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Conserved domains on  [gi|383417901|gb|AFH32164|]
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lymphoid-specific helicase [Macaca mulatta]

Protein Classification

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1; DEAD/DEAH box helicase family protein( domain architecture ID 13029275)

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1) is a DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization| DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
219-452 2.76e-167

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: 483.81  E-value: 2.76e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 219 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 299 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 452
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
220-822 1.80e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.02  E-value: 1.80e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  220 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  299 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 458
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  459 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketvelsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 538
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  539 DRERtvvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 616
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  617 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 695
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  696 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTVDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 775
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 383417901  776 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 822
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
 
Name Accession Description Interval E-value
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
219-452 2.76e-167

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: 483.81  E-value: 2.76e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 219 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 299 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 452
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
220-822 1.80e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.02  E-value: 1.80e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  220 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  299 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 458
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  459 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketvelsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 538
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  539 DRERtvvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 616
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  617 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 695
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  696 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTVDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 775
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 383417901  776 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 822
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
214-746 1.66e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 439.28  E-value: 1.66e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 214 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFA 293
Cdd:COG0553  235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 294 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 373
Cdd:COG0553  314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 453
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 454 DVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketvelspTGRPKRRTRKSInyskiddfpneleklisq 533
Cdd:COG0553  456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 534 iqpevdrertvvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 613
Cdd:COG0553  505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 614 GHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPEVFIFLVSTRAGGLGINLTAADTVIIYDS 693
Cdd:COG0553  549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 383417901 694 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTVDQKIVERAAAKRKLEKLII 746
Cdd:COG0553  629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
225-576 2.99e-85

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: 273.41  E-value: 2.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  225 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFA--PDIP 297
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  298 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 377
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  378 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 457
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  458 EVPPKREVVVYAPLSKKQEIFYTAIVnrtianmfgsseketvelsptgrpkrrtrksinyskiddfpneLEKLISQIQpe 537
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 383417901  538 vdrertvvevNIPVESEVNLKLQNIMMLLRKCCNHPYLI 576
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
597-722 1.29e-62

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: 206.94  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 597 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPEVFIFLVSTRAG 676
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 383417901 677 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 722
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
598-711 4.79e-30

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: 114.62  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  598 GKFLILDRMLPelKKRGHKVLLFSQMTSMLDILMdYCHLRDFNFSRLDGSMSYSEREKNMHSFNmdPEVFIFLVSTRAGG 677
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 383417901  678 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 711
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
214-402 2.29e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   214 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 292
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   293 APD---IPTMLYHGTQEERQKlvRNIYKRKgtlqiHPVVITSFEIAMRD--RNALQHCYWKYLIVDEGHRIKNM--KCRL 365
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQL--RKLESGK-----TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 383417901   366 IRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 402
Cdd:smart00487 151 EKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
HELICc smart00490
helicase superfamily c-terminal domain;
628-711 1.31e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   628 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 707
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 383417901   708 HRIG 711
Cdd:smart00490  79 GRAG 82
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
244-741 1.57e-22

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 103.61  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 244 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRFA--PDIPTMLYhgTQEERQKLVRNIYKRKG 320
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKFDleSLILDSLT--VEKDAKKWNKRLTDNKK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 321 TLqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSE 391
Cdd:NF038318 128 VR----IVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 392 LWSLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--LEVPPKREVVVYA 469
Cdd:NF038318 198 LYGLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdyMQFKKRKCITVDF 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 470 PLSK-------------KQEIFYtAI--VNRT-----IANMFGSSE----------KETVELSPTGRPKRRTRKSINY-- 517
Cdd:NF038318 262 ELSPdeielyvrvnnflKRDILY-SIptSNRTliilvIRKLLASSSfalaetfevlKKRLEKLKEGTRSANAQEGFDLfw 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 518 ----SKIDDFPNEL---EKLISQ---IQPEVDrertVVEVNIPVESEV--NLKLQNIMMLLRKCCNHpylieypidpvTQ 585
Cdd:NF038318 341 sfveDEIDESGFEEkqdELYTRQkefIQHEID----EVDAIIDVAKRIktNAKVTALKTALEIAFEY-----------QR 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 586 EFKIDEELV--TNS---GKFlildrMLPELKKRGHK---VLLFS-----QMTSMLdilmdYCHLRDFNFSRLDGSMSYSE 652
Cdd:NF038318 406 EEGIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNgdfddAMTKEI-----YRAWQVKNYGKANYGRSVEY 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 653 REKNMHSFNMDPEVfifLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTVDQKI 731
Cdd:NF038318 476 KHAIVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRV 552
                        570
                 ....*....|
gi 383417901 732 VERAAAKRKL 741
Cdd:NF038318 553 YEILSEKFEL 562
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
222-384 9.68e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.42  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFAPDIPTm 299
Cdd:COG1061   81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 300 lyHGTQEERQKlvrniykrkgtlqihPVVITSFEIAMRD--RNALQHcYWKYLIVDEGHRIKNMKCRLIreLKRFNADNK 377
Cdd:COG1061  157 --GGGKKDSDA---------------PITVATYQSLARRahLDELGD-RFGLVIIDEAHHAGAPSYRRI--LEAFPAAYR 216

