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Conserved domains on  [gi|574275428|ref|NP_001275999|]
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lymphoid-specific helicase isoform 5 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000678)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-725 9.07e-108

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: 352.18  E-value: 9.07e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNAL------------------------------------ 343
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALkrfswryiiideahriknensllsktmrlfstnyrl 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  344 ----------------------------------------------------QILTPFLLRRLKSDVALEVPPKREVVVY 371
Cdd:PLN03142  324 litgtplqnnlhelwallnfllpeifssaetfdewfqisgendqqevvqqlhKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  372 APLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDRERavvevn 451
Cdd:PLN03142  404 VGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGERKR------ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  452 ipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSM 529
Cdd:PLN03142  434 ----------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRL 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  530 LDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQD 608
Cdd:PLN03142  500 LDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQD 579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  609 RCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSRDYERE-IK 687
Cdd:PLN03142  580 RAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMVRYGAEmVF 648

                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 574275428  688 GSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 725
Cdd:PLN03142  649 SSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-725 9.07e-108

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 352.18  E-value: 9.07e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNAL------------------------------------ 343
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALkrfswryiiideahriknensllsktmrlfstnyrl 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  344 ----------------------------------------------------QILTPFLLRRLKSDVALEVPPKREVVVY 371
Cdd:PLN03142  324 litgtplqnnlhelwallnfllpeifssaetfdewfqisgendqqevvqqlhKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  372 APLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDRERavvevn 451
Cdd:PLN03142  404 VGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGERKR------ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  452 ipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSM 529
Cdd:PLN03142  434 ----------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRL 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  530 LDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQD 608
Cdd:PLN03142  500 LDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQD 579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  609 RCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSRDYERE-IK 687
Cdd:PLN03142  580 RAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMVRYGAEmVF 648

                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 574275428  688 GSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 725
Cdd:PLN03142  649 SSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 215-649 1.87e-100

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 324.10  E-value: 1.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 215 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 294
Cdd:COG0553  235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 295 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQ------------------------------ 344
Cdd:COG0553  314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAavdwdlvildeaqhiknpatkrakavralk 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 345 -----ILT-----------------------------------------------------PFLLRRLKSDVALEVPPKR 366
Cdd:COG0553  386 arhrlALTgtpvenrleelwslldflnpgllgslkafrerfarpiekgdeealerlrrllrPFLLRRTKEDVLKDLPEKT 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 367 EVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketielspTGRPKRRTRKSInyskiddfpneleklisqiqpevdrera 446
Cdd:COG0553  466 EETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI---------------------------- 504

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 447 vvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQM 526
Cdd:COG0553  505 -------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 527 TSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQA 606
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 574275428 607 QDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 649
Cdd:COG0553  639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 220-344 3.11e-82

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: 261.17  E-value: 3.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 300 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQ 344
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQ 125
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 226-479 1.18e-31

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: 125.10  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  226 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PDIP 298
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  299 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNAL----------------------------------- 343
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLkkvhwhrivldeghrlknsksklskalkslktrnr 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  344 ------------------------------------------------------QILTPFLLRRLKSDVALEVPPKREVV 369
Cdd:pfam00176 155 wiltgtplqnnleelwallnflrpgpfgslstfrnwfdrpiergggkkgvsrlhKLLKPFLLRRTKKDVEKSLPPKVEYI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  370 VYAPLSKKQEIFYTAIVnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQpevdreravve 449
Cdd:pfam00176 235 LFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK----------- 260

                         330       340       350
                  ....*....|....*....|....*....|
gi 574275428  450 vNIPVESEVNLKLQNIMMLLRKCCNHPYLI 479
Cdd:pfam00176 261 -TGEGGREIKASLLNILMRLRKICNHPGLI 289
HELICc smart00490
helicase superfamily c-terminal domain;
531-614 6.42e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.74  E-value: 6.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428   531 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 610
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                   ....
gi 574275428   611 HRIG 614
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 ...
 573-644 7.98e-09

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: 59.31  E-value: 7.98e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574275428 573 LVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTIDQKIVERAAAKRKL 644
Cdd:NF038318 490 LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFEL 562
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 221-725 9.07e-108

