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Conserved domains on  [gi|1002296320|ref|XP_015611621|]
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ATP-dependent DNA helicase DDM1 [Oryza sativa Japonica Group]

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
96-764 3.15e-165

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: 507.03  E-value: 3.15e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320   96 EEGQLLEPVKEEKADDFVDAVPSLPIDLEAKNGDASLITDAMKE----EEEKLHD-ARVKAEEEEVARKREEAARLAFDP 170
Cdd:PLN03142    13 EDEEELEAVARSAGSDSDDDEVPAEDEDEDEEDDEEAESPAKAEiskrEKARLKElKKQKKQEIQKILEQQNAAIDADMN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  171 NARFNKLDELLSQTQLYSEFLlekmetiadvEGVQTHAEEepveeKKNGRGRKrkatsapkyndkkakkavAVMLTRSHE 250
Cdd:PLN03142    93 NKGKGRLKYLLQQTEIFAHFA----------KGDQSASAK-----KAKGRGRH------------------ASKLTEEEE 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  251 DcspEDCTLTEEERWEKEQA-RLV--PLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGK 326
Cdd:PLN03142   140 D---EEYLKEEEDGLGGSGGtRLLvqPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLhEYR 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  327 GLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYHGDKAARAEIRRKFMPKTtgpDFPLIVTSYEMAMSDAKHLAHYKWK 406
Cdd:PLN03142   217 GITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAG---KFDVCVTSFEMAIKEKTALKRFSWR 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  407 YVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGeeeqeds 486
Cdd:PLN03142   294 YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEND------- 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  487 eekrKVDVVSKLHAILRPFLLRRMKEDVEHMLPRKKEIIIYANMTDHQKQIQNHLVEQTFDqylhekseiVLRKPGIKAK 566
Cdd:PLN03142   367 ----QQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLD---------VVNAGGERKR 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  567 LNNLLIQLRKNCNHPDLLESAYDSsglyPPV---EKLLEQCGKFQLLNRLLSLLLARKHKVLIFSQWTKVLDIIEYYLET 643
Cdd:PLN03142   434 LLNIAMQLRKCCNHPYLFQGAEPG----PPYttgEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  644 KGLQVCRIDGSVKLEERRRQIAEFNDLNSSMNIFILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRP 723
Cdd:PLN03142   510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002296320  724 VHVYRLATSHSVEGRIIKKAFGKLRLEHVVIGKGQFEQDRA 764
Cdd:PLN03142   590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKT 630
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
96-764 3.15e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 507.03  E-value: 3.15e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320   96 EEGQLLEPVKEEKADDFVDAVPSLPIDLEAKNGDASLITDAMKE----EEEKLHD-ARVKAEEEEVARKREEAARLAFDP 170
Cdd:PLN03142    13 EDEEELEAVARSAGSDSDDDEVPAEDEDEDEEDDEEAESPAKAEiskrEKARLKElKKQKKQEIQKILEQQNAAIDADMN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  171 NARFNKLDELLSQTQLYSEFLlekmetiadvEGVQTHAEEepveeKKNGRGRKrkatsapkyndkkakkavAVMLTRSHE 250
Cdd:PLN03142    93 NKGKGRLKYLLQQTEIFAHFA----------KGDQSASAK-----KAKGRGRH------------------ASKLTEEEE 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  251 DcspEDCTLTEEERWEKEQA-RLV--PLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGK 326
Cdd:PLN03142   140 D---EEYLKEEEDGLGGSGGtRLLvqPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLhEYR 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  327 GLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYHGDKAARAEIRRKFMPKTtgpDFPLIVTSYEMAMSDAKHLAHYKWK 406
Cdd:PLN03142   217 GITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAG---KFDVCVTSFEMAIKEKTALKRFSWR 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  407 YVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGeeeqeds 486
Cdd:PLN03142   294 YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEND------- 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  487 eekrKVDVVSKLHAILRPFLLRRMKEDVEHMLPRKKEIIIYANMTDHQKQIQNHLVEQTFDqylhekseiVLRKPGIKAK 566
Cdd:PLN03142   367 ----QQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLD---------VVNAGGERKR 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  567 LNNLLIQLRKNCNHPDLLESAYDSsglyPPV---EKLLEQCGKFQLLNRLLSLLLARKHKVLIFSQWTKVLDIIEYYLET 643
Cdd:PLN03142   434 LLNIAMQLRKCCNHPYLFQGAEPG----PPYttgEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  644 KGLQVCRIDGSVKLEERRRQIAEFNDLNSSMNIFILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRP 723
Cdd:PLN03142   510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002296320  724 VHVYRLATSHSVEGRIIKKAFGKLRLEHVVIGKGQFEQDRA 764
Cdd:PLN03142   590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKT 630
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
54-755 8.98e-145

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 443.13  E-value: 8.98e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  54 EEDHLDVLIEEKVDGFVDASSSLNVEPAANNSDLSPLTVPVKEEGQLLEPVKEEKADDFVDAVPSLPIDLEAKNGDASLI 133
Cdd:COG0553    12 ALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 134 TDAMKEEEEKLHDARVKAEEEEVARKREEAARLAFDPNARFNKLDELLSQTQLYSEFLLEKMETIADVEGVQTHAEEEPV 213
Cdd:COG0553    92 LLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 214 EEKKNGRGRKRKATSAPKYNDKKAKKAVAVMLTRSHEDCSPEDCTLTEEE---RWEKEQARLVPLMTGGKLKSYQIKGVK 290
Cdd:COG0553   172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAfrlRRLREALESLPAGLKATLRPYQLEGAA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 291 WLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYHGDKaARAEI 370
Cdd:COG0553   252 WLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR-ERAKG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 371 RRKFmpkttgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAEL 450
Cdd:COG0553   331 ANPF------EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 451 WSLLNFILPDIFSSHQEFESWFdfsakggeeeqEDSEEKRKVDVVSKLHAILRPFLLRRMKEDVEHMLPRKKEIIIYANM 530
Cdd:COG0553   405 WSLLDFLNPGLLGSLKAFRERF-----------ARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 531 TDHQKQIqnhlveqtFDQYLHEKSEIVLRKPGIKAKLNNL--LIQLRKNCNHPDLLESAYDSSGLYPP-VEKLLEQCGKF 607
Cdd:COG0553   474 TPEQRAL--------YEAVLEYLRRELEGAEGIRRRGLILaaLTRLRQICSHPALLLEEGAELSGRSAkLEALLELLEEL 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 608 qllnrllsllLARKHKVLIFSQWTKVLDIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDlNSSMNIFILSTRAGGLG 687
Cdd:COG0553   546 ----------LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEG 614
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 688 INLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRPVHVYRLATSHSVEGRIIKKAFGKLRLEHVVIG 755
Cdd:COG0553   615 LNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
278-511 5.98e-137

