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Conserved domains on  [gi|380798987|gb|AFE71369|]
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transcriptional regulator ATRX isoform 2, partial [Macaca mulatta]

Protein Classification

DEXHc_ATRX and SF2_C_SNF domain-containing protein( domain architecture ID 12785140)

DEXHc_ATRX and SF2_C_SNF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 104-347 2.15e-172

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: 503.65  E-value: 2.15e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 182
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 261
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  262 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 341
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240


                  ....*.
gi 380798987  342 RVMKKR 347
Cdd:cd18068   241 RVMKKR 246
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 87-735 9.15e-88

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 296.75  E-value: 9.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   87 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 166
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  167 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 246
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  247 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 326
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  327 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNNSE 406
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  407 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 486
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  487 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 566
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  567 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 646
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  647 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 726
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673


                  ....*....
gi 380798987  727 QSLSFRVVD 735
Cdd:COG0553   674 RALAESVLG 682
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 104-347 2.15e-172

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: 503.65  E-value: 2.15e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 182
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 261
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  262 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 341
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240


                  ....*.
gi 380798987  342 RVMKKR 347
Cdd:cd18068   241 RVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 107-433 6.12e-108

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 337.35  E-value: 6.12e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   107 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 186
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   187 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 266
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   267 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 346
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   347 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQ-YYLDHLTGVGNNSEGGRGKAgAKLFQDFQMLSR 425
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281


                   ....*...
gi 380798987   426 IWTHPWCL 433
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 87-735 9.15e-88

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 296.75  E-value: 9.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   87 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 166
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  167 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 246
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  247 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 326
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  327 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNNSE 406
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  407 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 486
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  487 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 566
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  567 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 646
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  647 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 726
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673


                  ....*....
gi 380798987  727 QSLSFRVVD 735
Cdd:COG0553   674 RALAESVLG 682
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 560-710 2.60e-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: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  560 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 639
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380798987  640 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 710
Cdd:cd18793    67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 135-759 1.86e-43

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 171.91  E-value: 1.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddeklevselaTVK---RPQERSY 211
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRFCPVLR-----------AVKfhgNPEERAH 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  212 MLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRII 289
Cdd:PLN03142  260 QREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  290 LTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTK 369
Cdd:PLN03142  325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEK 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  370 FLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNnseggRGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfded 449
Cdd:PLN03142  393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVN-----AGGERKRLLNIAMQLRKCCNHPYLFQ--------------- 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  450 smdefiasdsdetsmslssddytkkkkkgkkgkkdssssgsgsdndvevikvwnsrsrGGGEGNVDETGNNpsvslklee 529
Cdd:PLN03142  453 ----------------------------------------------------------GAEPGPPYTTGEH--------- 465

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  530 skatsssnpsspapdwykdfvtdadaeVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrektedk 609
Cdd:PLN03142  466 ---------------------------LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL----------- 507

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  610 dkplIYKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDI 689
Cdd:PLN03142  508 ----MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDL 575

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380798987  690 QSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMN--ELTELYTFEPDLL 759
Cdd:PLN03142  576 QAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNkdELLQMVRYGAEMV 647
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 562-699 6.14e-18

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: 80.33  E-value: 6.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   562 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 641
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 380798987   642 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 699
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
623-699 2.17e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.64  E-value: 2.17e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380798987    623 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 699
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
102-297 2.03e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 75.99  E-value: 2.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987    102 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 180
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987    181 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 259
Cdd:smart00487   73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 380798987    260 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 297
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 104-347 2.15e-172

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: 503.65  E-value: 2.15e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 182
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 261
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  262 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 341
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240


                  ....*.
gi 380798987  342 RVMKKR 347
Cdd:cd18068   241 RVMKKR 246
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 104-347 4.03e-119

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: 365.08  E-value: 4.03e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESvkKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKlDFSTALVVCPLNTALNWMNEFE 183
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-RRSRPLVLCPASTLYNWEDEFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLKDDEKLEVSeLATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNvKSRKLKEIFNKALVDPGPDFVVCD 263
Cdd:cd18007    78 KWLPPDLRPLLVLVS-LSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT-TDPRLKQEFIAALLDPGPDLLVLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  264 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRV 343
Cdd:cd18007   156 EGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRL 235


                  ....
gi 380798987  344 MKKR 347
Cdd:cd18007   236 MLKR 239
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 107-433 6.12e-108

