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Conserved domains on  [gi|12232371|ref|NP_032260|]
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lymphocyte-specific helicase [Mus musculus]

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 ...
203-436 2.59e-165

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: 478.03  E-value: 2.59e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 203 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 283 LLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 362
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 363 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 436
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
204-781 8.46e-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: 494.70  E-value: 8.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   204 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   283 LLYHGTREDRRklvkniHKRQGTLQI--HPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 360
Cdd:PLN03142  248 VKFHGNPEERA------HQREELLVAgkFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNY 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   361 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVA 440
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   441 LEVPPKREVVVYAPLCNKQEIFYTAIvnrtianmfgsceketvelsptgrpkrrsrksinyseldqfpseLEKLISQIQP 520
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNA 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   521 EVNRERtvvegnipiesevnlkLRNIMMLLRKCCNHPYMIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRG 598
Cdd:PLN03142  428 GGERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   599 HKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTD-PDVFLFLVSTRAGGLGINLTAADTVIIYDS 677
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   678 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHknhfkggQSGLSQSKNfLDAKELMEL 757
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ-------QGRLAEQKT-VNKDELLQM 639
                         570       580
                  ....*....|....*....|....*
gi 12232371   758 LKsrdYERE-VKGSREKVISDEDLE 781
Cdd:PLN03142  640 VR---YGAEmVFSSKDSTITDEDID 661
 
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 ...
203-436 2.59e-165

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: 478.03  E-value: 2.59e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 203 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 283 LLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 362
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 363 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 436
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
204-781 8.46e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 494.70  E-value: 8.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   204 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   283 LLYHGTREDRRklvkniHKRQGTLQI--HPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 360
Cdd:PLN03142  248 VKFHGNPEERA------HQREELLVAgkFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNY 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   361 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVA 440
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   441 LEVPPKREVVVYAPLCNKQEIFYTAIvnrtianmfgsceketvelsptgrpkrrsrksinyseldqfpseLEKLISQIQP 520
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNA 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   521 EVNRERtvvegnipiesevnlkLRNIMMLLRKCCNHPYMIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRG 598
Cdd:PLN03142  428 GGERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   599 HKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTD-PDVFLFLVSTRAGGLGINLTAADTVIIYDS 677
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   678 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHknhfkggQSGLSQSKNfLDAKELMEL 757
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ-------QGRLAEQKT-VNKDELLQM 639
                         570       580
                  ....*....|....*....|....*
gi 12232371   758 LKsrdYERE-VKGSREKVISDEDLE 781
Cdd:PLN03142  640 VR---YGAEmVFSSKDSTITDEDID 661
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
198-730 4.06e-142

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.42  E-value: 4.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 198 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 277
Cdd:COG0553 235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 278 PEIPTLLYHGTREdRRKLVKNIHKrqgtlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:COG0553 314 PGLRVLVLDGTRE-RAKGANPFED-------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 437
Cdd:COG0553 386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 438 DVALEVPPKREVVVYAPLCNKQEIFYTAIVNRTIANMfgsceketvelspTGRPKRRSRKSInyseldqfpseleklisq 517
Cdd:COG0553 456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 518 iqpevnrertvvegnipiesevnLKLrniMMLLRKCCNHPYMIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 597
Cdd:COG0553 505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 598 GHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAGGLGINLTAADTVIIYDS 677
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|...
gi 12232371 678 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 730
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
209-560 3.41e-84

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: 270.32  E-value: 3.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   209 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PEIP 281
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   282 TLLYHGTREDRRKlVKNIHKRQGTlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:pfam00176  79 VVVLHGNKRPQER-WKNDPNFLAD---FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 441
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   442 EVPPKREVVVYAPLCNKQEIFYTAIVnrtianmfgsceketvelsptgrpkrrsrksinyseldqfpseLEKLISQIQpe 521
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 12232371   522 vnrertvvegNIPIESEVNLKLRNIMMLLRKCCNHPYMI 560
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
581-706 8.08e-63

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: 8.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 581 SGKFLILDRMLPELKKRGHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAG 660
Cdd:cd18793  10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 12232371 661 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 706
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
582-695 1.42e-29

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: 113.07  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   582 GKFLILDRMLPelKKRGHKVLVFSQMTSMLDILMdYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPdvFLFLVSTRAGG 661
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 12232371   662 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 695
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
198-386 3.48e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 3.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    198 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 276
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    277 TPE---IPTLLYHGT--REDRRKLVKNihkrqgtlqIHPVVVTSFEIAMRD--QNALQHCYWKYLIVDEGHRIKNM--KC 347
Cdd:smart00487  78 GPSlglKVVGLYGGDskREQLRKLESG---------KTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGD 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 12232371    348 RLIRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 386
Cdd:smart00487 149 QLEKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
HELICc smart00490
helicase superfamily c-terminal domain;
612-695 8.46e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.05  E-value: 8.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    612 DILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLflVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 691
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVL--VATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 12232371    692 HRIG 695
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 ...
228-725 5.71e-19