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: 406.00  E-value: 5.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 278 GGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTG 357
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 358 LIYHGDKAARAEIRRKFMP-KTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKL 436
Cdd:cd18009    81 LLYHGTKEERERLRKKIMKrEGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKG-GEEEQEDSEEKRKVDVVSKLHAILRPFLLRRMK 511
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSdNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
284-584 3.51e-97

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: 304.99  E-value: 3.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 284 YQIKGVKWLISLWQN-GLNGILADQMGLGKTIQTIGFLAHLKG--KGLDGPYLIIAPLSTLSNWVNEISRFV--PSMTGL 358
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvdKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 359 IYHGDKAARAEIRRKFMpktTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLL 438
Cdd:pfam00176  81 VLHGNKRPQERWKNDPN---FLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 439 TGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEqedseekrkvDVVSKLHAILRPFLLRRMKEDVEHML 518
Cdd:pfam00176 158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK----------KGVSRLHKLLKPFLLRRTKKDVEKSL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002296320 519 PRKKEIIIYANMTDHQKQI-QNHLVEQTFDQYLHEKSEivlrkPGIKAKLNNLLIQLRKNCNHPDLL 584
Cdd:pfam00176 228 PPKVEYILFCRLSKLQRKLyQTFLLKKDLNAIKTGEGG-----REIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
273-465 1.22e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 119.52  E-value: 1.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  273 VPLMTGGKLKSYQIKGVKWLISLWQNGlngILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTL-SNWVNEISRF 351
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  352 VPSMTG---LIYHGDKaaraeiRRKFMPKTTGPDFPLIVTSYEMAMSDAKH--LAHYKWKYVIVDEGHRLKNS--KCLLL 424
Cdd:smart00487  78 GPSLGLkvvGLYGGDS------KREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGgfGDQLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1002296320  425 RELKRLPMDNK-LLLTGTP---LQNNLAELWSLLNFILPDIFSSH 465
Cdd:smart00487 152 KLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
303-729 1.56e-14

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: 77.80  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 303 ILADQMGLGKTIQT---IGFLAHLKGKGLdgpyLIIAPLSTLSNWVNEI-SRFvpSMTGLIYhgDKAARAEIRRKFMPKT 378
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELeEKF--DLESLIL--DSLTVEKDAKKWNKRL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 379 TGPDFPLIV-TSYEMAMSDAKHLAHYKWKYVIVDEGHRLKN-----SKCLLLREL-KRLPmdnKLLLTGTPLQNNLAELW 451
Cdd:NF038318  123 TDNKKVRIViTSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhkggKRAKNLYELtKGIP---KILLTATPLQNSLLDLY 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 452 SLLNFILPDIFSSHQEFESWF----DFSAkggeeeqedseekrkvdvvskLHAILRPFLLRRMKEDV-EHM-LPRKKEI- 524
Cdd:NF038318  200 GLVSFIDPRIFGSEKVFSKRYikdeDYSD---------------------LKRELSPVLYRTLRKDVaDYMqFKKRKCIt 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 525 -----------------------IIYANMTDHQ-------------------------KQIQNHLVEQT----------- 545
Cdd:NF038318  259 vdfelspdeielyvrvnnflkrdILYSIPTSNRtliilvirkllasssfalaetfevlKKRLEKLKEGTrsanaqegfdl 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 546 ----FDQYLHEKSE-------IVLRKPGIKAKLN------NLLIQLRKNCNhpdllesaydSSGLYPPVEKLLEqcgkFQ 608
Cdd:NF038318  339 fwsfVEDEIDESGFeekqdelYTRQKEFIQHEIDevdaiiDVAKRIKTNAK----------VTALKTALEIAFE----YQ 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 609 LLNRLlslllarKHKVLIFSQWTKVLDIIEYYLETKGLQVCRI--------DGSVKLEERRRQIAEFNDLNSSMNI---- 676
Cdd:NF038318  405 REEGI-------AQKVVVFTESKRTQKYIAEELRKSGYEGEDIllfngdfdDAMTKEIYRAWQVKNYGKANYGRSVeykh 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002296320 677 -----------FILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRPVHVYRL 729
Cdd:NF038318  478 aivdyfknnakILIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINL 541
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
96-764 3.15e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 507.03  E-value: 3.15e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320   96 EEGQLLEPVKEEKADDFVDAVPSLPIDLEAKNGDASLITDAMKE----EEEKLHD-ARVKAEEEEVARKREEAARLAFDP 170
Cdd:PLN03142    13 EDEEELEAVARSAGSDSDDDEVPAEDEDEDEEDDEEAESPAKAEiskrEKARLKElKKQKKQEIQKILEQQNAAIDADMN 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  171 NARFNKLDELLSQTQLYSEFLlekmetiadvEGVQTHAEEepveeKKNGRGRKrkatsapkyndkkakkavAVMLTRSHE 250
Cdd:PLN03142    93 NKGKGRLKYLLQQTEIFAHFA----------KGDQSASAK-----KAKGRGRH------------------ASKLTEEEE 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  251 DcspEDCTLTEEERWEKEQA-RLV--PLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGK 326
Cdd:PLN03142   140 D---EEYLKEEEDGLGGSGGtRLLvqPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLhEYR 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  327 GLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYHGDKAARAEIRRKFMPKTtgpDFPLIVTSYEMAMSDAKHLAHYKWK 406
Cdd:PLN03142   217 GITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAG---KFDVCVTSFEMAIKEKTALKRFSWR 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  407 YVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGeeeqeds 486
Cdd:PLN03142   294 YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEND------- 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  487 eekrKVDVVSKLHAILRPFLLRRMKEDVEHMLPRKKEIIIYANMTDHQKQIQNHLVEQTFDqylhekseiVLRKPGIKAK 566
Cdd:PLN03142   367 ----QQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLD---------VVNAGGERKR 433
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  567 LNNLLIQLRKNCNHPDLLESAYDSsglyPPV---EKLLEQCGKFQLLNRLLSLLLARKHKVLIFSQWTKVLDIIEYYLET 643
Cdd:PLN03142   434 LLNIAMQLRKCCNHPYLFQGAEPG----PPYttgEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  644 KGLQVCRIDGSVKLEERRRQIAEFNDLNSSMNIFILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRP 723
Cdd:PLN03142   510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002296320  724 VHVYRLATSHSVEGRIIKKAFGKLRLEHVVIGKGQFEQDRA 764
Cdd:PLN03142   590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKT 630
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
54-755 8.98e-145

