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Conserved domains on  [gi|21914927|ref|NP_060533|]
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lymphoid-specific helicase isoform 1 [Homo sapiens]

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 ...
 220-453 8.62e-168

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: 484.97  E-value: 8.62e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 300 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 453
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-823 3.11e-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: 496.63  E-value: 3.11e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 459
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   460 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 539
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   540 DRERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 617
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   618 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 696
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   697 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 776
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 21914927   777 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 823
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
 
Name Accession Description Interval E-value
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 220-453 8.62e-168

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: 484.97  E-value: 8.62e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 300 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 453
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-823 3.11e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 496.63  E-value: 3.11e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 459
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   460 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 539
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   540 DRERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 617
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   618 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 696
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   697 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 776
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 21914927   777 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 823
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 215-747 4.17e-144

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 441.20  E-value: 4.17e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 215 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 294
Cdd:COG0553 235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 295 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 374
Cdd:COG0553 314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 454
Cdd:COG0553 386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 455 DVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketielspTGRPKRRTRKSInyskiddfpneleklisq 534
Cdd:COG0553 456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 535 iqpevdreravvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 614
Cdd:COG0553 505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 615 GHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDS 694
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|...
gi 21914927 695 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 747
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 226-577 4.16e-85

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 273.02  E-value: 4.16e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   226 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PDIP 298
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   299 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 378
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   379 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 458
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   459 EVPPKREVVVYAPLSKKQEIFYTAIVnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQpe 538
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 21914927   539 vdreravvevNIPVESEVNLKLQNIMMLLRKCCNHPYLI 577
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 598-723 1.30e-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: 209.64  E-value: 1.30e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 598 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAG 677
Cdd:cd18793  10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21914927 678 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 723
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 599-712 2.36e-30

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 115.39  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   599 GKFLILDRMLPelKKRGHKVLLFSQMTSMLDILMdYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGG 678
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21914927   679 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 712
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
215-403 3.93e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 3.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    215 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 293
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    294 TPD---IPTMLYHGTQEERQKlvRNIYKRKgtlqiHPVVITSFEIAMRD--RNALQHCYWKYLIVDEGHRIKNM--KCRL 366
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQL--RKLESGK-----TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 21914927    367 IRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 403
Cdd:smart00487 151 EKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
HELICc smart00490
helicase superfamily c-terminal domain;
629-712 6.82e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.13  E-value: 6.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    629 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 708
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                   ....
gi 21914927    709 HRIG 712
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 ...
 245-742 1.32e-23

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: 107.08  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  245 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRF--TPDIPTMLYhgTQEERQKLVRNIYKRKG 321
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKFdlESLILDSLT--VEKDAKKWNKRLTDNKK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  322 TLqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSE 392
Cdd:NF038318 128 VR----IVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  393 LWSLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--LEVPPKREVVVYA 470
Cdd:NF038318 198 LYGLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdyMQFKKRKCITVDF 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  471 PLSK-------------KQEIFYtAI--VNRT-----IANMFGSSE----------KETIELSPTGRPKRRTRKSINY-- 518
Cdd:NF038318 262 ELSPdeielyvrvnnflKRDILY-SIptSNRTliilvIRKLLASSSfalaetfevlKKRLEKLKEGTRSANAQEGFDLfw 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  519 ----SKIDDFPNEL---EKLISQ---IQPEVDRERAVVEVNIPVESevNLKLQNIMMLLRKCCNHpylieypidpvTQEF 588
Cdd:NF038318 341 sfveDEIDESGFEEkqdELYTRQkefIQHEIDEVDAIIDVAKRIKT--NAKVTALKTALEIAFEY-----------QREE 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  589 KIDEELV--TNS---GKFlildrMLPELKKRGHK---VLLFS-----QMTSMLdilmdYCHLRDFNFSRLDGSMSYSERE 655
Cdd:NF038318 408 GIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNgdfddAMTKEI-----YRAWQVKNYGKANYGRSVEYKH 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  656 KNMHSFNTDPEVfifLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTIDQKIVE 734
Cdd:NF038318 478 AIVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYE 554


                 ....*...
gi 21914927  735 RAAAKRKL 742
Cdd:NF038318 555 ILSEKFEL 562
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
223-385 4.28e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.57  E-value: 4.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFTPDIPTm 300
Cdd:COG1061  81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 301 lyHGTQEERQKlvrniykrkgtlqihPVVITSFEIAMRD--RNALQHcYWKYLIVDEGHRIKNMKCRLIreLKRFNADNK 378
Cdd:COG1061 157 --GGGKKDSDA---------------PITVATYQSLARRahLDELGD-RFGLVIIDEAHHAGAPSYRRI--LEAFPAAYR 216