                 ....*..
gi 383417901 378 LLLTGTP 384
Cdd:COG1061  217 LGLTATP 223
 
Name Accession Description Interval E-value
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
219-452 2.76e-167

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: 483.81  E-value: 2.76e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 219 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 299 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 452
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
220-822 1.80e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.02  E-value: 1.80e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  220 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPT 298
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  299 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 378
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  379 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 458
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  459 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketvelsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 538
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  539 DRERtvvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 616
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  617 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 695
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  696 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTVDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 775
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 383417901  776 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 822
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
214-746 1.66e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 439.28  E-value: 1.66e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 214 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFA 293
Cdd:COG0553  235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 294 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 373
Cdd:COG0553  314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 453
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 454 DVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketvelspTGRPKRRTRKSInyskiddfpneleklisq 533
Cdd:COG0553  456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 534 iqpevdrertvvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 613
Cdd:COG0553  505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 614 GHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPEVFIFLVSTRAGGLGINLTAADTVIIYDS 693
Cdd:COG0553  549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 383417901 694 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTVDQKIVERAAAKRKLEKLII 746
Cdd:COG0553  629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
219-452 1.03e-87

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: 277.28  E-value: 1.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 219 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFAPDIP 297
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 298 TMLYHGTQEERQKLVRNIYKRKGtlqiHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 377
Cdd:cd17997   81 VVVLIGDKEERADIIRDVLLPGK----FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 378 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLK 452
Cdd:cd17997  157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQR---------LHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
225-576 2.99e-85

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: 273.41  E-value: 2.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  225 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFA--PDIP 297
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  298 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 377
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  378 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 457
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  458 EVPPKREVVVYAPLSKKQEIFYTAIVnrtianmfgsseketvelsptgrpkrrtrksinyskiddfpneLEKLISQIQpe 537
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 383417901  538 vdrertvvevNIPVESEVNLKLQNIMMLLRKCCNHPYLI 576
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
219-452 5.92e-85

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: 270.39  E-value: 5.92e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 219 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIP 297
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITyLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 298 TMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKR-FNADN 376
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQI--RAGKFN---VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARY 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383417901 377 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVL--HMLHQILTPFLLRRLK 452
Cdd:cd17996  156 RLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLiiRRLHKVLRPFLLRRLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
222-404 6.37e-80

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: 255.18  E-value: 6.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMI-QRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTML 300
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 301 YHGTQEERQKLVRNIYKRKGtlqihPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 380
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDKF-----DVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155
                        170       180
                 ....*....|....*....|....
gi 383417901 381 TGTPLQNNLSELWSLLNFLLPDVF 404
Cdd:cd17919  156 TGTPLQNNLEELWALLDFLDPPFL 179
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
222-450 2.66e-71

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: 233.78  E-value: 2.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTML 300
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 301 YHGTQEERQKlvrniyKRKGTLQ---IHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 377
Cdd:cd18003   81 YYGSAKERKL------KRQGWMKpnsFH-VCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 378 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 450
Cdd:cd18003  154 LLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpLTAMSEGSQEE-----NEELVRRLHKVLRPFLLRR 223
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
220-452 3.40e-69

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: 227.83  E-value: 3.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 220 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTM 299
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 300 LYHGTQEERQKLVRniykrkgtLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLL 379
Cdd:cd18012   83 VIHGTKRKREKLRA--------LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383417901 380 LTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITslsetaediIAKEREQNVLHMLHQILTPFLLRRLK 452
Cdd:cd18012  155 LTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP---------IEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
214-463 4.71e-69

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: 228.40  E-value: 4.71e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 214 PKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRF 292
Cdd:cd18064    8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 293 APDIPTMLYHGTQEERQKLVRNIYkRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRF 372
Cdd:cd18064   88 VPTLRAVCLIGDKDQRAAFVRDVL-LPGEWD---VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 373 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRRLK 452
Cdd:cd18064  164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG----------DQKLVERLHMVLRPFLLRRIK 233
                        250
                 ....*....|.
gi 383417901 453 SDVALEVPPKR 463
Cdd:cd18064  234 ADVEKSLPPKK 244
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
222-450 2.20e-66