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: 92.05  E-value: 5.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  228 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRFtpEIPTLLYhgTREDRRKLVKNIHKRQGTL 306
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKF--DLESLIL--DSLTVEKDAKKWNKRLTDN 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  307 QIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSELW 377
Cdd:NF038318 126 KKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLDLY 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  378 SLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--------------LEV 443
Cdd:NF038318 200 GLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdymqfkkrkcitvdFEL 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  444 PPKrEVVVYAPLCN--KQEIFYtAI--VNRT-----IANMFGSCE---KETVELSptgrpKRR------SRKSINYSE-L 504
Cdd:NF038318 264 SPD-EIELYVRVNNflKRDILY-SIptSNRTliilvIRKLLASSSfalAETFEVL-----KKRleklkeGTRSANAQEgF 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  505 DQFPSELEKLISQ-----------------IQPEVNRERTVVEGNIPIESevNLKLRNIMMLLRKCCNHpymieypidpv 567
Cdd:NF038318 337 DLFWSFVEDEIDEsgfeekqdelytrqkefIQHEIDEVDAIIDVAKRIKT--NAKVTALKTALEIAFEY----------- 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  568 TQEFKIDEELV--TNS---GKFlildrMLPELKKRGHK---VLVFSQMTS--MLDILMDYCHLRNF---IFSRldgSMSY 634
Cdd:NF038318 404 QREEGIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNGDFDdaMTKEIYRAWQVKNYgkaNYGR---SVEY 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  635 sereKN--IYSFNTDPDVflfLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTI 711
Cdd:NF038318 476 ----KHaiVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVA 548
                        570
                 ....*....|....
gi 12232371  712 DQKIVERAAAKRKL 725
Cdd:NF038318 549 DKRVYEILSEKFEL 562
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
206-368 8.36e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.80  E-value: 8.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFTPEIPTl 283
Cdd:COG1061  81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 284 lyHGTREDRRKlvknihkrqgtlqihPVVVTSFEIAMRDQNALQHC-YWKYLIVDEGHRIKNMKCRLIreLKRFNADNKL 362
Cdd:COG1061 157 --GGGKKDSDA---------------PITVATYQSLARRAHLDELGdRFGLVIIDEAHHAGAPSYRRI--LEAFPAAYRL 217

                ....*.
gi 12232371 363 LLTGTP 368
Cdd:COG1061 218 GLTATP 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 ...
203-436 2.59e-165

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: 478.03  E-value: 2.59e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 203 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 283 LLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 362
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 363 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 436
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
204-781 8.46e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 494.70  E-value: 8.46e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   204 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPT 282
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   283 LLYHGTREDRRklvkniHKRQGTLQI--HPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 360
Cdd:PLN03142  248 VKFHGNPEERA------HQREELLVAgkFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNY 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   361 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVA 440
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   441 LEVPPKREVVVYAPLCNKQEIFYTAIvnrtianmfgsceketvelsptgrpkrrsrksinyseldqfpseLEKLISQIQP 520
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNA 427
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   521 EVNRERtvvegnipiesevnlkLRNIMMLLRKCCNHPYMIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRG 598
Cdd:PLN03142  428 GGERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   599 HKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTD-PDVFLFLVSTRAGGLGINLTAADTVIIYDS 677
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   678 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHknhfkggQSGLSQSKNfLDAKELMEL 757
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ-------QGRLAEQKT-VNKDELLQM 639
                         570       580
                  ....*....|....*....|....*
gi 12232371   758 LKsrdYERE-VKGSREKVISDEDLE 781
Cdd:PLN03142  640 VR---YGAEmVFSSKDSTITDEDID 661
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
198-730 4.06e-142

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.42  E-value: 4.06e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 198 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 277
Cdd:COG0553 235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 278 PEIPTLLYHGTREdRRKLVKNIHKrqgtlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:COG0553 314 PGLRVLVLDGTRE-RAKGANPFED-------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 437
Cdd:COG0553 386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 438 DVALEVPPKREVVVYAPLCNKQEIFYTAIVNRTIANMfgsceketvelspTGRPKRRSRKSInyseldqfpseleklisq 517
Cdd:COG0553 456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 518 iqpevnrertvvegnipiesevnLKLrniMMLLRKCCNHPYMIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 597
Cdd:COG0553 505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 598 GHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAGGLGINLTAADTVIIYDS 677
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|...
gi 12232371 678 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 730
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
203-436 2.57e-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: 275.74  E-value: 2.57e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 203 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPEIP 281
Cdd:cd17997   1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 282 TLLYHGTREDRRKLVKNIHKRQGtlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:cd17997  81 VVVLIGDKEERADIIRDVLLPGK----FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12232371 362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLK 436
Cdd:cd17997 157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQR---------LHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
203-436 2.91e-84

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: 268.47  E-value: 2.91e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 203 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIP 281
Cdd:cd17996   1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITyLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 282 TLLYHGTREDRRKLVKNIhkRQGTLQihpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKR-FNADN 360
Cdd:cd17996  81 KIVYKGTPDVRKKLQSQI--RAGKFN---VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARY 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12232371 361 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVL--HMLHQILTPFLLRRLK 436
Cdd:cd17996 156 RLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLiiRRLHKVLRPFLLRRLK 233
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
209-560 3.41e-84

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: 270.32  E-value: 3.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   209 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PEIP 281
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   282 TLLYHGTREDRRKlVKNIHKRQGTlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:pfam00176  79 VVVLHGNKRPQER-WKNDPNFLAD---FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 441
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   442 EVPPKREVVVYAPLCNKQEIFYTAIVnrtianmfgsceketvelsptgrpkrrsrksinyseldqfpseLEKLISQIQpe 521
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 12232371   522 vnrertvvegNIPIESEVNLKLRNIMMLLRKCCNHPYMI 560
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
206-388 6.04e-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: 254.80  E-value: 6.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMI-QRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLL 284
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDRRKLvknihKRQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 364
Cdd:cd17919  81 YHGSQRERAQI-----RAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155
                       170       180
                ....*....|....*....|....
gi 12232371 365 TGTPLQNNLSELWSLLNFLLPDVF 388
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 ...
206-434 3.75e-70