                ....*..
gi 21914927 379 LLLTGTP 385
Cdd:COG1061 217 LGLTATP 223
 
Name Accession Description Interval E-value
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 220-453 8.62e-168

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: 484.97  E-value: 8.62e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 300 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:cd18009  81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 453
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-823 3.11e-161

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 496.63  E-value: 3.11e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 379
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   380 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALE 459
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKG 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   460 VPPKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEV 539
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGG 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   540 DRERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHK 617
Cdd:PLN03142  430 ERKR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSR 489

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   618 VLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDW 696
Cdd:PLN03142  490 VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDW 569

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   697 NPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLK 776
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQ 638

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 21914927   777 SRDYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 823
Cdd:PLN03142  639 MVRYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 215-747 4.17e-144

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 441.20  E-value: 4.17e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 215 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 294
Cdd:COG0553 235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 295 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 374
Cdd:COG0553 314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFditslsetaEDIIAKEREQNvLHMLHQILTPFLLRRLKS 454
Cdd:COG0553 386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF---------ARPIEKGDEEA-LERLRRLLRPFLLRRTKE 455

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 455 DVALEVPPKREVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketielspTGRPKRRTRKSInyskiddfpneleklisq 534
Cdd:COG0553 456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI------------------ 504

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 535 iqpevdreravvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKR 614
Cdd:COG0553 505 -----------------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAE 548

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 615 GHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDS 694
Cdd:COG0553 549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDL 628

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|...
gi 21914927 695 DWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 747
Cdd:COG0553 629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 220-453 2.86e-88

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: 278.82  E-value: 2.86e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17997   1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 299 TMLYHGTQEERQKLVRNIYKRKGtlqiHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 378
Cdd:cd17997  81 VVVLIGDKEERADIIRDVLLPGK----FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 379 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLK 453
Cdd:cd17997 157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQR---------LHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 226-577 4.16e-85

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 273.02  E-value: 4.16e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   226 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PDIP 298
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   299 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 378
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   379 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVAL 458
Cdd:pfam00176 155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR---------LHKLLKPFLLRRTKKDVEK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   459 EVPPKREVVVYAPLSKKQEIFYTAIVnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQpe 538
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK-- 260

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 21914927   539 vdreravvevNIPVESEVNLKLQNIMMLLRKCCNHPYLI 577
Cdd:pfam00176 261 ----------TGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 220-453 5.43e-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: 268.08  E-value: 5.43e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17996   1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITyLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 299 TMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKR-FNADN 377
Cdd:cd17996  81 KIVYKGTPDVRKKLQSQI--RAGKFN---VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARY 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21914927 378 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVL--HMLHQILTPFLLRRLK 453
Cdd:cd17996 156 RLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLiiRRLHKVLRPFLLRRLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 223-405 3.46e-80

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 255.95  E-value: 3.46e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMI-QRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 302 YHGTQEERQKLVRNIYKRKGtlqihPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 381
Cdd:cd17919  81 YHGSQRERAQIRAKEKLDKF-----DVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155

                       170       180
                ....*....|....*....|....
gi 21914927 382 TGTPLQNNLSELWSLLNFLLPDVF 405
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 ...
 223-451 3.98e-71

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 233.40  E-value: 3.98e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 302 YHGTQEERQKlvrniyKRKGTLQ---IHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNK 378
Cdd:cd18003  81 YYGSAKERKL------KRQGWMKpnsFH-VCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRR 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 379 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 451
Cdd:cd18003 154 LLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpLTAMSEGSQEE-----NEELVRRLHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 215-464 4.58e-69

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 228.40  E-value: 4.58e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 215 PKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18064   8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRW 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 294 TPDIPTMLYHGTQEERQKLVRNIYkRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRF 373
Cdd:cd18064  88 VPTLRAVCLIGDKDQRAAFVRDVL-LPGEWD---VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 374 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRRLK 453
Cdd:cd18064 164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG----------DQKLVERLHMVLRPFLLRRIK 233

                       250
                ....*....|.
gi 21914927 454 SDVALEVPPKR 464
Cdd:cd18064 234 ADVEKSLPPKK 244
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 221-453 7.44e-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: 7.44e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTM 300
Cdd:cd18012   3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 301 LYHGTQEERQKLVRniykrkgtLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLL 380
Cdd:cd18012  83 VIHGTKRKREKLRA--------LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLA 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21914927 381 LTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITslsetaediIAKEREQNVLHMLHQILTPFLLRRLK 453
Cdd:cd18012 155 LTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP---------IEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 223-451 1.18e-67

