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Conserved domains on  [gi|24644932|ref|NP_524850|]
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lodestar [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
439-686 2.97e-141

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: 423.43  E-value: 2.97e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKLPRGGILADDMGLGKTLTMISSVLACKNGQEMSEGKdessdsdseddknKKRKSVTGWKSKG 518
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEE-------------KEKALTEWESKKD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 RKDTRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVAREHKSL------SAV 592
Cdd:cd18072   68 STLVPSAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYkeesrsSPL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  593 FGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ 672
Cdd:cd18072  148 FRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG 227
                        250
                 ....*....|....
gi 24644932  673 NRLNLLMKSLMLRR 686
Cdd:cd18072  228 ERLNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
287-1041 1.88e-120

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 385.35  E-value: 1.88e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  287 VSQVVYDEEMRKLAEKRVQVSDAEKLFEKVAHKLPDKGSQIMKRIDTLRRELAMDEQWISALRVQQSNVPAVRVVKPTLN 366
Cdd:COG0553   77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  367 PPRAPSIDTLDWDELSEAVNEIKPVYTGAQGMATFNNQKALTLESLKDLHVSLEDLPGPEV-------------LAEDPV 433
Cdd:COG0553  157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAavdafrlrrlreaLESLPA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  434 GLKVSLMNHQKHALAWMsWRERKLPRGGILADDMGLGKTLTMISSVLACKNgqemsegkdessdsdseddknkkrksvtg 513
Cdd:COG0553  237 GLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKE----------------------------- 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  514 wkskgRKDTRRggTLVVCPASLLRQWESEVEskvsR--QKLTVCVHHG-NNRETKGKYLRDYDIVVTTYQIVAREHKSLS 590
Cdd:COG0553  287 -----RGLARP--VLIVAPTSLVGNWQRELA----KfaPGLRVLVLDGtRERAKGANPFEDADLVITSYGLLRRDIELLA 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  591 AVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRcsPfDDLHTWKKW------- 663
Cdd:COG0553  356 AV---DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN--P-GLLGSLKAFrerfarp 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  664 IDNKSAGGQNRLNLLMKSLMLRRTKAQLQSDgklnsLPNKELRLIEISLDKEEMNVYQTVMTYSRtlfaqflhqraeret 743
Cdd:COG0553  430 IEKGDEEALERLRRLLRPFLLRRTKEDVLKD-----LPEKTEETLYVELTPEQRALYEAVLEYLR--------------- 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  744 dfnyrsdankptynqikdpngayykmhekfARMAGSKKEVKSHDILVLLLRLRQICCHPGLidamldgeesqtmgdhssd 823
Cdd:COG0553  490 ------------------------------RELEGAEGIRRRGLILAALTRLRQICSHPAL------------------- 520
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  824 sdtpeidllaqlnklaitdtstdgqqsvanagddgppLLPDEARIAkasknllkrsnpvfnlhRPSSKINMVIQILKTsi 903
Cdd:COG0553  521 -------------------------------------LLEEGAELS-----------------GRSAKLEALLELLEE-- 544
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  904 LKSSDDKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDRNNqKRVLLLSLTAGGVGLNLIGANHL 983
Cdd:COG0553  545 LLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPE-APVFLISLKAGGEGLNLTAADHV 623
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644932  984 LLLDLHWNPQLEAQAQDRIYRVGQKKNVIIYKFMCVDTVEQRIKGLQDKKLDLADGVL 1041
Cdd:COG0553  624 IHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
439-686 2.97e-141

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: 423.43  E-value: 2.97e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKLPRGGILADDMGLGKTLTMISSVLACKNGQEMSEGKdessdsdseddknKKRKSVTGWKSKG 518
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEE-------------KEKALTEWESKKD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 RKDTRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVAREHKSL------SAV 592
Cdd:cd18072   68 STLVPSAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYkeesrsSPL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  593 FGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ 672
Cdd:cd18072  148 FRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG 227
                        250
                 ....*....|....
gi 24644932  673 NRLNLLMKSLMLRR 686
Cdd:cd18072  228 ERLNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
287-1041 1.88e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 385.35  E-value: 1.88e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  287 VSQVVYDEEMRKLAEKRVQVSDAEKLFEKVAHKLPDKGSQIMKRIDTLRRELAMDEQWISALRVQQSNVPAVRVVKPTLN 366
Cdd:COG0553   77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  367 PPRAPSIDTLDWDELSEAVNEIKPVYTGAQGMATFNNQKALTLESLKDLHVSLEDLPGPEV-------------LAEDPV 433
Cdd:COG0553  157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAavdafrlrrlreaLESLPA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  434 GLKVSLMNHQKHALAWMsWRERKLPRGGILADDMGLGKTLTMISSVLACKNgqemsegkdessdsdseddknkkrksvtg 513
Cdd:COG0553  237 GLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKE----------------------------- 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  514 wkskgRKDTRRggTLVVCPASLLRQWESEVEskvsR--QKLTVCVHHG-NNRETKGKYLRDYDIVVTTYQIVAREHKSLS 590
Cdd:COG0553  287 -----RGLARP--VLIVAPTSLVGNWQRELA----KfaPGLRVLVLDGtRERAKGANPFEDADLVITSYGLLRRDIELLA 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  591 AVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRcsPfDDLHTWKKW------- 663
Cdd:COG0553  356 AV---DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN--P-GLLGSLKAFrerfarp 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  664 IDNKSAGGQNRLNLLMKSLMLRRTKAQLQSDgklnsLPNKELRLIEISLDKEEMNVYQTVMTYSRtlfaqflhqraeret 743
Cdd:COG0553  430 IEKGDEEALERLRRLLRPFLLRRTKEDVLKD-----LPEKTEETLYVELTPEQRALYEAVLEYLR--------------- 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  744 dfnyrsdankptynqikdpngayykmhekfARMAGSKKEVKSHDILVLLLRLRQICCHPGLidamldgeesqtmgdhssd 823
Cdd:COG0553  490 ------------------------------RELEGAEGIRRRGLILAALTRLRQICSHPAL------------------- 520
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  824 sdtpeidllaqlnklaitdtstdgqqsvanagddgppLLPDEARIAkasknllkrsnpvfnlhRPSSKINMVIQILKTsi 903
Cdd:COG0553  521 -------------------------------------LLEEGAELS-----------------GRSAKLEALLELLEE-- 544
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  904 LKSSDDKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDRNNqKRVLLLSLTAGGVGLNLIGANHL 983
Cdd:COG0553  545 LLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPE-APVFLISLKAGGEGLNLTAADHV 623
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644932  984 LLLDLHWNPQLEAQAQDRIYRVGQKKNVIIYKFMCVDTVEQRIKGLQDKKLDLADGVL 1041
Cdd:COG0553  624 IHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
442-805 1.09e-96

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: 308.07  E-value: 1.09e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    442 HQKHALAWMSWRERKLPRGGILADDMGLGKTLTMISSVLACKNGQEMsegkdessdsdseddknkkrksvtgwkskgrkd 521
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKN--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    522 tRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRET-----KGKYLRDYDIVVTTYQIVaREHKSLSAVfgVK 596
Cdd:pfam00176   48 -WGGPTLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQerwknDPNFLADFDVVITTYETL-RKHKELLKK--VH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    597 WRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDN-----KSAGG 671
Cdd:pfam00176  124 WHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKG 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    672 QNRLNLLMKSLMLRRTKAQLQSdgklnSLPNKELRLIEISLDKEEMNVYQTVMTysrtlfaqflhqraeretdfnyrsda 751
Cdd:pfam00176  204 VSRLHKLLKPFLLRRTKKDVEK-----SLPPKVEYILFCRLSKLQRKLYQTFLL-------------------------- 252
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24644932    752 nKPTYNQIKDpngayykmhekfarmaGSKKEVKSHDILVLLLRLRQICCHPGLI 805
Cdd:pfam00176  253 -KKDLNAIKT----------------GEGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
889-1017 2.56e-51

