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Conserved domains on  [gi|2065627291|ref|XP_042192626|]
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DNA excision repair protein ERCC-6 [Callorhinchus milii]

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, ...
381-999 3.54e-139

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 445.05  E-value: 3.54e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  381 WREGDGSDSGESLYVPEEELFDPDEIEYEDDEGDGFLDRHQLNPLRKKKAQLKAQPSLSEDIDFLSSSEEDEPKGRKVNI 460
Cdd:COG0553    105 ALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  461 CRDDGNEDFYKKRLRSWRKKRLKAKEECRASEENGGSDESDAEFDEGFKVPGFLWRKLYKYQQTGVRWLWELHCQQAGGI 540
Cdd:COG0553    185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  541 LGDEMGLGKTIQIIAFLAGLsyskiRTRGLNyryeglGPVVIVCPATVMHQWVKEFHTWWPPFRVAILHEsgsfTTRKER 620
Cdd:COG0553    265 LADDMGLGKTIQALALLLEL-----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG----TRERAK 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  621 LIREIAACNgILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLF 700
Cdd:COG0553    330 GANPFEDAD-LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  701 DFVFPGKLGTLQVFMEQFSVPITMGGYQNASpvqvqtaykcacVLRDTINPYLLRRMKADVKMNLalPDKSEQVLFCRLT 780
Cdd:COG0553    409 DFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKEDVLKDL--PEKTEETLYVELT 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  781 EEQRQVYQTFIDskEVYQILNGE------MQIFTGLISLRKICNHPDLFsggpkilkgmtddhLTEEEHFGHWtrSGKMI 854
Cdd:COG0553    475 PEQRALYEAVLE--YLRRELEGAegirrrGLILAALTRLRQICSHPALL--------------LEEGAELSGR--SAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  855 VVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLFLLTTRVGGLGIN 934
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLN 616
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065627291  935 LTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLLTAGTIEEKIYHRQIFKQFLTNRVL 999
Cdd:COG0553    617 LTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
97-173 1.25e-33

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: 124.24  E-value: 1.25e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065627291   97 VEQSAQAMELQGLGVDVYDQDVLEQGVLQQVDRAISEASQATKRTDAEKEYHSVLDDLRSCTTSLKHINQIIEQLTP 173
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1473-1546 1.94e-29

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: 112.22  E-value: 1.94e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065627291 1473 ISTEHDELLVEMRNFIAFQAsiDGQATTQELLQEFQAKLSTAQTVIFRELLINLCTFHRTASGEGTWKLKPAFR 1546
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
381-999 3.54e-139

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 445.05  E-value: 3.54e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  381 WREGDGSDSGESLYVPEEELFDPDEIEYEDDEGDGFLDRHQLNPLRKKKAQLKAQPSLSEDIDFLSSSEEDEPKGRKVNI 460
Cdd:COG0553    105 ALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  461 CRDDGNEDFYKKRLRSWRKKRLKAKEECRASEENGGSDESDAEFDEGFKVPGFLWRKLYKYQQTGVRWLWELHCQQAGGI 540
Cdd:COG0553    185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  541 LGDEMGLGKTIQIIAFLAGLsyskiRTRGLNyryeglGPVVIVCPATVMHQWVKEFHTWWPPFRVAILHEsgsfTTRKER 620
Cdd:COG0553    265 LADDMGLGKTIQALALLLEL-----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG----TRERAK 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  621 LIREIAACNgILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLF 700
Cdd:COG0553    330 GANPFEDAD-LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  701 DFVFPGKLGTLQVFMEQFSVPITMGGYQNASpvqvqtaykcacVLRDTINPYLLRRMKADVKMNLalPDKSEQVLFCRLT 780
Cdd:COG0553    409 DFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKEDVLKDL--PEKTEETLYVELT 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  781 EEQRQVYQTFIDskEVYQILNGE------MQIFTGLISLRKICNHPDLFsggpkilkgmtddhLTEEEHFGHWtrSGKMI 854
Cdd:COG0553    475 PEQRALYEAVLE--YLRRELEGAegirrrGLILAALTRLRQICSHPALL--------------LEEGAELSGR--SAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  855 VVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLFLLTTRVGGLGIN 934
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLN 616
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065627291  935 LTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLLTAGTIEEKIYHRQIFKQFLTNRVL 999
Cdd:COG0553    617 LTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
518-705 2.31e-114

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: 358.17  E-value: 2.31e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrglnyryEGLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHESGSFT---------TRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTgseeklgsiERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFP 705
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
521-823 7.70e-108

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: 344.28  E-value: 7.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  521 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFHTW 599
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  600 W--PPFRVAILHESGSfTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:pfam00176   72 VspPALRVVVLHGNKR-PQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGyqnaspvqvqtAYKCACVLRDTINPYLLRRM 757
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065627291  758 KADVKMNlaLPDKSEQVLFCRLTEEQRQVYQTFIDSKEVYQILNGE------MQIFTGLISLRKICNHPDLF 823
Cdd:pfam00176  220 KKDVEKS--LPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
478-987 8.35e-90

