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Conserved domains on  [gi|157817975|ref|NP_001100889|]
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 [Rattus norvegicus]

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
12-955 0e+00

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: 1215.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   12 KQKEIQEPDPTYEEKMQTDRANRFE----YLLKQTELFAHFiqpaAQKTPTSPLKMKPGRprvkkdekqnllsvGDYRHR 87
Cdd:PLN03142   72 KKQEIQKILEQQNAAIDADMNNKGKgrlkYLLQQTEIFAHF----AKGDQSASAKKAKGR--------------GRHASK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   88 RTEQEEDEELLTESSKATNVC--TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYM 165
Cdd:PLN03142  134 LTEEEEDEEYLKEEEDGLGGSggTRLLVQPSCIK-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  166 KHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNW 245
Cdd:PLN03142  213 HEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSW 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  246 RYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVE 325
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQ 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  326 RLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGkmDKMRLLNILMQLRKCCNHPYL 405
Cdd:PLN03142  373 QLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYL 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  406 FDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSI 485
Cdd:PLN03142  451 FQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASI 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  486 NAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAE 565
Cdd:PLN03142  531 DAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAY 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  566 MKLRLDSIVIQQGRLVDQnlNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRn 645
Cdd:PLN03142  611 KKLALDALVIQQGRLAEQ--KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK- 687
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  646 FTMDTESSVYNFEGEDYREKQKIAF-----TEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFF 720
Cdd:PLN03142  688 FKMDDTAELYDFDDEDDKDENKLDFkkivsDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFF 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  721 -PPRLFELLEKEILYYRKTigykvprspDLPNAAQAQKEEQLKIDEAGPLNDEELEEKEKLLTQGFTNWNKRDFNQFIKA 799
Cdd:PLN03142  768 nVQRLTELYEKEVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRA 838
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  800 NEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLR 879
Cdd:PLN03142  839 CEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELK 918
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975  880 ISYGTNKGKNYTEEEDRFLICMLHKLGFDKenvYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIEREN 955
Cdd:PLN03142  919 IQYGQNKGKLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKEN 991
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
12-955 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1215.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   12 KQKEIQEPDPTYEEKMQTDRANRFE----YLLKQTELFAHFiqpaAQKTPTSPLKMKPGRprvkkdekqnllsvGDYRHR 87
Cdd:PLN03142   72 KKQEIQKILEQQNAAIDADMNNKGKgrlkYLLQQTEIFAHF----AKGDQSASAKKAKGR--------------GRHASK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   88 RTEQEEDEELLTESSKATNVC--TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYM 165
Cdd:PLN03142  134 LTEEEEDEEYLKEEEDGLGGSggTRLLVQPSCIK-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  166 KHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNW 245
Cdd:PLN03142  213 HEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSW 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  246 RYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVE 325
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQ 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  326 RLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGkmDKMRLLNILMQLRKCCNHPYL 405
Cdd:PLN03142  373 QLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYL 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  406 FDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSI 485
Cdd:PLN03142  451 FQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASI 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  486 NAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAE 565
Cdd:PLN03142  531 DAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAY 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  566 MKLRLDSIVIQQGRLVDQnlNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRn 645
Cdd:PLN03142  611 KKLALDALVIQQGRLAEQ--KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK- 687
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  646 FTMDTESSVYNFEGEDYREKQKIAF-----TEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFF 720
Cdd:PLN03142  688 FKMDDTAELYDFDDEDDKDENKLDFkkivsDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFF 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  721 -PPRLFELLEKEILYYRKTigykvprspDLPNAAQAQKEEQLKIDEAGPLNDEELEEKEKLLTQGFTNWNKRDFNQFIKA 799
Cdd:PLN03142  768 nVQRLTELYEKEVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRA 838
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  800 NEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLR 879
Cdd:PLN03142  839 CEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELK 918
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975  880 ISYGTNKGKNYTEEEDRFLICMLHKLGFDKenvYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIEREN 955
Cdd:PLN03142  919 IQYGQNKGKLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKEN 991
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
108-351 5.59e-174

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: 506.51  E-value: 5.59e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 108 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 187
Cdd:cd18064    1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 188 MSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 267
Cdd:cd18064   81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 268 REFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 347
Cdd:cd18064  161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                 ....
gi 157817975 348 PPKK 351
Cdd:cd18064  241 PPKK 244
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
85-574 1.36e-150