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: 223.66  E-value: 1.18e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTML 301
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 302 YHGTQEERQKL--------VRNIYKRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRF 373
Cdd:cd17995  80 YHGSGESRQIIqqyemyfkDAQGRKKKGVYKFD-VLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21914927 374 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF-DItslsETAEDIiakEReqnvlhmLHQILTPFLLRR 451
Cdd:cd17995 159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFgDL----KTAEQV---EK-------LQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 226-451 1.39e-64

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 215.83  E-value: 1.39e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18002   4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIYKRKGTLQIHP--VVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 382
Cdd:cd18002  84 NPKDRKVLRKFWDRKNLYTRDAPfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLT 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21914927 383 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF--DITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 451
Cdd:cd18002 164 GTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAENKTGL-----NEHQLKRLHMILKPFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 223-451 2.04e-64

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: 214.91  E-value: 2.04e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17993   2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSyLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 302 YHGTQEERQkLVRN----IYKRKgTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 377
Cdd:cd17993  82 YLGDIKSRD-TIREyefyFSQTK-KLKFN-VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21914927 378 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFEswfdiTSLSETAEDIIAKereqnvlhmLHQILTPFLLRR 451
Cdd:cd17993 159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-----EEHDEEQEKGIAD---------LHKELEPFILRR 218
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 213-453 2.31e-64

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 215.27  E-value: 2.31e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18065   6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 292 RFTPDIPTMLYHGTQEERQKLVRNIYKrKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 371
Cdd:cd18065  86 RWVPSLRAVCLIGDKDARAAFIRDVMM-PGEWD---VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 372 RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRR 451
Cdd:cd18065 162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG----------DQKLVERLHAVLKPFLLRR 231


                ..
gi 21914927 452 LK 453
Cdd:cd18065 232 IK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 598-723 1.30e-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: 209.64  E-value: 1.30e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 598 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAG 677
Cdd:cd18793  10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21914927 678 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 723
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 213-453 3.76e-61

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 207.20  E-value: 3.76e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18062  14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRINGPFLIIVPLSTLSNWVYEFD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 292 RFTPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 371
Cdd:cd18062  94 KWAPSVVKVSYKGSPAARRAFVPQL--RSGKFN---VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 372 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 449
Cdd:cd18062 169 tHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGEKVDLNEEETIlIIRRLHKVLRPFLL 247


                ....
gi 21914927 450 RRLK 453
Cdd:cd18062 248 RRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 213-453 6.75e-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: 206.45  E-value: 6.75e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18063  14 KQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 292 RFTPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 371
Cdd:cd18063  94 KWAPSVVKISYKGTPAMRRSLVPQL--RSGKFN---VLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 372 -RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLL 449
Cdd:cd18063 169 tHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGERVDLNEEETIlIIRRLHKVLRPFLL 247


                ....
gi 21914927 450 RRLK 453
Cdd:cd18063 248 RRLK 251
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 226-405 3.49e-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: 196.84  E-value: 3.49e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGT 305
Cdd:cd17998   4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 306 QEERQKLVRNIYKRKGTLQihpVVITSFEIAM---RDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 382
Cdd:cd17998  84 QEERKHLRYDILKGLEDFD---VIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160

                       170       180
                ....*....|....*....|...
gi 21914927 383 GTPLQNNLSELWSLLNFLLPDVF 405
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; ...
 226-451 2.83e-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: 191.88  E-value: 2.83e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATI-ALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd17994   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLySLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQeerqklvrniykrkgtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGT 384
Cdd:cd17994  84 DH---------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21914927 385 PLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetAEDIIAKereqnvlhmLHQILTPFLLRR 451
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFADIS----KEDQIKK---------LHDLLGPHMLRR 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 223-451 3.74e-56

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 192.27  E-value: 3.74e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 302 YHGTQEERQKLVRNIYKrkgTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 381
Cdd:cd18006  81 YMGDKEKRLDLQQDIKS---TNRFH-VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21914927 382 TGTPLQNNLSELWSLLNFLLPDVF--DDLKSFESWF-DITSLSETAEDiiakereqnvlhmLHQILTPFLLRR 451
Cdd:cd18006 157 TGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDDESETVEE-------------LHLLLQPFLLRR 216
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 213-451 5.29e-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: 189.83  E-value: 5.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 213 QQPKHFTGG--VMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAE 289
Cdd:cd18054   9 KQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSyLFHQHQLYGPFLLVVPLSTLTSWQRE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 290 FKRFTPDIPTMLYHGTQEERqKLVRN---IYKRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRL 366
Cdd:cd18054  89 FEIWAPEINVVVYIGDLMSR-NTIREyewIHSQTKRLKFN-ALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 367 IRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWFDItslsetaEDIIAKEREqNVLHMLHQILTP 446
Cdd:cd18054 167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFEFWEDF-------EEDHGKGRE-NGYQSLHKVLEP 232