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 337.35  E-value: 6.12e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   107 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 186
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   187 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 266
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   267 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 346
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   347 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQ-YYLDHLTGVGNNSEGGRGKAgAKLFQDFQMLSR 425
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281


                   ....*...
gi 380798987   426 IWTHPWCL 433
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 87-735 9.15e-88

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 296.75  E-value: 9.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   87 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 166
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  167 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 246
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  247 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 326
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  327 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNNSE 406
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  407 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 486
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  487 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 566
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  567 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 646
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  647 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 726
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673


                  ....*....
gi 380798987  727 QSLSFRVVD 735
Cdd:COG0553   674 RALAESVLG 682
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 104-347 1.61e-85

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: 275.16  E-value: 1.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFE 183
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGA--KTVLAIVPVNTLQNWLSEFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLKDDEKLEVSELAT------VKRPQERSYMLQRWQEDGGVMIIGYEMYRNlaqgrnvksrklkeifnkalvDPGP 257
Cdd:cd18069    79 KWLPPPEALPNVRPRPFKVfilndeHKTTAARAKVIEDWVKDGGVLLMGYEMFRL---------------------RPGP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  258 DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADST 337
Cdd:cd18069   138 DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDST 217

                         250
                  ....*....|
gi 380798987  338 MVDVRVMKKR 347
Cdd:cd18069   218 PQDVKLMRYR 227
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 104-362 9.71e-62

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: 210.22  E-value: 9.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVL---LCDKLDFSTALVVCPLNTALNWMN 180
Cdd:cd18004     1 LRPHQREGVQFLYDC----LTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLkqgPYGKPTAKKALIVCPSSLVGNWKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  181 EFEKWqegLKDdEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRklkeifnkalvdpgPDFV 260
Cdd:cd18004    77 EFDKW---LGL-RRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKIS--------------IDLL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  261 VCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVD 340
Cdd:cd18004   139 ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEED 218

                         250       260
                  ....*....|....*....|..
gi 380798987  341 VRVMKKRAHILYEMLAGCVQRK 362
Cdd:cd18004   219 KELGAERSQELSELTSRFILRR 240
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 104-309 1.96e-59

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: 201.26  E-value: 1.96e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCesvkktkksPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFE 183
Cdd:cd17919     1 LRPYQLEGLNFLLELYE---------NGPGGILADEMGLGKTLQAIAFLAY-LLKEGKERGPVLVVCPLSVLENWEREFE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLKddeklevseLATVKRPQERSYMLQ--RWQEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVV 261
Cdd:cd17919    71 KWTPDLR---------VVVYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKA---------------SLRKFRWDLVV 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 380798987  262 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 309
Cdd:cd17919   127 VDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 560-710 2.60e-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: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  560 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 639
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380798987  640 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 710
Cdd:cd18793    67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 104-362 2.64e-47

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: 169.19  E-value: 2.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCcesvkKTKKSPGS-GCILAHCMGLGKTLQVVSFLHTVL----LCdKLDFSTALVVCPLNTALNW 178
Cdd:cd18067     1 LRPHQREGVKFLYRCV-----TGRRIRGShGCIMADEMGLGKTLQCITLMWTLLrqspQC-KPEIDKAIVVSPSSLVKNW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  179 MNEFEKWQEGlkddeklEVSELATV-KRPQERSYMLQRWQEDGG------VMIIGYEMYRNLAqgrnvksrklkEIFNKA 251
Cdd:cd18067    75 ANELGKWLGG-------RLQPLAIDgGSKKEIDRKLVQWASQQGrrvstpVLIISYETFRLHV-----------EVLQKG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  252 LVDpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 331
Cdd:cd18067   137 EVG----LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKG 212

                         250       260       270
                  ....*....|....*....|....*....|.
gi 380798987  332 QCADSTMVDVRVMKKRAHILYEMLAGCVQRK 362
Cdd:cd18067   213 RDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 104-337 4.41e-44

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: 159.46  E-value: 4.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMNEFE 183
Cdd:cd18001     1 LYPHQREGVAWLW---------SLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIK--SVLVVMPTSLIPHWVKEFA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLkddeklevselaTVK-----RPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEIFNKALVdpgPD 258
Cdd:cd18001    70 KWTPGL------------RVKvfhgtSKKERERNLERIQRGGGVLLTTYGMVLSNTE-------QLSADDHDEFK---WD 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  259 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI-KENLLGSIKEFRNRFINPIQNGQCADST 337
Cdd:cd18001   128 YVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDAT 207
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 135-759 1.86e-43