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 316.36  E-value: 8.35e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  478 RKKRLKAKEECRASEEnggsdESDAEF----DEGFKV---------PGFLWRKLYKYQQTGVRWLWELHCQQAGGILGDE 544
Cdd:PLN03142   122 KKAKGRGRHASKLTEE-----EEDEEYlkeeEDGLGGsggtrllvqPSCIKGKMRDYQLAGLNWLIRLYENGINGILADE 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  545 MGLGKTIQIIAFLAGLSyskiRTRGLNyryeglGPVVIVCPATVMHQWVKEFHTWWPPFRVAILHEsgsfTTRKERLIRE 624
Cdd:PLN03142   197 MGLGKTLQTISLLGYLH----EYRGIT------GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHG----NPEERAHQRE 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  625 IAACNG---ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFD 701
Cdd:PLN03142   263 ELLVAGkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLN 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  702 FVFPGKLGTLQVFMEQFSvpitMGGYQNASPVqVQTAYKcacVLRdtinPYLLRRMKADVKMNLalPDKSEQVLFCRLTE 781
Cdd:PLN03142   343 FLLPEIFSSAETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQ 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  782 EQRQVY----QTFIDS----KEVYQILNGEMQiftglisLRKICNHPDLFSG---GPKILkgmTDDHLTEEehfghwtrS 850
Cdd:PLN03142   409 MQKQYYkallQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYT---TGEHLVEN--------S 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  851 GKMIVVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYN-ENASIFLFLLTTRVG 929
Cdd:PLN03142   471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAG 550
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065627291  930 GLGINLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLLTAGTIEEKIYHR 987
Cdd:PLN03142   551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
97-173 1.25e-33

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: 124.24  E-value: 1.25e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065627291   97 VEQSAQAMELQGLGVDVYDQDVLEQGVLQQVDRAISEASQATKRTDAEKEYHSVLDDLRSCTTSLKHINQIIEQLTP 173
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1473-1546 1.94e-29

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: 112.22  E-value: 1.94e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065627291 1473 ISTEHDELLVEMRNFIAFQAsiDGQATTQELLQEFQAKLSTAQTVIFRELLINLCTFHRTASGEGTWKLKPAFR 1546
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
DEXDc smart00487
DEAD-like helicases superfamily;
510-703 1.08e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 100.64  E-value: 1.08e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291   510 VPGFLWRKLYKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgLNYRYEGLGPVVIVCP-ATV 588
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPtREL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291   589 MHQWVKEFHTWWPPFRVAILHESGSfTTRKERLIREIAACNGILVTSYSYIR--IMQESIGQYKWHYAILDEGHKIRNPN 666
Cdd:smart00487   67 AEQWAEELKKLGPSLGLKVVGLYGG-DSKREQLRKLESGKTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 2065627291   667 AGVTVACKQFQTP---HRIILSGSP---MQNNLKELWSLFDFV 703
Cdd:smart00487  146 FGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFI 188
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
381-999 3.54e-139

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 445.05  E-value: 3.54e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  381 WREGDGSDSGESLYVPEEELFDPDEIEYEDDEGDGFLDRHQLNPLRKKKAQLKAQPSLSEDIDFLSSSEEDEPKGRKVNI 460
Cdd:COG0553    105 ALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLAL 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  461 CRDDGNEDFYKKRLRSWRKKRLKAKEECRASEENGGSDESDAEFDEGFKVPGFLWRKLYKYQQTGVRWLWELHCQQAGGI 540
Cdd:COG0553    185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGL 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  541 LGDEMGLGKTIQIIAFLAGLsyskiRTRGLNyryeglGPVVIVCPATVMHQWVKEFHTWWPPFRVAILHEsgsfTTRKER 620
Cdd:COG0553    265 LADDMGLGKTIQALALLLEL-----KERGLA------RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG----TRERAK 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  621 LIREIAACNgILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLF 700
Cdd:COG0553    330 GANPFEDAD-LVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  701 DFVFPGKLGTLQVFMEQFSVPITMGGYQNASpvqvqtaykcacVLRDTINPYLLRRMKADVKMNLalPDKSEQVLFCRLT 780
Cdd:COG0553    409 DFLNPGLLGSLKAFRERFARPIEKGDEEALE------------RLRRLLRPFLLRRTKEDVLKDL--PEKTEETLYVELT 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  781 EEQRQVYQTFIDskEVYQILNGE------MQIFTGLISLRKICNHPDLFsggpkilkgmtddhLTEEEHFGHWtrSGKMI 854
Cdd:COG0553    475 PEQRALYEAVLE--YLRRELEGAegirrrGLILAALTRLRQICSHPALL--------------LEEGAELSGR--SAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  855 VVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLFLLTTRVGGLGIN 934
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLN 616
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065627291  935 LTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLLTAGTIEEKIYHRQIFKQFLTNRVL 999
Cdd:COG0553    617 LTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
518-705 2.31e-114

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: 358.17  E-value: 2.31e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrglnyryEGLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHESGSFT---------TRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTgseeklgsiERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFP 705
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
521-823 7.70e-108

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: 344.28  E-value: 7.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  521 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFHTW 599
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  600 W--PPFRVAILHESGSfTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:pfam00176   72 VspPALRVVVLHGNKR-PQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGyqnaspvqvqtAYKCACVLRDTINPYLLRRM 757
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065627291  758 KADVKMNlaLPDKSEQVLFCRLTEEQRQVYQTFIDSKEVYQILNGE------MQIFTGLISLRKICNHPDLF 823
Cdd:pfam00176  220 KKDVEKS--LPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
478-987 8.35e-90