                ....*
gi 21914927 447 FLLRR 451
Cdd:cd18054 233 FLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 223-451 4.46e-51

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: 178.31  E-value: 4.46e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18058   1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 303 HGTQEERQKLVR-NIYKR-------KGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 374
Cdd:cd18058  80 HGSQISRQMIQQyEMYYRdeqgnplSGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDItslsetaediiaKEREQnvLHMLHQILTPFLLRR 451
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFlEEFGDL------------KTEEQ--VKKLQSILKPMMLRR 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 225-451 4.92e-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: 178.72  E-value: 4.92e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 225 WYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18001   3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 T-QEERQKLVRNIYKRKGtlqihpVVITSFEIAMRDRNALQHCY-----WKYLIVDEGHRIKNMKCRLIRELKRFNADNK 378
Cdd:cd18001  83 TsKKERERNLERIQRGGG------VLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 379 LLLTGTPLQNNLSELWSLLNFLLP-DVFDDLKSFESWFDITSLSETAEDIIAKERE--QNVLHMLHQILTPFLLRR 451
Cdd:cd18001 157 IILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgSEVAENLRQIIKPYFLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 226-451 9.84e-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: 9.84e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18055   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 368
Cdd:cd18055  84 DKDSRAIIRENEFsfddnavkggkkafkmKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 369 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 447
Cdd:cd18055 163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228


                ....
gi 21914927 448 LLRR 451
Cdd:cd18055 229 MLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 223-451 2.06e-50

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 176.77  E-value: 2.06e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIAL------MIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPD 296
Cdd:cd17999   1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 297 --IPTMLYHGTQEERQKLVRNIYKrkgtlqiHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 374
Cdd:cd17999  81 afLKPLAYVGPPQERRRLREQGEK-------HNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETAEdiiAKEREQNVLHM--LHQILTPFLL 449
Cdd:cd17999 154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpiLASRDSKAS---AKEQEAGALALeaLHKQVLPFLL 230


                ..
gi 21914927 450 RR 451
Cdd:cd17999 231 RR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 223-451 4.35e-49

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: 172.91  E-value: 4.35e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18059   1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 303 HGTQEERQKL-VRNIYKR-------KGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFN 374
Cdd:cd18059  80 HGSQASRRTIqLYEMYFKdpqgrviKGSYKFH-AIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 451
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 226-451 4.31e-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: 170.63  E-value: 4.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18057   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 368
Cdd:cd18057  84 DKESRSVIRENEFsfednairsgkkvfrmKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 369 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPF 447
Cdd:cd18057 163 VLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPH 228


                ....
gi 21914927 448 LLRR 451
Cdd:cd18057 229 MLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 223-451 6.62e-48

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: 169.46  E-value: 6.62e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18060   1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 303 HGTQEERQKLVR-NIYKRKGTLQIHP------VVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNA 375
Cdd:cd18060  80 HGSLASRQMIQQyEMYCKDSRGRLIPgaykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 376 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 451
Cdd:cd18060 160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 226-451 3.95e-46

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: 164.85  E-value: 3.95e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18056   4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIR 368
Cdd:cd18056  84 DKDSRAIIRENEFsfednairggkkasrmKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 369 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFeswfditsLSETAEdiIAKEREqnvLHMLHQILTPFL 448
Cdd:cd18056 163 VLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF--------LEEFAD--IAKEDQ---IKKLHDMLGPHM 229


                ...
gi 21914927 449 LRR 451
Cdd:cd18056 230 LRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 223-451 3.70e-43

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: 156.32  E-value: 3.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 303 HGTQEERQKLVR-NIYKRKGTLQI------HPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNA 375
Cdd:cd18061  80 HGSLISRQMIQQyEMYFRDSQGRIirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21914927 376 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 451
Cdd:cd18061 160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 226-402 1.18e-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: 153.63  E-value: 1.18e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALM--IQRGVpGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYH 303
Cdd:cd18000   4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhhSKLGL-GPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 304 ------------GTQEERQKLVRNIYKRKGtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK 371
Cdd:cd18000  83 ssgsgtgseeklGSIERKSQLIRKVVGDGG------ILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACK 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 21914927 372 RFNADNKLLLTGTPLQNNLSELWSLLNFLLP 402
Cdd:cd18000 157 QLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 210-451 5.01e-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: 153.67  E-value: 5.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 210 VPFQQPKHFTGGV----MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLP 284
Cdd:cd18053   4 VALKKQPSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNyLFHEHQLYGPFLLVVPLSTLT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 285 NWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRKGTLQIH-PVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMK 363
Cdd:cd18053  84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 364 CRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWfditslsETAEDIIAKEREQNVLHmLHQI 443
Cdd:cd18053 164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFSSW-------EDFEEEHGKGREYGYAS-LHKE 229