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: 230.32  E-value: 3.75e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLL 284
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDRRKlvknihKRQGTLQ---IHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:cd18003  81 YYGSAKERKL------KRQGWMKpnsFH-VCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12232371 362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 434
Cdd:cd18003 154 LLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpLTAMSEGSQEE-----NEELVRRLHKVLRPFLLRR 223
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
204-436 4.45e-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: 227.06  E-value: 4.45e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 204 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTL 283
Cdd:cd18012   3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 284 LYHGTREDRRKLVKnihkrqgtLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLL 363
Cdd:cd18012  83 VIHGTKRKREKLRA--------LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12232371 364 LTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITslsetaediIAKEREQNVLHMLHQILTPFLLRRLK 436
Cdd:cd18012 155 LTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP---------IEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
198-447 8.24e-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: 227.63  E-value: 8.24e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 198 PKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRF 276
Cdd:cd18064   8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRW 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 277 TPEIPTLLYHGTREDRRKLVKNIhkrqgtlqIHP----VVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRE 352
Cdd:cd18064  88 VPTLRAVCLIGDKDQRAAFVRDV--------LLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 353 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLL 432
Cdd:cd18064 160 VREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG----------DQKLVERLHMVLRPFLL 229
                       250
                ....*....|....*
gi 12232371 433 RRLKSDVALEVPPKR 447
Cdd:cd18064 230 RRIKADVEKSLPPKK 244
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
209-434 7.64e-65

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: 216.22  E-value: 7.64e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18002   4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TREDRRKLVKNIHKRQGTLQIHP--VVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 365
Cdd:cd18002  84 NPKDRKVLRKFWDRKNLYTRDAPfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLT 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12232371 366 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF--DITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 434
Cdd:cd18002 164 GTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAENKTGL-----NEHQLKRLHMILKPFMLRR 229
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
206-434 1.99e-64

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: 214.80  E-value: 1.99e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPeIPTLL 284
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDR--RKLVKNIHKRQGTLQIHP-----VVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:cd17995  80 YHGSGESRqiIQQYEMYFKDAQGRKKKGvykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF-DItslsETAEDIiakEReqnvlhmLHQILTPFLLRR 434
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFgDL----KTAEQV---EK-------LQALLKPYMLRR 223
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
196-436 3.64e-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: 214.50  E-value: 3.64e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 196 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFK 274
Cdd:cd18065   6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 275 RFTPEIPTLLYHGTREDRRKLVKNIhkrqgtlqIHP----VVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLI 350
Cdd:cd18065  86 RWVPSLRAVCLIGDKDARAAFIRDV--------MMPgewdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 351 RELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPF 430
Cdd:cd18065 158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG----------DQKLVERLHAVLKPF 227

                ....*.
gi 12232371 431 LLRRLK 436
Cdd:cd18065 228 LLRRIK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
581-706 8.08e-63

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: 8.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 581 SGKFLILDRMLPELKKRGHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLFLVSTRAG 660
Cdd:cd18793  10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 12232371 661 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 706
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
206-434 8.50e-63

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: 210.29  E-value: 8.50e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLL 284
Cdd:cd17993   2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSyLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDRrKLVKN---IHKRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:cd17993  82 YLGDIKSR-DTIREyefYFSQTKKLKFN-VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNR 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12232371 362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFEswfdiTSLSETAEDIIAKereqnvlhmLHQILTPFLLRR 434
Cdd:cd17993 160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-----EEHDEEQEKGIAD---------LHKELEPFILRR 218
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
196-436 5.45e-62

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: 209.52  E-value: 5.45e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 196 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 274
Cdd:cd18062  14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRINGPFLIIVPLSTLSNWVYEFD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 275 RFTPEIPTLLYHGTREDRRKLVKNIhkRQGTLQihpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 354
Cdd:cd18062  94 KWAPSVVKVSYKGSPAARRAFVPQL--RSGKFN---VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 355 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 432
Cdd:cd18062 169 tHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGEKVDLNEEETIlIIRRLHKVLRPFLL 247

                ....
gi 12232371 433 RRLK 436
Cdd:cd18062 248 RRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
196-436 1.43e-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: 1.43e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 196 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 274
Cdd:cd18063  14 KQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 275 RFTPEIPTLLYHGTREDRRKLVKNIhkRQGTLQihpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 354
Cdd:cd18063  94 KWAPSVVKISYKGTPAMRRSLVPQL--RSGKFN---VLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 355 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 432
Cdd:cd18063 169 tHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGERVDLNEEETIlIIRRLHKVLRPFLL 247

                ....
gi 12232371 433 RRLK 436
Cdd:cd18063 248 RRLK 251
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
209-388 6.02e-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: 196.07  E-value: 6.02e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHGT 288
Cdd:cd17998   4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 289 REDRRKLVKNIHKRQGTLQihpVVVTSFEIAM---RDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 365
Cdd:cd17998  84 QEERKHLRYDILKGLEDFD---VIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                       170       180
                ....*....|....*....|...
gi 12232371 366 GTPLQNNLSELWSLLNFLLPDVF 388
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; ...
209-434 4.14e-56