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 462.77  E-value: 1.36e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  85 RHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGY 164
Cdd:COG0553  205 LELLLELELLAEAAVDAFRLRRLREALESLPAGLK-ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLE 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 165 MKHyRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEqRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFN 244
Cdd:COG0553  284 LKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVD 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 245 WRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLV 324
Cdd:COG0553  359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 325 ERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMK-DIDILNSAGKMDKMRLLNILMQLRKCCNHP 403
Cdd:COG0553  439 ERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHP 518
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 404 YLFDGAEPgppyttdmHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQD 483
Cdd:COG0553  519 ALLLEEGA--------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 484 SINAYNEPNSTKfVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVER 563
Cdd:COG0553  591 LVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILEL 669
                        490
                 ....*....|..
gi 157817975 564 AEMKLRL-DSIV 574
Cdd:COG0553  670 LEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-406 2.95e-136

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: 410.54  E-value: 2.95e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  126 YQVRGLNWLISLYEN-GINGILADEMGLGKTLQTISLLGYMKHYRNIPG-PHMVLVPKSTLHNWMSEFKRWV--PTLRSV 201
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  202 CLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGT 281
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  282 PLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQ-KLVERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLS 360
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 157817975  361 KMQREWYTR-ILMKDIDILNSAGKMDK--MRLLNILMQLRKCCNHPYLF 406
Cdd:pfam00176 241 KLQRKLYQTfLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
119-300 7.26e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.67  E-value: 7.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   119 KWGKLRDYQVRGLNWLISLYENGIngiLADEMGLGKTLQ-TISLLGYMKhyRNIPGPHMVLVP-KSTLHNWMSEFKRWVP 196
Cdd:smart00487   5 GFEPLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   197 --TLRSVCLIGDKEQRAafVRDVLLPGEWDVCVTSYEMLIK--EKSVFKKFNWRYLVIDEAHRIKNE--KSKLSEIVREF 270
Cdd:smart00487  80 slGLKVVGLYGGDSKRE--QLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....
gi 157817975   271 -KTTNRLLLTGTP---LQNNLHELWSLLNFLLPD 300
Cdd:smart00487 158 pKNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
12-955 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1215.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   12 KQKEIQEPDPTYEEKMQTDRANRFE----YLLKQTELFAHFiqpaAQKTPTSPLKMKPGRprvkkdekqnllsvGDYRHR 87
Cdd:PLN03142   72 KKQEIQKILEQQNAAIDADMNNKGKgrlkYLLQQTEIFAHF----AKGDQSASAKKAKGR--------------GRHASK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   88 RTEQEEDEELLTESSKATNVC--TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYM 165
Cdd:PLN03142  134 LTEEEEDEEYLKEEEDGLGGSggTRLLVQPSCIK-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  166 KHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNW 245
Cdd:PLN03142  213 HEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSW 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  246 RYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVE 325
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQ 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  326 RLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMKDIDILNSAGkmDKMRLLNILMQLRKCCNHPYL 405
Cdd:PLN03142  373 QLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYL 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  406 FDGAEPGPPYTTDMHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSI 485
Cdd:PLN03142  451 FQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASI 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  486 NAYNEPNSTKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVERAE 565
Cdd:PLN03142  531 DAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAY 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  566 MKLRLDSIVIQQGRLVDQnlNKIGKDEMLQMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRn 645
Cdd:PLN03142  611 KKLALDALVIQQGRLAEQ--KTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK- 687
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  646 FTMDTESSVYNFEGEDYREKQKIAF-----TEWIEPPKRERKANYAVDAYFREALRVSEPKAPKAPRPPKQPNVQDFQFF 720
Cdd:PLN03142  688 FKMDDTAELYDFDDEDDKDENKLDFkkivsDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFF 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  721 -PPRLFELLEKEILYYRKTigykvprspDLPNAAQAQKEEQLKIDEAGPLNDEELEEKEKLLTQGFTNWNKRDFNQFIKA 799
Cdd:PLN03142  768 nVQRLTELYEKEVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRA 838
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  800 NEKWGRDDIENIAREVEGKTPEEVIEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLR 879
Cdd:PLN03142  839 CEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELK 918
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975  880 ISYGTNKGKNYTEEEDRFLICMLHKLGFDKenvYDELRQCIRNSPQFRFDWFLKSRTAMELQRRCNTLITLIEREN 955
Cdd:PLN03142  919 IQYGQNKGKLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKEN 991
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
108-351 5.59e-174

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: 506.51  E-value: 5.59e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 108 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 187
Cdd:cd18064    1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 188 MSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 267
Cdd:cd18064   81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 268 REFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 347
Cdd:cd18064  161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                 ....
gi 157817975 348 PPKK 351
Cdd:cd18064  241 PPKK 244
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
120-340 1.17e-159