                ....*...
gi 21914927 444 LTPFLLRR 451
Cdd:cd18053 230 LEPFLLRR 237
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 226-451 3.76e-41

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: 150.90  E-value: 3.76e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWlrMLWeNGinGILADEMGLGKTVQCIATIAL------------------MIQRGVPGPFLVCGPLSTLPNWM 287
Cdd:cd18008   4 YQKQGLAW--MLP-RG--GILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLSQWK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 288 AEFKRFT--PDIPTMLYHGTQeerqklvRNIYKRKgtLQIHPVVITSFEI----------------AMRDRNALQHCYWK 349
Cdd:cd18008  79 DEIEKHTkpGSLKVYVYHGSK-------RIKSIEE--LSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWY 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 350 YLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFesWFDITSLSetaediia 429
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF--NSDISKPF-------- 219

                       250       260
                ....*....|....*....|..
gi 21914927 430 KEREQNVLHMLHQILTPFLLRR 451
Cdd:cd18008 220 SKNDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 223-451 8.70e-39

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 144.35  E-value: 8.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWL--RMLWENGING---ILADEMGLGKTVQCIATIALMIQRGVPGP-----FLVCGPLSTLPNWMAEFKR 292
Cdd:cd18004   1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 293 FTPDIPTMLYhgTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQH---CywKYLIVDEGHRIKNMKCRLIRE 369
Cdd:cd18004  81 WLGLRRIKVV--TADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkisI--DLLICDEGHRLKNSESKTTKA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 370 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIIAKEREQNVLHMLHQILTPF 447
Cdd:cd18004 157 LNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepILRSRDPDASEEDKELGAERSQELSELTSRF 236


                ....
gi 21914927 448 LLRR 451
Cdd:cd18004 237 ILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 223-451 7.48e-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: 141.75  E-value: 7.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR---------------------GVPGPFLVCGPLS 281
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 282 TLPNWMAEFKR---FTpdipTMLYHGTQEERQKLVRniYKRkGTLQihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHR 358
Cdd:cd18005  81 VLYNWKDELDTwghFE----VGVYHGSRKDDELEGR--LKA-GRLE---VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 359 IKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDI-----TSLSETAEDI-IAKER 432
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgQRHTATARELrLGRKR 230

                       250
                ....*....|....*....
gi 21914927 433 EQnvlhMLHQILTPFLLRR 451
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 ...
 223-415 3.59e-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: 122.40  E-value: 3.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGmewLRMLWEN---------GING-ILADEMGLGKTVQCIATIALMIQRGVPG--PFLVCgPLSTLPNWMAEF 290
Cdd:cd18007   1 LKPHQVEG---VRFLWSNlvgtdvgsdEGGGcILAHTMGLGKTLQVITFLHTYLAAAPRRsrPLVLC-PASTLYNWEDEF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 291 KRFTPD---IPTMLY----HGTQEERQKLVRNIYKRKGTLqihpvVIT--SFEIAMRDRNALQHCYWKY----------- 350
Cdd:cd18007  77 KKWLPPdlrPLLVLVslsaSKRADARLRKINKWHKEGGVL-----LIGyeLFRNLASNATTDPRLKQEFiaalldpgpdl 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 351 LIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 415
Cdd:cd18007 152 LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 599-712 2.36e-30

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 115.39  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   599 GKFLILDRMLPelKKRGHKVLLFSQMTSMLDILMdYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGG 678
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21914927   679 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 712
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 223-451 1.35e-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: 114.87  E-value: 1.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGmewLRMLWE-------NGING-ILADEMGLGKTVQCIATI-ALMIQRGVPGPFL----VCGPLSTLPNWMAE 289
Cdd:cd18067   1 LRPHQREG---VKFLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMwTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 290 F-KRFTPDIPTMLYHGTQ--EERQKLVRNIYKRkGTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRL 366
Cdd:cd18067  78 LgKWLGGRLQPLAIDGGSkkEIDRKLVQWASQQ-GRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 367 IRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNV--LHMLHQIL 444
Cdd:cd18067 157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEekLQELISIV 236


                ....*..
gi 21914927 445 TPFLLRR 451
Cdd:cd18067 237 NRCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
215-403 3.93e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 3.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    215 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 293
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    294 TPD---IPTMLYHGTQEERQKlvRNIYKRKgtlqiHPVVITSFEIAMRD--RNALQHCYWKYLIVDEGHRIKNM--KCRL 366
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQL--RKLESGK-----TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 21914927    367 IRELKRFNADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 403
Cdd:smart00487 151 EKLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
HELICc smart00490
helicase superfamily c-terminal domain;
629-712 6.82e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.13  E-value: 6.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927    629 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 708
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                   ....
gi 21914927    709 HRIG 712
Cdd:smart00490  79 GRAG 82
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 226-411 6.88e-24