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 352.18  E-value: 9.07e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  300 MLYHGTQEERQKlVRNIYKRKGTLQihpVVITSFEIAMRDRNAL------------------------------------ 343
Cdd:PLN03142  248 VKFHGNPEERAH-QREELLVAGKFD---VCVTSFEMAIKEKTALkrfswryiiideahriknensllsktmrlfstnyrl 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  344 ----------------------------------------------------QILTPFLLRRLKSDVALEVPPKREVVVY 371
Cdd:PLN03142  324 litgtplqnnlhelwallnfllpeifssaetfdewfqisgendqqevvqqlhKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  372 APLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDRERavvevn 451
Cdd:PLN03142  404 VGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGERKR------ 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  452 ipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSM 529
Cdd:PLN03142  434 ----------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRL 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  530 LDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQD 608
Cdd:PLN03142  500 LDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQD 579

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  609 RCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSRDYERE-IK 687
Cdd:PLN03142  580 RAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMVRYGAEmVF 648

                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 574275428  688 GSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 725
Cdd:PLN03142  649 SSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 215-649 1.87e-100

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 324.10  E-value: 1.87e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 215 PKHFtGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT 294
Cdd:COG0553  235 PAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 295 PDIPTMLYHGTQEERQKLvrniykrkGTLQIHPVVITSFEIAMRDRNALQ------------------------------ 344
Cdd:COG0553  314 PGLRVLVLDGTRERAKGA--------NPFEDADLVITSYGLLRRDIELLAavdwdlvildeaqhiknpatkrakavralk 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 345 -----ILT-----------------------------------------------------PFLLRRLKSDVALEVPPKR 366
Cdd:COG0553  386 arhrlALTgtpvenrleelwslldflnpgllgslkafrerfarpiekgdeealerlrrllrPFLLRRTKEDVLKDLPEKT 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 367 EVVVYAPLSKKQEIFYTAIVNRTIANMfgsseketielspTGRPKRRTRKSInyskiddfpneleklisqiqpevdrera 446
Cdd:COG0553  466 EETLYVELTPEQRALYEAVLEYLRREL-------------EGAEGIRRRGLI---------------------------- 504

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 447 vvevnipvesevnLKLqniMMLLRKCCNHPYLIeypidpvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQM 526
Cdd:COG0553  505 -------------LAA---LTRLRQICSHPALL----------LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 527 TSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQA 606
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 574275428 607 QDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLII 649
Cdd:COG0553  639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 220-344 3.11e-82

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: 261.17  E-value: 3.11e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 300 MLYHGTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQ 344
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQ 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 500-625 2.17e-64

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: 210.03  E-value: 2.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 500 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAG 579
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 574275428 580 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 625
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 223-351 1.69e-44

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: 157.73  E-value: 1.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMI-QRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 574275428 302 YHGTQEERQKLVRNIYKRKgtlqiHPVVITSFEIAMRDRNALQILTPFLL 351
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDK-----FDVVLTTYETLRRDKASLRKFRWDLV 125
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 220-343 3.52e-40

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: 147.08  E-value: 3.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 299 TMLYHGTQEERQKLVRNIYKRKGtlqiHPVVITSFEIAMRDRNAL 343
Cdd:cd17997   81 VVVLIGDKEERADIIRDVLLPGK----FDVCITSYEMVIKEKTVL 121
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 221-344 1.49e-35

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: 133.85  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTM 300
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 574275428 301 LYHGTQEERQKLVRniykrkgtLQIHPVVITSFEIAMRDRNALQ 344
Cdd:cd18012   83 VIHGTKRKREKLRA--------LEDYDLVITSYGLLRRDIELLK 118
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 220-343 1.43e-33

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: 128.64  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITyLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 299 TMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNAL 343
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQI--RAGKFN---VLLTTYEYIIKDKPLL 120
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 226-360 9.42e-33

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: 124.81  E-value: 9.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGT 305
Cdd:cd17998    4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGS 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 306 QEERQKLVRNIYKRKGTLQihpVVITSFEIAMRDRNALQiltpfLLRRLKSDVAL 360
Cdd:cd17998   84 QEERKHLRYDILKGLEDFD---VIVTTYNLATSNPDDRS-----FFKRLKLNYVV 130
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 226-479 1.18e-31