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 171.91  E-value: 1.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddeklevselaTVK---RPQERSY 211
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRFCPVLR-----------AVKfhgNPEERAH 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  212 MLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRII 289
Cdd:PLN03142  260 QREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  290 LTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTK 369
Cdd:PLN03142  325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEK 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  370 FLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNnseggRGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfded 449
Cdd:PLN03142  393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVN-----AGGERKRLLNIAMQLRKCCNHPYLFQ--------------- 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  450 smdefiasdsdetsmslssddytkkkkkgkkgkkdssssgsgsdndvevikvwnsrsrGGGEGNVDETGNNpsvslklee 529
Cdd:PLN03142  453 ----------------------------------------------------------GAEPGPPYTTGEH--------- 465

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  530 skatsssnpsspapdwykdfvtdadaeVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrektedk 609
Cdd:PLN03142  466 ---------------------------LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL----------- 507

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  610 dkplIYKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDI 689
Cdd:PLN03142  508 ----MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDL 575

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380798987  690 QSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMN--ELTELYTFEPDLL 759
Cdd:PLN03142  576 QAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNkdELLQMVRYGAEMV 647
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 104-347 4.79e-42

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: 154.07  E-value: 4.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVL----------------LCDKLDFS--- 164
Cdd:cd18005     1 LRDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSakk 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  165 TALVVCPLNTALNWMNEFEKWQEglkddekLEVSELATVKRPQERSYMLQRWQEDggVMIIGYEMYRNLAQGrnvksrkL 244
Cdd:cd18005    72 PVLIVAPLSVLYNWKDELDTWGH-------FEVGVYHGSRKDDELEGRLKAGRLE--VVVTTYDTLRRCIDS-------L 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  245 KEIfnkalvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18005   136 NSI--------NWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207

                         250       260
                  ....*....|....*....|...
gi 380798987  325 INPIQNGQCADSTMVDVRVMKKR 347
Cdd:cd18005   208 SEPIKRGQRHTATARELRLGRKR 230
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 104-362 6.01e-38

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: 142.29  E-value: 6.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLD-----FSTALVVCPLNTALNW 178
Cdd:cd18066     1 LRPHQREGIEFLYEC----VMGMRVNERFGAILADEMGLGKTLQCISLIWT-LLRQGPYggkpvIKRALIVTPGSLVKNW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  179 MNEFEKWQeglkDDEKLEVSELATVKRPQE--RSYMLQrwqedggVMIIGYEMY-RNLAQGRNVKSrklkeifnkalvdp 255
Cdd:cd18066    76 KKEFQKWL----GSERIKVFTVDQDHKVEEfiASPLYS-------VLIISYEMLlRSLDQISKLNF-------------- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  256 gpDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 335
Cdd:cd18066   131 --DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPT 208

                         250       260
                  ....*....|....*....|....*..
gi 380798987  336 STMVDVRVMKKRAHILYEMLAGCVQRK 362
Cdd:cd18066   209 ATPEEKKLGEARAAELTRLTGLFILRR 235
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 104-336 1.49e-32

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: 126.14  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGV---QFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMN 180
Cdd:cd18012     5 LRPYQKEGFnwlSFLRHY------------GLGGILADDMGLGKTLQTLALLLSRKEEGRKG--PSLVVAPTSLIYNWEE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  181 EFEKWQEGLKddeklevselATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpdF 259
Cdd:cd18012    71 EAAKFAPELK----------VLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIE-------LLKEVkFH---------Y 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380798987  260 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADS 336
Cdd:cd18012   125 LVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA 201
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 104-310 6.62e-32

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: 123.20  E-value: 6.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCESVkktkkspgsGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 183
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRV---------GGILGDEMGLGKTIQIIAFL-AALHHSKLGLGPSLIVCPATVLKQWVKEFH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KW------------QEGLKDDEKLEVSELATVKRPQERsymlqrwqEDGGVMIIGYEMYRnlaqgrnvksrklkeIFNKA 251
Cdd:cd18000    71 RWwppfrvvvlhssGSGTGSEEKLGSIERKSQLIRKVV--------GDGGILITTYEGFR---------------KHKDL 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 380798987  252 LVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 310
Cdd:cd18000   128 LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVF 186
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 104-328 1.69e-28