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 100.36  E-value: 6.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEW-LRmlweNGINGILADEMGLGKTVQCIAtIALMIQRgvPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18010   4 FQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA-IAAYYRE--EWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIYKrkgtlqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMK---CRLIRELKRfNADNKLLL 381
Cdd:cd18010  77 IVKSKDGLRDGDAK---------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAALPLLK-RAKRVILL 146

                       170       180       190
                ....*....|....*....|....*....|
gi 21914927 382 TGTPLQNNLSELWSLLNFLLPDVFDDLKSF 411
Cdd:cd18010 147 SGTPALSRPIELFTQLDALDPKLFGRFHDF 176
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
 245-742 1.32e-23

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: 107.08  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  245 ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCgPLSTLPNWMAEF-KRF--TPDIPTMLYhgTQEERQKLVRNIYKRKG 321
Cdd:NF038318  51 ILADEVGLGKTIEAGLVLKYVLESGAKKILIIL-PANLRKQWEIELeEKFdlESLILDSLT--VEKDAKKWNKRLTDNKK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  322 TLqihpVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNmkcrLIRELKRfnADN---------KLLLTGTPLQNNLSE 392
Cdd:NF038318 128 VR----IVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRN----VHKGGKR--AKNlyeltkgipKILLTATPLQNSLLD 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  393 LWSLLNFLLPDVFDDLKSFESWFdITSlsetaEDIIAKEREqnvlhmlhqiLTPFLLRRLKSDVA--LEVPPKREVVVYA 470
Cdd:NF038318 198 LYGLVSFIDPRIFGSEKVFSKRY-IKD-----EDYSDLKRE----------LSPVLYRTLRKDVAdyMQFKKRKCITVDF 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  471 PLSK-------------KQEIFYtAI--VNRT-----IANMFGSSE----------KETIELSPTGRPKRRTRKSINY-- 518
Cdd:NF038318 262 ELSPdeielyvrvnnflKRDILY-SIptSNRTliilvIRKLLASSSfalaetfevlKKRLEKLKEGTRSANAQEGFDLfw 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  519 ----SKIDDFPNEL---EKLISQ---IQPEVDRERAVVEVNIPVESevNLKLQNIMMLLRKCCNHpylieypidpvTQEF 588
Cdd:NF038318 341 sfveDEIDESGFEEkqdELYTRQkefIQHEIDEVDAIIDVAKRIKT--NAKVTALKTALEIAFEY-----------QREE 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  589 KIDEELV--TNS---GKFlildrMLPELKKRGHK---VLLFS-----QMTSMLdilmdYCHLRDFNFSRLDGSMSYSERE 655
Cdd:NF038318 408 GIAQKVVvfTESkrtQKY-----IAEELRKSGYEgedILLFNgdfddAMTKEI-----YRAWQVKNYGKANYGRSVEYKH 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927  656 KNMHSFNTDPEVfifLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTIDQKIVE 734
Cdd:NF038318 478 AIVDYFKNNAKI---LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYE 554


                 ....*...
gi 21914927  735 RAAAKRKL 742
Cdd:NF038318 555 ILSEKFEL 562
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 223-451 1.14e-22

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 97.61  E-value: 1.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLR-----MLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGP------FLVCGPLSTLPNWMAEFK 291
Cdd:cd18066   1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 292 RFTpdiptmlyhGTQEERQKLVRNIYKRKGTLQ--IHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRE 369
Cdd:cd18066  81 KWL---------GSERIKVFTVDQDHKVEEFIAspLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 370 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETA---EDIIAKEREQNvlhmLHQI 443
Cdd:cd18066 152 LTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepiVRSREPTAtpeEKKLGEARAAE----LTRL 227


                ....*...
gi 21914927 444 LTPFLLRR 451
Cdd:cd18066 228 TGLFILRR 235
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 226-413 1.28e-22

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: 96.59  E-value: 1.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGmewLRMLWENGING-ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18011   4 HQIDA---VLRALRKPPVRlLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 305 TQEERQKLVRNIYKRkgtlqiHPVVITSFEIAMRDRNALQHCY---WKYLIVDEGHRIKNMKC-------RLIRELKRfN 374
Cdd:cd18011  81 TAAQLRRLIGNPFEE------FPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRNSGGgketkryKLGRLLAK-R 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21914927 375 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFES 413
Cdd:cd18011 154 ARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 226-416 3.48e-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: 96.04  E-value: 3.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGmewLRMLWEN------------GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18069   4 HQIGG---IRFLYDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 294 TP---DIPTMLY-----------HGTQEERQKLVRNIYKRKGtlqihpVVITSFEIaMRDRNALQhcywkYLIVDEGHRI 359
Cdd:cd18069  81 LPppeALPNVRPrpfkvfilndeHKTTAARAKVIEDWVKDGG------VLLMGYEM-FRLRPGPD-----VVICDEGHRI 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21914927 360 KNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD 416
Cdd:cd18069 149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 239-400 2.01e-21