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: 220.58  E-value: 2.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFApDIPTML 300
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 301 YHGTQEERQKL--------VRNIYKRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRF 372
Cdd:cd17995   80 YHGSGESRQIIqqyemyfkDAQGRKKKGVYKFD-VLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383417901 373 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF-DItslsETAEDIiakEReqnvlhmLHQILTPFLLRR 450
Cdd:cd17995  159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFgDL----KTAEQV---EK-------LQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
222-450 4.45e-65

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: 216.84  E-value: 4.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTML 300
Cdd:cd17993    2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSyLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 301 YHGTQEERQkLVRN----IYKRKgTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 376
Cdd:cd17993   82 YLGDIKSRD-TIREyefyFSQTK-KLKFN-VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383417901 377 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFEswfdiTSLSETAEDIIAKereqnvlhmLHQILTPFLLRR 450
Cdd:cd17993  159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-----EEHDEEQEKGIAD---------LHKELEPFILRR 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
225-450 1.72e-64

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: 215.45  E-value: 1.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18002    4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIYKRKGTLQIHP--VVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 381
Cdd:cd18002   84 NPKDRKVLRKFWDRKNLYTRDAPfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383417901 382 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF--DITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 450
Cdd:cd18002  164 GTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAENKTGL-----NEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
212-452 2.71e-64

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: 215.27  E-value: 2.71e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 212 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFK 290
Cdd:cd18065    6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 291 RFAPDIPTMLYHGTQEERQKLVRNIYKrKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 370
Cdd:cd18065   86 RWVPSLRAVCLIGDKDARAAFIRDVMM-PGEWD---VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 371 RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRR 450
Cdd:cd18065  162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG----------DQKLVERLHAVLKPFLLRR 231

                 ..
gi 383417901 451 LK 452
Cdd:cd18065  232 IK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
597-722 1.29e-62

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: 206.94  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 597 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPEVFIFLVSTRAG 676
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 383417901 677 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 722
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
212-452 1.03e-61

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: 208.75  E-value: 1.03e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 212 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 290
Cdd:cd18062   14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRINGPFLIIVPLSTLSNWVYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 291 RFAPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 370
Cdd:cd18062   94 KWAPSVVKVSYKGSPAARRAFVPQL--RSGKFN---VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 371 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 448
Cdd:cd18062  169 tHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGEKVDLNEEETIlIIRRLHKVLRPFLL 247

                 ....
gi 383417901 449 RRLK 452
Cdd:cd18062  248 RRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
212-452 1.70e-61

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: 208.38  E-value: 1.70e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 212 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 290
Cdd:cd18063   14 KQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 291 RFAPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 370
Cdd:cd18063   94 KWAPSVVKISYKGTPAMRRSLVPQL--RSGKFN---VLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 371 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 448
Cdd:cd18063  169 tHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGERVDLNEEETIlIIRRLHKVLRPFLL 247

                 ....
gi 383417901 449 RRLK 452
Cdd:cd18063  248 RRLK 251
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
225-404 2.38e-58

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: 197.22  E-value: 2.38e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHGT 304
Cdd:cd17998    4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 305 QEERQKLVRNIYKRKGTLQihpVVITSFEIAM---RDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 381
Cdd:cd17998   84 QEERKHLRYDILKGLEDFD---VIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                        170       180
                 ....*....|....*....|...
gi 383417901 382 GTPLQNNLSELWSLLNFLLPDVF 404
Cdd:cd17998  161 GTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
225-450 3.25e-57

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: 194.58  E-value: 3.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATI-ALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd17994    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLySLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQeerqklvrniykrkgtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGT 383
Cdd:cd17994   84 DH---------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383417901 384 PLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetAEDIIAKereqnvlhmLHQILTPFLLRR 450
Cdd:cd17994  143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFADIS----KEDQIKK---------LHDLLGPHMLRR 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
222-450 4.32e-56

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: 192.27  E-value: 4.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTML 300
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 301 YHGTQEERQKLVRNIYKrkgTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 380
Cdd:cd18006   81 YMGDKEKRLDLQQDIKS---TNRFH-VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383417901 381 TGTPLQNNLSELWSLLNFLLPDVF--DDLKSFESWF-DITSLSETAEDiiakereqnvlhmLHQILTPFLLRR 450
Cdd:cd18006  157 TGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDDESETVEE-------------LHLLLQPFLLRR 216
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
212-450 1.24e-55