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 316.36  E-value: 8.35e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  478 RKKRLKAKEECRASEEnggsdESDAEF----DEGFKV---------PGFLWRKLYKYQQTGVRWLWELHCQQAGGILGDE 544
Cdd:PLN03142   122 KKAKGRGRHASKLTEE-----EEDEEYlkeeEDGLGGsggtrllvqPSCIKGKMRDYQLAGLNWLIRLYENGINGILADE 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  545 MGLGKTIQIIAFLAGLSyskiRTRGLNyryeglGPVVIVCPATVMHQWVKEFHTWWPPFRVAILHEsgsfTTRKERLIRE 624
Cdd:PLN03142   197 MGLGKTLQTISLLGYLH----EYRGIT------GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHG----NPEERAHQRE 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  625 IAACNG---ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFD 701
Cdd:PLN03142   263 ELLVAGkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLN 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  702 FVFPGKLGTLQVFMEQFSvpitMGGYQNASPVqVQTAYKcacVLRdtinPYLLRRMKADVKMNLalPDKSEQVLFCRLTE 781
Cdd:PLN03142   343 FLLPEIFSSAETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQ 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  782 EQRQVY----QTFIDS----KEVYQILNGEMQiftglisLRKICNHPDLFSG---GPKILkgmTDDHLTEEehfghwtrS 850
Cdd:PLN03142   409 MQKQYYkallQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYT---TGEHLVEN--------S 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  851 GKMIVVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYN-ENASIFLFLLTTRVG 929
Cdd:PLN03142   471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkPGSEKFVFLLSTRAG 550
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065627291  930 GLGINLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLLTAGTIEEKIYHR 987
Cdd:PLN03142   551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
518-705 4.03e-72

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: 238.62  E-value: 4.03e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrglnyryegLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE----------RGPVLVVCPLSVLENWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHesGSFTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:cd17919     71 KWTPDLRVVVYH--GSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFP 705
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
518-756 2.00e-70

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: 235.73  E-value: 2.00e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIrtrgLNYryeglgpVVIVCPATVMHQWVKEFH 597
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGL----IKS-------VLVVMPTSLIPHWVKEFA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHesGSFTTRKERLIREIAACNGILVTSYSYIRIMQESIG-----QYKWHYAILDEGHKIRNPNAGVTVA 672
Cdd:cd18001     70 KWTPGLRVKVFH--GTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  673 CKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGK-LGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVLRDTINP 751
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                   ....*
gi 2065627291  752 YLLRR 756
Cdd:cd18001    228 YFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
518-758 3.27e-64

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: 217.43  E-value: 3.27e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsyskirtrgLNYRYEGLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLL-----------SRKEEGRKGPSLVVAPTSLIYNWEEEAA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHESGsfttRKERLIREIAAcNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:cd18012     74 KFAPELKVLVIHGTK----RKREKLRALED-YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITmggYQNASPVQVQtaykcacvLRDTINPYLLRRM 757
Cdd:cd18012    149 ADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIE---KDGDEEALEE--------LKKLISPFILRRL 217

                   .
gi 2065627291  758 K 758
Cdd:cd18012    218 K 218
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
518-756 2.79e-61

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: 209.51  E-value: 2.79e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsySKIRTRGLNYRYEGLgPVVIVCPATVMHQWVKEFH 597
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILA----SDHHKRANSFNSENL-PSLVVCPPTLVGHWVAEIK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHESGSFTTRkeRLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:cd17999     76 KYFPNAFLKPLAYVGPPQER--RRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVLRDTINPYLLRR 756
Cdd:cd17999    154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
518-756 3.63e-60

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: 206.85  E-value: 3.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRG-----LNYRYEGLG------PVVIVCPA 586
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAV-LGKTGTRRdrennRPRFKKKPPassakkPVLIVAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  587 TVMHQWVKEFHTW-WppFRVAILHESGSFTTRKERLIReiAACNgILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNP 665
Cdd:cd18005     80 SVLYNWKDELDTWgH--FEVGVYHGSRKDDELEGRLKA--GRLE-VVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNP 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  666 NAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVL 745
Cdd:cd18005    155 KSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQEL 234
                          250
                   ....*....|.
gi 2065627291  746 RDTINPYLLRR 756
Cdd:cd18005    235 AVKLSKFFLRR 245
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
848-975 6.85e-58

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: 195.77  E-value: 6.85e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  848 TRSGKMIVVEALLRLWHKQGHRVLLFSQSRQLLNIMEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLFLLTTR 927
Cdd:cd18793      8 VVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2065627291  928 VGGLGINLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTIYRLL 975
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
518-740 9.13e-47

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: 168.24  E-value: 9.13e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWE-----LHCQQAGG--ILGDEMGLGKTIQIIAFL-AGLSYSKIRTRglnyryeglgpVVIVCPATVM 589
Cdd:cd18007      1 LKPHQVEGVRFLWSnlvgtDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSR-----------PLVLCPASTL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  590 HQWVKEFHTWWPPFRV--AILHESGSFTTRKERL--IREIAACNGILVTSY-SYIRIMQESIGQYKWHYA---------- 654
Cdd:cd18007     70 YNWEDEFKKWLPPDLRplLVLVSLSASKRADARLrkINKWHKEGGVLLIGYeLFRNLASNATTDPRLKQEfiaalldpgp 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  655 ---ILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNAS 731
Cdd:cd18007    150 dllVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDST 229

                   ....*....
gi 2065627291  732 PVQVQTAYK 740
Cdd:cd18007    230 EEDVRLMLK 238
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
517-758 2.15e-46

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: 166.78  E-value: 2.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGLNyryeglGPVVIVCPATVMHQWVKEF 596
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYL----MEKKKNN------GPYLVIVPLSTLSNWVSEF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPpfRVAILHESGSFTTRKErLIREIAACN-GILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQ 675
Cdd:cd17996     73 EKWAP--SVSKIVYKGTPDVRKK-LQSQIRAGKfNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNT 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  676 -FQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPV----QVQTAYKCACVLRdtin 750
Cdd:cd17996    150 yYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELneeeTLLIIRRLHKVLR---- 225