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 443.13  E-value: 8.98e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  54 EEDHLDVLIEEKVDGFVDASSSLNVEPAANNSDLSPLTVPVKEEGQLLEPVKEEKADDFVDAVPSLPIDLEAKNGDASLI 133
Cdd:COG0553    12 ALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 134 TDAMKEEEEKLHDARVKAEEEEVARKREEAARLAFDPNARFNKLDELLSQTQLYSEFLLEKMETIADVEGVQTHAEEEPV 213
Cdd:COG0553    92 LLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 214 EEKKNGRGRKRKATSAPKYNDKKAKKAVAVMLTRSHEDCSPEDCTLTEEE---RWEKEQARLVPLMTGGKLKSYQIKGVK 290
Cdd:COG0553   172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAfrlRRLREALESLPAGLKATLRPYQLEGAA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 291 WLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYHGDKaARAEI 370
Cdd:COG0553   252 WLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR-ERAKG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 371 RRKFmpkttgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAEL 450
Cdd:COG0553   331 ANPF------EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEEL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 451 WSLLNFILPDIFSSHQEFESWFdfsakggeeeqEDSEEKRKVDVVSKLHAILRPFLLRRMKEDVEHMLPRKKEIIIYANM 530
Cdd:COG0553   405 WSLLDFLNPGLLGSLKAFRERF-----------ARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 531 TDHQKQIqnhlveqtFDQYLHEKSEIVLRKPGIKAKLNNL--LIQLRKNCNHPDLLESAYDSSGLYPP-VEKLLEQCGKF 607
Cdd:COG0553   474 TPEQRAL--------YEAVLEYLRRELEGAEGIRRRGLILaaLTRLRQICSHPALLLEEGAELSGRSAkLEALLELLEEL 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 608 qllnrllsllLARKHKVLIFSQWTKVLDIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDlNSSMNIFILSTRAGGLG 687
Cdd:COG0553   546 ----------LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEG 614
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 688 INLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRPVHVYRLATSHSVEGRIIKKAFGKLRLEHVVIG 755
Cdd:COG0553   615 LNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
278-511 5.98e-137

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: 406.00  E-value: 5.98e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 278 GGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTG 357
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 358 LIYHGDKAARAEIRRKFMP-KTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKL 436
Cdd:cd18009    81 LLYHGTKEERERLRKKIMKrEGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKG-GEEEQEDSEEKRKVDVVSKLHAILRPFLLRRMK 511
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSdNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
284-584 3.51e-97

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: 304.99  E-value: 3.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 284 YQIKGVKWLISLWQN-GLNGILADQMGLGKTIQTIGFLAHLKG--KGLDGPYLIIAPLSTLSNWVNEISRFV--PSMTGL 358
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvdKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 359 IYHGDKAARAEIRRKFMpktTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLL 438
Cdd:pfam00176  81 VLHGNKRPQERWKNDPN---FLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 439 TGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEqedseekrkvDVVSKLHAILRPFLLRRMKEDVEHML 518
Cdd:pfam00176 158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK----------KGVSRLHKLLKPFLLRRTKKDVEKSL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002296320 519 PRKKEIIIYANMTDHQKQI-QNHLVEQTFDQYLHEKSEivlrkPGIKAKLNNLLIQLRKNCNHPDLL 584
Cdd:pfam00176 228 PPKVEYILFCRLSKLQRKLyQTFLLKKDLNAIKTGEGG-----REIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
278-511 8.62e-95

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: 296.16  E-value: 8.62e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 278 GGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKG-KGLDGPYLIIAPLSTLSNWVNEISRFVPSMT 356
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 357 GLIYHGDKAARAEI-RRKFMPKttgpDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNK 435
Cdd:cd17997    81 VVVLIGDKEERADIiRDVLLPG----KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002296320 436 LLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDfsakggeeeqEDSEEKRKVDVVSKLHAILRPFLLRRMK 511
Cdd:cd17997   157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN----------VNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
278-511 4.39e-90

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: 284.26  E-value: 4.39e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 278 GGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMT 356
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLmEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 357 GLIYHGDKAARAEIRRKFMPKttgpDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKR-LPMDNK 435
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAG----KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 436 LLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFD--FsAKGGEEEQEDSEEKRKVDVVSKLHAILRPFLLRRMK 511
Cdd:cd17996   157 LLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpF-ANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
281-462 6.44e-81

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: 257.88  E-value: 6.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLK-GKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRKFMPkttgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLT 439
Cdd:cd17919    81 YHGSQRERAQIRAKEKL----DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLT 156
                         170       180
                  ....*....|....*....|...
gi 1002296320 440 GTPLQNNLAELWSLLNFILPDIF 462
Cdd:cd17919   157 GTPLQNNLEELWALLDFLDPPFL 179
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
281-509 6.62e-78

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: 251.40  E-value: 6.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGK-GLDGPYLIIAPLSTLSNWVNEISRFVPsMTGLI 359
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIR---RKFMPKTTGPD-----FPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLP 431
Cdd:cd17995    80 YHGSGESRQIIQqyeMYFKDAQGRKKkgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 432 MDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFdfsakGGEeeqedseekRKVDVVSKLHAILRPFLLRR 509
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF-----GDL---------KTAEQVEKLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
281-509 2.86e-74

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: 242.03  E-value: 2.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLaEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRKFMPKT-TGPD--FPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKL 436
Cdd:cd18002    81 YWGNPKDRKVLRKFWDRKNlYTRDapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFdfsaKGGEEEQEDSEEKRKVDVVSKLHAILRPFLLRR 509
Cdd:cd18002   161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWF----SKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
281-509 1.22e-72

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: 237.25  E-value: 1.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLK-GKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLAcEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRKFMPKTTgpdFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLT 439
Cdd:cd18003    81 YYGSAKERKLKRQGWMKPNS---FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLT 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 440 GTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEQEDSEEKrkvdVVSKLHAILRPFLLRR 509
Cdd:cd18003   158 GTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
279-522 3.91e-71

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: 234.17  E-value: 3.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 279 GKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKG-KGLDGPYLIIAPLSTLSNWVNEISRFVPSMTG 357
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 358 LIYHGDKAARAE-IRRKFMPKttgpDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKL 436
Cdd:cd18064    94 VCLIGDKDQRAAfVRDVLLPG----EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEqedseekrkvdVVSKLHAILRPFLLRRMKEDVEH 516
Cdd:cd18064   170 LLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK-----------LVERLHMVLRPFLLRRIKADVEK 238

                  ....*.
gi 1002296320 517 MLPRKK 522
Cdd:cd18064   239 SLPPKK 244
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
263-511 5.28e-71

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: 234.17  E-value: 5.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 263 ERWEKEQArlvpLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTL 341
Cdd:cd18062    10 EKVEKQSS----LLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLmEHKRINGPFLIIVPLSTL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 342 SNWVNEISRFVPSMTGLIYHGDKAAraeiRRKFMPKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKC 421
Cdd:cd18062    86 SNWVYEFDKWAPSVVKVSYKGSPAA----RRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 422 LLLRELK-RLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFD--FSAKGgeeEQEDSEEKRKVDVVSKL 498
Cdd:cd18062   162 KLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapFAMTG---EKVDLNEEETILIIRRL 238
                         250
                  ....*....|...
gi 1002296320 499 HAILRPFLLRRMK 511
Cdd:cd18062   239 HKVLRPFLLRRLK 251
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
280-509 7.63e-71