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: 125.10  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  226 YQVEGMEWLRMLWEN-GINGILADEMGLGKTVQCIATIALM----IQRGvpGPFLVCGPLSTLPNWMAEFKRFT--PDIP 298
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLkhvdKNWG--GPTLIVVPLSLLHNWMNEFERWVspPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  299 TMLYHGTQEERQKLVRNiykrKGTLQIHPVVITSFEIAMRDRNAL----------------------------------- 343
Cdd:pfam00176  79 VVVLHGNKRPQERWKND----PNFLADFDVVITTYETLRKHKELLkkvhwhrivldeghrlknsksklskalkslktrnr 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  344 ------------------------------------------------------QILTPFLLRRLKSDVALEVPPKREVV 369
Cdd:pfam00176 155 wiltgtplqnnleelwallnflrpgpfgslstfrnwfdrpiergggkkgvsrlhKLLKPFLLRRTKKDVEKSLPPKVEYI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  370 VYAPLSKKQEIFYTAIVnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQpevdreravve 449
Cdd:pfam00176 235 LFCRLSKLQRKLYQTFL-------------------------------------------LKKDLNAIK----------- 260

                         330       340       350
                  ....*....|....*....|....*....|
gi 574275428  450 vNIPVESEVNLKLQNIMMLLRKCCNHPYLI 479
Cdd:pfam00176 261 -TGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 226-344 1.95e-31

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: 122.61  E-value: 1.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18002    4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 574275428 305 TQEERQKLVRNIYKRKGTLQIHP--VVITSFEIAMRDRNALQ 344
Cdd:cd18002   84 NPKDRKVLRKFWDRKNLYTRDAPfhVVITSYQLVVQDEKYFQ 125
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 223-343 3.60e-31

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: 121.59  E-value: 3.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTML 301
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 574275428 302 YHGTQEERQKL--------VRNIYKRKGTLQIHpVVITSFEIAMRDRNAL 343
Cdd:cd17995   80 YHGSGESRQIIqqyemyfkDAQGRKKKGVYKFD-VLITTYEMVIADAEEL 128
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 501-614 2.00e-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: 2.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  501 GKFLILDRMLPelKKRGHKVLLFSQMTSMLDILMdYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGG 580
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 574275428  581 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 614
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 223-342 4.94e-30

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: 118.22  E-value: 4.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 574275428 302 YHGTQEERQKlvrniyKRKGTLQ---IHpVVITSFEIAMRDRNA 342
Cdd:cd18003   81 YYGSAKERKL------KRQGWMKpnsFH-VCITSYQLVVQDHQV 117
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 223-360 1.21e-28

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: 114.38  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17993    2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSyLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574275428 302 YHGTQEERQkLVRN----IYKRKgTLQIHpVVITSFEIAMRDRNAL-QILTPFLL----RRLKSDVAL 360
Cdd:cd17993   82 YLGDIKSRD-TIREyefyFSQTK-KLKFN-VLLTTYEIILKDKAFLgSIKWQYLAvdeaHRLKNDESL 146
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 215-344 3.15e-26

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: 108.21  E-value: 3.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 215 PKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18064    8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRW 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 574275428 294 TPDIPTMLYHGTQEERQKLVRNIYkRKGTLQihpVVITSFEIAMRDRNALQ 344
Cdd:cd18064   88 VPTLRAVCLIGDKDQRAAFVRDVL-LPGEWD---VCVTSYEMLIKEKSVFK 134
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 213-344 7.71e-26

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: 106.64  E-value: 7.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18065    6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFK 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 574275428 292 RFTPDIPTMLYHGTQEERQKLVRNIYKrKGTLQihpVVITSFEIAMRDRNALQ 344
Cdd:cd18065   86 RWVPSLRAVCLIGDKDARAAFIRDVMM-PGEWD---VCVTSYEMVIKEKSVFK 134
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 223-339 4.16e-25

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: 104.35  E-value: 4.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 303 HGTQEERQKLVR-NIYKR-------KGTLQIHpVVITSFEIAMRD 339
Cdd:cd18058   80 HGSQISRQMIQQyEMYYRdeqgnplSGIFKFQ-VVITTFEMILAD 123
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 223-343 5.88e-25

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: 103.67  E-value: 5.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 574275428 302 YHGTQEERQKLVRNIYKrkgTLQIHpVVITSFEIAMRDRNAL 343
Cdd:cd18006   81 YMGDKEKRLDLQQDIKS---TNRFH-VLLTTYEICLKDASFL 118
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 213-343 1.76e-24