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: 191.11  E-value: 4.14e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATI-ALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd17994   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLySLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TRedrrklvknihkrqgtlqihpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGT 367
Cdd:cd17994  84 DH---------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12232371 368 PLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetAEDIIAKereqnvlhmLHQILTPFLLRR 434
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFADIS----KEDQIKK---------LHDLLGPHMLRR 196
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
196-434 3.81e-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: 190.22  E-value: 3.81e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 196 QQPKHFTGG--VMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAE 272
Cdd:cd18054   9 KQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSyLFHQHQLYGPFLLVVPLSTLTSWQRE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 273 FKRFTPEIPTLLYHGTREDRRKLVKN--IHKRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLI 350
Cdd:cd18054  89 FEIWAPEINVVVYIGDLMSRNTIREYewIHSQTKRLKFN-ALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 351 RELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWFDItslsetaEDIIAKEREqNVLHMLHQILTPF 430
Cdd:cd18054 168 KTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFEFWEDF-------EEDHGKGRE-NGYQSLHKVLEPF 233

                ....
gi 12232371 431 LLRR 434
Cdd:cd18054 234 LLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
206-434 7.81e-55

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: 188.42  E-value: 7.81e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLL 284
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDRRKLVKNIHKrqgTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 364
Cdd:cd18006  81 YMGDKEKRLDLQQDIKS---TNRFH-VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12232371 365 TGTPLQNNLSELWSLLNFLLPDVF--DDLKSFESWF-DITSLSETAEDiiakereqnvlhmLHQILTPFLLRR 434
Cdd:cd18006 157 TGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDDESETVEE-------------LHLLLQPFLLRR 216
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
206-434 4.49e-52

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: 181.40  E-value: 4.49e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIAL------MIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPE 279
Cdd:cd17999   1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 280 --IPTLLYHGTREDRRKLVKNIHKrqgtlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:cd17999  81 afLKPLAYVGPPQERRRLREQGEK-------HNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETAEdiiAKEREQNVLHM--LHQILTPFLL 432
Cdd:cd17999 154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpiLASRDSKAS---AKEQEAGALALeaLHKQVLPFLL 230

                ..
gi 12232371 433 RR 434
Cdd:cd17999 231 RR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
208-434 7.39e-51

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: 177.95  E-value: 7.39e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 208 WYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18001   3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TRED-RRKLVKNIHKRQGtlqihpVVVTSFEIAMRDQNALQHCY-----WKYLIVDEGHRIKNMKCRLIRELKRFNADNK 361
Cdd:cd18001  83 TSKKeRERNLERIQRGGG------VLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 362 LLLTGTPLQNNLSELWSLLNFLLP-DVFDDLKSFESWFDITSLSETAEDIIAKERE--QNVLHMLHQILTPFLLRR 434
Cdd:cd18001 157 IILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgSEVAENLRQIIKPYFLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
209-434 9.46e-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: 177.90  E-value: 9.46e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18055   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TREDRRKLVKNIH----------------KRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIR 351
Cdd:cd18055  84 DKDSRAIIRENEFsfddnavkggkkafkmKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 352 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 430
Cdd:cd18055 163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228

                ....
gi 12232371 431 LLRR 434
Cdd:cd18055 229 MLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
206-434 2.14e-49

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: 173.69  E-value: 2.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpEIPTLLY 285
Cdd:cd18058   1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 286 HGTREDRRKLVK-NIHKRQ-------GTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:cd18058  80 HGSQISRQMIQQyEMYYRDeqgnplsGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDItslsetaediiaKEREQnvLHMLHQILTPFLLRR 434
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFlEEFGDL------------KTEEQ--VKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
206-434 1.54e-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: 171.37  E-value: 1.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpEIPTLLY 285
Cdd:cd18059   1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 286 HGTREDRRKL------VKNIHKR--QGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 357
Cdd:cd18059  80 HGSQASRRTIqlyemyFKDPQGRviKGSYKFH-AIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12232371 358 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 434
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
209-434 8.85e-48

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: 169.47  E-value: 8.85e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18057   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TREDRRKLVKNIH----------------KRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIR 351
Cdd:cd18057  84 DKESRSVIRENEFsfednairsgkkvfrmKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 352 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 430
Cdd:cd18057 163 VLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228

                ....
gi 12232371 431 LLRR 434
Cdd:cd18057 229 MLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
206-434 5.52e-46

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: 164.07  E-value: 5.52e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpEIPTLLY 285
Cdd:cd18060   1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 286 HGTREDRRKLVK-NIHKRQGTLQIHP------VVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNA 358
Cdd:cd18060  80 HGSLASRQMIQQyEMYCKDSRGRLIPgaykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 359 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 434
Cdd:cd18060 160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
209-434 2.21e-45

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: 162.93  E-value: 2.21e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18056   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TREDRRKLVKNIH----------------KRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIR 351
Cdd:cd18056  84 DKDSRAIIRENEFsfednairggkkasrmKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 352 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFeswfditsLSETAEdiIAKEREqnvLHMLHQILTPFL 431
Cdd:cd18056 163 VLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF--------LEEFAD--IAKEDQ---IKKLHDMLGPHM 229

                ...
gi 12232371 432 LRR 434
Cdd:cd18056 230 LRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
193-434 1.72e-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: 154.82  E-value: 1.72e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 193 VPFQQPKHFTGGV----MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLP 267
Cdd:cd18053   4 VALKKQPSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNyLFHEHQLYGPFLLVVPLSTLT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 268 NWMAEFKRFTPEIPTLLYHGTREDRRKLVKN--IHKRQGTLQIHpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNM 345
Cdd:cd18053  84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHewMHPQTKRLKFN-ILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKND 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 346 KCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWfditslsETAEDIIAKEREQNVLHmLHQ 425
Cdd:cd18053 163 DSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFSSW-------EDFEEEHGKGREYGYAS-LHK 228