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: 232.25  E-value: 7.63e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 280 KLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGL 358
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLfHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 359 IYHGDKAARAEIRR-KFMPKTTGP-DFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKL 436
Cdd:cd17993    81 VYLGDIKSRDTIREyEFYFSQTKKlKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGeeeqedseekrkvdvVSKLHAILRPFLLRR 509
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKG---------------IADLHKELEPFILRR 218
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
276-511 1.16e-69

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: 229.90  E-value: 1.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 276 MTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKG-KGLDGPYLIIAPLSTLSNWVNEISRFVPS 354
Cdd:cd18065    11 VKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 355 MTGLIYHGDKAARAE-IRRKFMPKttgpDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMD 433
Cdd:cd18065    91 LRAVCLIGDKDARAAfIRDVMMPG----EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 434 NKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEqedseekrkvdVVSKLHAILRPFLLRRMK 511
Cdd:cd18065   167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK-----------LVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
263-511 7.18e-69

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: 228.41  E-value: 7.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 263 ERWEKEQArlvpLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTL 341
Cdd:cd18063    10 ERVEKQSS----LLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLmEHKRLNGPYLIIVPLSTL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 342 SNWVNEISRFVPSMTGLIYHGDKAaraeIRRKFMPKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKC 421
Cdd:cd18063    86 SNWTYEFDKWAPSVVKISYKGTPA----MRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 422 LLLRELK-RLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFD--FSAKGgeeEQEDSEEKRKVDVVSKL 498
Cdd:cd18063   162 KLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapFAMTG---ERVDLNEEETILIIRRL 238
                         250
                  ....*....|...
gi 1002296320 499 HAILRPFLLRRMK 511
Cdd:cd18063   239 HKVLRPFLLRRLK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
279-511 4.43e-68

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: 224.75  E-value: 4.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 279 GKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGL 358
Cdd:cd18012     3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 359 IYHGDKAARAEIRRKfmpkttgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLL 438
Cdd:cd18012    83 VIHGTKRKREKLRAL-------EDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002296320 439 TGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKggeeeqedseEKRKVDVVSKLHAILRPFLLRRMK 511
Cdd:cd18012   156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIE----------KDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
281-462 1.85e-67

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: 222.26  E-value: 1.85e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIY 360
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGDKAARAEIRRKFMPKTTgpDFPLIVTSYEMAMS---DAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLL 437
Cdd:cd17998    81 YGSQEERKHLRYDILKGLE--DFDVIVTTYNLATSnpdDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                         170       180
                  ....*....|....*....|....*
gi 1002296320 438 LTGTPLQNNLAELWSLLNFILPDIF 462
Cdd:cd17998   159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
281-509 8.96e-66

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: 218.46  E-value: 8.96e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGK-GLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRKFMpktTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLT 439
Cdd:cd18006    81 YMGDKEKRLDLQQDIK---STNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLT 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 440 GTPLQNNLAELWSLLNFILPDIFSShqefESWFDFSAKggeeeqeDSEEKRKVDVVSKLHAILRPFLLRR 509
Cdd:cd18006   158 GTPIQNSLQELYALLSFIEPNVFPK----DKLDDFIKA-------YSETDDESETVEELHLLLQPFLLRR 216
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
274-509 1.39e-58

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: 199.85  E-value: 1.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 274 PLMTGGK---LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTLSNWVNEIS 349
Cdd:cd18054    11 PSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLfHQHQLYGPFLLVVPLSTLTSWQREFE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 350 RFVPSMTGLIYHGDKAARAEIRRK--FMPKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLREL 427
Cdd:cd18054    91 IWAPEINVVVYIGDLMSRNTIREYewIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 428 KRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDifsshqEFESWFDFSAKGGeeeqedseeKRKVDVVSKLHAILRPFLL 507
Cdd:cd18054   171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFEFWEDFEEDHG---------KGRENGYQSLHKVLEPFLL 235

                  ..
gi 1002296320 508 RR 509
Cdd:cd18054   236 RR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
604-729 6.52e-56

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: 188.45  E-value: 6.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 604 CGKFQLLNRLLSLLLARKHKVLIFSQWTKVLDIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDlNSSMNIFILSTRA 683
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002296320 684 GGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRPVHVYRL 729
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
281-509 6.84e-56

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: 191.81  E-value: 6.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVpSMTGLIY 360
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGDKAARAEIRR----------KFMPKTTgpDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRL 430
Cdd:cd18060    80 HGSLASRQMIQQyemyckdsrgRLIPGAY--KFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 431 PMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF-DFSAKggeeeqedseekrkvDVVSKLHAILRPFLLRR 509
Cdd:cd18060   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFgDLKTE---------------EQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
281-509 1.34e-55

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: 191.02  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEIsRFVPSMTGLIY 360
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREF-RTWTEMNAIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGDKAARAEIRRKFM--------PKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPM 432
Cdd:cd18058    80 HGSQISRQMIQQYEMyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMAL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 433 DNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEF-ESWFDFSAKggeeeqedseekrkvDVVSKLHAILRPFLLRR 509
Cdd:cd18058   160 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFlEEFGDLKTE---------------EQVKKLQSILKPMMLRR 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
281-509 2.75e-53

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: 183.79  E-value: 2.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKG-LDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKaaraeirrkfmpkttgpdfpLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLT 439
Cdd:cd17994    81 YVGDH--------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLT 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 440 GTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGgeeeqedseekrkvDVVSKLHAILRPFLLRR 509
Cdd:cd17994   141 GTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKE--------------DQIKKLHDLLGPHMLRR 196
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
281-509 8.59e-53

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: 183.31  E-value: 8.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEIsRFVPSMTGLIY 360
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREF-RTWTELNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGDKAARAEIR--RKFMPKTTGP------DFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPM 432
Cdd:cd18059    80 HGSQASRRTIQlyEMYFKDPQGRvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 433 DNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF-DFSAKggeeeqedseekrkvDVVSKLHAILRPFLLRR 509
Cdd:cd18059   160 EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFgDLKTE---------------EQVQKLQAILKPMMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
267-509 1.76e-51

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: 180.25  E-value: 1.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 267 KEQARLVPLMTGGKLKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHL-KGKGLDGPYLIIAPLSTLSNWV 345
Cdd:cd18053     7 KKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLfHEHQLYGPFLLVVPLSTLTSWQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 346 NEISRFVPSMTGLIYHGDKAARAEIR-RKFM-PKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLL 423
Cdd:cd18053    87 REIQTWAPQMNAVVYLGDINSRNMIRtHEWMhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 424 LRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPdifsshQEFESWFDFSAKGGeeeqedseeKRKVDVVSKLHAILR 503
Cdd:cd18053   167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP------EKFSSWEDFEEEHG---------KGREYGYASLHKELE 231