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: 176.51  E-value: 2.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  889 SSKINMVIQILKTsiLKSSDDKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDrNNQKRVLLLSL 968
Cdd:cd18793   10 SGKLEALLELLEE--LREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLST 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24644932  969 TAGGVGLNLIGANHLLLLDLHWNPQLEAQAQDRIYRVGQKKNVIIYKFM 1017
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
447-1036 1.07e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 159.97  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   447 LAWMSWRERKLPRG--GILADDMGLGKTLTMISSVlackngqemsegkdessdsdseddknkkrksvtGWKSKGRKDTrr 524
Cdd:PLN03142  175 LAGLNWLIRLYENGinGILADEMGLGKTLQTISLL---------------------------------GYLHEYRGIT-- 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   525 GGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHGNNRETKgkYLRD-------YDIVVTTYQIVAREHKSLSAVfgvKW 597
Cdd:PLN03142  220 GPHMVVAPKSTLGNWMNEIRRFCP--VLRAVKFHGNPEERA--HQREellvagkFDVCVTSFEMAIKEKTALKRF---SW 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   598 RRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ----N 673
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevvQ 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   674 RLNLLMKSLMLRRTKAQLQSdgklnSLPNKELRLIEISLDKEEMNVYqtvmtysrtlfaqflhqRAERETDfnyrsdank 753
Cdd:PLN03142  373 QLHKVLRPFLLRRLKSDVEK-----GLPPKKETILKVGMSQMQKQYY-----------------KALLQKD--------- 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   754 ptynqIKDPNGAyykmhekfarmaGSKKEvkshdILVLLLRLRQICCHPGLidamLDGEESqtmgdhssdsdtpeidlla 833
Cdd:PLN03142  422 -----LDVVNAG------------GERKR-----LLNIAMQLRKCCNHPYL----FQGAEP------------------- 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   834 qlnklaitdtstdgqqsvanagddGPPLLPDEARIAKASK-----NLLKRsnpvfnlhrpsskinmviqilktsiLKSSD 908
Cdd:PLN03142  457 ------------------------GPPYTTGEHLVENSGKmvlldKLLPK-------------------------LKERD 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   909 DKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDRNNQKRVLLLSLTAGGVGLNLIGANHLLLLDL 988
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 24644932   989 HWNPQLEAQAQDRIYRVGQKKNVIIYKFMCVDTVEQRIKGLQDKKLDL 1036
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
DEXDc smart00487
DEAD-like helicases superfamily;
439-647 1.15e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.10  E-value: 1.15e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     439 LMNHQKHALAWMswreRKLPRGGILADDMGLGKTLTMISSVLACKngqemsegkdessdsdseddknkkrksvtgwkskg 518
Cdd:smart00487    9 LRPYQKEAIEAL----LSGLRDVILAAPTGSGKTLAALLPALEAL----------------------------------- 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     519 rKDTRRGGTLVVCP-ASLLRQWESEVESKVSRQKL-TVCVHHGNNRETKGKYLR--DYDIVVTTYQIVAReHKSLSAVFG 594
Cdd:smart00487   50 -KRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGLkVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLD-LLENDKLSL 127
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644932     595 VKWRRIILDEAHVVRN--HKSQSSLAVCDLRGK-YRWALTGTPIQNKELDVYALLK 647
Cdd:smart00487  128 SNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNvQLLLLSATPPEEIENLLELFLN 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
890-1006 1.28e-19

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: 84.95  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    890 SKINMVIQILKtsilKSSDDKAIVVSQWTSVLDIlRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNdrnNQKRVLLLSLT 969
Cdd:pfam00271    1 EKLEALLELLK----KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATD 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 24644932    970 AGGVGLNLIGANHLLLLDLHWNPQLEAQAQDRIYRVG 1006
Cdd:pfam00271   73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
922-1006 7.07e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 73.40  E-value: 7.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     922 DILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNdrnNQKRVLLLSLTAGGVGLNLIGANHLLLLDLHWNPQLEAQAQDR 1001
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 24644932    1002 IYRVG 1006
Cdd:smart00490   78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
428-634 7.72e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 62.73  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  428 LAEDPVGLKVSLMNHQKHAL-AWMSWRERKlPRGGILADDMGLGKTLTMISSVLACKNGQEmsegkdessdsdseddknk 506
Cdd:COG1061   70 AGDEASGTSFELRPYQQEALeALLAALERG-GGRGLVVAPTGTGKTVLALALAAELLRGKR------------------- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  507 krksvtgwkskgrkdtrrggTLVVCP-ASLLRQWESEVeskvsRQKLTVCVHHGNNREtkgkylRDYDIVVTTYQIVAR- 584
Cdd:COG1061  130 --------------------VLVLVPrRELLEQWAEEL-----RRFLGDPLAGGGKKD------SDAPITVATYQSLARr 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24644932  585 -EHKSLSAVFGVkwrrIILDEAHVVRnhkSQSSLAVCD-LRGKYRWALTGTP 634
Cdd:COG1061  179 aHLDELGDRFGL----VIIDEAHHAG---APSYRRILEaFPAAYRLGLTATP 223
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
439-686 2.97e-141

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: 423.43  E-value: 2.97e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKLPRGGILADDMGLGKTLTMISSVLACKNGQEMSEGKdessdsdseddknKKRKSVTGWKSKG 518
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEE-------------KEKALTEWESKKD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 RKDTRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVAREHKSL------SAV 592
Cdd:cd18072   68 STLVPSAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYkeesrsSPL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  593 FGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ 672
Cdd:cd18072  148 FRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG 227
                        250
                 ....*....|....
gi 24644932  673 NRLNLLMKSLMLRR 686
Cdd:cd18072  228 ERLNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
287-1041 1.88e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 385.35  E-value: 1.88e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  287 VSQVVYDEEMRKLAEKRVQVSDAEKLFEKVAHKLPDKGSQIMKRIDTLRRELAMDEQWISALRVQQSNVPAVRVVKPTLN 366
Cdd:COG0553   77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  367 PPRAPSIDTLDWDELSEAVNEIKPVYTGAQGMATFNNQKALTLESLKDLHVSLEDLPGPEV-------------LAEDPV 433
Cdd:COG0553  157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAavdafrlrrlreaLESLPA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  434 GLKVSLMNHQKHALAWMsWRERKLPRGGILADDMGLGKTLTMISSVLACKNgqemsegkdessdsdseddknkkrksvtg 513
Cdd:COG0553  237 GLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKE----------------------------- 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  514 wkskgRKDTRRggTLVVCPASLLRQWESEVEskvsR--QKLTVCVHHG-NNRETKGKYLRDYDIVVTTYQIVAREHKSLS 590
Cdd:COG0553  287 -----RGLARP--VLIVAPTSLVGNWQRELA----KfaPGLRVLVLDGtRERAKGANPFEDADLVITSYGLLRRDIELLA 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  591 AVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRcsPfDDLHTWKKW------- 663
Cdd:COG0553  356 AV---DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN--P-GLLGSLKAFrerfarp 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  664 IDNKSAGGQNRLNLLMKSLMLRRTKAQLQSDgklnsLPNKELRLIEISLDKEEMNVYQTVMTYSRtlfaqflhqraeret 743
Cdd:COG0553  430 IEKGDEEALERLRRLLRPFLLRRTKEDVLKD-----LPEKTEETLYVELTPEQRALYEAVLEYLR--------------- 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  744 dfnyrsdankptynqikdpngayykmhekfARMAGSKKEVKSHDILVLLLRLRQICCHPGLidamldgeesqtmgdhssd 823
Cdd:COG0553  490 ------------------------------RELEGAEGIRRRGLILAALTRLRQICSHPAL------------------- 520
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  824 sdtpeidllaqlnklaitdtstdgqqsvanagddgppLLPDEARIAkasknllkrsnpvfnlhRPSSKINMVIQILKTsi 903
Cdd:COG0553  521 -------------------------------------LLEEGAELS-----------------GRSAKLEALLELLEE-- 544
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  904 LKSSDDKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDRNNqKRVLLLSLTAGGVGLNLIGANHL 983
Cdd:COG0553  545 LLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPE-APVFLISLKAGGEGLNLTAADHV 623
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644932  984 LLLDLHWNPQLEAQAQDRIYRVGQKKNVIIYKFMCVDTVEQRIKGLQDKKLDLADGVL 1041
Cdd:COG0553  624 IHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
442-805 1.09e-96