                ....*....
gi 12232371 426 ILTPFLLRR 434
Cdd:cd18053 229 ELEPFLLRR 237
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
209-385 7.98e-42

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: 151.32  E-value: 7.98e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALM--IQRGVpGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYH 286
Cdd:cd18000   4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhhSKLGL-GPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 287 GTREDRRKLVKNIHKRQGTLQI------HPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 360
Cdd:cd18000  83 SSGSGTGSEEKLGSIERKSQLIrkvvgdGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
                       170       180
                ....*....|....*....|....*
gi 12232371 361 KLLLTGTPLQNNLSELWSLLNFLLP 385
Cdd:cd18000 163 RLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
206-434 3.28e-41

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: 150.54  E-value: 3.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpEIPTLLY 285
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 286 HGT--------------REDRRKLVKNIHKRQGtlqihpvVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIR 351
Cdd:cd18061  80 HGSlisrqmiqqyemyfRDSQGRIIRGAYRFQA-------IITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 352 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFL 431
Cdd:cd18061 153 GLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG---------DLKTEEQVQK----LQAILKPMM 219

                ...
gi 12232371 432 LRR 434
Cdd:cd18061 220 LRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
209-434 3.24e-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: 148.20  E-value: 3.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWlrMLWeNGinGILADEMGLGKTVQCIATIAL------------------MIQRGVPGPFLVCGPLSTLPNWM 270
Cdd:cd18008   4 YQKQGLAW--MLP-RG--GILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLSQWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 271 AEFKRFTPE--IPTLLYHGtrEDRRKLVKnihkrqgTLQIHPVVVTSFEI----------------AMRDQNALQHCYWK 332
Cdd:cd18008  79 DEIEKHTKPgsLKVYVYHG--SKRIKSIE-------ELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 333 YLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFesWFDITSLSetaediia 412
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF--NSDISKPF-------- 219
                       250       260
                ....*....|....*....|..
gi 12232371 413 KEREQNVLHMLHQILTPFLLRR 434
Cdd:cd18008 220 SKNDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
206-434 7.58e-40

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: 147.43  E-value: 7.58e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWL--RMLWENGING---ILADEMGLGKTVQCIATIALMIQRGVPGP-----FLVCGPLSTLPNWMAEFKR 275
Cdd:cd18004   1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 276 FTP-EIPTLLyhgTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAMRDQNALQH---CywKYLIVDEGHRIKNMKCRLIR 351
Cdd:cd18004  81 WLGlRRIKVV---TADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkisI--DLLICDEGHRLKNSESKTTK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 352 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIIAKEREQNVLHMLHQILTP 429
Cdd:cd18004 156 ALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepILRSRDPDASEEDKELGAERSQELSELTSR 235

                ....*
gi 12232371 430 FLLRR 434
Cdd:cd18004 236 FILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
206-434 1.77e-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: 143.67  E-value: 1.77e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR---------------------GVPGPFLVCGPLS 264
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 265 TLPNWMAEFKR---FTPEIptllYHGtreDRRKLVKNIHKRQGTLQihpVVVTSFEIAMRDQNALQHCYWKYLIVDEGHR 341
Cdd:cd18005  81 VLYNWKDELDTwghFEVGV----YHG---SRKDDELEGRLKAGRLE---VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 342 IKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDI-----TSLSETAEDI-IAKER 415
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgQRHTATARELrLGRKR 230
                       250
                ....*....|....*....
gi 12232371 416 EQnvlhMLHQILTPFLLRR 434
Cdd:cd18005 231 KQ----ELAVKLSKFFLRR 245
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
206-398 8.96e-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: 8.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGmewLRMLWEN---------GING-ILADEMGLGKTVQCIATIALMIQRGVPG--PFLVCgPLSTLPNWMAEF 273
Cdd:cd18007   1 LKPHQVEG---VRFLWSNlvgtdvgsdEGGGcILAHTMGLGKTLQVITFLHTYLAAAPRRsrPLVLC-PASTLYNWEDEF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 274 KRFTP--EIPTLLYHGT----REDRR-KLVKNIHKRQGTLQIHpvvVTSFEIAMRDQNALQHCYWKY-----------LI 335
Cdd:cd18007  77 KKWLPpdLRPLLVLVSLsaskRADARlRKINKWHKEGGVLLIG---YELFRNLASNATTDPRLKQEFiaalldpgpdlLV 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12232371 336 VDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 398
Cdd:cd18007 154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
582-695 1.42e-29

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: 113.07  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   582 GKFLILDRMLPelKKRGHKVLVFSQMTSMLDILMdYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPdvFLFLVSTRAGG 661
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 12232371   662 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 695
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
206-434 2.60e-28

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: 114.10  E-value: 2.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGmewLRMLWE-------NGING-ILADEMGLGKTVQCIATI-ALMIQRGVPGPFL----VCGPLSTLPNWMAE 272
Cdd:cd18067   1 LRPHQREG---VKFLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMwTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 273 F-KRFTPEIPTLLYHG--TREDRRKLVKNIHKrQGTLQIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRL 349
Cdd:cd18067  78 LgKWLGGRLQPLAIDGgsKKEIDRKLVQWASQ-QGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 350 IRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNV--LHMLHQIL 427
Cdd:cd18067 157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEekLQELISIV 236