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: 191.76  E-value: 1.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 212 QQPKHFTGG--VMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAE 288
Cdd:cd18054    9 KQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSyLFHQHQLYGPFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 289 FKRFAPDIPTMLYHGTQEERqKLVRN---IYKRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRL 365
Cdd:cd18054   89 FEIWAPEINVVVYIGDLMSR-NTIREyewIHSQTKRLKFN-ALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 366 IRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWFDItslsetaEDIIAKEREqNVLHMLHQILTP 445
Cdd:cd18054  167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFEFWEDF-------EEDHGKGRE-NGYQSLHKVLEP 232

                 ....*
gi 383417901 446 FLLRR 450
Cdd:cd18054  233 FLLRR 237
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
225-450 2.14e-51

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: 179.82  E-value: 2.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18055    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 367
Cdd:cd18055   84 DKDSRAIIRENEFsfddnavkggkkafkmKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 368 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 446
Cdd:cd18055  163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228

                 ....
gi 383417901 447 LLRR 450
Cdd:cd18055  229 MLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
222-450 1.19e-50

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: 177.54  E-value: 1.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIAL------MIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPD 295
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 296 --IPTMLYHGTQEERQKLVRNIYKrkgtlqiHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 373
Cdd:cd17999   81 afLKPLAYVGPPQERRRLREQGEK-------HNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETAEdiiAKEREQNVLHM--LHQILTPFLL 448
Cdd:cd17999  154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpiLASRDSKAS---AKEQEAGALALeaLHKQVLPFLL 230

                 ..
gi 383417901 449 RR 450
Cdd:cd17999  231 RR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
224-450 1.31e-50

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: 177.56  E-value: 1.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 224 WYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18001    3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 T-QEERQKLVRNIYKRKGtlqihpVVITSFEIAMRDRNALQHCY-----WKYLIVDEGHRIKNMKCRLIRELKRFNADNK 377
Cdd:cd18001   83 TsKKERERNLERIQRGGG------VLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 378 LLLTGTPLQNNLSELWSLLNFLLP-DVFDDLKSFESWFDITSLSETAEDIIAKERE--QNVLHMLHQILTPFLLRR 450
Cdd:cd18001  157 IILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgSEVAENLRQIIKPYFLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
222-450 2.52e-50

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: 176.39  E-value: 2.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFApDIPTMLY 301
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 302 HGTQEERQKLVR-NIYKR-------KGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 373
Cdd:cd18058   80 HGSQISRQMIQQyEMYYRdeqgnplSGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDItslsetaediiaKEREQnvLHMLHQILTPFLLRR 450
Cdd:cd18058  159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFlEEFGDL------------KTEEQ--VKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
225-450 9.64e-49

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: 172.17  E-value: 9.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18057    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 367
Cdd:cd18057   84 DKESRSVIRENEFsfednairsgkkvfrmKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 368 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 446
Cdd:cd18057  163 VLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228

                 ....
gi 383417901 447 LLRR 450
Cdd:cd18057  229 MLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
222-450 2.32e-48

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: 170.98  E-value: 2.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFApDIPTMLY 301
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 302 HGTQEERQKL-VRNIYKR-------KGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 373
Cdd:cd18059   80 HGSQASRRTIqLYEMYFKdpqgrviKGSYKFH-AIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 450
Cdd:cd18059  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
222-450 3.52e-47

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: 167.54  E-value: 3.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFApDIPTMLY 301
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 302 HGTQEERQKLVR-NIYKRKGTLQIHP------VVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNA 374
Cdd:cd18060   80 HGSLASRQMIQQyEMYCKDSRGRLIPgaykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 375 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 450
Cdd:cd18060  160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
225-450 8.65e-47

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: 166.78  E-value: 8.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18056    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 367
Cdd:cd18056   84 DKDSRAIIRENEFsfednairggkkasrmKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 368 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFeswfditsLSETAEdiIAKEREqnvLHMLHQILTPFL 447
Cdd:cd18056  163 VLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF--------LEEFAD--IAKEDQ---IKKLHDMLGPHM 229

                 ...
gi 383417901 448 LRR 450
Cdd:cd18056  230 LRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
225-401 3.20e-43

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: 155.17  E-value: 3.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALM--IQRGVpGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYH 302
Cdd:cd18000    4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhhSKLGL-GPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 303 ------------GTQEERQKLVRNIYKRKGtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 370
Cdd:cd18000   83 ssgsgtgseeklGSIERKSQLIRKVVGDGG------ILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACK 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 383417901 371 RFNADNKLLLTGTPLQNNLSELWSLLNFLLP 401
Cdd:cd18000  157 QLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
209-450 1.34e-42