                   ....*...
gi 2065627291  751 PYLLRRMK 758
Cdd:cd17996    226 PFLLRRLK 233
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
518-756 3.41e-46

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: 165.99  E-value: 3.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrglnyryEGLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK----------GNWGPHLIVVPTSVMLNWEMEFK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRvaILHESGSFTTRKERliREIAA---CNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACK 674
Cdd:cd18003     71 RWCPGFK--ILTYYGSAKERKLK--RQGWMkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  675 QFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITmggyqnaSPVQVQTAYKCACV--LRDTINPY 752
Cdd:cd18003    147 NFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT-------AMSEGSQEENEELVrrLHKVLRPF 219

                   ....
gi 2065627291  753 LLRR 756
Cdd:cd18003    220 LLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
517-758 1.45e-45

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: 164.48  E-value: 1.45e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGLnyryegLGPVVIVCPATVMHQWVKEF 596
Cdd:cd18009      3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL-----RERGV------WGPFLVIAPLSTLPNWVNEF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAILHESGSfttRKERLIREIAA------CNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVT 670
Cdd:cd18009     72 ARFTPSVPVLLYHGTKE---ERERLRKKIMKregtlqDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  671 VACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVLRDTIN 750
Cdd:cd18009    149 QELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILK 228

                   ....*...
gi 2065627291  751 PYLLRRMK 758
Cdd:cd18009    229 PFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
517-758 1.88e-45

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: 163.65  E-value: 1.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLS-YSKIRtrglnyryeglGPVVIVCPATVMHQWVKE 595
Cdd:cd17997      3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKhYKNIN-----------GPHLIIVPKSTLDNWMRE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  596 FHTWWPPFRVAILHesGSFTTRKErLIREIAaCNG---ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVA 672
Cdd:cd17997     72 FKRWCPSLRVVVLI--GDKEERAD-IIRDVL-LPGkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  673 CKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNAspvqVQTAYKcacVLRdtinPY 752
Cdd:cd17997    148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEV----VQRLHK---VLR----PF 216

                   ....*.
gi 2065627291  753 LLRRMK 758
Cdd:cd17997    217 LLRRIK 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
518-756 1.87e-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: 158.60  E-value: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWE-LHCQQAGG----ILGDEMGLGKTIQIIAflagLSYSKIRTRglnyryEGLGP----VVIVCPATV 588
Cdd:cd18004      1 LRPHQREGVQFLYDcLTGRRGYGgggaILADEMGLGKTLQAIA----LVWTLLKQG------PYGKPtakkALIVCPSSL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  589 MHQWVKEFHTWWPPFRVAILHESGS--FTTRKERLIREIAACNgILVTSYSYIRIMQESIGQYK-WHYAILDEGHKIRNP 665
Cdd:cd18004     71 VGNWKAEFDKWLGLRRIKVVTADGNakDVKASLDFFSSASTYP-VLIISYETLRRHAEKLSKKIsIDLLICDEGHRLKNS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  666 NAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVL 745
Cdd:cd18004    150 ESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQEL 229
                          250
                   ....*....|.
gi 2065627291  746 RDTINPYLLRR 756
Cdd:cd18004    230 SELTSRFILRR 240
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
521-756 3.77e-43

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 157.02  E-value: 3.77e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  521 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGlNYRyeglGPVVIVCPATVMHQWVKEFHTWw 600
Cdd:cd17995      4 YQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFL-----EHLYQVE-GIR----GPFLVIAPLSTIPNWQREFETW- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  601 PPFRVAILHesGSFTTRKERLIREIAACNG------------ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd17995     73 TDMNVVVYH--GSGESRQIIQQYEMYFKDAqgrkkkgvykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFsvpitmGGYQNASpvQVQTaykcacvLRDT 748
Cdd:cd17995    151 LLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTAE--QVEK-------LQAL 215

                   ....*...
gi 2065627291  749 INPYLLRR 756
Cdd:cd17995    216 LKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
517-756 1.29e-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: 146.73  E-value: 1.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglSYskirtrgLNYRYEGLGPVVIVCPATVMHQWVKEF 596
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFL---SY-------LFHSQQQYGPFLVVVPLSTMPAWQREF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAILheSGSFTTRKerLIREIAACNG--------ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd17993     71 AKWAPDMNVIVY--LGDIKSRD--TIREYEFYFSqtkklkfnVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITmGGYQNaspvqvqtaykcacvLRDT 748
Cdd:cd17993    147 LYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQE-KGIAD---------------LHKE 210

                   ....*...
gi 2065627291  749 INPYLLRR 756
Cdd:cd17993    211 LEPFILRR 218
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
518-756 4.82e-39