                  ....*.
gi 1002296320 504 PFLLRR 509
Cdd:cd18053   232 PFLLRR 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
281-509 5.29e-51

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 178.72  E-value: 5.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIY 360
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGdkAARAEIRRKFMPKTTGpdFPLIVTSYEMAMSDAKHLAHY-----KWKYVIVDEGHRLKNSKCLLLRELKRLPMDNK 435
Cdd:cd18001    81 HG--TSKKERERNLERIQRG--GGVLLTTYGMVLSNTEQLSADdhdefKWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002296320 436 LLLTGTPLQNNLAELWSLLNFILP-DIFSSHQEFESWFDFSAKGGEEEQEDSEEKRKVDVVSK-LHAILRPFLLRR 509
Cdd:cd18001   157 IILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAEnLRQIIKPYFLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
284-459 1.16e-48

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: 170.58  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 284 YQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKG-KGLDGPYLIIAPLSTLSNWVNEISRFVPSMTGLIYH- 361
Cdd:cd18000     4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHsKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVLHs 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 362 -------GDKAARAEIRRKFMPKTTgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDN 434
Cdd:cd18000    84 sgsgtgsEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
                         170       180
                  ....*....|....*....|....*
gi 1002296320 435 KLLLTGTPLQNNLAELWSLLNFILP 459
Cdd:cd18000   163 RLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
281-509 1.32e-47

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: 169.04  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKG-LDGPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIR---------------RKFMPKTTGP-DFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLL 423
Cdd:cd18055    81 YTGDKDSRAIIRenefsfddnavkggkKAFKMKREAQvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 424 LRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEF-ESWFDFSakggeeeqedseekrKVDVVSKLHAIL 502
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADIS---------------KEDQIKKLHDLL 225

                  ....*..
gi 1002296320 503 RPFLLRR 509
Cdd:cd18055   226 GPHMLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
281-509 7.00e-47

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: 167.14  E-value: 7.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLA--HLKGKGLDG----PYLIIAPLSTLSNWVNEISRFVP- 353
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdHHKRANSFNsenlPSLVVCPPTLVGHWVAEIKKYFPn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 354 -SMTGLIYHGDKAARAEIRRKFmpkttgPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPM 432
Cdd:cd17999    81 aFLKPLAYVGPPQERRRLREQG------EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 433 DNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF----------DFSAKggeeeqedsEEKRKVDVVSKLHAIL 502
Cdd:cd17999   155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrdsKASAK---------EQEAGALALEALHKQV 225

                  ....*..
gi 1002296320 503 RPFLLRR 509
Cdd:cd17999   226 LPFLLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
281-509 8.38e-47

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: 166.33  E-value: 8.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEIsRFVPSMTGLIY 360
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 HGDKAARAEIRR--KFMPKTTGP------DFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPM 432
Cdd:cd18061    80 HGSLISRQMIQQyeMYFRDSQGRiirgayRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320 433 DNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF-DFSAKggeeeqedseekrkvDVVSKLHAILRPFLLRR 509
Cdd:cd18061   160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFgDLKTE---------------EQVQKLQAILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
281-509 1.05e-46

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: 166.78  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLD-GPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSkGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRK----------------FMPKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLL 423
Cdd:cd18057    81 YTGDKESRSVIRENefsfednairsgkkvfRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 424 LRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEF-ESWFDFSakggeeeqedseekrKVDVVSKLHAIL 502
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADIS---------------KEDQIKKLHDLL 225

                  ....*..
gi 1002296320 503 RPFLLRR 509
Cdd:cd18057   226 GPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
281-509 9.38e-45

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 161.00  E-value: 9.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLD-GPYLIIAPLSTLSNWVNEISRFVPSMTGLI 359
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSkGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YHGDKAARAEIRRK----------------FMPKTTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLL 423
Cdd:cd18056    81 YVGDKDSRAIIRENefsfednairggkkasRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 424 LRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEF-ESWFDFSakggeeeqedseekrKVDVVSKLHAIL 502
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFlEEFADIA---------------KEDQIKKLHDML 225

                  ....*..
gi 1002296320 503 RPFLLRR 509
Cdd:cd18056   226 GPHMLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
281-509 9.23e-44

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: 158.60  E-value: 9.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISlwqNGlnGILADQMGLGKTIQTIGFLAHLKGKGLDGPY------------------LIIAPLSTLS 342
Cdd:cd18008     1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALILATRPQDPKIPEeleenssdpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 343 NWVNEISRFV--PSMTGLIYHGDKaaraeiRRKFMPKTTGPDfpLIVTSY-EMAMSDAKH---------------LAHYK 404
Cdd:cd18008    76 QWKDEIEKHTkpGSLKVYVYHGSK------RIKSIEELSDYD--IVITTYgTLASEFPKNkkgggrdskekeaspLHRIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 405 WKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEQe 484
Cdd:cd18008   148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKA- 226
                         250       260
                  ....*....|....*....|....*
gi 1002296320 485 dseekrkvdvVSKLHAILRPFLLRR 509
Cdd:cd18008   227 ----------LERLQALLKPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
281-509 3.86e-42

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 154.07  E-value: 3.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGKGLDG---------------------PYLIIAPLS 339
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakkPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 340 TLSNWVNEISRFvPSMTGLIYHGDK-----AARAEIRRkfmpkttgpdFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGH 414
Cdd:cd18005    81 VLYNWKDELDTW-GHFEVGVYHGSRkddelEGRLKAGR----------LEVVVTTYDTLRRCIDSLNSINWSAVIADEAH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 415 RLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEQEDSEEKRKVD- 493
Cdd:cd18005   150 RIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRk 229
                         250
                  ....*....|....*.
gi 1002296320 494 VVSKLHAILRPFLLRR 509
Cdd:cd18005   230 RKQELAVKLSKFFLRR 245
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
281-509 1.57e-38

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: 143.58  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLIS--LWQNGLNG---ILADQMGLGKTIQTIGFL-AHLKGKGLDGP----YLIIAPLSTLSNWVNEISR 350
Cdd:cd18004     1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVwTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 351 FVPSMTGLIYHGDKAARAEIRRKfMPKTTGPDFPLIVTSYEMAMSDAKHLAHYK-WKYVIVDEGHRLKNSKCLLLRELKR 429
Cdd:cd18004    81 WLGLRRIKVVTADGNAKDVKASL-DFFSSASTYPVLIISYETLRRHAEKLSKKIsIDLLICDEGHRLKNSESKTTKALNS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 430 LPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGGEEEQEDSEEKRKVDVVSK-LHAILRPFLLR 508
Cdd:cd18004   160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQeLSELTSRFILR 239

                  .
gi 1002296320 509 R 509
Cdd:cd18004   240 R 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
281-472 1.07e-35