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: 155.21  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 209 VPFQQPKHFTGGV----MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLP 283
Cdd:cd18053    4 VALKKQPSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNyLFHEHQLYGPFLLVVPLSTLT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 284 NWMAEFKRFAPDIPTMLYHGTQEERQKLVRNIYKRKGTLQIH-PVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMK 362
Cdd:cd18053   84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 363 CRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWfditslsETAEDIIAKEREQNVLHmLHQI 442
Cdd:cd18053  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFSSW-------EDFEEEHGKGREYGYAS-LHKE 229

                 ....*...
gi 383417901 443 LTPFLLRR 450
Cdd:cd18053  230 LEPFLLRR 237
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
222-450 1.81e-42

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: 154.39  E-value: 1.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFApDIPTMLY 301
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 302 HGTQEERQKLVR-NIYKRKGTLQI------HPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNA 374
Cdd:cd18061   80 HGSLISRQMIQQyEMYFRDSQGRIirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383417901 375 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 450
Cdd:cd18061  160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
225-450 2.33e-40

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: 148.97  E-value: 2.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWlrMLWeNGinGILADEMGLGKTVQCIATIAL------------------MIQRGVPGPFLVCGPLSTLPNWM 286
Cdd:cd18008    4 YQKQGLAW--MLP-RG--GILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLSQWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 287 AEFKRF--APDIPTMLYHGTQeerqklvRNIYKRKgtLQIHPVVITSFEI----------------AMRDRNALQHCYWK 348
Cdd:cd18008   79 DEIEKHtkPGSLKVYVYHGSK-------RIKSIEE--LSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 349 YLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFesWFDITSLSetaediia 428
Cdd:cd18008  150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF--NSDISKPF-------- 219
                        250       260
                 ....*....|....*....|..
gi 383417901 429 KEREQNVLHMLHQILTPFLLRR 450
Cdd:cd18008  220 SKNDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
222-450 9.29e-39

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: 144.35  E-value: 9.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWL--RMLWENGING---ILADEMGLGKTVQCIATIALMIQRGVPGP-----FLVCGPLSTLPNWMAEFKR 291
Cdd:cd18004    1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 292 FAPDIPTMLYhgTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQH---CywKYLIVDEGHRIKNMKCRLIRE 368
Cdd:cd18004   81 WLGLRRIKVV--TADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkisI--DLLICDEGHRLKNSESKTTKA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 369 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIIAKEREQNVLHMLHQILTPF 446
Cdd:cd18004  157 LNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepILRSRDPDASEEDKELGAERSQELSELTSRF 236

                 ....
gi 383417901 447 LLRR 450
Cdd:cd18004  237 ILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
222-450 5.86e-38

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: 142.13  E-value: 5.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR---------------------GVPGPFLVCGPLS 280
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 281 TLPNWMAEFKRFApDIPTMLYHGTQEERQKLVRniYKRkGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKN 360
Cdd:cd18005   81 VLYNWKDELDTWG-HFEVGVYHGSRKDDELEGR--LKA-GRLE---VVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 361 MKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDI-----TSLSETAEDI-IAKEREQn 434
Cdd:cd18005  154 PKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgQRHTATARELrLGRKRKQ- 232
                        250
                 ....*....|....*.
gi 383417901 435 vlhMLHQILTPFLLRR 450
Cdd:cd18005  233 ---ELAVKLSKFFLRR 245
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
222-414 9.46e-31

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: 121.24  E-value: 9.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGmewLRMLWEN---------GING-ILADEMGLGKTVQCIATIALMIQRGVPG--PFLVCgPLSTLPNWMAEF 289
Cdd:cd18007    1 LKPHQVEG---VRFLWSNlvgtdvgsdEGGGcILAHTMGLGKTLQVITFLHTYLAAAPRRsrPLVLC-PASTLYNWEDEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 290 KRFAPD---IPTMLY----HGTQEERQKLVRNIYKRKGTLqihpvVIT--SFEIAMRDRNALQHCYWKY----------- 349
Cdd:cd18007   77 KKWLPPdlrPLLVLVslsaSKRADARLRKINKWHKEGGVL-----LIGyeLFRNLASNATTDPRLKQEFiaalldpgpdl 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 350 LIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 414
Cdd:cd18007  152 LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
598-711 4.79e-30

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: 114.62  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  598 GKFLILDRMLPelKKRGHKVLLFSQMTSMLDILMdYCHLRDFNFSRLDGSMSYSEREKNMHSFNmdPEVFIFLVSTRAGG 677
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 383417901  678 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 711
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
222-450 8.45e-29

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 115.64  E-value: 8.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGmewLRMLWE-------NGING-ILADEMGLGKTVQCIATI-ALMIQRGVPGPFL----VCGPLSTLPNWMAE 288
Cdd:cd18067    1 LRPHQREG---VKFLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMwTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 289 F-KRFAPDIPTMLYHGTQ--EERQKLVRNIYKRkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRL 365
Cdd:cd18067   78 LgKWLGGRLQPLAIDGGSkkEIDRKLVQWASQQ-GRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 366 IRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNV--LHMLHQIL 443
Cdd:cd18067  157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEekLQELISIV 236