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: 114.76  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWdcccesvkKTKKSPGSGcILAHCMGLGKTLQVVSFLHTVLLCDKLDFST----ALVVCPLNTALNWM 179
Cdd:cd17999     1 LRPYQQEGINWLA--------FLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSenlpSLVVCPPTLVGHWV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  180 NEFEKWqeglKDDEKLEVseLATVKRPQERSyMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpd 258
Cdd:cd17999    72 AEIKKY----FPNAFLKP--LAYVGPPQERR-RLREQGEKHNVIVASYDVLRNDIE-------VLTKIeWN--------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  259 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 328
Cdd:cd17999   129 YCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPI 198
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 103-324 9.21e-28

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: 112.86  E-value: 9.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  103 KLKPHQVDGVQFMwdcccesvkKTKKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEF 182
Cdd:cd18009     3 VMRPYQLEGMEWL---------RMLWENGINGILADEMGLGKTIQTIALL--AHLRERGVWGPFLVIAPLSTLPNWVNEF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQ--------EGLKDDEKlevsELATVKRPQERSYMlqrwqeDGGVMIIGYEMYRNLAqgrnvksrklkeifnKALVD 254
Cdd:cd18009    72 ARFTpsvpvllyHGTKEERE----RLRKKIMKREGTLQ------DFPVVVTSYEIAMRDR---------------KALQH 126

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  255 PGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18009   127 YAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF 196
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 104-324 1.41e-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: 108.87  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFE 183
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYN---------RRNCILADEMGLGKTIQSIAFLEHLYQVEGIR-GPFLVIAPLSTIPNWQREFE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWqeglkddeklevSELATVkrpqersymLQRWQEDGGVMIIGYEMYRNLAQGRnVKSRKLK--------EIFNK---AL 252
Cdd:cd17995    71 TW------------TDMNVV---------VYHGSGESRQIIQQYEMYFKDAQGR-KKKGVYKfdvlittyEMVIAdaeEL 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380798987  253 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd17995   129 RKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 103-330 8.84e-26

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: 107.07  E-value: 8.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  103 KLKPHQVDGVQFMWdccceSVKKTKKSPgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 182
Cdd:cd17996     3 TLKEYQLKGLQWMV-----SLYNNNLNG----ILADEMGLGKTIQTISLI-TYLMEKKKNNGPYLVIVPLSTLSNWVSEF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEglkddeklEVSELATVKRPQERSyMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSR-KLKEIFNKalvdpgpdF 259
Cdd:cd17996    73 EKWAP--------SVSKIVYKGTPDVRK-KLQSQIRAGkfNVLLTTYEYI--------IKDKpLLSKIKWK--------Y 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380798987  260 VVCDEGHILKNEASAVSKAMNS-IRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 330
Cdd:cd17996   128 MIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFAN 199
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 104-309 7.22e-25

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: 102.85  E-value: 7.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMwdcccESVKKTKKSpgsgCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEFE 183
Cdd:cd17998     1 LKDYQLIGLNWL-----NLLYQKKLS----GILADEMGLGKTIQVIAFL--AYLKEIGIPGPHLVVVPSSTLDNWLREFK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLKddekLEVSELATVKRPQERsYMLQRWQEDGGVMIIGYemyrNLAQGrNVKSRKLKEIFNKalvdpgpDFVVCD 263
Cdd:cd17998    70 RWCPSLK----VEPYYGSQEERKHLR-YDILKGLEDFDVIVTTY----NLATS-NPDDRSFFKRLKL-------NYVVYD 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 380798987  264 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 309
Cdd:cd17998   133 EGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 135-328 1.43e-24

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: 103.20  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFL-HtvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLKddeklevsELATVKRPQERSYML 213
Cdd:cd18003    23 ILADEMGLGKTIQTIALLaH--LACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFK--------ILTYYGSAKERKLKR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  214 QRWQEDGG--VMIIGYEMyrnLAQGRNV-KSRKLKeifnkalvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIIL 290
Cdd:cd18003    93 QGWMKPNSfhVCITSYQL---VVQDHQVfKRKKWK-------------YLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 380798987  291 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 328
Cdd:cd18003   157 TGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL 194
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 135-320 1.70e-22

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: 97.01  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddekleVSELATVKrpQERSYMLQ 214
Cdd:cd17997    26 ILADEMGLGKTLQTISLLGYLKHYKNIN-GPHLIIVPKSTLDNWMREFKRWCPSLR------VVVLIGDK--EERADIIR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  215 RWQEDG--GVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTG 292
Cdd:cd17997    97 DVLLPGkfDVCITSYEMVI-----------KEKTVLKKF----NWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161