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: 308.07  E-value: 1.09e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    442 HQKHALAWMSWRERKLPRGGILADDMGLGKTLTMISSVLACKNGQEMsegkdessdsdseddknkkrksvtgwkskgrkd 521
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKN--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    522 tRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRET-----KGKYLRDYDIVVTTYQIVaREHKSLSAVfgVK 596
Cdd:pfam00176   48 -WGGPTLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQerwknDPNFLADFDVVITTYETL-RKHKELLKK--VH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    597 WRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDN-----KSAGG 671
Cdd:pfam00176  124 WHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKG 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    672 QNRLNLLMKSLMLRRTKAQLQSdgklnSLPNKELRLIEISLDKEEMNVYQTVMTysrtlfaqflhqraeretdfnyrsda 751
Cdd:pfam00176  204 VSRLHKLLKPFLLRRTKKDVEK-----SLPPKVEYILFCRLSKLQRKLYQTFLL-------------------------- 252
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24644932    752 nKPTYNQIKDpngayykmhekfarmaGSKKEVKSHDILVLLLRLRQICCHPGLI 805
Cdd:pfam00176  253 -KKDLNAIKT----------------GEGGREIKASLLNILMRLRKICNHPGLI 289
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
439-686 5.48e-87

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: 279.94  E-value: 5.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMswrerkLPRGGILADDMGLGKTLTMISSVLACKNGqemsegkdessdsdseddKNKKRKSVTGWKSKG 518
Cdd:cd18008    1 LLPYQKQGLAWM------LPRGGILADEMGLGKTIQALALILATRPQ------------------DPKIPEELEENSSDP 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 RKDTRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVAREH------------ 586
Cdd:cd18008   57 KKLYLSKTTLIVVPLSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFpknkkgggrdsk 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  587 -KSLSAVFGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWI- 664
Cdd:cd18008  137 eKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDIs 216
                        250       260
                 ....*....|....*....|....*
gi 24644932  665 ---DNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18008  217 kpfSKNDRKALERLQALLKPILLRR 241
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
439-686 2.07e-57

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: 198.08  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRE-------------------------RKLP---RGGILADDMGLGKTLTMISSVLACKngqemse 490
Cdd:cd18071    1 LLPHQKQALAWMVSREnsqdlppfweeavglflntitnfsqKKRPelvRGGILADDMGLGKTLTTISLILANF------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  491 gkdessdsdseddknkkrksvtgwkskgrkdtrrggTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLR 570
Cdd:cd18071   74 ------------------------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLS 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  571 DYDIVVTTYQIVAREH--KSLSAVFGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKF 648
Cdd:cd18071  118 KYDIVLTTYNTLASDFgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 24644932  649 LRCSPFDDLHTWKKWIDNK----SAGGQNRLNLLMKSLMLRR 686
Cdd:cd18071  198 LHLKPFSNPEYWRRLIQRPltmgDPTGLKRLQVLMKQITLRR 239
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
889-1017 2.56e-51

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: 176.51  E-value: 2.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  889 SSKINMVIQILKTsiLKSSDDKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDrNNQKRVLLLSL 968
Cdd:cd18793   10 SGKLEALLELLEE--LREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLST 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24644932  969 TAGGVGLNLIGANHLLLLDLHWNPQLEAQAQDRIYRVGQKKNVIIYKFM 1017
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
439-654 9.64e-47

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: 165.43  E-value: 9.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKlPRGGILADDMGLGKTLTMISsVLAckngqemsegkdessdsdseddknkkrksvtgWKSKG 518
Cdd:cd17919    1 LRPYQLEGLNFLLELYEN-GPGGILADEMGLGKTLQAIA-FLA--------------------------------YLLKE 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 RKDTRRggTLVVCPASLLRQWESEVEsKVSRQkLTVCVHHGNNRE----TKGKYLRDYDIVVTTYQIVAREHKSLSAVfg 594
Cdd:cd17919   47 GKERGP--VLVVCPLSVLENWEREFE-KWTPD-LRVVVYHGSQREraqiRAKEKLDKFDVVLTTYETLRRDKASLRKF-- 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  595 vKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCsPF 654
Cdd:cd17919  121 -RWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP-PF 178
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
439-685 1.68e-44

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: 161.74  E-value: 1.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMswrerkLPRGGILADDMGLGKTLTMISSVLACKNGQEMSEGKDESSDSDSEDDKNKKRKSVTGWKSkg 518
Cdd:cd18070    1 LLPYQRRAVNWM------LVPGGILADEMGLGKTVEVLALILLHPRPDNDLDAADDDSDEMVCCPDCLVAETPVSSKA-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 rkdtrrggTLVVCPASLLRQWESEVEsKVSRQKLTVCVHHGNNRETKGK-----YLRDYDIVVTTYQIVARE-------H 586
Cdd:cd18070   73 --------TLIVCPSAILAQWLDEIN-RHVPSSLKVLTYQGVKKDGALAspapeILAEYDIVVTTYDVLRTElhyaeanR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  587 KSL------------SAVFGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPF 654
Cdd:cd18070  144 SNRrrrrqkryeappSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPF 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 24644932  655 DDLHTWKK-WIDN-KSAGGQNRLNLLMKSLMLR 685
Cdd:cd18070  224 CDSDWWARvLIRPqGRNKAREPLAALLKELLWR 256
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
435-688 1.31e-43

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: 157.73  E-value: 1.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  435 LKVSLMNHQKHALAWMSwRERKLPRGGILADDMGLGKTLTMISSVLACKNgqemsegkdessdsdseddKNKKRKSvtgw 514
Cdd:cd18012    1 LKATLRPYQKEGFNWLS-FLRHYGLGGILADDMGLGKTLQTLALLLSRKE-------------------EGRKGPS---- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  515 kskgrkdtrrggtLVVCPASLLRQWESEVeskvsrQK----LTVCVHHGNNRETKGKY-LRDYDIVVTTYQIVAREHKSL 589
Cdd:cd18012   57 -------------LVVAPTSLIYNWEEEA------AKfapeLKVLVIHGTKRKREKLRaLEDYDLVITSYGLLRRDIELL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  590 SAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLrcSP--------FDDLhtWK 661
Cdd:cd18012  118 KEV---KFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPgllgsykrFKKR--FA 190
                        250       260
                 ....*....|....*....|....*...
gi 24644932  662 KWIDN-KSAGGQNRLNLLMKSLMLRRTK 688
Cdd:cd18012  191 KPIEKdGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
447-1036 1.07e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 159.97  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   447 LAWMSWRERKLPRG--GILADDMGLGKTLTMISSVlackngqemsegkdessdsdseddknkkrksvtGWKSKGRKDTrr 524
Cdd:PLN03142  175 LAGLNWLIRLYENGinGILADEMGLGKTLQTISLL---------------------------------GYLHEYRGIT-- 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   525 GGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHGNNRETKgkYLRD-------YDIVVTTYQIVAREHKSLSAVfgvKW 597
Cdd:PLN03142  220 GPHMVVAPKSTLGNWMNEIRRFCP--VLRAVKFHGNPEERA--HQREellvagkFDVCVTSFEMAIKEKTALKRF---SW 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   598 RRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ----N 673
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevvQ 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   674 RLNLLMKSLMLRRTKAQLQSdgklnSLPNKELRLIEISLDKEEMNVYqtvmtysrtlfaqflhqRAERETDfnyrsdank 753
Cdd:PLN03142  373 QLHKVLRPFLLRRLKSDVEK-----GLPPKKETILKVGMSQMQKQYY-----------------KALLQKD--------- 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   754 ptynqIKDPNGAyykmhekfarmaGSKKEvkshdILVLLLRLRQICCHPGLidamLDGEESqtmgdhssdsdtpeidlla 833
Cdd:PLN03142  422 -----LDVVNAG------------GERKR-----LLNIAMQLRKCCNHPYL----FQGAEP------------------- 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   834 qlnklaitdtstdgqqsvanagddGPPLLPDEARIAKASK-----NLLKRsnpvfnlhrpsskinmviqilktsiLKSSD 908
Cdd:PLN03142  457 ------------------------GPPYTTGEHLVENSGKmvlldKLLPK-------------------------LKERD 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932   909 DKAIVVSQWTSVLDILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNDRNNQKRVLLLSLTAGGVGLNLIGANHLLLLDL 988
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 24644932   989 HWNPQLEAQAQDRIYRVGQKKNVIIYKFMCVDTVEQRIKGLQDKKLDL 1036
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
439-649 1.92e-32