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: 103.20  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18062   14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRINGPFLIIVPLSTLSNWVYEFD 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 574275428 292 RFTPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNAL 343
Cdd:cd18062   94 KWAPSVVKVSYKGSPAARRAFVPQL--RSGKFN---VLLTTYEYIIKDKQIL 140
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 213-343 1.93e-24

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: 103.22  E-value: 1.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18063   14 KQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 574275428 292 RFTPDIPTMLYHGTQEERQKLVRNIykRKGTLQihpVVITSFEIAMRDRNAL 343
Cdd:cd18063   94 KWAPSVVKISYKGTPAMRRSLVPQL--RSGKFN---VLLTTYEYIIKDKHIL 140
HELICc smart00490
helicase superfamily c-terminal domain;
531-614 6.42e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.74  E-value: 6.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428   531 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 610
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                   ....
gi 574275428   611 HRIG 614
Cdd:smart00490  79 GRAG 82
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 223-339 1.52e-23

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: 99.72  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 574275428 303 HGTQEERQKL-VRNIYKR-------KGTLQIHpVVITSFEIAMRD 339
Cdd:cd18059   80 HGSQASRRTIqLYEMYFKdpqgrviKGSYKFH-AIITTFEMILTD 123
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 226-304 3.50e-23

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: 97.90  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATI-ALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd17994    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLySLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 223-339 4.51e-23

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: 98.20  E-value: 4.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 574275428 303 HGTQEERQKLVR-NIYKRKGTLQIHP------VVITSFEIAMRD 339
Cdd:cd18060   80 HGSLASRQMIQQyEMYCKDSRGRLIPgaykfdALITTFEMILSD 123
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 225-344 1.10e-22

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: 97.44  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 225 WYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18001    3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 574275428 305 T-QEERQKLVRNIYKRKGtlqihpVVITSFEIAMRDRNALQ 344
Cdd:cd18001   83 TsKKERERNLERIQRGGG------VLLTTYGMVLSNTEQLS 117
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 226-343 4.64e-22

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: 95.46  E-value: 4.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18055    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNAL 343
Cdd:cd18055   84 DKDSRAIIRENEFsfddnavkggkkafkmKREAQVKFH-VLLTSYELVTIDQAAL 137
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 213-360 6.80e-22

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: 95.46  E-value: 6.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 213 QQPKHFTGG--VMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAE 289
Cdd:cd18054    9 KQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSyLFHQHQLYGPFLLVVPLSTLTSWQRE 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574275428 290 FKRFTPDIPTMLYHGTQEERqKLVRN---IYKRKGTLQIHpVVITSFEIAMRDRNAL-QILTPFL----LRRLKSDVAL 360
Cdd:cd18054   89 FEIWAPEINVVVYIGDLMSR-NTIREyewIHSQTKRLKFN-ALITTYEILLKDKTVLgSINWAFLgvdeAHRLKNDDSL 165
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 226-343 1.80e-20

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: 90.89  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18057    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRDRNAL 343
Cdd:cd18057   84 DKESRSVIRENEFsfednairsgkkvfrmKKEAQIKFH-VLLTSYELITIDQAIL 137
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 223-337 4.06e-20

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: 89.68  E-value: 4.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 574275428 303 HGTQEERQKLVR-NIYKRKGTLQI------HPVVITSFEIAM 337
Cdd:cd18061   80 HGSLISRQMIQQyEMYFRDSQGRIirgayrFQAIITTFEMIL 121
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 226-339 2.63e-19

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: 87.81  E-value: 2.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18056    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 574275428 305 TQEERQKLVRNIY----------------KRKGTLQIHpVVITSFEIAMRD 339
Cdd:cd18056   84 DKDSRAIIRENEFsfednairggkkasrmKKEASVKFH-VLLTSYELITID 133
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 223-349 1.79e-17

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: 82.40  E-value: 1.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIAL------MIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPD 296
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 297 --IPTMLYHGTQEERQKLVRNIYKrkgtlqiHPVVITSFEIAmrdRNALQILTPF 349
Cdd:cd17999   81 afLKPLAYVGPPQERRRLREQGEK-------HNVIVASYDVL---RNDIEVLTKI 125
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 210-360 2.71e-17