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: 145.89  E-value: 4.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLweLHCqqaGGILGDEMGLGKTIQIIAF-LAGLSYSKIRTRGLNYRYEGLGPVV------IVCPATVMH 590
Cdd:cd18008      1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALALiLATRPQDPKIPEELEENSSDPKKLYlskttlIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  591 QWVKEF--HTWWPPFRVAILHESGsfttrKERLIREIAACNgILVTSYSyiRIMQE------------------SIGQYK 650
Cdd:cd18008     76 QWKDEIekHTKPGSLKVYVYHGSK-----RIKSIEELSDYD-IVITTYG--TLASEfpknkkgggrdskekeasPLHRIR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  651 WHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNA 730
Cdd:cd18008    148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKAL 227
                          250       260
                   ....*....|....*....|....*.
gi 2065627291  731 SPVQVqtaykcacvlrdTINPYLLRR 756
Cdd:cd18008    228 ERLQA------------LLKPILLRR 241
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
518-756 1.11e-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: 144.12  E-value: 1.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWE-LHCQQaGGILGDEMGLGKTIQIIAFLAGLSYskirtrglnyRYEGLGPVVIVCPATVMHQWVKEF 596
Cdd:cd18006      1 LRPYQLEGVNWLLQcRAEQH-GCILGDEMGLGKTCQTISLLWYLAG----------RLKLLGPFLVLCPLSVLDNWKEEL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPpfRVAILHESGSFTTRKErLIREIAACN--GILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACK 674
Cdd:cd18006     70 NRFAP--DLSVITYMGDKEKRLD-LQQDIKSTNrfHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  675 QFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLG--TLQVFMEQFSvpitmggyqnaspvQVQTAYKCACVLRDTINPY 752
Cdd:cd18006    147 EFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYS--------------ETDDESETVEELHLLLQPF 212

                   ....
gi 2065627291  753 LLRR 756
Cdd:cd18006    213 LLRR 216
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
518-705 5.42e-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: 140.98  E-value: 5.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrglnyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIP-----------GPHLVVVPSSTLDNWLREFK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHesGSFTTRKErlIREIAACN----GILVTSY----------SYIRIMqesigqyKWHYAILDEGHKIR 663
Cdd:cd17998     70 RWCPSLKVEPYY--GSQEERKH--LRYDILKGledfDVIVTTYnlatsnpddrSFFKRL-------KLNYVVYDEGHMLK 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2065627291  664 NPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFP 705
Cdd:cd17998    139 NMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
515-765 4.91e-37

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: 140.57  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  515 WRKLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrglnyrYEGL-GPVVIVCPATVMHQWV 593
Cdd:cd18064     13 WGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKH-----------YRNIpGPHMVLVPKSTLHNWM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  594 KEFHTWWPPFRVAIL---HESGSFTTRKERLIREIAACngilVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVT 670
Cdd:cd18064     82 AEFKRWVPTLRAVCLigdKDQRAAFVRDVLLPGEWDVC----VTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  671 VACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVqtaykcacVLRdtin 750
Cdd:cd18064    158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHM--------VLR---- 225
                          250
                   ....*....|....*
gi 2065627291  751 PYLLRRMKADVKMNL 765
Cdd:cd18064    226 PFLLRRIKADVEKSL 240
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
521-736 6.44e-36

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: 136.48  E-value: 6.44e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  521 YQQTGVRWLWELHCQQA---------GGILGDEMGLGKTIQIIAFLAGLsyskirtrglnYRYEGLGPVVIVCPATVMHQ 591
Cdd:cd18069      4 HQIGGIRFLYDNIIESLerykgssgfGCILAHSMGLGKTLQVISFLDVL-----------LRHTGAKTVLAIVPVNTLQN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  592 WVKEFHTWWPP-----------FRVAILHESGSFTTRKERLIREIAACNGILVTSYSYIRIMQESigqykwHYAILDEGH 660
Cdd:cd18069     73 WLSEFNKWLPPpealpnvrprpFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGP------DVVICDEGH 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065627291  661 KIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQ 736
Cdd:cd18069    147 RIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
518-758 1.58e-35

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: 136.33  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGLNyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18062     24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYL----MEHKRIN------GPFLIIVPLSTLSNWVYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPpfRVAILHESGSFTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVT-VACKQF 676
Cdd:cd18062     94 KWAP--SVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTqVLNTHY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  677 QTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQnaspVQVQTAYKCACV--LRDTINPYLL 754
Cdd:cd18062    172 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEK----VDLNEEETILIIrrLHKVLRPFLL 247

                   ....
gi 2065627291  755 RRMK 758
Cdd:cd18062    248 RRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
518-758 6.10e-35

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: 134.81  E-value: 6.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGLNyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYL----MEHKRLN------GPYLIIVPLSTLSNWTYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPpfRVAILHESGSFTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVT-VACKQF 676
Cdd:cd18063     94 KWAP--SVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTqVLNTHY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  677 QTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQnaspVQVQTAYKCACV--LRDTINPYLL 754
Cdd:cd18063    172 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGER----VDLNEEETILIIrrLHKVLRPFLL 247

                   ....
gi 2065627291  755 RRMK 758
Cdd:cd18063    248 RRLK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
517-756 4.07e-34

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 131.67  E-value: 4.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglSYskirtrgLNYRYEGLGPVVIVCPATVMHQWVKEF 596
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFL---SY-------LFHQHQLYGPFLLVVPLSTLTSWQREF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAILheSGSFTTRKErlIREIAACN--------GILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd18054     90 EIWAPEINVVVY--IGDLMSRNT--IREYEWIHsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPiTMGGYQNaspvqvqtaykcacvLRDT 748
Cdd:cd18054    166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKG-RENGYQS---------------LHKV 229

                   ....*...
gi 2065627291  749 INPYLLRR 756
Cdd:cd18054    230 LEPFLLRR 237
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
97-173 1.25e-33

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: 124.24  E-value: 1.25e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065627291   97 VEQSAQAMELQGLGVDVYDQDVLEQGVLQQVDRAISEASQATKRTDAEKEYHSVLDDLRSCTTSLKHINQIIEQLTP 173
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
518-756 6.23e-33