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: 126.31  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRER-KLprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdsedDKNKKRKSvtgwksk 517
Cdd:cd17999    1 LRPYQQEGINWLAFLNKyNL--HGILCDDMGLGKTLQTLCILASDHHKRANS-------------FNSENLPS------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 grkdtrrggtLVVCPASLLRQWESEVESKVSRQKLTVCVHHG--NNRETKGKYLRDYDIVVTTYQIVAREHKSLSAVFgv 595
Cdd:cd17999   59 ----------LVVCPPTLVGHWVAEIKKYFPNAFLKPLAYVGppQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIE-- 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24644932  596 kWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFL 649
Cdd:cd17999  127 -WNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL 179
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
439-686 1.00e-31

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: 124.41  E-value: 1.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKlPRGGILADDMGLGKTLTMISSVLAC--KNGQEmsegkdessdsdSEDDKNKKRKsvtgwKS 516
Cdd:cd18005    1 LRDYQREGVEFMYDLYKN-GRGGILGDDMGLGKTVQVIAFLAAVlgKTGTR------------RDRENNRPRF-----KK 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 KGRKDTRRGGTLVVCPASLLRQWESEVESKVSrqkLTVCVHHGNNR--ETKGKY-LRDYDIVVTTYQIVAREHKSLSavf 593
Cdd:cd18005   63 KPPASSAKKPVLIVAPLSVLYNWKDELDTWGH---FEVGVYHGSRKddELEGRLkAGRLEVVVTTYDTLRRCIDSLN--- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  594 GVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQN 673
Cdd:cd18005  137 SINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQR 216
                        250       260
                 ....*....|....*....|....*....
gi 24644932  674 R----------------LNLLMKSLMLRR 686
Cdd:cd18005  217 HtatarelrlgrkrkqeLAVKLSKFFLRR 245
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
439-649 1.72e-31

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: 123.25  E-value: 1.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMsWRERKLPRGGILADDMGLGKTLTMISSVlackngQEMSEGKDEssdsdseddknkkrKSVtgwkskg 518
Cdd:cd18001    1 LYPHQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAFL------SGMFDSGLI--------------KSV------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 rkdtrrggtLVVCPASLLRQWESEVESKVSRqkLTVCVHHGNNRETKGKYL----RDYDIVVTTYQIVAREHKSLSAVF- 593
Cdd:cd18001   53 ---------LVVMPTSLIPHWVKEFAKWTPG--LRVKVFHGTSKKERERNLeriqRGGGVLLTTYGMVLSNTEQLSADDh 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24644932  594 -GVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFL 649
Cdd:cd18001  122 dEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
439-688 3.05e-30

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: 119.35  E-value: 3.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISsvlackngqemsegkdessdsdseddknkkrksVTGWKSK 517
Cdd:cd17997    4 MRDYQIRGLNWLiSLFENGI--NGILADEMGLGKTLQTIS---------------------------------LLGYLKH 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 GRKDTrrGGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHGNnRETKGKYLRD------YDIVVTTYQIVAREHKSLSA 591
Cdd:cd17997   49 YKNIN--GPHLIIVPKSTLDNWMREFKRWCP--SLRVVVLIGD-KEERADIIRDvllpgkFDVCITSYEMVIKEKTVLKK 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  592 VfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGG 671
Cdd:cd17997  124 F---NWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDD 200
                        250       260
                 ....*....|....*....|..
gi 24644932  672 QN-----RLNLLMKSLMLRRTK 688
Cdd:cd17997  201 DNqevvqRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
439-686 1.12e-27

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: 112.06  E-value: 1.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMIS--SVLACKNGQemsegkdessdsdseddknkkrksvtgWk 515
Cdd:cd18003    1 LREYQHIGLDWLaTLYEKNL--NGILADEMGLGKTIQTIAllAHLACEKGN---------------------------W- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  516 skgrkdtrrGGTLVVCPASLLRQWESEVeskvsrQK----LTVCVHHGNNRETKGKY-----LRDYDIVVTTYQIVAREH 586
Cdd:cd18003   51 ---------GPHLIVVPTSVMLNWEMEF------KRwcpgFKILTYYGSAKERKLKRqgwmkPNSFHVCITSYQLVVQDH 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  587 KSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDN 666
Cdd:cd18003  116 QVFKRK---KWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSN 192
                        250       260       270
                 ....*....|....*....|....*....|.
gi 24644932  667 K----SAGGQN-------RLNLLMKSLMLRR 686
Cdd:cd18003  193 PltamSEGSQEeneelvrRLHKVLRPFLLRR 223
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
439-686 1.01e-26

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: 109.26  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMS--WRERklpRGGILADDMGLGKT---LTMISSVLackngQEMSEgkdessdsdseddknkkrksvtg 513
Cdd:cd17995    1 LRDYQLEGVNWLLfnWYNR---RNCILADEMGLGKTiqsIAFLEHLY-----QVEGI----------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  514 wkskgrkdtrRGGTLVVCPASLLRQWESEVESKVSrqkLTVCVHHGN--NRETKGKYLRDY--------------DIVVT 577
Cdd:cd17995   50 ----------RGPFLVIAPLSTIPNWQREFETWTD---MNVVVYHGSgeSRQIIQQYEMYFkdaqgrkkkgvykfDVLIT 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  578 TYQIVAREHKSLSAVfgvKWRRIILDEAHVVRNhkSQSSLAVCdLRgKYRWA----LTGTPIQNKELDVYALLKFLRCSP 653
Cdd:cd17995  117 TYEMVIADAEELRKI---PWRVVVVDEAHRLKN--RNSKLLQG-LK-KLTLEhkllLTGTPLQNNTEELWSLLNFLEPEK 189
                        250       260       270
                 ....*....|....*....|....*....|....
gi 24644932  654 FDDLHTWK-KWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd17995  190 FPSSEEFLeEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
439-640 2.20e-25

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: 104.71  E-value: 2.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWRERKLPrGGILADDMGLGKTLtMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwkskg 518
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRV-GGILGDEMGLGKTI-QIIAFLAALHHSKLG----------------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 rkdtrRGGTLVVCPASLLRQWESEVESKVSrqKLTVCVHH-----GNNRETKGKYLR----------DYDIVVTTYQIVa 583
Cdd:cd18000   50 -----LGPSLIVCPATVLKQWVKEFHRWWP--PFRVVVLHssgsgTGSEEKLGSIERksqlirkvvgDGGILITTYEGF- 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24644932  584 REHKSLsaVFGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQN--KEL 640
Cdd:cd18000  122 RKHKDL--LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNnlKEL 178
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
461-686 1.44e-23

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: 100.27  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  461 GILADDMGLGKTLTMISsVLAckngqEMSEGKDEssdsdseddknkkrksvtgWkskgrkdtrrGGTLVVCPASLLRQWE 540
Cdd:cd18002   22 GILADEMGLGKTVQSIA-VLA-----HLAEEHNI-------------------W----------GPFLVIAPASTLHNWQ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  541 SEVESKVSRQKLTVCVHHGNNRET-------KGKYLRD--YDIVVTTYQIVAREHKSLSavfGVKWRRIILDEAHVVRNH 611
Cdd:cd18002   67 QEISRFVPQFKVLPYWGNPKDRKVlrkfwdrKNLYTRDapFHVVITSYQLVVQDEKYFQ---RVKWQYMVLDEAQAIKSS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  612 KSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKW----IDNKSAGGQ-------NRLNLLMK 680
Cdd:cd18002  144 SSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWfskdIESHAENKTglnehqlKRLHMILK 223

                 ....*.
gi 24644932  681 SLMLRR 686
Cdd:cd18002  224 PFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
439-704 1.14e-22