                         170       180
                  ....*....|....*....|....*...
gi 380798987  293 TPLQNNLIEYHCMVNFIKENLLGSIKEF 320
Cdd:cd17997   162 TPLQNNLHELWALLNFLLPDVFTSSEDF 189
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 103-320 3.57e-22

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: 95.89  E-value: 3.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  103 KLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 182
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCK---------GNNGILADEMGLGKTVQTISFL-SYLFHSQQQYGPFLVVVPLSTMPAWQREF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKddeklEVSELATVKRPQersymlqrwqedggvMIIGYEMYRNlaqgrnvKSRKLK--------EIFNKALVD 254
Cdd:cd17993    71 AKWAPDMN-----VIVYLGDIKSRD---------------TIREYEFYFS-------QTKKLKfnvllttyEIILKDKAF 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380798987  255 PGP---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 320
Cdd:cd17993   124 LGSikwQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF 192
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 104-332 1.84e-21

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: 94.66  E-value: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMwdCCCesvkktkkspgsGCILAHCMGLGKTLQVVSFLHTVLLCD---------------KLDFSTA-L 167
Cdd:cd18008     1 LLPYQKQGLAWM--LPR------------GGILADEMGLGKTIQALALILATRPQDpkipeeleenssdpkKLYLSKTtL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  168 VVCPLNTALNWMNEFEK-------------WQEGLKDDEKLEvselatvkrpqerSYMlqrwqedggVMIIGYEMYRNLA 234
Cdd:cd18008    67 IVVPLSLLSQWKDEIEKhtkpgslkvyvyhGSKRIKSIEELS-------------DYD---------IVITTYGTLASEF 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  235 QGRNVKSRKLKEifnkaLVDPGPDF------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNF 308
Cdd:cd18008   125 PKNKKGGGRDSK-----EKEASPLHrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRF 199

                         250       260
                  ....*....|....*....|....
gi 380798987  309 IKENLLGSIKEFRNRFINPIQNGQ 332
Cdd:cd18008   200 LRVEPFGDYPWFNSDISKPFSKND 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 104-326 3.11e-21

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: 93.27  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 183
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAE---------QHGCILGDEMGLGKTCQTISLL-WYLAGRLKLLGPFLVLCPLSVLDNWKEELN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLK----DDEKLEVSELatvkrpQERSYMLQRWQedggVMIIGYEMYrnLAQGRNVKSRKLKeifnkalvdpgpdF 259
Cdd:cd18006    71 RFAPDLSvityMGDKEKRLDL------QQDIKSTNRFH----VLLTTYEIC--LKDASFLKSFPWA-------------S 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380798987  260 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGsiKEFRNRFIN 326
Cdd:cd18006   126 LVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP--KDKLDDFIK 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 104-335 4.85e-21

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: 92.65  E-value: 4.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFmwdccceSVKKtkkspGSGCILAHCMGLGKTLQVVsflhTVLLCDKLDFStALVVCPLNTALNWMNEFE 183
Cdd:cd18010     1 LLPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAI----AIAAYYREEWP-LLIVCPSSLRLTWADEIE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWqegLKDDEKLEVSELATVKRPQERSymlqrwqeDGGVMIIGYEMyrnlaqgrnvkSRKLKEIFNKAlvdpGPDFVVCD 263
Cdd:cd18010    64 RW---LPSLPPDDIQVIVKSKDGLRDG--------DAKVVIVSYDL-----------LRRLEKQLLAR----KFKVVICD 117

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380798987  264 EGHILKNEASAVSKAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 335
Cdd:cd18010   118 ESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWD 191
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 102-331 1.42e-19

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: 88.91  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  102 IKLKPHQVDGVQFM---WdCCCESVkktkkspgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNW 178
Cdd:cd18054    19 LELRDYQLEGLNWLahsW-CKNNSV-----------ILADEMGLGKTIQTISFL-SYLFHQHQLYGPFLLVVPLSTLTSW 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  179 MNEFEKWQEGLkdDEKLEVSELATVKRPQERSYMLQRWQE-DGGVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 257
Cdd:cd18054    86 QREFEIWAPEI--NVVVYIGDLMSRNTIREYEWIHSQTKRlKFNALITTYEIL--------LKDKTVLGSINWA------ 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380798987  258 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 331
Cdd:cd18054   150 -FLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 562-699 6.14e-18