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: 82.02  E-value: 2.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 210 VPFQQPKHFTGGV----MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLP 284
Cdd:cd18053    4 VALKKQPSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNyLFHEHQLYGPFLLVVPLSTLT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 285 NWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRKGTLQIH-PVVITSFEIAMRDRNALQILTPFLL-----RRLKSDV 358
Cdd:cd18053   84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKfNILLTTYEILLKDKSFLGGLNWAFIgvdeaHRLKNDD 163


                 ..
gi 574275428 359 AL 360
Cdd:cd18053  164 SL 165
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 226-353 3.50e-17

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: 80.45  E-value: 3.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALM--IQRGVpGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYH 303
Cdd:cd18000    4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhhSKLGL-GPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574275428 304 ------------GTQEERQKLVRNIYKRKGtlqihpVVITSFEiamrdrnALQILTPFLLRR 353
Cdd:cd18000   83 ssgsgtgseeklGSIERKSQLIRKVVGDGG------ILITTYE-------GFRKHKDLLLNH 131
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 223-334 4.42e-15

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: 75.49  E-value: 4.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR---------------------GVPGPFLVCGPLS 281
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574275428 282 TLPNWMAEFKR---FTpdipTMLYHGTQEERQKLVRniYKRkGTLQihpVVITSFE 334
Cdd:cd18005   81 VLYNWKDELDTwghFE----VGVYHGSRKDDELEGR--LKA-GRLE---VVVTTYD 126
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 226-339 3.99e-14

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: 72.71  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEWlrMLWeNGinGILADEMGLGKTVQCIATIAL------------------MIQRGVPGPFLVCGPLSTLPNWM 287
Cdd:cd18008    4 YQKQGLAW--MLP-RG--GILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLSQWK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 574275428 288 AEFKRFT--PDIPTMLYHGTQeerqklvRNIYKRKgtLQIHPVVITSFEIAMRD 339
Cdd:cd18008   79 DEIEKHTkpGSLKVYVYHGSK-------RIKSIEE--LSDYDIVITTYGTLASE 123
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 223-356 1.09e-12

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: 68.47  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWL--RMLWENGING---ILADEMGLGKTVQCIATIALMIQRGVPGP-----FLVCGPLSTLPNWMAEFKR 292
Cdd:cd18004    1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 293 FTPDIPTMLYhgTQEERQKLVRNIYKRKGTLQIHPVVITSFEIAMRDRNALQILTPFLL------RRLKS 356
Cdd:cd18004   81 WLGLRRIKVV--TADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLlicdegHRLKN 148
DEXDc smart00487
DEAD-like helicases superfamily;
215-339 2.39e-12

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 66.36  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428   215 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 293
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 574275428   294 TPD---IPTMLYHGTQEERQKlvRNIYKRKgtlqiHPVVITSFEIAMRD 339
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQL--RKLESGK-----TDILVTTPGRLLDL 119
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 223-323 1.33e-10

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: 62.31  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGmewLRMLWEN---------GING-ILADEMGLGKTVQCIATIALMIQRGVPG--PFLVCgPLSTLPNWMAEF 290
Cdd:cd18007    1 LKPHQVEG---VRFLWSNlvgtdvgsdEGGGcILAHTMGLGKTLQVITFLHTYLAAAPRRsrPLVLC-PASTLYNWEDEF 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 574275428 291 KRFTPD---IPTMLY----HGTQEERQKLVRNIYKRKGTL 323
Cdd:cd18007   77 KKWLPPdlrPLLVLVslsaSKRADARLRKINKWHKEGGVL 116
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 223-335 8.68e-10

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: 60.05  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWlrMLWENGIngiLADEMGLGKTVQCIATIAL-------------------MIQRGVP-------GPFLV 276
Cdd:cd18070    1 LLPYQRRAVNW--MLVPGGI---LADEMGLGKTVEVLALILLhprpdndldaadddsdemvCCPDCLVaetpvssKATLI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 574275428 277 CGPLSTLPNWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRkgtLQIHPVVITSFEI 335
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEI---LAEYDIVVTTYDV 131
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 226-344 2.77e-09