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: 128.42  E-value: 6.23e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWEL-----HCQQAGGILGDEMGLGKTIQIIAFLAGLsyskirtrgLNYRYEGLGPVV----IVCPATV 588
Cdd:cd18066      1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTL---------LRQGPYGGKPVIkralIVTPGSL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  589 MHQWVKEFHTWWPPFRVAIlhesgsFTTRKERLIREIAACN--GILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPN 666
Cdd:cd18066     72 VKNWKKEFQKWLGSERIKV------FTVDQDHKVEEFIASPlySVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  667 AGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACVLR 746
Cdd:cd18066    146 IKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELT 225
                          250
                   ....*....|
gi 2065627291  747 DTINPYLLRR 756
Cdd:cd18066    226 RLTGLFILRR 235
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
518-758 1.08e-32

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: 127.44  E-value: 1.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrglnyrYEGL-GPVVIVCPATVMHQWVKEF 596
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKH-----------YRNIpGPHMVLVPKSTLHNWMNEF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAIL---HESGSFTTRKERLIREIAACngilVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVAC 673
Cdd:cd18065     85 KRWVPSLRAVCLigdKDARAAFIRDVMMPGEWDVC----VTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  674 KQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGyqnaspvqvqtaYKCACVLRDTINPYL 753
Cdd:cd18065    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD------------QKLVERLHAVLKPFL 228

                   ....*
gi 2065627291  754 LRRMK 758
Cdd:cd18065    229 LRRIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
518-756 1.68e-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: 126.85  E-value: 1.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSyskirtrglnYRYEGLGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLA----------EEHNIWGPFLVIAPASTLHNWQQEIS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVaiLHESGSFTTRK--------ERLIREIAACNgILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGV 669
Cdd:cd18002     71 RFVPQFKV--LPYWGNPKDRKvlrkfwdrKNLYTRDAPFH-VVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  670 TVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGyQNASPVQVQTAYKCACVLRdti 749
Cdd:cd18002    148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHA-ENKTGLNEHQLKRLHMILK--- 223

                   ....*..
gi 2065627291  750 nPYLLRR 756
Cdd:cd18002    224 -PFMLRR 229
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
518-756 1.12e-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: 120.24  E-value: 1.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFH 597
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAILHEsgsfttrkerlireiaacNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQ 677
Cdd:cd17994     71 MWAPDFYVVTYVG------------------DHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065627291  678 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPitmggyqnASPVQVQTaykcacvLRDTINPYLLRR 756
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADI--------SKEDQIKK-------LHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
518-756 1.78e-29

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: 118.19  E-value: 1.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFH 597
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHTKG---------PFLVSAPLSTIINWEREFQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRV----------AILHESgSFT---------TRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDE 658
Cdd:cd18055     71 MWAPDFYVvtytgdkdsrAIIREN-EFSfddnavkggKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  659 GHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSvpitmggyQNASPVQVQTa 738
Cdd:cd18055    150 AHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK- 220
                          250
                   ....*....|....*...
gi 2065627291  739 ykcacvLRDTINPYLLRR 756
Cdd:cd18055    221 ------LHDLLGPHMLRR 232
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1473-1546 1.94e-29

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: 112.22  E-value: 1.94e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065627291 1473 ISTEHDELLVEMRNFIAFQAsiDGQATTQELLQEFQAKLSTAQTVIFRELLINLCTFHRTASGEGTWKLKPAFR 1546
Cdd:cd22254      1 ASTEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
518-756 2.13e-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: 118.34  E-value: 2.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWElhCQQA-------GGILGDEMGLGKTIQIIAFL-AGLSYSKIRTRGLNyryeglgPVVIVCPATVM 589
Cdd:cd18067      1 LRPHQREGVKFLYR--CVTGrrirgshGCIMADEMGLGKTLQCITLMwTLLRQSPQCKPEID-------KAIVVSPSSLV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  590 HQWVKEFHTWWPPFRVAILHESGSFTTRKERLIREIAA-----CNGILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRN 664
Cdd:cd18067     72 KNWANELGKWLGGRLQPLAIDGGSKKEIDRKLVQWASQqgrrvSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  665 PNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGYQNASPVQVQTAYKCACV 744
Cdd:cd18067    152 SDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQE 231
                          250
                   ....*....|..
gi 2065627291  745 LRDTINPYLLRR 756
Cdd:cd18067    232 LISIVNRCIIRR 243
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
518-736 7.38e-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: 116.91  E-value: 7.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQ---------AGGILGDEMGLGKTIQIIAFLaglsyskiRTRGLNYRYEGLGPVVIVCPATV 588
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFL--------HTVLLCEKLENFSRVLVVCPLNT 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  589 MHQWVKEFHTWWPPFR---VAILHESGSFTTRKERLIR--EIAACNGILVTSYSYIRIM------------QESIGQYKW 651
Cdd:cd18068     73 VLNWLNEFEKWQEGLKdeeKIEVNELATYKRPQERSYKlqRWQEEGGVMIIGYDMYRILaqernvksreklKEIFNKALV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  652 H----YAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMGGY 727
Cdd:cd18068    153 DpgpdFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQC 232

                   ....*....
gi 2065627291  728 QNASPVQVQ 736
Cdd:cd18068    233 ADSTLVDVR 241
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
518-756 2.10e-28