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 94.07  E-value: 2.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 239 ENGINGILADEMGLGKTVQCIATIalmiqrgVPGPFLVCGPLSTLPNWMAEFKRFT-PDIPTM-LYHGTqeERQKLVRNI 316
Cdd:cd18071  46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVkPGQLKVyTYHGG--ERNRDPKLL 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 317 YKRKgtlqihpVVITSFEIAMRDRNA-----LQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLS 391
Cdd:cd18071 117 SKYD-------IVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189


                ....*....
gi 21914927 392 ELWSLLNFL 400
Cdd:cd18071 190 DLGSLLSFL 198
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 226-451 3.80e-20

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 90.62  E-value: 3.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 226 YQVEGMEWlrMLW---ENGINGILADEMGLGKTVQCIATIaLMIQRG-----------------------VP--GPFLVC 277
Cdd:cd18072   4 HQKQALAW--LLWrerQKPRGGILADDMGLGKTLTMIALI-LAQKNTqnrkeeekekalteweskkdstlVPsaGTLVVC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 278 gPLSTLPNWMAEFKRFTPD--IPTMLYHGTQEERQKLVrniykrkgtLQIHPVVITSFEIAMRD---------RNALQHC 346
Cdd:cd18072  81 -PASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEV---------LRDYDIVITTYSLVAKEiptykeesrSSPLFRI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 347 YWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSetaed 426
Cdd:cd18072 151 AWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRK----- 225

                       250       260
                ....*....|....*....|....*
gi 21914927 427 iiAKEReqnvlhmLHQILTPFLLRR 451
Cdd:cd18072 226 --GGER-------LNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 241-415 1.78e-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: 79.93  E-value: 1.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 241 GINGILADEMGLGKTVQCIA---TIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF--------TPDIPTMLYHGTQEER 309
Cdd:cd18068  28 GSGCILAHCMGLGKTLQVVTflhTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWqeglkdeeKIEVNELATYKRPQER 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 310 qklvrnIYKRKGTLQIHPVVITSFEI--------AMRDRNALQHCYWKYL--------IVDEGHRIKNMKCRLIRELKRF 373
Cdd:cd18068 108 ------SYKLQRWQEEGGVMIIGYDMyrilaqerNVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21914927 374 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 415
Cdd:cd18068 182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 223-450 3.76e-16

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 79.31  E-value: 3.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWlrMLWENGIngiLADEMGLGKTVQCIATIAL-------------------MIQRGVP-------GPFLV 276
Cdd:cd18070   1 LLPYQRRAVNW--MLVPGGI---LADEMGLGKTVEVLALILLhprpdndldaadddsdemvCCPDCLVaetpvssKATLI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 277 CGPLSTLPNWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRkgtLQIHPVVITSFEI--------------------- 335
Cdd:cd18070  76 VCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEI---LAEYDIVVTTYDVlrtelhyaeanrsnrrrrrqk 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 336 -AMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDlksfESW 414
Cdd:cd18070 153 rYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD----SDW 228

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21914927 415 FditslsetAEDIIAKEREQNVLHMLHQILTPFLLR 450
Cdd:cd18070 229 W--------ARVLIRPQGRNKAREPLAALLKELLWR 256
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 223-400 1.56e-09

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 58.90  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEWLRmlwENGINGILADeMGLGKTVQCIATIALMIQRGVPGPFLVCGPL----STLPNWMAEFKRFTpDIP 298
Cdd:cd18013   1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLrvarSTWPDEVEKWNHLR-NLT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 299 TMLYHGTQEERQKLVrniykrkgTLQIHPVVITSFEIAMRDRNALQHCYWKYLIVDEGHRIKNMKCRLIRELK--RFNAD 376
Cdd:cd18013  76 VSVAVGTERQRSKAA--------NTPADLYVINRENLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRkvRPVIK 147

                       170       180
                ....*....|....*....|....
gi 21914927 377 NKLLLTGTPLQNNLSELWSLLNFL 400
Cdd:cd18013 148 RLIGLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
223-385 4.28e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.57  E-value: 4.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGME-WLRMLWENGINGILADEMGLGKTVqcIAtIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKRFTPDIPTm 300
Cdd:COG1061  81 LRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LA-LALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLA- 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 301 lyHGTQEERQKlvrniykrkgtlqihPVVITSFEIAMRD--RNALQHcYWKYLIVDEGHRIKNMKCRLIreLKRFNADNK 378
Cdd:COG1061 157 --GGGKKDSDA---------------PITVATYQSLARRahLDELGD-RFGLVIIDEAHHAGAPSYRRI--LEAFPAAYR 216