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: 98.20  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwksk 517
Cdd:cd18064   16 LRDYQVRGLNWLiSLYENGI--NGILADEMGLGKTLQTISLLGYMKHYRNIP---------------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 grkdtrrGGTLVVCPASLLRQWESEVESKVSRQKlTVCVHhgNNRETKGKYLRD------YDIVVTTYQIVAREhKSLSA 591
Cdd:cd18064   66 -------GPHMVLVPKSTLHNWMAEFKRWVPTLR-AVCLI--GDKDQRAAFVRDvllpgeWDVCVTSYEMLIKE-KSVFK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  592 VFgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWID-NKSAG 670
Cdd:cd18064  135 KF--NWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDtNNCLG 212
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 24644932  671 GQN---RLNLLMKSLMLRRTKAQLQsdgklNSLPNKE 704
Cdd:cd18064  213 DQKlveRLHMVLRPFLLRRIKADVE-----KSLPPKK 244
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
439-688 1.84e-22

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: 97.44  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISsvLACKngqeMSEGKDEssdsdseddknkkrksvtgwksk 517
Cdd:cd17996    4 LKEYQLKGLQWMvSLYNNNL--NGILADEMGLGKTIQTIS--LITY----LMEKKKN----------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 grkdtrRGGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHG--NNRETKGKYLR--DYDIVVTTYQIVAREHKSLSAVf 593
Cdd:cd17996   53 ------NGPYLVIVPLSTLSNWVSEFEKWAP--SVSKIVYKGtpDVRKKLQSQIRagKFNVLLTTYEYIIKDKPLLSKI- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  594 gvKWRRIILDEAHVVRNHKSQSSLavcDL----RGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSA 669
Cdd:cd17996  124 --KWKYMIIDEGHRMKNAQSKLTQ---TLntyyHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFA 198
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 24644932  670 --GGQ--------------NRLNLLMKSLMLRRTK 688
Cdd:cd17996  199 ntGEQvkielneeetlliiRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
447-688 2.08e-22

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: 97.46  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  447 LAWMSWRERKLPRG--GILADDMGLGKTLTMISsVLACkngqeMSEGKDEssdsdseddknkkrksvtgwkskgrkdtrr 524
Cdd:cd18009    9 LEGMEWLRMLWENGinGILADEMGLGKTIQTIA-LLAH-----LRERGVW------------------------------ 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  525 GGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHGNNRE---------TKGKYLRDYDIVVTTYQIVAREHKSLSAVfgv 595
Cdd:cd18009   53 GPFLVIAPLSTLPNWVNEFARFTP--SVPVLLYHGTKEErerlrkkimKREGTLQDFPVVVTSYEIAMRDRKALQHY--- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  596 KWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWID----NKSAGG 671
Cdd:cd18009  128 AWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslSDNAAD 207
                        250       260
                 ....*....|....*....|....*....
gi 24644932  672 ---------QNRLNLL---MKSLMLRRTK 688
Cdd:cd18009  208 isnlseereQNIVHMLhaiLKPFLLRRLK 236
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
442-686 4.28e-22

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: 96.59  E-value: 4.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  442 HQKHALAWMsWR----ERKLPRGG-ILADDMGLGKTLTMISSVLACkngqeMSEGKDessdsdseddknkkrksvtgwks 516
Cdd:cd18004    4 HQREGVQFL-YDcltgRRGYGGGGaILADEMGLGKTLQAIALVWTL-----LKQGPY----------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kGRKDTRRggTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETK-----GKYLRDYDIVVTTYQIVAREHKSLSA 591
Cdd:cd18004   55 -GKPTAKK--ALIVCPSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKasldfFSSASTYPVLIISYETLRRHAEKLSK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  592 --VFGVkwrrIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDN--- 666
Cdd:cd18004  132 kiSIDL----LICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpil 207
                        250       260       270
                 ....*....|....*....|....*....|...
gi 24644932  667 -------------KSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18004  208 rsrdpdaseedkeLGAERSQELSELTSRFILRR 240
DEXDc smart00487
DEAD-like helicases superfamily;
439-647 1.15e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.10  E-value: 1.15e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     439 LMNHQKHALAWMswreRKLPRGGILADDMGLGKTLTMISSVLACKngqemsegkdessdsdseddknkkrksvtgwkskg 518
Cdd:smart00487    9 LRPYQKEAIEAL----LSGLRDVILAAPTGSGKTLAALLPALEAL----------------------------------- 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     519 rKDTRRGGTLVVCP-ASLLRQWESEVESKVSRQKL-TVCVHHGNNRETKGKYLR--DYDIVVTTYQIVAReHKSLSAVFG 594
Cdd:smart00487   50 -KRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGLkVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLD-LLENDKLSL 127
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644932     595 VKWRRIILDEAHVVRN--HKSQSSLAVCDLRGK-YRWALTGTPIQNKELDVYALLK 647
Cdd:smart00487  128 SNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNvQLLLLSATPPEEIENLLELFLN 183
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
438-688 4.17e-21

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: 93.54  E-value: 4.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  438 SLMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwks 516
Cdd:cd18065   15 TLRDYQVRGLNWMiSLYENGV--NGILADEMGLGKTLQTIALLGYLKHYRNIP--------------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrrGGTLVVCPASLLRQWESEVESKVSRQKLTVCVhhgNNRETKGKYLRD------YDIVVTTYQIVAREhKSLS 590
Cdd:cd18065   66 --------GPHMVLVPKSTLHNWMNEFKRWVPSLRAVCLI---GDKDARAAFIRDvmmpgeWDVCVTSYEMVIKE-KSVF 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  591 AVFgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAG 670
Cdd:cd18065  134 KKF--NWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCL 211
                        250       260
                 ....*....|....*....|..
gi 24644932  671 GQN----RLNLLMKSLMLRRTK 688
Cdd:cd18065  212 GDQklveRLHAVLKPFLLRRIK 233
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
439-686 1.68e-20

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: 91.11  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAW-MSWRERKLprggiLADDMGLGKTLTMISSVLACKNGqemsegkdessdsdseddknkkrksvtgWKsk 517
Cdd:cd18010    1 LLPFQREGVCFaLRRGGRVL-----IADEMGLGKTVQAIAIAAYYREE----------------------------WP-- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 grkdtrrggTLVVCPASLLRQWESEVESKVSRQKLT--VCVHHGNNretkGKYLRDYDIVVTTYQIVAREHKSLSAVfgv 595
Cdd:cd18010   46 ---------LLIVCPSSLRLTWADEIERWLPSLPPDdiQVIVKSKD----GLRDGDAKVVIVSYDLLRRLEKQLLAR--- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  596 KWRRIILDEAHVVRNHKSQSSLAVCDL--RGKYRWALTGTPIQNKELDVYALLKFLR---CSPFDDLH---------TWK 661
Cdd:cd18010  110 KFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDpklFGRFHDFGrrycaakqgGFG 189
                        250       260
                 ....*....|....*....|....*...
gi 24644932  662 KWIDnksaGGQNR---LNLLMKSLMLRR 686
Cdd:cd18010  190 WDYS----GSSNLeelHLLLLATIMIRR 213
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
439-654 8.47e-20

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: 88.21  E-value: 8.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMS-WRERKLprGGILADDMGLGKTLTMIS--SVLackngqemsegkdessdsdseddknkkrksvtgwK 515
Cdd:cd17998    1 LKDYQLIGLNWLNlLYQKKL--SGILADEMGLGKTIQVIAflAYL----------------------------------K 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  516 SKGRKdtrrGGTLVVCPASLLRQWESEVESKVSrqKLTVCVHHGNNRETKgkYLR--------DYDIVVTTYQIV--ARE 585
Cdd:cd17998   45 EIGIP----GPHLVVVPSSTLDNWLREFKRWCP--SLKVEPYYGSQEERK--HLRydilkgleDFDVIVTTYNLAtsNPD 116
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644932  586 HKSLSAVFgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPF 654
Cdd:cd17998  117 DRSFFKRL--KLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
890-1006 1.28e-19

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: 84.95  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    890 SKINMVIQILKtsilKSSDDKAIVVSQWTSVLDIlRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNdrnNQKRVLLLSLT 969
Cdd:pfam00271    1 EKLEALLELLK----KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATD 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 24644932    970 AGGVGLNLIGANHLLLLDLHWNPQLEAQAQDRIYRVG 1006
Cdd:pfam00271   73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
439-686 6.95e-19