                 ....*..
gi 383417901 444 TPFLLRR 450
Cdd:cd18067  237 NRCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
214-402 2.29e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 2.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   214 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 292
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   293 APD---IPTMLYHGTQEERQKlvRNIYKRKgtlqiHPVVITSFEIAMRD--RNALQHCYWKYLIVDEGHRIKNM--KCRL 365
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQL--RKLESGK-----TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 383417901   366 IRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 402
Cdd:smart00487 151 EKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
225-410 7.93e-24

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: 100.36  E-value: 7.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEW-LRmlweNGINGILADEMGLGKTVQCIAtIALMIQRgvPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18010    4 FQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA-IAAYYRE--EWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIYKrkgtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMK---CRLIRELKRfNADNKLLL 380
Cdd:cd18010   77 IVKSKDGLRDGDAK---------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAALPLLK-RAKRVILL 146
                        170       180       190
                 ....*....|....*....|....*....|
gi 383417901 381 TGTPLQNNLSELWSLLNFLLPDVFDDLKSF 410
Cdd:cd18010  147 SGTPALSRPIELFTQLDALDPKLFGRFHDF 176
HELICc smart00490
helicase superfamily c-terminal domain;
628-711 1.31e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901   628 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNMDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 707
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 383417901   708 HRIG 711
Cdd:smart00490  79 GRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
225-412 6.46e-23

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: 97.36  E-value: 6.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGmewLRMLWENGING-ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFAPDIPTMLYHG 303
Cdd:cd18011    4 HQIDA---VLRALRKPPVRlLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 304 TQEERQKLVRNIYKRkgtlqiHPVVITSFEIAMRDRNALQHCY---WKYLIVDEGHRIKNMKC-------RLIRELKRfN 373
Cdd:cd18011   81 TAAQLRRLIGNPFEE------FPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRNSGGgketkryKLGRLLAK-R 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 383417901 374 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFES 412
Cdd:cd18011  154 ARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
222-450 1.16e-22

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: 97.61  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLR-----MLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGP------FLVCGPLSTLPNWMAEFK 290
Cdd:cd18066    1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 291 RFApdiptmlyhGTQEERQKLVRNIYKRKGTLQ--IHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRE 368
Cdd:cd18066   81 KWL---------GSERIKVFTVDQDHKVEEFIAspLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 369 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETA---EDIIAKEREQNvlhmLHQI 442
Cdd:cd18066  152 LTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepiVRSREPTAtpeEKKLGEARAAE----LTRL 227

                 ....*...
gi 383417901 443 LTPFLLRR 450
Cdd:cd18066  228 TGLFILRR 235
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
244-741 1.57e-22

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 103.61  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 244 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRFA--PDIPTMLYhgTQEERQKLVRNIYKRKG 320
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKFDleSLILDSLT--VEKDAKKWNKRLTDNKK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 321 TLqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSE 391
Cdd:NF038318 128 VR----IVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 392 LWSLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--LEVPPKREVVVYA 469
Cdd:NF038318 198 LYGLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdyMQFKKRKCITVDF 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 470 PLSK-------------KQEIFYtAI--VNRT-----IANMFGSSE----------KETVELSPTGRPKRRTRKSINY-- 517
Cdd:NF038318 262 ELSPdeielyvrvnnflKRDILY-SIptSNRTliilvIRKLLASSSfalaetfevlKKRLEKLKEGTRSANAQEGFDLfw 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 518 ----SKIDDFPNEL---EKLISQ---IQPEVDrertVVEVNIPVESEV--NLKLQNIMMLLRKCCNHpylieypidpvTQ 585
Cdd:NF038318 341 sfveDEIDESGFEEkqdELYTRQkefIQHEID----EVDAIIDVAKRIktNAKVTALKTALEIAFEY-----------QR 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 586 EFKIDEELV--TNS---GKFlildrMLPELKKRGHK---VLLFS-----QMTSMLdilmdYCHLRDFNFSRLDGSMSYSE 652
Cdd:NF038318 406 EEGIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNgdfddAMTKEI-----YRAWQVKNYGKANYGRSVEY 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 653 REKNMHSFNMDPEVfifLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTVDQKI 731
Cdd:NF038318 476 KHAIVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRV 552
                        570
                 ....*....|
gi 383417901 732 VERAAAKRKL 741
Cdd:NF038318 553 YEILSEKFEL 562
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
225-415 4.29e-22