                ....*..
gi 21914927 379 LLLTGTP 385
Cdd:COG1061 217 LGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 223-385 7.08e-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: 52.31  E-value: 7.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 223 MRWYQVEGMEwlRMLWENGIN-GILADEMGLGKTVqcIAtIALMIQRGvPGPFLVCGPLSTLPN-WMAEFKRFTPDIPTM 300
Cdd:cd17926   1 LRPYQEEALE--AWLAHKNNRrGILVLPTGSGKTL--TA-LALIAYLK-ELRTLIVVPTDALLDqWKERFEDFLGDSSIG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 301 LYhgtQEERQKLVRNIykrkgtlqihPVVITSFEIAMRDRNALQHCY--WKYLIVDEGHRIknmKCRLIRE-LKRFNADN 377
Cdd:cd17926  75 LI---GGGKKKDFDDA----------NVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL---PAKTFSEiLKELNAKY 138


                ....*...
gi 21914927 378 KLLLTGTP 385
Cdd:cd17926 139 RLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 243-384 4.10e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 50.09  E-value: 4.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 243 NGILADEMGLGKTVqcIATIALmIQRGVP--GPFLVCGPLSTL-PNWMAEFK-RFTPDIPT-MLYHGTQEERQKlvrniY 317
Cdd:cd00046   3 NVLITAPTGSGKTL--AALLAA-LLLLLKkgKKVLVLVPTKALaLQTAERLReLFGPGIRVaVLVGGSSAEERE-----K 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 318 KRKGTLQIhpVVITSFEIAMRDRNALQHCY--WKYLIVDEGHRI------KNMKCRLIRELKRFNADnKLLLTGT 384
Cdd:cd00046  75 NKLGDADI--IIATPDMLLNLLLREDRLFLkdLKLIIVDEAHALlidsrgALILDLAVRKAGLKNAQ-VILLSAT 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 666-720 1.88e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 46.16  E-value: 1.88e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 666 EVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 720
Cdd:cd18785  21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
 565-730 2.47e-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: 50.02  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   565 MLLRKCC---NHPYLIEYPIDPVTQEFK-IDEELVTNSGKFLILDRMLPEL----KKRGHKVLLFSQMTSMLDILMDYCH 636
Cdd:pfam11496  52 LCLENLSlvaTHPYLLVDHYMPKSLLLKdEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEALLL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   637 LRDFNFSRLDGSMSYSE-REKNMHSFNTDPE-VFIFLVSTR-----AGGLGInlTAADTVIIYDSDWNPQSDLQAQDRCH 709
Cdd:pfam11496 132 GKGLSYKRYSGEMLYGEnKKVSDSGNKKIHStTCHLLSSTGqltndDSLLEN--YKFDLIIAFDSSVDTSSPSVEHLRTQ 209

                         170       180
                  ....*....|....*....|.
gi 21914927   710 RIGQTKPVVVYRLVTANTIDQ 730
Cdd:pfam11496 210 NRRKGNLAPIIRLVVINSIEH 230
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 584-714 5.75e-06

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 46.35  E-value: 5.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927 584 VTQEFkideELVTNSGKFLILDRMLPELKKRGhKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNT 663
Cdd:cd18787   1 IKQLY----VVVEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21914927 664 DpEVFIfLVST----RagglGINLTAADTVIIYDsdwNPQSdlqAQDRCHRIGQT 714
Cdd:cd18787  76 G-KVRV-LVATdvaaR----GLDIPGVDHVINYD---LPRD---AEDYVHRIGRT 118
ResIII pfam04851
Type III restriction enzyme, res subunit;
222-385 5.51e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   222 VMRWYQVEGME-WLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGP-LSTLPNWMAEFKRFTPDiPT 299
Cdd:pfam04851   3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPN-YV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21914927   300 MLYHGTQEERQKLVRNIYKrkgtlqihpVVITSFEIAMRDRNALQHCY----WKYLIVDEGHRI--KNMkcrliRELKRF 373
Cdd:pfam04851  82 EIGEIISGDKKDESVDDNK---------IVVTTIQSLYKALELASLELlpdfFDVIIIDEAHRSgaSSY-----RNILEY 147

                         170
                  ....*....|...
gi 21914927   374 NADNKLL-LTGTP 385
Cdd:pfam04851 148 FKPAFLLgLTATP 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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