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: 115.16  E-value: 2.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFH 597
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSL-YKEGHSKG---------PYLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRVAIL---HESGSFTTRKE---------------RLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEG 659
Cdd:cd18057     71 MWAPDFYVVTYtgdKESRSVIRENEfsfednairsgkkvfRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  660 HKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSvpitmggyQNASPVQVQTay 739
Cdd:cd18057    151 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 2065627291  740 kcacvLRDTINPYLLRR 756
Cdd:cd18057    221 -----LHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
517-717 3.40e-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: 3.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  517 KLYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglSYskirtrgLNYRYEGLGPVVIVCPATVMHQWVKEF 596
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL---NY-------LFHEHQLYGPFLLVVPLSTLTSWQREI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAILheSGSFTTRKerLIREIAACN--------GILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAG 668
Cdd:cd18053     90 QTWAPQMNAVVY--LGDINSRN--MIRTHEWMHpqtkrlkfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2065627291  669 VTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQ 717
Cdd:cd18053    166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEE 214
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
518-756 2.15e-27

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: 112.08  E-value: 2.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGlnyryeglgPVVIVCPATVMHQWVKEFH 597
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWWPPFRV----------AILHESG-SFT-------TRKERLIREIAACNGILVTSYSYIRIMQESIGQYKWHYAILDEG 659
Cdd:cd18056     71 MWAPDMYVvtyvgdkdsrAIIRENEfSFEdnairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  660 HKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFSvpitmggyQNASPVQVQTay 739
Cdd:cd18056    151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA--------DIAKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 2065627291  740 kcacvLRDTINPYLLRR 756
Cdd:cd18056    221 -----LHDMLGPHMLRR 232
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
518-710 6.79e-27

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: 109.99  E-value: 6.79e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRW-LwelhcqQAGG--ILGDEMGLGKTIQIIAFLAglsyskirtrglNYRYEglGPVVIVCPATVMHQWVK 594
Cdd:cd18010      1 LLPFQREGVCFaL------RRGGrvLIADEMGLGKTVQAIAIAA------------YYREE--WPLLIVCPSSLRLTWAD 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  595 EFHTWwppFRVAILHESGSFTTRKERLIREIAAcngILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACK 674
Cdd:cd18010     61 EIERW---LPSLPPDDIQVIVKSKDGLRDGDAK---VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAAL 134
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2065627291  675 QF--QTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGT 710
Cdd:cd18010    135 PLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGR 172
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
518-718 9.99e-26

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: 107.05  E-value: 9.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGLNyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFL-----SEIFLMGIR------GPFLIIAPLSTITNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWwPPFRVAILHesGSFTTRKERLIREIAACNG------------ILVTSYSYIRIMQESIGQYKWHYAILDEGHKIRNP 665
Cdd:cd18058     70 TW-TEMNAIVYH--GSQISRQMIQQYEMYYRDEqgnplsgifkfqVVITTFEMILADCPELKKINWSCVIIDEAHRLKNR 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2065627291  666 NAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQF 718
Cdd:cd18058    147 NCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
851-964 5.47e-25

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: 100.75  E-value: 5.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  851 GKMIVVEALLRlwHKQGHRVLLFSQSRQLLNImEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLflLTTRVGG 930
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVL--VATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2065627291  931 LGINLTGANRVIIYDPDWNPSTDTQARERAWRIG 964
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
518-756 5.49e-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: 104.73  E-value: 5.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGLNyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-----YEIYLKGIH------GPFLVIAPLSTIPNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWwPPFRVAILHesGSFTTRKE-------------RLIREIAACNGIlVTSYSYIRIMQESIGQYKWHYAILDEGHKIRN 664
Cdd:cd18059     70 TW-TELNVVVYH--GSQASRRTiqlyemyfkdpqgRVIKGSYKFHAI-ITTFEMILTDCPELRNIPWRCVVIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  665 PNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFsvpitmGGYQNASPVQvqtaykcacV 744
Cdd:cd18059    146 RNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF------GDLKTEEQVQ---------K 210
                          250
                   ....*....|..
gi 2065627291  745 LRDTINPYLLRR 756
Cdd:cd18059    211 LQAILKPMMLRR 222
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
538-725 1.45e-24

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: 104.09  E-value: 1.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  538 GGILGDEMGLGKTIQIIAFLAGlsyskirtrglnyryeglGPVVIVCPATVMHQWVKEF--HTWWPPFRVAILHesGSFT 615
Cdd:cd18071     50 GGILADDMGLGKTLTTISLILA------------------NFTLIVCPLSVLSNWETQFeeHVKPGQLKVYTYH--GGER 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  616 TRKERLIREiaacNGILVTSYS-----YIRIMQESIGQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQ 690
Cdd:cd18071    110 NRDPKLLSK----YDIVLTTYNtlasdFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQ 185
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2065627291  691 NNLKELWSLFDFVFPGKLGTLQVFMEQFSVPITMG 725
Cdd:cd18071    186 NSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMG 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
518-756 3.25e-24

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


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 102.82  E-value: 3.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrglnyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIH-----------GPFLVIAPLSTITNWEREFN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWwPPFRVAILHesGSFTTR-------------KERLIREIAACNGiLVTSYSYIRIMQESIGQYKWHYAILDEGHKIRN 664
Cdd:cd18060     70 TW-TEMNTIVYH--GSLASRqmiqqyemyckdsRGRLIPGAYKFDA-LITTFEMILSDCPELREIEWRCVIIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  665 PNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFsvpitmGGYQNASPVQvqtaykcacV 744
Cdd:cd18060    146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF------GDLKTEEQVQ---------K 210
                          250
                   ....*....|..
gi 2065627291  745 LRDTINPYLLRR 756
Cdd:cd18060    211 LQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
518-756 8.67e-24