                ....*..
gi 12232371 428 TPFLLRR 434
Cdd:cd18067 237 NRCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
198-386 3.48e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 3.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    198 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 276
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    277 TPE---IPTLLYHGT--REDRRKLVKNihkrqgtlqIHPVVVTSFEIAMRD--QNALQHCYWKYLIVDEGHRIKNM--KC 347
Cdd:smart00487  78 GPSlglKVVGLYGGDskREQLRKLESG---------KTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGD 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 12232371    348 RLIRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 386
Cdd:smart00487 149 QLEKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
206-434 2.45e-23

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: 99.53  E-value: 2.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLR-----MLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGP------FLVCGPLSTLPNWMAEFK 274
Cdd:cd18066   1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 275 RFTpeiptllyhGTREDRRKLVKNIHKRQGTLQ--IHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMKCRLIRE 352
Cdd:cd18066  81 KWL---------GSERIKVFTVDQDHKVEEFIAspLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 353 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETA---EDIIAKEREQNvlhmLHQI 426
Cdd:cd18066 152 LTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepiVRSREPTAtpeEKKLGEARAAE----LTRL 227

                ....*...
gi 12232371 427 LTPFLLRR 434
Cdd:cd18066 228 TGLFILRR 235
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
209-394 6.39e-23

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: 97.66  E-value: 6.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEW-LRmlweNGINGILADEMGLGKTVQCIAtIALMIQRgvPGPFLVCGPLSTLPNWMAEFKRFTPEIPT---LL 284
Cdd:cd18010   4 FQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA-IAAYYRE--EWPLLIVCPSSLRLTWADEIERWLPSLPPddiQV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 285 YHGTREDRRKLVknihkrqgtlqiHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNMK---CRLIRELKRfNADNK 361
Cdd:cd18010  77 IVKSKDGLRDGD------------AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAALPLLK-RAKRV 143
                       170       180       190
                ....*....|....*....|....*....|...
gi 12232371 362 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF 394
Cdd:cd18010 144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
HELICc smart00490
helicase superfamily c-terminal domain;
612-695 8.46e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.05  E-value: 8.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371    612 DILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNTDPDVFLflVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 691
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVL--VATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 12232371    692 HRIG 695
Cdd:smart00490  79 GRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
209-399 1.09e-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: 97.58  E-value: 1.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGmewLRMLWEN------------GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 276
Cdd:cd18069   4 HQIGG---IRFLYDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 277 TPEIPTLLY--------------HGTREDRRKLVKNIHKRQGtlqihpVVVTSFEI-AMRDQNALqhcywkyLIVDEGHR 341
Cdd:cd18069  81 LPPPEALPNvrprpfkvfilndeHKTTAARAKVIEDWVKDGG------VLLMGYEMfRLRPGPDV-------VICDEGHR 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 12232371 342 IKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD 399
Cdd:cd18069 148 IKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
222-383 5.96e-22

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: 95.61  E-value: 5.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 222 ENGINGILADEMGLGKTVQCIATIalmiqrgVPGPFLVCGPLSTLPNWMAEFKRFTPE--IPTLLYHGTreDRRKLVKNI 299
Cdd:cd18071  46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGG--ERNRDPKLL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 300 HKRQgtlqihpVVVTSFEIAMRDQNA-----LQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLS 374
Cdd:cd18071 117 SKYD-------IVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189

                ....*....
gi 12232371 375 ELWSLLNFL 383
Cdd:cd18071 190 DLGSLLSFL 198
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
209-396 1.01e-21

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: 93.89  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGmewLRMLWENGING-ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHG 287
Cdd:cd18011   4 HQIDA---VLRALRKPPVRlLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 288 TREDRRKLVKNIHKRqgtlqiHPVVVTSFEIAmRDQNALQHCY----WKYLIVDEGHRIKNMKC-------RLIRELKRf 356
Cdd:cd18011  81 TAAQLRRLIGNPFEE------FPIVIVSLDLL-KRSEERRGLLlseeWDLVVVDEAHKLRNSGGgketkryKLGRLLAK- 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 12232371 357 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFES 396
Cdd:cd18011 153 RARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
209-434 8.00e-21

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: 92.54  E-value: 8.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 209 YQVEGMEWlrMLW---ENGINGILADEMGLGKTVQCIATIaLMIQRG-----------------------VP--GPFLVC 260
Cdd:cd18072   4 HQKQALAW--LLWrerQKPRGGILADDMGLGKTLTMIALI-LAQKNTqnrkeeekekalteweskkdstlVPsaGTLVVC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 261 gPLSTLPNWMAEFKRFTPE--IPTLLYHGTredrrklvkNIHKRQGTLQIHPVVVTSFEIAMRD---------QNALQHC 329
Cdd:cd18072  81 -PASLVHQWKNEVESRVASnkLRVCLYHGP---------NRERIGEVLRDYDIVITTYSLVAKEiptykeesrSSPLFRI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 330 YWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSetaed 409
Cdd:cd18072 151 AWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRK----- 225
                       250       260
                ....*....|....*....|....*
gi 12232371 410 iiAKEReqnvlhmLHQILTPFLLRR 434
Cdd:cd18072 226 --GGER-------LNILTKSLLLRR 241
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
228-725 5.71e-19