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: 80.33  E-value: 6.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   562 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 641
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 380798987   642 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 699
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 103-374 2.12e-17

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: 82.79  E-value: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  103 KLKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEF 182
Cdd:cd18064    15 KLRDYQVRGLNWLI---------SLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIP-GPHMVLVPKSTLHNWMAEF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKD-----DEKLEVSELATVKRPQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 257
Cdd:cd18064    85 KRWVPTLRAvcligDKDQRAAFVRDVLLPGE-------WD----VCVTSYEML--------IKEKSVFKKFNWR------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  258 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINpiqNGQCADST 337
Cdd:cd18064   140 -YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT---NNCLGDQK 215

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 380798987  338 MVDVRVMKKRAHILyemlagcvqRKDYTALTKFLPPK 374
Cdd:cd18064   216 LVERLHMVLRPFLL---------RRIKADVEKSLPPK 243
HELICc smart00490
helicase superfamily c-terminal domain;
623-699 2.17e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.64  E-value: 2.17e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380798987    623 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 699
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 131-324 9.98e-17

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: 80.83  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  131 GSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLK-----DDEKLEVSELATVKR 205
Cdd:cd18065    34 GVNGILADEMGLGKTLQTIALLGYLKHYRNIP-GPHMVLVPKSTLHNWMNEFKRWVPSLRavcliGDKDARAAFIRDVMM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  206 PQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSR 285
Cdd:cd18065   113 PGE-------WD----VCVTSYEMV--------IKEKSVFKKFNWR-------YLVIDEAHRIKNEKSKLSEIVREFKTT 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 380798987  286 RRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18065   167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 205
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 104-320 1.08e-16

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: 80.49  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 180
Cdd:cd18057     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTIVFLYS-LYKEGHSKGPYLVSAPLSTIINWER 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  181 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMIiGYEMYRnLAQGRNVKSRKLKEIFNKALVDPGP--- 257
Cdd:cd18057    68 EFEMWAPDFYVVTYTGDKESRSVIRENEFSF------EDNAIRS-GKKVFR-MKKEAQIKFHVLLTSYELITIDQAIlgs 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  258 ---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 320
Cdd:cd18057   140 iewACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTperfNNLEGFLEEF 209
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 104-329 2.12e-16

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: 79.32  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMwdcccesvkktKKSPGSGCILAhcMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALN-WMNEF 182
Cdd:cd18013     1 PHPYQKVAINFI-----------IEHPYCGLFLD--MGLGKTVTTLTALSDLQLDDFT--RRVLVIAPLRVARStWPDEV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWqEGLKDdekLEVSelATVKRPQERSYMLQRwqeDGGVMIIGYEmyrnlaqgrNVKsrKLKEIFNkalvDPGP-DFVV 261
Cdd:cd18013    66 EKW-NHLRN---LTVS--VAVGTERQRSKAANT---PADLYVINRE---------NLK--WLVNKSG----DPWPfDMVV 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380798987  262 CDEGHILKNEASAVSKAMNSIRSR-RRII-LTGTPLQNNLIEYHCMVNFIK--ENLLGSIKEFRNRFINPIQ 329
Cdd:cd18013   122 IDELSSFKSPRSKRFKALRKVRPViKRLIgLTGTPSPNGLMDLWAQIALLDqgERLGRSITAYRERWFDPDK 193
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 104-324 4.21e-16

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: 77.86  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 180
Cdd:cd17994     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTIQTIVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  181 EFEKWqeglkddekleVSELATVkrpqerSYMLQRwqedggVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALVdpgpdfv 260
Cdd:cd17994    68 EFEMW-----------APDFYVV------TYVGDH------VLLTSYELI-------SIDQAILGSIDWAVLV------- 110

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380798987  261 vCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd17994   111 -VDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF 173
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 102-320 7.92e-16