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: 86.34  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMSWReRKLPRGGILADDMGLGKTLTMISsVLACKNGQEMSEGKDessdsdseddknkkrksvtgwkskg 518
Cdd:cd18006    1 LRPYQLEGVNWLLQC-RAEQHGCILGDEMGLGKTCQTIS-LLWYLAGRLKLLGPF------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  519 rkdtrrggtLVVCPASLLRQWESEVESKVSRQKltvCVHHGNNRETKGKYLRD------YDIVVTTYQIVAREHKSLSAV 592
Cdd:cd18006   54 ---------LVLCPLSVLDNWKEELNRFAPDLS---VITYMGDKEKRLDLQQDikstnrFHVLLTTYEICLKDASFLKSF 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  593 fgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPF------DDLHTWKKwIDN 666
Cdd:cd18006  122 ---PWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdkldDFIKAYSE-TDD 197
                        250       260
                 ....*....|....*....|
gi 24644932  667 KSAGGQNrLNLLMKSLMLRR 686
Cdd:cd18006  198 ESETVEE-LHLLLQPFLLRR 216
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
460-662 8.37e-18

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: 83.74  E-value: 8.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  460 GGILADDMGLGKTLTMISSVLACKngqemsegkdessdsdseddknkkRKSVTGWKSKGRKdtrrggTLVVCPASLLRQW 539
Cdd:cd18066   26 GAILADEMGLGKTLQCISLIWTLL------------------------RQGPYGGKPVIKR------ALIVTPGSLVKNW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  540 ESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVARehkSLSAVFGVKWRRIILDEAHVVRNHKSQSSLAV 619
Cdd:cd18066   76 KKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLR---SLDQISKLNFDLVICDEGHRLKNTSIKTTTAL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24644932  620 CDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKK 662
Cdd:cd18066  153 TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRK 195
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
439-686 1.21e-17

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: 82.79  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwks 516
Cdd:cd17993    2 LRDYQLTGLNWLahSWCKGN---NGILADEMGLGKTVQTISFLSYLFHSQQQY--------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrrGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRET---------KGKYLRdYDIVVTTYQIVAREHK 587
Cdd:cd17993   52 --------GPFLVVVPLSTMPAWQREFAKWAPDMNVIVYLGDIKSRDTireyefyfsQTKKLK-FNVLLTTYEIILKDKA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  588 SLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQN--KELdvYALLKFLRCSPFddlHTWKKWID 665
Cdd:cd17993  123 FLGSI---KWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNslKEL--WALLHFLMPGKF---DIWEEFEE 194
                        250       260
                 ....*....|....*....|....
gi 24644932  666 NKSAG---GQNRLNLLMKSLMLRR 686
Cdd:cd17993  195 EHDEEqekGIADLHKELEPFILRR 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
434-686 1.73e-16

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: 80.05  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  434 GLKVSLMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksv 511
Cdd:cd18054   16 GENLELRDYQLEGLNWLahSWCKNN---SVILADEMGLGKTIQTISFLSYLFHQHQLY---------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  512 tgwkskgrkdtrrGGTLVVCPASLLRQWESEVEskVSRQKLTVCVHHGN--NRETkgkyLRDYD------------IVVT 577
Cdd:cd18054   71 -------------GPFLLVVPLSTLTSWQREFE--IWAPEINVVVYIGDlmSRNT----IREYEwihsqtkrlkfnALIT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  578 TYQIVAREHKSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDdl 657
Cdd:cd18054  132 TYEILLKDKTVLGSI---NWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFE-- 206
                        250       260       270
                 ....*....|....*....|....*....|..
gi 24644932  658 hTWKKWIDNKSAGGQN---RLNLLMKSLMLRR 686
Cdd:cd18054  207 -FWEDFEEDHGKGRENgyqSLHKVLEPFLLRR 237
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
439-650 2.43e-16

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: 79.64  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMsWR-------ERKLPRGGILADDMGLGKTLTMIS---SVLACkngqemsegkdessdsdsedDKNKKR 508
Cdd:cd18007    1 LKPHQVEGVRFL-WSnlvgtdvGSDEGGGCILAHTMGLGKTLQVITflhTYLAA--------------------APRRSR 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  509 ksvtgwkskgrkdtrrggTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKG--------KYLRDYDIVVTTYQ 580
Cdd:cd18007   60 ------------------PLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKRAdarlrkinKWHKEGGVLLIGYE 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  581 I---VAREHKSLSAVFG--VKWRR------IILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFL 649
Cdd:cd18007  122 LfrnLASNATTDPRLKQefIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201

                 .
gi 24644932  650 R 650
Cdd:cd18007  202 R 202
HELICc smart00490
helicase superfamily c-terminal domain;
922-1006 7.07e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 73.40  E-value: 7.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932     922 DILRDHLSKDGVATLSLNGTIPVKNRQDIVNEFNdrnNQKRVLLLSLTAGGVGLNLIGANHLLLLDLHWNPQLEAQAQDR 1001
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 24644932    1002 IYRVG 1006
Cdd:smart00490   78 AGRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
439-649 7.46e-16

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: 77.33  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALawmswRE--RKLPRGGILADDMGLGKTLT--MISSVLAckngqemsegkdessdsdseddknkkrksvtgw 514
Cdd:cd18011    1 PLPHQIDAV-----LRalRKPPVRLLLADEVGLGKTIEagLIIKELL--------------------------------- 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  515 kskGRKDTRRggTLVVCPASLLRQWESEVESK-------VSRQKLTVCVHHGNNretkgkYLRDYDIVVTTYQIVAREHK 587
Cdd:cd18011   43 ---LRGDAKR--VLILCPASLVEQWQDELQDKfglpfliLDRETAAQLRRLIGN------PFEEFPIVIVSLDLLKRSEE 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644932  588 SLSAVFGVKWRRIILDEAHVVRNH----KSQSSLAVCDLRGK--YRWALTGTPIQNKELDVYALLKFL 649
Cdd:cd18011  112 RRGLLLSEEWDLVVVDEAHKLRNSgggkETKRYKLGRLLAKRarHVLLLTATPHNGKEEDFRALLSLL 179
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
439-686 3.08e-15

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: 76.25  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVlackngQEMSEGKDessdsdseddknkkrksvtgwks 516
Cdd:cd18060    1 LREYQLEGVNWLlfNWYNRQ---NCILADEMGLGKTIQSIAFL------QEVYNVGI----------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrRGGTLVVCPASLLRQWESEVESKVsrqKLTVCVHHGN-------------NRETKGKYL---RDYDIVVTTYQ 580
Cdd:cd18060   49 -------HGPFLVIAPLSTITNWEREFNTWT---EMNTIVYHGSlasrqmiqqyemyCKDSRGRLIpgaYKFDALITTFE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  581 IVAREHKSLSAVfgvKWRRIILDEAHVV--RNHKSQSSLAVCDLrgKYRWALTGTPIQNKELDVYALLKFLRCSPF-DDL 657
Cdd:cd18060  119 MILSDCPELREI---EWRCVIIDEAHRLknRNCKLLDSLKHMDL--EHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSES 193
                        250       260
                 ....*....|....*....|....*....
gi 24644932  658 HTWKKWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18060  194 EFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
439-686 9.05e-15

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: 74.69  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSvlackngqeMSEGKDESSdsdseddknkkrksvtgwks 516
Cdd:cd18058    1 LREYQLEGMNWLlfNWYNRK---NCILADEMGLGKTIQSITF---------LSEIFLMGI-------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrRGGTLVVCPASLLRQWESEVESKVsrqKLTVCVHHGNN-------------RETKGKYLR---DYDIVVTTYQ 580
Cdd:cd18058   49 -------RGPFLIIAPLSTITNWEREFRTWT---EMNAIVYHGSQisrqmiqqyemyyRDEQGNPLSgifKFQVVITTFE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  581 IVAREHKSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTW 660
Cdd:cd18058  119 MILADCPELKKI---NWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTF 195
                        250       260
                 ....*....|....*....|....*..
gi 24644932  661 -KKWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18058  196 lEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
439-686 2.31e-14