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: 135.50  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLislWQNgLNG-----------ILADQMGLGKTIQTIGFL-AHLKGKGLDGPYLIIAPLSTLSNWVNEI 348
Cdd:cd18007     1 LKPHQVEGVRFL---WSN-LVGtdvgsdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPASTLYNWEDEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 349 SRFVPSMTgLIYHGDKAARAEIRRKFMPKT-----TGPDFPLIvtSYEM-------AMSDAK-HLAHYKW------KYVI 409
Cdd:cd18007    77 KKWLPPDL-RPLLVLVSLSASKRADARLRKinkwhKEGGVLLI--GYELfrnlasnATTDPRlKQEFIAAlldpgpDLLV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002296320 410 VDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF 472
Cdd:cd18007   154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
281-468 1.46e-32

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: 125.40  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISlwQNGlNGILADQMGLGKTIQTIGFLAHLKGkglDGPYLIIAPLSTLSNWVNEISRFVPSMTgliy 360
Cdd:cd18010     1 LLPFQREGVCFALR--RGG-RVLIADEMGLGKTVQAIAIAAYYRE---EWPLLIVCPSSLRLTWADEIERWLPSLP---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 361 hgdkaaRAEIRRKFMPKTTGPDF-PLIV-TSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNK--L 436
Cdd:cd18010    71 ------PDDIQVIVKSKDGLRDGdAKVViVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKrvI 144
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1002296320 437 LLTGTPLQNNLAELWSLLNFILPDIFSSHQEF 468
Cdd:cd18010   145 LLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXDc smart00487
DEAD-like helicases superfamily;
273-465 1.22e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 119.52  E-value: 1.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  273 VPLMTGGKLKSYQIKGVKWLISLWQNGlngILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTL-SNWVNEISRF 351
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  352 VPSMTG---LIYHGDKaaraeiRRKFMPKTTGPDFPLIVTSYEMAMSDAKH--LAHYKWKYVIVDEGHRLKNS--KCLLL 424
Cdd:smart00487  78 GPSLGLkvvGLYGGDS------KREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGgfGDQLE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1002296320  425 RELKRLPMDNK-LLLTGTP---LQNNLAELWSLLNFILPDIFSSH 465
Cdd:smart00487 152 KLLKLLPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
281-509 7.85e-29

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


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 115.64  E-value: 7.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWL----ISLWQNGLNG-ILADQMGLGKTIQTIGFLAHLKGKGLDGPYLI-----IAPLSTLSNWVNEISR 350
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 351 FV-PSMTGLIYHGDKAARAEIRRKFMPKTTGPDF--PLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLREL 427
Cdd:cd18067    81 WLgGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVstPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 428 KRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSA-KGGEEEQEDSEEKRKVDVVSKLHAILRPFL 506
Cdd:cd18067   161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlKGRDADASEKERQLGEEKLQELISIVNRCI 240

                  ...
gi 1002296320 507 LRR 509
Cdd:cd18067   241 IRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
619-719 7.76e-28

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: 108.07  E-value: 7.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 619 ARKHKVLIFSQWTKVLDIiEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDLNSsmnIFILSTRAGGLGINLTSADTCIL 698
Cdd:pfam00271  13 ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKI---DVLVATDVAERGLDLPDVDLVIN 88
                          90       100
                  ....*....|....*....|.
gi 1002296320 699 YDSDWNPQMDLQAMDRCHRIG 719
Cdd:pfam00271  89 YDLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
281-479 4.14e-26

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: 107.21  E-value: 4.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLislWQN------------GLNGILADQMGLGKTIQTIGF----LAHLKGKGLdgpyLIIAPLSTLSNW 344
Cdd:cd18069     1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFldvlLRHTGAKTV----LAIVPVNTLQNW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 345 VNEISRFVPSMTGLIYH----------GDKAARAEIRRKFMPKTTGpDFPLIVTSYEMamsdakhlahYKWK----YVIV 410
Cdd:cd18069    74 LSEFNKWLPPPEALPNVrprpfkvfilNDEHKTTAARAKVIEDWVK-DGGVLLMGYEM----------FRLRpgpdVVIC 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296320 411 DEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAKGG 479
Cdd:cd18069   143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNG 211
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
297-470 8.76e-25

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: 104.09  E-value: 8.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 297 QNGLNGILADQMGLGKTIQTIGFLahlkgkgLDGPYLIIAPLSTLSNWVNEISRFVPS--MTGLIYHGdkAARAEIRRKF 374
Cdd:cd18071    46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHG--GERNRDPKLL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 375 MPKTtgpdfpLIVTSY-----EMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAE 449
Cdd:cd18071   117 SKYD------IVLTTYntlasDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKD 190
                         170       180
                  ....*....|....*....|.
gi 1002296320 450 LWSLLNFILPDIFSSHQEFES 470
Cdd:cd18071   191 LGSLLSFLHLKPFSNPEYWRR 211
HELICc smart00490
helicase superfamily c-terminal domain;
635-719 1.93e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.89  E-value: 1.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  635 DIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDlnsSMNIFILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDR 714
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 1002296320  715 CHRIG 719
Cdd:smart00490  78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
281-472 4.33e-22

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: 96.11  E-value: 4.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWL---------ISLWQNGLNGILADQMGLGKTIQTIGF----LAHLKGKGLDgPYLIIAPLSTLSNWVNE 347
Cdd:cd18068     1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFlhtvLLCEKLENFS-RVLVVCPLNTVLNWLNE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 348 ISRFvpsMTGL-------IYHGDKAARAEIRRkFMPKTTGPDFPLIVTSYEM----AMSDAKHLAHyKWK---------- 406
Cdd:cd18068    80 FEKW---QEGLkdeekieVNELATYKRPQERS-YKLQRWQEEGGVMIIGYDMyrilAQERNVKSRE-KLKeifnkalvdp 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296320 407 ---YVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWF 472
Cdd:cd18068   155 gpdFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
281-473 4.80e-22

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 95.68  E-value: 4.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWL----ISLWQNGLNG-ILADQMGLGKTIQTIGFLAHLKGKGLDGP------YLIIAPLSTLSNWVNEIS 349
Cdd:cd18066     1 LRPHQREGIEFLyecvMGMRVNERFGaILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 350 RFVPSMTGLIYHGDKAARAEirrKFMpktTGPDFPLIVTSYEMAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKR 429
Cdd:cd18066    81 KWLGSERIKVFTVDQDHKVE---EFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1002296320 430 LPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFD 473
Cdd:cd18066   155 LSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYE 198
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
281-509 2.83e-21