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: 95.65  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGmewLRMLWEN------------GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 292
Cdd:cd18069    4 HQIGG---IRFLYDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 293 AP---DIPTMLY-----------HGTQEERQKLVRNIYKRKGtlqihpVVITSFEIaMRDRNALQhcywkYLIVDEGHRI 358
Cdd:cd18069   81 LPppeALPNVRPrpfkvfilndeHKTTAARAKVIEDWVKDGG------VLLMGYEM-FRLRPGPD-----VVICDEGHRI 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 383417901 359 KNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD 415
Cdd:cd18069  149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
238-399 5.01e-21

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: 92.92  E-value: 5.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 238 ENGINGILADEMGLGKTVQCIATIalmiqrgVPGPFLVCGPLSTLPNWMAEFKR-FAPDIPTM-LYHGTqeERQKLVRNI 315
Cdd:cd18071   46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEhVKPGQLKVyTYHGG--ERNRDPKLL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 316 YKRKgtlqihpVVITSFEIAMRDRNA-----LQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLS 390
Cdd:cd18071  117 SKYD-------IVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189

                 ....*....
gi 383417901 391 ELWSLLNFL 399
Cdd:cd18071  190 DLGSLLSFL 198
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
225-450 2.57e-20

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: 91.00  E-value: 2.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 225 YQVEGMEWlrMLW---ENGINGILADEMGLGKTVQCIATIaLMIQRG-----------------------VP--GPFLVC 276
Cdd:cd18072    4 HQKQALAW--LLWrerQKPRGGILADDMGLGKTLTMIALI-LAQKNTqnrkeeekekalteweskkdstlVPsaGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 277 gPLSTLPNWMAEF-KRFAPD-IPTMLYHGTQEERQKLVrniykrkgtLQIHPVVITSFEIAMRD---------RNALQHC 345
Cdd:cd18072   81 -PASLVHQWKNEVeSRVASNkLRVCLYHGPNRERIGEV---------LRDYDIVITTYSLVAKEiptykeesrSSPLFRI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 346 YWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSetaed 425
Cdd:cd18072  151 AWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRK----- 225
                        250       260
                 ....*....|....*....|....*
gi 383417901 426 iiAKEReqnvlhmLHQILTPFLLRR 450
Cdd:cd18072  226 --GGER-------LNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
240-414 4.29e-16

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: 78.78  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 240 GINGILADEMGLGKTVQCIA---TIALMIQRGVPGPFLVCGPLSTLPNWMAEFKR---FAPDIPTM------LYHGTQEE 307
Cdd:cd18068   28 GSGCILAHCMGLGKTLQVVTflhTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKwqeGLKDEEKIevnelaTYKRPQER 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 308 RQKLVRniYKRKGTLQI---HPVVITSFEIAMRDRNALQHCYWKYL--------IVDEGHRIKNMKCRLIRELKRFNADN 376
Cdd:cd18068  108 SYKLQR--WQEEGGVMIigyDMYRILAQERNVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSIRTKR 185
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 383417901 377 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 414
Cdd:cd18068  186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
222-449 4.66e-16

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 78.92  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWlrMLWENGIngiLADEMGLGKTVQCIATIAL-------------------MIQRGVP-------GPFLV 275
Cdd:cd18070    1 LLPYQRRAVNW--MLVPGGI---LADEMGLGKTVEVLALILLhprpdndldaadddsdemvCCPDCLVaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 276 CGPLSTLPNWMAEFKRFAPDIPTMLYHGTQEERQKLVRNIYKRkgtLQIHPVVITSFEI--------------------- 334
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEI---LAEYDIVVTTYDVlrtelhyaeanrsnrrrrrqk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 335 -AMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDlksfESW 413
Cdd:cd18070  153 rYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD----SDW 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 383417901 414 FditslsetAEDIIAKEREQNVLHMLHQILTPFLLR 449
Cdd:cd18070  229 W--------ARVLIRPQGRNKAREPLAALLKELLWR 256
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
222-399 1.58e-09

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: 58.90  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEWLRmlwENGINGILADeMGLGKTVQCIATIALMIQRGVPGPFLVCGPL----STLPNWMAEFKRFApDIP 297
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLrvarSTWPDEVEKWNHLR-NLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 298 TMLYHGTQEERQKLVrniykrkgTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK--RFNAD 375
Cdd:cd18013   76 VSVAVGTERQRSKAA--------NTPADLYVINRENLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRkvRPVIK 147
                        170       180
                 ....*....|....*....|....
gi 383417901 376 NKLLLTGTPLQNNLSELWSLLNFL 399
Cdd:cd18013  148 RLIGLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
222-384 9.68e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.42  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFAPDIPTm 299
Cdd:COG1061   81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 300 lyHGTQEERQKlvrniykrkgtlqihPVVITSFEIAMRD--RNALQHcYWKYLIVDEGHRIKNMKCRLIreLKRFNADNK 377
Cdd:COG1061  157 --GGGKKDSDA---------------PITVATYQSLARRahLDELGD-RFGLVIIDEAHHAGAPSYRRI--LEAFPAAYR 216