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: 78.17  E-value: 7.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  102 IKLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdFSTALVVCPLNTALNWMNE 181
Cdd:cd18053    19 LELRDYQLNGLNWLAHSWCK---------GNSCILADEMGLGKTIQTISFLNYLFHEHQL-YGPFLLVVPLSTLTSWQRE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  182 FEKWQEG------LKDDEKLEVSELATVKRPQERSYMLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdp 255
Cdd:cd18053    89 IQTWAPQmnavvyLGDINSRNMIRTHEWMHPQTKRLKFN-------ILLTTYEIL--------LKDKSFLGGLNWA---- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380798987  256 gpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 320
Cdd:cd18053   150 ---FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF 211
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 134-324 1.77e-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: 76.62  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  134 CILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPLNTALNWMNEFEKWQEglkddEKLEVSELATVKRPqersyml 213
Cdd:cd18058    22 CILADEMGLGKTIQSITFLSEIFLMGI--RGPFLIIAPLSTITNWEREFRTWTE-----MNAIVYHGSQISRQ------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  214 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 282
Cdd:cd18058    88 ---------MIQQYEMYYRDEQGNPLsgifKFQVVITTFEMILAD-CPELkkinwscVIIDEAHRLKNRNCKLLEGLKLM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 380798987  283 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18058   158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXDc smart00487
DEAD-like helicases superfamily;
102-297 2.03e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 75.99  E-value: 2.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987    102 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 180
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987    181 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 259
Cdd:smart00487   73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 380798987    260 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 297
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 134-324 2.79e-15

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: 76.22  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  134 CILAHCMGLGKTLQVVSFLHTVLLcdKLDFSTALVVCPLNTALNWMNEFEKWQEglkddeklevselatvkrpqeRSYML 213
Cdd:cd18059    22 CILADEMGLGKTIQSITFLYEIYL--KGIHGPFLVIAPLSTIPNWEREFRTWTE---------------------LNVVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  214 QRWQEDGGVMIIGYEMYRNLAQGRNVK-SRKLKEI---FNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 282
Cdd:cd18059    79 YHGSQASRRTIQLYEMYFKDPQGRVIKgSYKFHAIittFEMILTD-CPELrnipwrcVVIDEAHRLKNRNCKLLEGLKMM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 380798987  283 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18059   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 131-324 3.88e-15

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: 75.82  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  131 GSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ--------EGLKDDEKL----EVS 198
Cdd:cd18055    19 GTDTILADEMGLGKTIQTIVFLYS-LYKEGHTKGPFLVSAPLSTIINWEREFQMWApdfyvvtyTGDKDSRAIirenEFS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  199 ELATVKRPQERSYMLQRW-QEDGGVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSK 277
Cdd:cd18055    98 FDDNAVKGGKKAFKMKREaQVKFHVLLTSYELV-------TIDQAALGSIRWACL--------VVDEAHRLKNNQSKFFR 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 380798987  278 AMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18055   163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 104-320 4.73e-15

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: 75.87  E-value: 4.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 180
Cdd:cd18056     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTAVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  181 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMiiGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGP--- 257
Cdd:cd18056    68 EFEMWAPDMYVVTYVGDKDSRAIIRENEFSF------EDNAIR--GGKKASRMKKEASVKFHVLLTSYELITIDMAIlgs 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  258 -DF--VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 320
Cdd:cd18056   140 iDWacLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTperfHNLEGFLEEF 209
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 135-349 1.53e-14

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: 74.71  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddeKLEVSELATVKR---PQERSY 211
Cdd:cd18063    46 ILADEMGLGKTIQTIALITYLMEHKRLN-GPYLIIVPLSTLSNWTYEFDKWAPSVV---KISYKGTPAMRRslvPQLRSG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  212 MLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIIL 290
Cdd:cd18063   122 KFN-------VLLTTYEYI--------IKDKHI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILL 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  291 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 349
Cdd:cd18063   180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLH 239
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 104-330 1.69e-14

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: 74.08  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLD-FSTALVVCPLNTALNWMNEF 182
Cdd:cd18002     1 LKEYQLKGLNWLANL---------YEQGINGILADEMGLGKTVQSIAVL--AHLAEEHNiWGPFLVIAPASTLHNWQQEI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  183 EKWQEGLKddeklevsELATVKRPQERSYMLQRWQ------EDGG--VMIIGYEMY-RNLAQGRNVKSRklkeifnkalv 253
Cdd:cd18002    70 SRFVPQFK--------VLPYWGNPKDRKVLRKFWDrknlytRDAPfhVVITSYQLVvQDEKYFQRVKWQ----------- 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380798987  254 dpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 330
Cdd:cd18002   131 -----YMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIES 202
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 96-331 2.53e-14