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: 92.05  E-value: 5.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  228 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRFtpEIPTLLYhgTREDRRKLVKNIHKRQGTL 306
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKF--DLESLIL--DSLTVEKDAKKWNKRLTDN 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  307 QIHPVVVTSFEIAMRDQNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSELW 377
Cdd:NF038318 126 KKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLDLY 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  378 SLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--------------LEV 443
Cdd:NF038318 200 GLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdymqfkkrkcitvdFEL 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  444 PPKrEVVVYAPLCN--KQEIFYtAI--VNRT-----IANMFGSCE---KETVELSptgrpKRR------SRKSINYSE-L 504
Cdd:NF038318 264 SPD-EIELYVRVNNflKRDILY-SIptSNRTliilvIRKLLASSSfalAETFEVL-----KKRleklkeGTRSANAQEgF 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  505 DQFPSELEKLISQ-----------------IQPEVNRERTVVEGNIPIESevNLKLRNIMMLLRKCCNHpymieypidpv 567
Cdd:NF038318 337 DLFWSFVEDEIDEsgfeekqdelytrqkefIQHEIDEVDAIIDVAKRIKT--NAKVTALKTALEIAFEY----------- 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  568 TQEFKIDEELV--TNS---GKFlildrMLPELKKRGHK---VLVFSQMTS--MLDILMDYCHLRNF---IFSRldgSMSY 634
Cdd:NF038318 404 QREEGIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNGDFDdaMTKEIYRAWQVKNYgkaNYGR---SVEY 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371  635 sereKN--IYSFNTDPDVflfLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTI 711
Cdd:NF038318 476 ----KHaiVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVA 548
                        570
                 ....*....|....
gi 12232371  712 DQKIVERAAAKRKL 725
Cdd:NF038318 549 DKRVYEILSEKFEL 562
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
224-398 2.92e-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: 79.16  E-value: 2.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 224 GINGILADEMGLGKTVQCIA---TIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF--------TPEIPTLLYHGTREDR 292
Cdd:cd18068  28 GSGCILAHCMGLGKTLQVVTflhTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWqeglkdeeKIEVNELATYKRPQER 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 293 RKLVKNIHKRQGtlqihpVVVTSFEI--------AMRDQNALQHCYWKYL--------IVDEGHRIKNMKCRLIRELKRF 356
Cdd:cd18068 108 SYKLQRWQEEGG------VMIIGYDMyrilaqerNVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 12232371 357 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 398
Cdd:cd18068 182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
206-433 2.98e-15

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 76.61  E-value: 2.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWlrMLWENGIngiLADEMGLGKTVQCIATIAL-------------------MIQRGVP-------GPFLV 259
Cdd:cd18070   1 LLPYQRRAVNW--MLVPGGI---LADEMGLGKTVEVLALILLhprpdndldaadddsdemvCCPDCLVaetpvssKATLI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 260 CGPLSTLPNWMAEFKRFTPEIP-TLLYHGTREDrRKLVKNIHKRqgtLQIHPVVVTS-----FEIAMRDQNA-------- 325
Cdd:cd18070  76 VCPSAILAQWLDEINRHVPSSLkVLTYQGVKKD-GALASPAPEI---LAEYDIVVTTydvlrTELHYAEANRsnrrrrrq 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 326 ---------LQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDlksfES 396
Cdd:cd18070 152 kryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD----SD 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 12232371 397 WFditslsetAEDIIAKEREQNVLHMLHQILTPFLLR 433
Cdd:cd18070 228 WW--------ARVLIRPQGRNKAREPLAALLKELLWR 256
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
206-383 9.22e-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: 56.59  E-value: 9.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEWLRmlwENGINGILADeMGLGKTVQCIATIALMIQRGVPGPFLVCGPL----STLPNWMAEFKRFTPEIP 281
Cdd:cd18013   1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLrvarSTWPDEVEKWNHLRNLTV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 282 TLLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEiamrdqnalQHCYWKYLIVDEGHRIKNMKCRLIRELK--RFNAD 359
Cdd:cd18013  77 SVAVGTERQRSKAANTPADLYVINRENLKWLVNKSG---------DPWPFDMVVIDELSSFKSPRSKRFKALRkvRPVIK 147
                       170       180
                ....*....|....*....|....
gi 12232371 360 NKLLLTGTPLQNNLSELWSLLNFL 383
Cdd:cd18013 148 RLIGLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
206-368 8.36e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.80  E-value: 8.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFTPEIPTl 283
Cdd:COG1061  81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 284 lyHGTREDRRKlvknihkrqgtlqihPVVVTSFEIAMRDQNALQHC-YWKYLIVDEGHRIKNMKCRLIreLKRFNADNKL 362
Cdd:COG1061 157 --GGGKKDSDA---------------PITVATYQSLARRAHLDELGdRFGLVIIDEAHHAGAPSYRRI--LEAFPAAYRL 217

                ....*.
gi 12232371 363 LLTGTP 368
Cdd:COG1061 218 GLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
206-368 9.06e-08

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: 51.92  E-value: 9.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 206 MRWYQVEGMEwlRMLWENGIN-GILADEMGLGKTVqcIAtIALMIQRGvPGPFLVCGPLSTLPN-WMAEFKRFTPEIPTL 283
Cdd:cd17926   1 LRPYQEEALE--AWLAHKNNRrGILVLPTGSGKTL--TA-LALIAYLK-ELRTLIVVPTDALLDqWKERFEDFLGDSSIG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 284 LYhgtREDRRKLVKNIhkrqgtlqihPVVVTSFEIAMRDQNALQHCY--WKYLIVDEGHRIknmKCRLIRE-LKRFNADN 360
Cdd:cd17926  75 LI---GGGKKKDFDDA----------NVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL---PAKTFSEiLKELNAKY 138