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: 73.50  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERklpRGGILADDMGLGKTLTMISSVlackngqemsegkdessdsdseddknkKRKSVTGWks 516
Cdd:cd18061    1 LREYQLEGLNWLlfNWYNR---RNCILADEMGLGKTIQSITFL---------------------------YEILLTGI-- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrRGGTLVVCPASLLRQWESEVESKVSrqkLTVCVHHGN-------------NRETKGKYLRD---YDIVVTTYQ 580
Cdd:cd18061   49 -------RGPFLIIAPLSTIANWEREFRTWTD---LNVVVYHGSlisrqmiqqyemyFRDSQGRIIRGayrFQAIITTFE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  581 IVAREHKSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTW 660
Cdd:cd18061  119 MILGGCPELNAI---DWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF 195
                        250       260
                 ....*....|....*....|....*..
gi 24644932  661 -KKWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18061  196 mQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
439-686 2.89e-13

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: 70.45  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRErklPRGGILADDMGLGKTLTMISSVLACKngqemsegkdessdsdseddknkkrksvtgwkS 516
Cdd:cd18059    1 LREYQLEGVNWLlfNWYN---TRNCILADEMGLGKTIQSITFLYEIY--------------------------------L 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 KGRkdtrRGGTLVVCPASLLRQWESEVESKVsrqKLTVCVHHGNN-------------RETKGKYLR---DYDIVVTTYQ 580
Cdd:cd18059   46 KGI----HGPFLVIAPLSTIPNWEREFRTWT---ELNVVVYHGSQasrrtiqlyemyfKDPQGRVIKgsyKFHAIITTFE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  581 IVAREHKSLSavfGVKWRRIILDEAHVV--RNHKSQSSLAVCDLrgKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLH 658
Cdd:cd18059  119 MILTDCPELR---NIPWRCVVIDEAHRLknRNCKLLEGLKMMDL--EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSET 193
                        250       260
                 ....*....|....*....|....*....
gi 24644932  659 TW-KKWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18059  194 TFmQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
439-686 5.31e-13

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: 69.01  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLACkngqeMSEGKDessdsdseddknkkrksvtgwks 516
Cdd:cd17994    1 LHPYQLEGLNWLrfSWAQGT---DTILADEMGLGKTIQTIVFLYSL-----YKEGHS----------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrRGGTLVVCPASLLRQWESEVEskVSRQKLTVCVHHGNNretkgkylrdydIVVTTYQIVAREHKSLSAVfgvK 596
Cdd:cd17994   50 -------KGPFLVSAPLSTIINWEREFE--MWAPDFYVVTYVGDH------------VLLTSYELISIDQAILGSI---D 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  597 WRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQ-NRL 675
Cdd:cd17994  106 WAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQiKKL 185
                        250
                 ....*....|.
gi 24644932  676 NLLMKSLMLRR 686
Cdd:cd17994  186 HDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
437-686 7.50e-13

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: 69.31  E-value: 7.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  437 VSLMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgw 514
Cdd:cd18053   19 LELRDYQLNGLNWLahSWCKGN---SCILADEMGLGKTIQTISFLNYLFHEHQLY------------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  515 kskgrkdtrrGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNRET---------KGKYLRdYDIVVTTYQIVARE 585
Cdd:cd18053   71 ----------GPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRNMirthewmhpQTKRLK-FNILLTTYEILLKD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  586 HKSLSavfGVKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFddlHTWKKWID 665
Cdd:cd18053  140 KSFLG---GLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF---SSWEDFEE 213
                        250       260
                 ....*....|....*....|....
gi 24644932  666 NKSAG---GQNRLNLLMKSLMLRR 686
Cdd:cd18053  214 EHGKGreyGYASLHKELEPFLLRR 237
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
438-688 1.13e-12

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: 69.32  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  438 SLMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwks 516
Cdd:cd18063   23 TLKHYQLQGLEWMvSLYNNNL--NGILADEMGLGKTIQTIALITYLMEHKRLN--------------------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 kgrkdtrrGGTLVVCPASLLRQWESEVES------KVSRQKLTVCVHHGNNRETKGKYlrdyDIVVTTYQIVAREHKSLS 590
Cdd:cd18063   74 --------GPYLIIVPLSTLSNWTYEFDKwapsvvKISYKGTPAMRRSLVPQLRSGKF----NVLLTTYEYIIKDKHILA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  591 AVfgvKWRRIILDEAHVVRNHKSQ-SSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSA 669
Cdd:cd18063  142 KI---RWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFA 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 24644932  670 GGQNRLNL--------------LMKSLMLRRTK 688
Cdd:cd18063  219 MTGERVDLneeetiliirrlhkVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
439-686 3.51e-11

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: 64.68  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM-SWRERKLprGGILADDMGLGKTLTMISSVLACKNGQEMSegkdessdsdseddknkkrksvtgwksk 517
Cdd:cd18062   24 LKQYQIKGLEWLvSLYNNNL--NGILADEMGLGKTIQTIALITYLMEHKRIN---------------------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  518 grkdtrrGGTLVVCPASLLRQWESEVESKVSRqklTVCVHHGNNRETKGKYLR-----DYDIVVTTYQIVAREHKSLSAV 592
Cdd:cd18062   74 -------GPFLIIVPLSTLSNWVYEFDKWAPS---VVKVSYKGSPAARRAFVPqlrsgKFNVLLTTYEYIIKDKQILAKI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  593 fgvKWRRIILDEAHVVRNHKSQ-SSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSA-- 669
Cdd:cd18062  144 ---RWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmt 220
                        250
                 ....*....|....*..
gi 24644932  670 GGQNRLNLLMKSLMLRR 686
Cdd:cd18062  221 GEKVDLNEEETILIIRR 237
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
453-673 1.64e-10

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: 62.49  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  453 RERKLPRGGILADDMGLGKTL---TMISSVLackngQEMSEGKDESsdsdseddkNKkrksvtgwkskgrkdtrrggTLV 529
Cdd:cd18067   19 RRIRGSHGCIMADEMGLGKTLqciTLMWTLL-----RQSPQCKPEI---------DK--------------------AIV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  530 VCPASLLRQWESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDI----VVTTYQIVAREHKSLSAVFGVKWR--RIILD 603
Cdd:cd18067   65 VSPSSLVKNWANELGKWLGGRLQPLAIDGGSKKEIDRKLVQWASQqgrrVSTPVLIISYETFRLHVEVLQKGEvgLVICD 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  604 EAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKSAGGQN 673
Cdd:cd18067  145 EGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRD 214
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
428-634 7.72e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 62.73  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  428 LAEDPVGLKVSLMNHQKHAL-AWMSWRERKlPRGGILADDMGLGKTLTMISSVLACKNGQEmsegkdessdsdseddknk 506
Cdd:COG1061   70 AGDEASGTSFELRPYQQEALeALLAALERG-GGRGLVVAPTGTGKTVLALALAAELLRGKR------------------- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  507 krksvtgwkskgrkdtrrggTLVVCP-ASLLRQWESEVeskvsRQKLTVCVHHGNNREtkgkylRDYDIVVTTYQIVAR- 584
Cdd:COG1061  130 --------------------VLVLVPrRELLEQWAEEL-----RRFLGDPLAGGGKKD------SDAPITVATYQSLARr 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24644932  585 -EHKSLSAVFGVkwrrIILDEAHVVRnhkSQSSLAVCD-LRGKYRWALTGTP 634
Cdd:COG1061  179 aHLDELGDRFGL----VIIDEAHHAG---APSYRRILEaFPAAYRLGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
442-634 9.22e-09

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 55.39  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  442 HQKHALAwmSWRERKLPRGGILADDMGLGKTLTMISsvLACKngqemsegkdessdsdseddknkkrksvtgwkskgrkd 521
Cdd:cd17926    4 YQEEALE--AWLAHKNNRRGILVLPTGSGKTLTALA--LIAY-------------------------------------- 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  522 TRRGGTLVVCP-ASLLRQWESEVEskvsrqKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVAREHKSLSAVFGVKWrRI 600
Cdd:cd17926   42 LKELRTLIVVPtDALLDQWKERFE------DFLGDSSIGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG-LL 114
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24644932  601 ILDEAHvvrnHKSQSSLAVC--DLRGKYRWALTGTP 634
Cdd:cd17926  115 IVDEAH----HLPAKTFSEIlkELNAKYRLGLTATP 146
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
439-686 1.17e-08