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: 73.66  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987   96 VHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSflhtVLLCDKldfstALVVCPLNTA 175
Cdd:cd18071    13 VSRENSQDLPPFWEEAVGLFLNTITNFSQKKRPELVRGGILADDMGLGKTLTTIS----LILANF-----TLIVCPLSVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  176 LNWMNEFEKwqeglkddeklevselaTVKRPQERSYMlqrwqedggvmiigyemYRNLAQGRNVKSRKLKEI----FNKA 251
Cdd:cd18071    84 SNWETQFEE-----------------HVKPGQLKVYT-----------------YHGGERNRDPKLLSKYDIvlttYNTL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  252 LVDPG--PDF---------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLgSIKEF 320
Cdd:cd18071   130 ASDFGakGDSplhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPF-SNPEY 208

                         250
                  ....*....|..
gi 380798987  321 RNRFI-NPIQNG 331
Cdd:cd18071   209 WRRLIqRPLTMG 220
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 135-349 1.07e-13

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: 72.00  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  135 ILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEglkddeklEVSELATVKRPQ-ERSYML 213
Cdd:cd18062    46 ILADEMGLGKTIQTIALI-TYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAP--------SVVKVSYKGSPAaRRAFVP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  214 QRWQEDGGVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIILTG 292
Cdd:cd18062   117 QLRSGKFNVLLTTYEYI--------IKDKQI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTG 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 380798987  293 TPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 349
Cdd:cd18062   182 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLH 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 134-324 1.18e-13

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: 71.24  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  134 CILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFEKWQEGlkdDEKLEVSELATVKrpqersyml 213
Cdd:cd18060    22 CILADEMGLGKTIQSIAFLQEVYNVGIH--GPFLVIAPLSTITNWEREFNTWTEM---NTIVYHGSLASRQ--------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  214 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 282
Cdd:cd18060    88 ---------MIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLDSLKHM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 380798987  283 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18060   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 134-324 4.10e-13

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: 69.65  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  134 CILAHCMGLGKTLQVVSFLHTVLLCD-KLDFstaLVVCPLNTALNWMNEFEKWQeglkdDEKLEVSELATVKRPqersyM 212
Cdd:cd18061    22 CILADEMGLGKTIQSITFLYEILLTGiRGPF---LIIAPLSTIANWEREFRTWT-----DLNVVVYHGSLISRQ-----M 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  213 LQRwqedggvmiigYEMYRNLAQGRNVK-SRKLKEIFN--KALVDPGPDF-------VVCDEGHILKNEASAVSKAMNSI 282
Cdd:cd18061    89 IQQ-----------YEMYFRDSQGRIIRgAYRFQAIITtfEMILGGCPELnaidwrcVIIDEAHRLKNKNCKLLEGLKLM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 380798987  283 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 324
Cdd:cd18061   158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 104-321 1.62e-10

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: 61.92  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFMWDcccesvkktKKSPGsgCILAHCMGLGKTLQVVSFLHTVLLCDKLDFstALVVCPlnTALNwmnefE 183
Cdd:cd18011     1 PLPHQIDAVLRALR---------KPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKR--VLILCP--ASLV-----E 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  184 KWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEdGGVMIIGYEMYRnlaqgRNVKSRKLkeifnkaLVDPGPDFVVCD 263
Cdd:cd18011    61 QWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEE-FPIVIVSLDLLK-----RSEERRGL-------LLSEEWDLVVVD 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380798987  264 EGHILKNEASAVS----KAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFR 321
Cdd:cd18011   128 EAHKLRNSGGGKEtkryKLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 104-310 2.31e-09

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: 59.03  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  104 LKPHQVDGVQFM-WdcccesvkKTKKSPgSGCILAHCMGLGKTLQVVSF------------------LHTVLLC-DKLDF 163
Cdd:cd18072     1 LLLHQKQALAWLlW--------RERQKP-RGGILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKkDSTLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380798987  164 STA--LVVCPLNTALNWMNEFEKWQEGlkddEKLEVSELATVKRpQERSYMLQRWQedggVMIIGYemyrnlaqgrNVKS 241
Cdd:cd18072    72 PSAgtLVVCPASLVHQWKNEVESRVAS----NKLRVCLYHGPNR-ERIGEVLRDYD----IVITTY----------SLVA 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380798987  242 RKLKEIFNKALVDPGPDF----VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 310
Cdd:cd18072   133 KEIPTYKEESRSSPLFRIawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 657-709 1.16e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.23  E-value: 1.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 380798987  657 FIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQtKPVYVYRF 709
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILF 76
 
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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