                ....*...
gi 12232371 361 KLLLTGTP 368
Cdd:cd17926 139 RLGLTATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
558-795 1.91e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.56  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 558 YMIEYPIDPVTQEFKIDEELVT------NSGKFLILDRMLPELKKrGHKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGS 631
Cdd:COG1061 260 YGIRVDLTDERAEYDALSERLRealaadAERKDKILRELLREHPD-DRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGD 338
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 632 MSYSEREKNIYSFNTDPDVflFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTI 711
Cdd:COG1061 339 TPKKEREEILEAFRDGELR--ILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDV 416
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 712 DqkIVERAAAKRKLEKLIIHKNHFKGGQSGLSQSKNFLDAKELMELLKSRDYEREVKGSREKVISDEDLELLLDRSDLID 791
Cdd:COG1061 417 P--VLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALE 494

                ....
gi 12232371 792 QMKA 795
Cdd:COG1061 495 LLEL 498
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
226-367 2.65e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 47.78  E-value: 2.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 226 NGILADEMGLGKTVqcIATIALmIQRGVP--GPFLVCGPLSTL-PNWMAEFK-RFTPEIPTLLYHGTREDRRKLVKNIhk 301
Cdd:cd00046   3 NVLITAPTGSGKTL--AALLAA-LLLLLKkgKKVLVLVPTKALaLQTAERLReLFGPGIRVAVLVGGSSAEEREKNKL-- 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12232371 302 rqGTLQIhpVVVTSFEIAMRDQNALQHCY--WKYLIVDEGHRI------KNMKCRLIRELKRFNADnKLLLTGT 367
Cdd:cd00046  78 --GDADI--IIATPDMLLNLLLREDRLFLkdLKLIIVDEAHALlidsrgALILDLAVRKAGLKNAQ-VILLSAT 146
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
548-713 3.88e-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: 49.25  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   548 MLLRKCC---NHPYMIEYPIDPVTQEFK-IDEELVTNSGKFLILDRMLPEL----KKRGHKVLVFSQMTSMLDILMDYCH 619
Cdd:pfam11496  52 LCLENLSlvaTHPYLLVDHYMPKSLLLKdEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEALLL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   620 LRNFIFSRLDGSMSYSEREKNIYSFNTDP--DVFLFLVSTR-----AGGLGInlTAADTVIIYDSDWNPQSDLQAQDRCH 692
Cdd:pfam11496 132 GKGLSYKRYSGEMLYGENKKVSDSGNKKIhsTTCHLLSSTGqltndDSLLEN--YKFDLIIAFDSSVDTSSPSVEHLRTQ 209
                         170       180
                  ....*....|....*....|.
gi 12232371   693 RIGQTKPVVVYRLVTANTIDQ 713
Cdd:pfam11496 210 NRRKGNLAPIIRLVVINSIEH 230
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
649-703 6.84e-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: 44.62  E-value: 6.84e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12232371 649 DVFLFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 703
Cdd:cd18785  21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
ResIII pfam04851
Type III restriction enzyme, res subunit;
205-368 7.27e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.90  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   205 VMRWYQVEGME-WLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGP-LSTLPNWMAEFKRFTP---E 279
Cdd:pfam04851   3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPnyvE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371   280 IPTLLyhgtrEDRRKLVKNIHKRqgtlqihpVVVTS----FEIAMRDQNALQHCYWKYLIVDEGHRI--KNMkcrliREL 353
Cdd:pfam04851  83 IGEII-----SGDKKDESVDDNK--------IVVTTiqslYKALELASLELLPDFFDVIIIDEAHRSgaSSY-----RNI 144
                         170
                  ....*....|....*.
gi 12232371   354 KRFNADNKLL-LTGTP 368
Cdd:pfam04851 145 LEYFKPAFLLgLTATP 160
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
567-697 2.03e-05

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: 44.81  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232371 567 VTQEFkideELVTNSGKFLILDRMLPELKKRGhKVLVFSQMTSMLDILMDYCHLRNFIFSRLDGSMSYSEREKNIYSFNT 646
Cdd:cd18787   1 IKQLY----VVVEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRS 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 12232371 647 -DPDVflfLVST----RagglGINLTAADTVIIYDsdwNPQSdlqAQDRCHRIGQT 697
Cdd:cd18787  76 gKVRV---LVATdvaaR----GLDIPGVDHVINYD---LPRD---AEDYVHRIGRT 118
SbnI_like_N cd16388
N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin ...
283-350 5.89e-03

N-terminal domain of transcriptional regulators similar to SbnI; Siderophore staphylobactin biosynthesis protein SbnI of Staphylococcus aureus is a ParB/Spo0J like protein required for the expression of genes in the sbn operon, which is responsible for staphyloferrin B (SB) biosynthesis. SnbI forms dimers and binds DNA upstream of sdnD. SbnI binds heme, which inhibits DNA binding of SbnI, leading to a suppression of sbn operon expression.


Pssm-ID: 319247 [Multi-domain]  Cd Length: 77  Bit Score: 36.33  E-value: 5.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12232371 283 LLYHGTREDRR--KLVKNIhKRQGTLqIHPVVVTsfeiAMRDQnalqhcywKYLIVDEGHR---IKNMKCRLI 350
Cdd:cd16388   9 IRLHEEHEPNRleKLVERI-EAEGVL-RNPPIVT----PLQDG--------RYLILDGAHRttaLKKLGCKRI 67
 
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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