------AILHETG-SYT-------HKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18055   71 MWAPDFYVvtytgdkdsrAIIRENEfSFDdnavkggKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18055  151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                        250
                 ....*....|....*..
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIR-----------GPFLIIAPLSTITNWEREFR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWwPPFRVAILHETG---SYTHKKEKLIRD--------VAHCHGIlITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPN 655
Cdd:cd18058   70 TW-TEMNAIVYHGSQisrQMIQQYEMYYRDeqgnplsgIFKFQVV-ITTFEMILADCPELKKINWSCVIIDEAHRLKNRN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   656 AAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTaykcacvLR 735
Cdd:cd18058  148 CKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG--------DLKTEEQVKK-------LQ 212
                        250
                 ....*....|
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSL-YKEGHSKG---------PYLVSAPLSTIINWEREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRVAIL---HETGSYTHKKEKLIRDVAHCHG---------------ILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18057   71 MWAPDFYVVTYtgdKESRSVIRENEFSFEDNAIRSGkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLVVDEA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18057  151 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                        250
                 ....*....|....*..
gi 4557565   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 4557565     839 GKMIVVESLLKiwHKQGQRVLLFSQSRQMLDIlEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTsiFVFLLTTRVGG 918
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 4557565     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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyrfeglgPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWWPPFRV----------AILHETG-SYT-------HKKEKLIRDVAHCHGILITSYSYIRLMQDDISRYDWHYVILDEG 648
Cdd:cd18056   71 MWAPDMYVvtyvgdkdsrAIIRENEfSFEdnairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   649 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 728
Cdd:cd18056  151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA--------DIAKEDQIKK-- 220
                        250
                 ....*....|....*..
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIH-----------GPFLVIAPLSTIPNWEREFR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWwPPFRVAILHETGS-----------YTHKKEKLIRDVAHCHGIlITSYSYIRLMQDDISRYDWHYVILDEGHKIRNPN 655
Cdd:cd18059   70 TW-TELNVVVYHGSQAsrrtiqlyemyFKDPQGRVIKGSYKFHAI-ITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4557565   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 4557565   507 LFKYQQTGVRWL-WELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRG-------------SNYRFEGLGpTVIV 572
Cdd:cd18072    1 LLLHQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEekekalteweskkDSTLVPSAG-TLVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   573 CPTTVMHQWVKEF--HTWWPPFRVAILHetGSYTHKKEKLIRDvahcHGILITSYSyirLMQDDISRYD----------- 639
Cdd:cd18072   80 CPASLVHQWKNEVesRVASNKLRVCLYH--GPNRERIGEVLRD----YDIVITTYS---LVAKEIPTYKeesrssplfri 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4557565   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 4557565   527 GGILGDEMGLGKTIQIIAFLAGlsyskirtrgsnyrfeglGPTVIVCPTTVMHQWVKEFHTWWPPFRVAIlhetgsYTHK 606
Cdd:cd18071   50 GGILADDMGLGKTLTTISLILA------------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKV------YTYH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   607 KEKLIRDVAHCHG--ILITSYSYirLMQDD-------ISRYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSP 677
Cdd:cd18071  106 GGERNRDPKLLSKydIVLTTYNT--LASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTP 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIR-----------GPFLIIAPLSTIANWEREFR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWwPPFRVAILHetGSYTHKK-----EKLIRDV-------AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18061   70 TW-TDLNVVVYH--GSLISRQmiqqyEMYFRDSqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNK 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4557565   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 4557565   507 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyrfeglGPTVIVCPTTVMHQWVKEFH 586
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIH-----------GPFLVIAPLSTITNWEREFN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   587 TWwPPFRVAILHetGSYTHKK-----EKLIRDV-------AHCHGILITSYSYIRLMQDDISRYDWHYVILDEGHKIRNP 654
Cdd:cd18060   70 TW-TEMNTIVYH--GSLASRQmiqqyEMYCKDSrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   655 NAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacVL 734
Cdd:cd18060  147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF------GDLKTEEQVQ---------KL 211
                        250
                 ....*....|.
gi 4557565   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 4557565   507 LFKYQQTGVRWLWElhcqqAGGILGDEMGLGKTIQIIAFLA-------GLSYSKIRTRGSNYRFEGL--------GPTVI 571
Cdd:cd18070    1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILlhprpdnDLDAADDDSDEMVCCPDCLvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   572 VCPTTVMHQWVKEFHTWWPPfRVAILHETGSYTHKKEKL--IRDVAHcHGILITSYSYIR--LMQDDI----------SR 637
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPS-SLKVLTYQGVKKDGALASpaPEILAE-YDIVVTTYDVLRteLHYAEAnrsnrrrrrqKR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557565   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 4557565      869 DILEVFLRAQKYTYLKMDGTTTIASRQPLITRYNEDTSifVFLLTTRVGGLGVNLTGANRVVIYDPDWNPSTDTQARERA 948
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 4557565      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 4557565   507 LFKYQQTGVRWLWELhcQQAGGILGDEMGLGKTIQiiaflAGL--SYSKIRTRGsnyrfeglGPTVIVCPTTVMHQWVKE 584
Cdd:cd18011    1 PLPHQIDAVLRALRK--PPVRLLLADEVGLGKTIE-----AGLiiKELLLRGDA--------KRVLILCPASLVEQWQDE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   585 -FHTWWPPFRVAilheTGSYTHKKEKLIRDVAHCHGILITSYSYIRLM---QDDISRYDWHYVILDEGHKIRN-PNAAVT 659
Cdd:cd18011   66 lQDKFGLPFLIL----DRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNsGGGKET 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4557565   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 4557565   452 YRDDGDEDYYKQRLRRWNKLRLQDKEKRLKLEDDSEESDAeFDEGFKVPGFLFKkLFKYQQTGVRWLWELHCQQAG-GIL 530
Cdd:COG1061   28 LSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEA-LEAGDEASGTSFE-LRPYQQEALEALLAALERGGGrGLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   531 gdEM--GLGKTIqIIAFLAglsyskirtrgsnYRFEGLGPTVIVCPTTV-MHQWVKEFHTWwppfrvaiLHETGSYTHKK 607
Cdd:COG1061  106 --VAptGTGKTV-LALALA-------------AELLRGKRVLVLVPRRElLEQWAEELRRF--------LGDPLAGGGKK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557565   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 4557565   507 LFKYQQTGVRWLWElhcQQAGGILGDeMGLGKTIQIIAFLAGLsyskirtrgsnyRFEGL-GPTVIVCPTTVM-HQWVKE 584
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDL------------QLDDFtRRVLVIAPLRVArSTWPDE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557565   585 FHTWWPPF--RVAILHETGSythKKEKLIRDVAHCHGILITSYSYIRLMQDDisRYDWHYVILDEGHKIRNPNAAVTLAC 662
Cdd:cd18013   65 VEKWNHLRnlTVSVAVGTER---QRSKAANTPADLYVINRENLKWLVNKSGD--PWPFDMVVIDELSSFKSPRSKRFKAL 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557565   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 4557565   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 4557565   527 GGILGDEMGLGKTIqiIAFLAGLSYskIRTRGsnyrfeglGPTVIVCPT-TVMHQWVKEFHTWW-PPFRVAILHetGSYT 604
Cdd:cd00046    3 NVLITAPTGSGKTL--AALLAALLL--LLKKG--------KKVLVLVPTkALALQTAERLRELFgPGIRVAVLV--GGSS 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557565   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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