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 93.70  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLisLW---QNGLNGILADQMGLGKTIQTIGFL----------AHLKGKGLD-------------GPYLI 334
Cdd:cd18072     1 LLLHQKQALAWL--LWrerQKPRGGILADDMGLGKTLTMIALIlaqkntqnrkEEEKEKALTeweskkdstlvpsAGTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 335 IAPLSTLSNWVNEISRFVPS--MTGLIYHGdkAARAEIRRKFMpkttgpDFPLIVTSYEMAMSDAKH---------LAHY 403
Cdd:cd18072    79 VCPASLVHQWKNEVESRVASnkLRVCLYHG--PNRERIGEVLR------DYDIVITTYSLVAKEIPTykeesrsspLFRI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 404 KWKYVIVDEGHRLKNSK------CLLLRELKRLpmdnklLLTGTPLQNNLAELWSLLNFILPDIFSSHQEFESWFDFSAK 477
Cdd:cd18072   151 AWARIILDEAHNIKNPKvqasiaVCKLRAHARW------ALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSR 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1002296320 478 GGEEeqedseekrkvdvvsKLHAILRPFLLRR 509
Cdd:cd18072   225 KGGE---------------RLNILTKSLLLRR 241
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
284-463 9.45e-20

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: 88.50  E-value: 9.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 284 YQIKGVKWLISLWQNGLngILADQMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWVNEISRF----VPSMTGLI 359
Cdd:cd18011     4 HQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKfglpFLILDRET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 360 YhgdKAARAEIRRKFMPkttgpdFPLIVTSYEMAMSDAKHLAHYK---WKYVIVDEGHRLKNSKCL-------LLRELKR 429
Cdd:cd18011    82 A---AQLRRLIGNPFEE------FPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRNSGGGketkrykLGRLLAK 152
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1002296320 430 LpMDNKLLLTGTPLQNNLAELWSLLNFILPDIFS 463
Cdd:cd18011   153 R-ARHVLLLTATPHNGKEEDFRALLSLLDPGRFA 185
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
281-463 6.14e-15

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 75.46  E-value: 6.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISLwqnglNGILADQMGLGKTIQTIGF-LAHLKGKGLD-------------------------GPYLI 334
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALiLLHPRPDNDLdaadddsdemvccpdclvaetpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 335 IAPLSTLSNWVNEISRFVP-SMTGLIYHGDKAARAeirrkfmPKTTGPDF----PLIVTSY-----EMAMSDAKH----- 399
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKDGA-------LASPAPEIlaeyDIVVTTYdvlrtELHYAEANRsnrrr 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002296320 400 ------------LAHYKWKYVIVDEGHRLKNSKCLLLRELKRLPMDNKLLLTGTPLQNNLAELWSLLNFILPDIFS 463
Cdd:cd18070   149 rrqkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
303-729 1.56e-14

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: 77.80  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 303 ILADQMGLGKTIQT---IGFLAHLKGKGLdgpyLIIAPLSTLSNWVNEI-SRFvpSMTGLIYhgDKAARAEIRRKFMPKT 378
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELeEKF--DLESLIL--DSLTVEKDAKKWNKRL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 379 TGPDFPLIV-TSYEMAMSDAKHLAHYKWKYVIVDEGHRLKN-----SKCLLLREL-KRLPmdnKLLLTGTPLQNNLAELW 451
Cdd:NF038318  123 TDNKKVRIViTSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhkggKRAKNLYELtKGIP---KILLTATPLQNSLLDLY 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 452 SLLNFILPDIFSSHQEFESWF----DFSAkggeeeqedseekrkvdvvskLHAILRPFLLRRMKEDV-EHM-LPRKKEI- 524
Cdd:NF038318  200 GLVSFIDPRIFGSEKVFSKRYikdeDYSD---------------------LKRELSPVLYRTLRKDVaDYMqFKKRKCIt 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 525 -----------------------IIYANMTDHQ-------------------------KQIQNHLVEQT----------- 545
Cdd:NF038318  259 vdfelspdeielyvrvnnflkrdILYSIPTSNRtliilvirkllasssfalaetfevlKKRLEKLKEGTrsanaqegfdl 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 546 ----FDQYLHEKSE-------IVLRKPGIKAKLN------NLLIQLRKNCNhpdllesaydSSGLYPPVEKLLEqcgkFQ 608
Cdd:NF038318  339 fwsfVEDEIDESGFeekqdelYTRQKEFIQHEIDevdaiiDVAKRIKTNAK----------VTALKTALEIAFE----YQ 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 609 LLNRLlslllarKHKVLIFSQWTKVLDIIEYYLETKGLQVCRI--------DGSVKLEERRRQIAEFNDLNSSMNI---- 676
Cdd:NF038318  405 REEGI-------AQKVVVFTESKRTQKYIAEELRKSGYEGEDIllfngdfdDAMTKEIYRAWQVKNYGKANYGRSVeykh 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002296320 677 -----------FILSTRAGGLGINLTSADTCILYDSDWNPQMDLQAMDRCHRIGQTRPVHVYRL 729
Cdd:NF038318  478 aivdyfknnakILIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINL 541
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
281-473 1.72e-13

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: 70.46  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGVKWLISlwqNGLNGILADqMGLGKTIQTIGFLAHLKGKGLDGPYLIIAPLSTLSN-WVNEISRF--VPSMTG 357
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWnhLRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 358 LIYHGDKAAraeiRRKFMpkTTGPDfpLIVTSYE-MAMSDAKHLAHYKWKYVIVDEGHRLKNSKCLLLRELKRL-PMDNK 435
Cdd:cd18013    77 SVAVGTERQ----RSKAA--NTPAD--LYVINREnLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1002296320 436 LL-LTGTPLQNNLAELWSLLNFI-----LPDIFSSHQefESWFD 473
Cdd:cd18013   149 LIgLTGTPSPNGLMDLWAQIALLdqgerLGRSITAYR--ERWFD 190
ResIII pfam04851
Type III restriction enzyme, res subunit;
280-442 7.89e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 55.37  E-value: 7.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 280 KLKSYQIKGVKWLISLWQNGLNGILAdQM--GLGKTIQTIGFLAHLKGKGLDGPYLIIAP-LSTLSNWVNEISRFVPSMT 356
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNGQKRGLI-VMatGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 357 --GLIYHGDKAaraeirrkfmpKTTGPDFPLIVTSYEMAMSDAK----HLAHYKWKYVIVDEGHRL----------KNSK 420
Cdd:pfam04851  82 eiGEIISGDKK-----------DESVDDNKIVVTTIQSLYKALElaslELLPDFFDVIIIDEAHRSgassyrnileYFKP 150
                         170       180
                  ....*....|....*....|..
gi 1002296320 421 CLLLRelkrlpmdnkllLTGTP 442
Cdd:pfam04851 151 AFLLG------------LTATP 160
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
301-441 1.28e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.55  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 301 NGILADQMGLGKTIQ-TIGFLAHLKGKGldGPYLIIAPLSTLSNWVNEI--SRFVPSMTGLIYHGDKaaRAEIRRKFmpk 377
Cdd:cd00046     3 NVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALQTAERlrELFGPGIRVAVLVGGS--SAEEREKN--- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002296320 378 tTGPDFPLIVTSYEMAMSDAKHLAHY---KWKYVIVDEGHR-LKNSK---CLLLRELKRLPMDNK-LLLTGT 441
Cdd:cd00046    76 -KLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHAlLIDSRgalILDLAVRKAGLKNAQvILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
250-442 1.02e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 49.25  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 250 EDCSPEDCTLTEEERWEKE--QARLVPLMTGGKLKSYQIKGV-KWLISLWQNGLNGILADQMGLGKTIQTIGFLAHLKGK 326
Cdd:COG1061    48 EDGRRLPEEDTERELAEAEalEAGDEASGTSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 327 GldgPYLIIAPLSTLSN-WVNEISRFVPSmtGLIYHGDKAaraeirrkfmpkttgPDFPLIVTSYEMAMSDA--KHLAHY 403
Cdd:COG1061   128 K---RVLVLVPRRELLEqWAEELRRFLGD--PLAGGGKKD---------------SDAPITVATYQSLARRAhlDELGDR 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002296320 404 kWKYVIVDEGHRLKNSKcllLRE-LKRLPMDNKLLLTGTP 442
Cdd:COG1061   188 -FGLVIIDEAHHAGAPS---YRRiLEAFPAAYRLGLTATP 223
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
530-736 8.09e-05