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: 57.60  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGMEW-LRmlweNGINGILADEMGLGKTVQCIAtIALMIQRgvPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18010    4 FQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA-IAAYYRE--EWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 574275428 305 TQEERQKLVRNIYKrkgtlqihpVVITSFEIAMRDRNALQ 344
Cdd:cd18010   77 IVKSKDGLRDGDAK---------VVIVSYDLLRRLEKQLL 107
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
 573-644 7.98e-09

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: 59.31  E-value: 7.98e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574275428 573 LVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV-TANTIDQKIVERAAAKRKL 644
Cdd:NF038318 490 LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFEL 562
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 223-334 2.70e-08

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: 55.55  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGmewLRMLWE-------NGING-ILADEMGLGKTVQCIATI-ALMIQRGVPGPFL----VCGPLSTLPNWMAE 289
Cdd:cd18067    1 LRPHQREG---VKFLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMwTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 574275428 290 F-KRFTPDIPTMLYHGTQ--EERQKLVRNIYKRkGTLQIHPVVITSFE 334
Cdd:cd18067   78 LgKWLGGRLQPLAIDGGSkkEIDRKLVQWASQQ-GRRVSTPVLIISYE 124
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 226-295 5.13e-07

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 51.35  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGmewLRMLWEN------------GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18069    4 HQIGG---IRFLYDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80


                 ..
gi 574275428 294 TP 295
Cdd:cd18069   81 LP 82
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 223-293 5.28e-07

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: 51.38  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 223 MRWYQVEGMEWLR-----MLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGP------FLVCGPLSTLPNWMAEFK 291
Cdd:cd18066    1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80


                 ..
gi 574275428 292 RF 293
Cdd:cd18066   81 KW 82
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 239-309 9.14e-07

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: 50.55  E-value: 9.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574275428 239 ENGINGILADEMGLGKTVQCIATIalmiqrgVPGPFLVCGPLSTLPNWMAEFKRFT-PDIPTM-LYHGTQEER 309
Cdd:cd18071   46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVkPGQLKVyTYHGGERNR 111
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
 467-632 1.46e-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: 50.40  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  467 MLLRKCC---NHPYLIEYPIDPVTQEFK-IDEELVTNSGKFLILDRMLPEL----KKRGHKVLLFSQMTSMLDILMDYCH 538
Cdd:pfam11496  52 LCLENLSlvaTHPYLLVDHYMPKSLLLKdEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEALLL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428  539 LRDFNFSRLDGSMSYSE-REKNMHSFNTDPE-VFIFLVSTR-----AGGLGInlTAADTVIIYDSDWNPQSDLQAQDRCH 611
Cdd:pfam11496 132 GKGLSYKRYSGEMLYGEnKKVSDSGNKKIHStTCHLLSSTGqltndDSLLEN--YKFDLIIAFDSSVDTSSPSVEHLRTQ 209

                         170       180
                  ....*....|....*....|.
gi 574275428  612 RIGQTKPVVVYRLVTANTIDQ 632
Cdd:pfam11496 210 NRRKGNLAPIIRLVVINSIEH 230
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 568-622 1.67e-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: 1.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 568 EVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 622
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 226-340 2.08e-06

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: 49.21  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 226 YQVEGmewLRMLWENGING-ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18011    4 HQIDA---VLRALRKPPVRlLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 574275428 305 TQEERQKLVRNIYKRkgtlqiHPVVITSFEIAMRDR 340
Cdd:cd18011   81 TAAQLRRLIGNPFEE------FPIVIVSLDLLKRSE 110
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 486-616 4.97e-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: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275428 486 VTQEFkideELVTNSGKFLILDRMLPELKKRGhKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNT 565
Cdd:cd18787    1 IKQLY----VVVEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275428 566 DpEVFIfLVST----RagglGINLTAADTVIIYDsdwNPQSdlqAQDRCHRIGQT 616
Cdd:cd18787   76 G-KVRV-LVATdvaaR----GLDIPGVDHVINYD---LPRD---AEDYVHRIGRT 118
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 241-293 5.99e-04

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: 42.18  E-value: 5.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574275428 241 GINGILADEMGLGKTVQCIA---TIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18068   28 GSGCILAHCMGLGKTLQVVTflhTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKW 83
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 223-285 2.63e-03

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: 40.03  E-value: 2.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574275428 223 MRWYQVEGMEWLRmlwENGINGILADeMGLGKTVQCIATIALMIQRGVPGPFLVCGPL----STLPN 285
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLrvarSTWPD 63
 
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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