                 ....*..
gi 383417901 378 LLLTGTP 384
Cdd:COG1061  217 LGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
222-384 1.73e-07

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 51.15  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 222 MRWYQVEGMEwlRMLWENGIN-GILADEMGLGKTVqcIAtIALMIQRGvPGPFLVCGPLSTLPN-WMAEFKRFAPDIPTM 299
Cdd:cd17926    1 LRPYQEEALE--AWLAHKNNRrGILVLPTGSGKTL--TA-LALIAYLK-ELRTLIVVPTDALLDqWKERFEDFLGDSSIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 300 LYhgtQEERQKLVRNIykrkgtlqihPVVITSFEIAMRDRNALQHCY--WKYLIVDEGHRIknmKCRLIRE-LKRFNADN 376
Cdd:cd17926   75 LI---GGGKKKDFDDA----------NVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL---PAKTFSEiLKELNAKY 138

                 ....*...
gi 383417901 377 KLLLTGTP 384
Cdd:cd17926  139 RLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
242-383 4.73e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 50.09  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 242 NGILADEMGLGKTVqcIATIALmIQRGVP--GPFLVCGPLSTL-PNWMAEFK-RFAPDIPT-MLYHGTQEERQKlvrniY 316
Cdd:cd00046    3 NVLITAPTGSGKTL--AALLAA-LLLLLKkgKKVLVLVPTKALaLQTAERLReLFGPGIRVaVLVGGSSAEERE-----K 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 317 KRKGTLQIhpVVITSFEIAMRDRNALQHCY--WKYLIVDEGHRI------KNMKCRLIRELKRFNADnKLLLTGT 383
Cdd:cd00046   75 NKLGDADI--IIATPDMLLNLLLREDRLFLkdLKLIIVDEAHALlidsrgALILDLAVRKAGLKNAQ-VILLSAT 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
665-719 1.88e-06

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: 46.16  E-value: 1.88e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 665 EVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 719
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
564-729 6.35e-06

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 48.86  E-value: 6.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  564 MLLRKCC---NHPYLIEYPIDPVTQEFK-IDEELVTNSGKFLILDRMLPEL----KKRGHKVLLFSQMTSMLDILMDYCH 635
Cdd:pfam11496  52 LCLENLSlvaTHPYLLVDHYMPKSLLLKdEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEALLL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  636 LRDFNFSRLDGSMSYSEREKNmhSFNMDPE----VFIFLVSTR-----AGGLGInlTAADTVIIYDSDWNPQSDLQAQDR 706
Cdd:pfam11496 132 GKGLSYKRYSGEMLYGENKKV--SDSGNKKihstTCHLLSSTGqltndDSLLEN--YKFDLIIAFDSSVDTSSPSVEHLR 207
                         170       180
                  ....*....|....*....|...
gi 383417901  707 CHRIGQTKPVVVYRLVTANTVDQ 729
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEH 230
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
583-713 6.83e-06

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 46.35  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901 583 VTQEFkideELVTNSGKFLILDRMLPELKKRGhKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNm 662
Cdd:cd18787    1 IKQLY----VVVEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 383417901 663 DPEVFIfLVST----RagglGINLTAADTVIIYDsdwNPQSdlqAQDRCHRIGQT 713
Cdd:cd18787   75 SGKVRV-LVATdvaaR----GLDIPGVDHVINYD---LPRD---AEDYVHRIGRT 118
ResIII pfam04851
Type III restriction enzyme, res subunit;
221-384 6.52e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 6.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  221 VMRWYQVEGME-WLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGP-LSTLPNWMAEFKRFAPDiPT 298
Cdd:pfam04851   3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPN-YV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383417901  299 MLYHGTQEERQKLVRNIYKrkgtlqihpVVITSFEIAMRDRNALQHCY----WKYLIVDEGHRI--KNMkcrliRELKRF 372
Cdd:pfam04851  82 EIGEIISGDKKDESVDDNK---------IVVTTIQSLYKALELASLELlpdfFDVIIIDEAHRSgaSSY-----RNILEY 147
                         170
                  ....*....|...
gi 383417901  373 NADNKLL-LTGTP 384
Cdd:pfam04851 148 FKPAFLLgLTATP 160
 
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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