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: 101.62  E-value: 8.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrglnyryeglGPVVIVCPATVMHQWVKEFH 597
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIR-----------GPFLIIAPLSTIANWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  598 TWwPPFRVAILHesGSFTTRKE-------------RLIREIAACNGIlVTSYSYIRIMQESIGQYKWHYAILDEGHKIRN 664
Cdd:cd18061     70 TW-TDLNVVVYH--GSLISRQMiqqyemyfrdsqgRIIRGAYRFQAI-ITTFEMILGGCPELNAIDWRCVIIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  665 PNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLQVFMEQFsvpitmGGYQNASPVQvqtaykcacV 744
Cdd:cd18061    146 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF------GDLKTEEQVQ---------K 210
                          250
                   ....*....|..
gi 2065627291  745 LRDTINPYLLRR 756
Cdd:cd18061    211 LQAILKPMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
510-703 1.08e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 100.64  E-value: 1.08e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291   510 VPGFLWRKLYKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgLNYRYEGLGPVVIVCP-ATV 588
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPtREL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291   589 MHQWVKEFHTWWPPFRVAILHESGSfTTRKERLIREIAACNGILVTSYSYIR--IMQESIGQYKWHYAILDEGHKIRNPN 666
Cdd:smart00487   67 AEQWAEELKKLGPSLGLKVVGLYGG-DSKREQLRKLESGKTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 2065627291   667 AGVTVACKQFQTP---HRIILSGSP---MQNNLKELWSLFDFV 703
Cdd:smart00487  146 FGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFI 188
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
518-703 1.30e-23

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 101.40  E-value: 1.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWL-WELHCQQAGGILGDEMGLGKTIQIIAFL---------AGLSYSKIRTRGLNYRYEGLGP---VVIVC 584
Cdd:cd18072      1 LLLHQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIALIlaqkntqnrKEEEKEKALTEWESKKDSTLVPsagTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  585 PATVMHQWVKEF--HTWWPPFRVAILHesGSFTTRKERLIREIaacnGILVTSYSYI-----RIMQES----IGQYKWHY 653
Cdd:cd18072     81 PASLVHQWKNEVesRVASNKLRVCLYH--GPNRERIGEVLRDY----DIVITTYSLVakeipTYKEESrsspLFRIAWAR 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2065627291  654 AILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDFV 703
Cdd:cd18072    155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
HELICc smart00490
helicase superfamily c-terminal domain;
882-964 2.81e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 80.72  E-value: 2.81e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291   882 IMEMFVRNLGYSYVKMDGTTAVASRQPLISKYNENASIFLflLTTRVGGLGINLTGANRVIIYDPDWNPSTDTQARERAW 961
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVL--VATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                    ...
gi 2065627291   962 RIG 964
Cdd:smart00490   80 RAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
518-699 5.41e-17

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: 81.18  E-value: 5.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWELhcQQAGGILGDEMGLGKTIQiiaflAGLSYSKIRTRGLnyryegLGPVVIVCPATVMHQWVKE-F 596
Cdd:cd18011      1 PLPHQIDAVLRALRK--PPVRLLLADEVGLGKTIE-----AGLIIKELLLRGD------AKRVLILCPASLVEQWQDElQ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPFRVAilheSGSFTTRKERLIREIAACNGILVTSYSYIRIMQESIGQYK---WHYAILDEGHKIRNPNAGVTVAC 673
Cdd:cd18011     68 DKFGLPFLIL----DRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRNSGGGKETKR 143
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2065627291  674 KQF------QTPHRIILSGSPMQNNLKELWSL 699
Cdd:cd18011    144 YKLgrllakRARHVLLLTATPHNGKEEDFRAL 175
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
518-702 1.00e-15

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 78.92  E-value: 1.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWElhcqqAGGILGDEMGLGKTIQIIAFLA---------GLSYSKIRTRGLNYRYEGLGPVV------I 582
Cdd:cd18070      1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILlhprpdndlDAADDDSDEMVCCPDCLVAETPVsskatlI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  583 VCPATVMHQWVKEFHTWWPP-FRVAI---LHESGSF---------------TT----RKERLIREIAACNGILVTSYSYI 639
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSsLKVLTyqgVKKDGALaspapeilaeydivvTTydvlRTELHYAEANRSNRRRRRQKRYE 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065627291  640 RIMQESIgQYKWHYAILDEGHKIRNPNAGVTVACKQFQTPHRIILSGSPMQNNLKELWSLFDF 702
Cdd:cd18070    156 APPSPLV-LVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSF 217
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
910-967 1.01e-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: 50.78  E-value: 1.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2065627291  910 ISKYNENASIFLFLLTTRVGGLGINLTGANRVIIYDPDWNPSTDTQARERAWRIGQKK 967
Cdd:cd18785     13 IEHAEEIASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
518-728 1.29e-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: 53.89  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  518 LYKYQQTGVRWLWElhcQQAGGILGDeMGLGKTIqiiAFLAGLSYSKIRtrglnyryEGLGPVVIVCPATVM-HQWVKEF 596
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTV---TTLTALSDLQLD--------DFTRRVLVIAPLRVArSTWPDEV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065627291  597 HTWWPPF--RVAILHESGsfttrKERlireIAACNG---ILVTSYSYIR-IMQESIGQYKWHYAILDEGHKIRNPNAGVT 670
Cdd:cd18013     66 EKWNHLRnlTVSVAVGTE-----RQR----SKAANTpadLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFKSPRSKRF 136
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065627291  671 VACKQ--FQTPHRIILSGSPMQNNLKELWSLFDFVFPGK-LG-TLQVFMEQFSVPITMGGYQ 728
Cdd:cd18013    137 KALRKvrPVIKRLIGLTGTPSPNGLMDLWAQIALLDQGErLGrSITAYRERWFDPDKRNGQQ 198
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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