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: 45.40  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 530 MTDHQKQIQNHLVE---QTFDQYL---HEKSEIVLRKpgikaKLNNLLIQLRKNCNHPDLLESAY--DSSGLYPPVEKLL 601
Cdd:pfam11496  12 MTSYQKELTEQIVSlhySDILKYCetsDSKEDISLIK-----SMTLCLENLSLVATHPYLLVDHYmpKSLLLKDEPEKLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 602 EQCGKFQLLNRLLSLLLARKHK----VLIFSQWTKVLDIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDLNSSMNIF 677
Cdd:pfam11496  87 YTSGKFLVLNDLVNLLIERDRKepinVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSDSGNKKIHSTTCH 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002296320 678 ILS-----TRAGGLGINlTSADTCILYDSDWNP-QMDLQAMDRCHRIGQTRPVhVYRLATSHSVE 736
Cdd:pfam11496 167 LLSstgqlTNDDSLLEN-YKFDLIIAFDSSVDTsSPSVEHLRTQNRRKGNLAP-IIRLVVINSIE 229
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
281-442 3.23e-04

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 41.91  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 281 LKSYQIKGV-KWLISlwQNGLNGILADQMGLGKTIQTIGFLAHLKgkglDGPYLIIAP-LSTLSNWVNEISRFVP-SMTG 357
Cdd:cd17926     1 LRPYQEEALeAWLAH--KNNRRGILVLPTGSGKTLTALALIAYLK----ELRTLIVVPtDALLDQWKERFEDFLGdSSIG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 358 LIYHGDKAARaeirrkfmpkttgPDFPLIVTSYEMAMSDAKHLAHYK--WKYVIVDEGHRL---KNSKClllreLKRLPM 432
Cdd:cd17926    75 LIGGGKKKDF-------------DDANVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHLpakTFSEI-----LKELNA 136
                         170
                  ....*....|
gi 1002296320 433 DNKLLLTGTP 442
Cdd:cd17926   137 KYRLGLTATP 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
309-442 1.13e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 309 GLGKT-IQTIGFLAHLKGKGLDGPYLIIAPLSTLSNWV----NEISRFVPSMTGLIYHGDKaaRAEIRRKFmpktTGPDf 383
Cdd:pfam00270  24 GSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEQIyeelKKLGKGLGLKVASLLGGDS--RKEQLEKL----KGPD- 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002296320 384 pLIVTSYEMAMSDAKHLAHYK-WKYVIVDEGHRL--KNSKCLLLRELKRLPMDNK-LLLTGTP 442
Cdd:pfam00270  97 -ILVGTPGRLLDLLQERKLLKnLKLLVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATL 158
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
299-444 1.82e-03

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.87  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 299 GLNGILADQMGLGKTIQT-IGFLAHLKGKGLDGPYLI-IAPLSTLSN--------WVNEISrfvPSMTGLIYHGDKAARa 368
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAfLPALSSLADEPEKGVQVLyISPLKALINdqerrleePLDEID---LEIPVAVRHGDTSQS- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 369 eIRRKFMPKTtgPDFpLIVT--SYEMAMSDAKH---LAHYKwkYVIVDEGHRLKNSK--CLLLRELKRLpmdnkLLLTGT 441
Cdd:cd17922    77 -EKAKQLKNP--PGI-LITTpeSLELLLVNKKLrelFAGLR--YVVVDEIHALLGSKrgVQLELLLERL-----RKLTGR 145

                  ...
gi 1002296320 442 PLQ 444
Cdd:cd17922   146 PLR 148
PTZ00121 PTZ00121
MAEBL; Provisional
135-271 2.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  135 DAMKEEEEKLHDARVKAEEEEvaRKREEAARLAFDPNARfnKLDELLSQTqlysefllEKMETIADVEGVQTHAEEEPVE 214
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEE--KKKVEQLKKKEAEEKK--KAEELKKAE--------EENKIKAAEEAKKAEEDKKKAE 1678
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002296320  215 EKKNGRGRKRKATSAPKYNDKKAKKAVAVMLTRSHEDCSPEDCTLTEEERWEK-EQAR 271
Cdd:PTZ00121  1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaEEAK 1736
SF2_C_suv3 cd18805
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ...
624-690 4.60e-03

C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 is a DEAD-like helicase 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: 350192 [Multi-domain]  Cd Length: 135  Bit Score: 38.31  E-value: 4.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002296320 624 VLIFSQWtKVLDIIEYYLETKGLQVCRIDGSVKLEERRRQIAEFNDLNSSMNIfILSTRAGGLGINL 690
Cdd:cd18805    22 VVAFSRK-DIFSLKREIEKRTGLKCAVIYGALPPETRRQQARLFNDPESGYDV-LVASDAIGMGLNL 86
PTZ00121 PTZ00121
MAEBL; Provisional
138-240 5.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320  138 KEEEEKLHDARVKAEEEEVARKREEAARLAFDPNARFNKLDELLSQTQLYSEFLLEKMETIADVEGVQTHAEEE--PVEE 215
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkKAEE 1720
                           90       100
                   ....*....|....*....|....*.
gi 1002296320  216 -KKNGRGRKRKATSAPKYNDKKAKKA 240
Cdd:PTZ00121  1721 lKKAEEENKIKAEEAKKEAEEDKKKA 1746
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
139-197 6.60e-03

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 37.52  E-value: 6.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296320 139 EEEEKlhDARVKAE-EEEVARKREEAARLAfDPNARfnKLDELLSQTQLYSEFLLEKMET 197
Cdd:pfam13892  79 EKEER--ELRKRAEkEALEQAKKEEELREA-KRQQR--KLNFLITQTELYSHFMGKKLKT 133
 
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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