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: 57.00  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLAC-KNGQemSEGKDESSDSDSEDDKNKKRKSVtgWK 515
Cdd:cd18057    1 LHPYQLEGLNWLrfSWAQGT---DTILADEMGLGKTVQTIVFLYSLyKEGH--SKGPYLVSAPLSTIINWEREFEM--WA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  516 S-------KGRKDTRrggtlvvcpaSLLRQWESEVESKVSRQKLTVCvhhgnnRETKGKYLRdYDIVVTTYQIVAREHKS 588
Cdd:cd18057   74 PdfyvvtyTGDKESR----------SVIRENEFSFEDNAIRSGKKVF------RMKKEAQIK-FHVLLTSYELITIDQAI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  589 LSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDLHTWKKWIDNKS 668
Cdd:cd18057  137 LGSI---EWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADIS 213
                        250
                 ....*....|....*....
gi 24644932  669 AGGQ-NRLNLLMKSLMLRR 686
Cdd:cd18057  214 KEDQiKKLHDLLGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
442-686 1.20e-08

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: 56.94  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  442 HQKHALAWM--SWRERKlprGGILADDMGLGKTLTMISSVLACkngqeMSEGKDessdsdseddknkkrksvtgwkskgr 519
Cdd:cd18055    4 YQLEGLNWLrfSWAQGT---DTILADEMGLGKTIQTIVFLYSL-----YKEGHT-------------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  520 kdtrRGGTLVVCPASLLRQWESEVE-------------SKVSRQKLTVCVHHGNNRETKG-----KYLRD----YDIVVT 577
Cdd:cd18055   50 ----KGPFLVSAPLSTIINWEREFQmwapdfyvvtytgDKDSRAIIRENEFSFDDNAVKGgkkafKMKREaqvkFHVLLT 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  578 TYQIVAREHKSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPFDDL 657
Cdd:cd18055  126 SYELVTIDQAALGSI---RWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNL 202
                        250       260       270
                 ....*....|....*....|....*....|
gi 24644932  658 HTWKKWIDNKSAGGQ-NRLNLLMKSLMLRR 686
Cdd:cd18055  203 EGFLEEFADISKEDQiKKLHDLLGPHMLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
439-650 8.02e-08

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: 54.51  E-value: 8.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWMsW---------RERKLPRGGILADDMGLGKTLTMIS---SVLACKngqemsegkdessdsdseddKNK 506
Cdd:cd18068    1 LKPHQVDGVQFM-WdccceslkkTKKSPGSGCILAHCMGLGKTLQVVTflhTVLLCE--------------------KLE 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  507 KRKSVtgwkskgrkdtrrggtLVVCPASLLRQWESEVES--------------KVSRQKLTVCVHHGNNR--ETKGKYLR 570
Cdd:cd18068   60 NFSRV----------------LVVCPLNTVLNWLNEFEKwqeglkdeekievnELATYKRPQERSYKLQRwqEEGGVMII 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  571 DYDIvvttYQIVARE-----HKSLSAVFGVKWRR-----IILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKEL 640
Cdd:cd18068  124 GYDM----YRILAQErnvksREKLKEIFNKALVDpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLI 199
                        250
                 ....*....|
gi 24644932  641 DVYALLKFLR 650
Cdd:cd18068  200 EYHCMVNFVK 209
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
460-650 2.33e-07

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: 52.90  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  460 GGILADDMGLGKTLTMISSVlackngqemsegkdessdsdSEDDKNKKRKSVtgwkskgrkdtrrggtLVVCPASLLRQW 539
Cdd:cd18069   30 GCILAHSMGLGKTLQVISFL--------------------DVLLRHTGAKTV----------------LAIVPVNTLQNW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  540 ESEVESKVSRQKLTVCVHhgnnretkgkyLRDYDIvvttyQIVAREHKSLSAVFGV--KWRR------------------ 599
Cdd:cd18069   74 LSEFNKWLPPPEALPNVR-----------PRPFKV-----FILNDEHKTTAARAKVieDWVKdggvllmgyemfrlrpgp 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24644932  600 --IILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLR 650
Cdd:cd18069  138 dvVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
441-649 3.67e-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: 51.97  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  441 NHQKHALAWMswreRKLPRGGILADdMGLGKTLTMISSVlackngqemsegkdessdsdseddknkkrksvtgwkSKGRK 520
Cdd:cd18013    3 PYQKVAINFI----IEHPYCGLFLD-MGLGKTVTTLTAL------------------------------------SDLQL 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  521 DTRRGGTLVVCPASLLRQ-WESEVESKVSRQKLTVCVHHGNNRETKGKYLRDYDIVVTTYQIVarehKSLSAVFGVKW-- 597
Cdd:cd18013   42 DDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTVSVAVGTERQRSKAANTPADLYVINRENL----KWLVNKSGDPWpf 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24644932  598 RRIILDEAHVVRNHKSQSSLAVCDLRGKYRW--ALTGTPIQNKELDVYALLKFL 649
Cdd:cd18013  118 DMVVIDELSSFKSPRSKRFKALRKVRPVIKRliGLTGTPSPNGLMDLWAQIALL 171
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
439-686 2.35e-06

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: 50.06  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  439 LMNHQKHALAWM--SWRERKlprGGILADDMGLGKTLtmissvlackngqemsegkdessdsdseddknkkrKSVTGWKS 516
Cdd:cd18056    1 LHPYQLEGLNWLrfSWAQGT---DTILADEMGLGKTV-----------------------------------QTAVFLYS 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  517 KGRKDTRRGGTLVVCPASLLRQWESEVESKVSRQKLTVCVHHGNNR----------------------ETKGKYLRDYDI 574
Cdd:cd18056   43 LYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRaiirenefsfednairggkkasRMKKEASVKFHV 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  575 VVTTYQIVAREHKSLSAVfgvKWRRIILDEAHVVRNHKSQSSLAVCDLRGKYRWALTGTPIQNKELDVYALLKFLRCSPF 654
Cdd:cd18056  123 LLTSYELITIDMAILGSI---DWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF 199
                        250       260       270
                 ....*....|....*....|....*....|...
gi 24644932  655 DDLHTW-KKWIDNKSAGGQNRLNLLMKSLMLRR 686
Cdd:cd18056  200 HNLEGFlEEFADIAKEDQIKKLHDMLGPHMLRR 232
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
521-608 2.44e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.17  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  521 DTRRGGTLVVCP-ASLLRQWESEVeSKVSRQKLTVCVHHGNN--RETKGKYLRDYDIVVTTYQIVAREHKSLSAVFGVKW 597
Cdd:cd00046   27 LKKGKKVLVLVPtKALALQTAERL-RELFGPGIRVAVLVGGSsaEEREKNKLGDADIIIATPDMLLNLLLREDRLFLKDL 105
                         90
                 ....*....|.
gi 24644932  598 RRIILDEAHVV 608
Cdd:cd00046  106 KLIIVDEAHAL 116
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
527-608 2.69e-05

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 45.76  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932  527 TLVVCPASL-LRQWESEVESKVSRQKLTVCVHHGNNRETkgkyLRDYDIVVTTYQIVAREHKS-------LSAVFGVKWR 598
Cdd:cd18029   54 TLVLCTSAVsVEQWRRQFLDWTTIDDEQIGRFTSDKKEI----FPEAGVTVSTYSMLANTRKRspesekfMEFITEREWG 129
                         90
                 ....*....|
gi 24644932  599 RIILDEAHVV 608
Cdd:cd18029  130 LIILDEVHVV 139
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
527-637 3.90e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.15  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644932    527 TLVVCP-ASLLRQWESEVESKVSRQKLTV-CVHHGNNRETKGKYLRDYDIVVTTYQIVAREHKSLSAVFGVKWrrIILDE 604
Cdd:pfam00270   48 ALVLAPtRELAEQIYEELKKLGKGLGLKVaSLLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKL--LVLDE 125
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 24644932    605 AHVVRNHKSQSSLAVC--DLRGKYRW-ALTGTPIQN 637
Cdd:pfam00270  126 AHRLLDMGFGPDLEEIlrRLPKKRQIlLLSATLPRN 161
 
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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