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: 468.34  E-value: 1.17e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 120 WGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLR 199
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 200 SVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLT 279
Cdd:cd17997   81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817975 280 GTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGD-QKLVERLHMVLRPFLLRRIK 340
Cdd:cd17997  161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnQEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
108-340 1.37e-153

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: 453.32  E-value: 1.37e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 108 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 187
Cdd:cd18065    1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 188 MSEFKRWVPTLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 267
Cdd:cd18065   81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817975 268 REFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIK 340
Cdd:cd18065  161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
85-574 1.36e-150

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 462.77  E-value: 1.36e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  85 RHRRTEQEEDEELLTESSKATNVCTRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGY 164
Cdd:COG0553  205 LELLLELELLAEAAVDAFRLRRLREALESLPAGLK-ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLE 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 165 MKHyRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVCLIGDKEqRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFN 244
Cdd:COG0553  284 LKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVD 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 245 WRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQKLV 324
Cdd:COG0553  359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 325 ERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLSKMQREWYTRILMK-DIDILNSAGKMDKMRLLNILMQLRKCCNHP 403
Cdd:COG0553  439 ERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHP 518
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 404 YLFDGAEPgppyttdmHLVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQD 483
Cdd:COG0553  519 ALLLEEGA--------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 484 SINAYNEPNSTKfVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFITDNTVEERIVER 563
Cdd:COG0553  591 LVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILEL 669
                        490
                 ....*....|..
gi 157817975 564 AEMKLRL-DSIV 574
Cdd:COG0553  670 LEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-406 2.95e-136

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: 410.54  E-value: 2.95e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  126 YQVRGLNWLISLYEN-GINGILADEMGLGKTLQTISLLGYMKHYRNIPG-PHMVLVPKSTLHNWMSEFKRWV--PTLRSV 201
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  202 CLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGT 281
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  282 PLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQ-KLVERLHMVLRPFLLRRIKADVEKSLPPKKEVKIYVGLS 360
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 157817975  361 KMQREWYTR-ILMKDIDILNSAGKMDK--MRLLNILMQLRKCCNHPYLF 406
Cdd:pfam00176 241 KLQRKLYQTfLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
121-340 2.56e-94

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: 298.13  E-value: 2.56e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 121 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRS 200
Cdd:cd17996    2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLIGDKEQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV-REFKTTNRLLLT 279
Cdd:cd17996   82 IVYKGTPDVRKKLQSQ-IRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817975 280 GTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDT---------NNCLGDQK---LVERLHMVLRPFLLRRIK 340
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvKIELNEEEtllIIRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
121-340 2.34e-93

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: 295.83  E-value: 2.34e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 121 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRS 200
Cdd:cd18009    2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLIGDKEQRAAFVRDVLLP----GEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL 276
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKRegtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975 277 LLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFD---------TNNCLGD---QKLVERLHMVLRPFLLRRIK 340
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaaDISNLSEereQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
123-338 6.25e-88

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: 280.78  E-value: 6.25e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 282
Cdd:cd18003   81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817975 283 LQNNLHELWSLLNFLLPDVFNSADDFDSWFD-------TNNCLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18003  161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
123-302 2.57e-86

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: 274.83  E-value: 2.57e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRaAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 282
Cdd:cd17919   81 YHGSQRER-AQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                        170       180
                 ....*....|....*....|
gi 157817975 283 LQNNLHELWSLLNFLLPDVF 302
Cdd:cd17919  160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
122-338 1.66e-79

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: 258.05  E-value: 1.66e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 122 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSV 201
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 202 CLIGDKEQraafvRDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 271
Cdd:cd17993   81 VYLGDIKS-----RDTIREYEFyfsqtkklkfNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 272 TTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDswFDTNNclGDQKLVERLHMVLRPFLLRR 338
Cdd:cd17993  156 TNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE--EEHDE--EQEKGIADLHKELEPFILRR 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
123-338 9.09e-72

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: 236.95  E-value: 9.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 282
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157817975 283 LQNNLHELWSLLNFLLPDVF--NSADDFDSWF-DTNNclgDQKLVERLHMVLRPFLLRR 338
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDD---ESETVEELHLLLQPFLLRR 216
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
123-338 1.04e-71

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: 236.76  E-value: 1.04e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVpTLRSVC 202
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRA-AFVRDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 271
Cdd:cd17995   80 YHGSGESRQiIQQYEMYFKDAQgrkkkgvykfDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 272 TTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFdtnnclGDQKL---VERLHMVLRPFLLRR 338
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTaeqVEKLQALLKPYMLRR 223
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
104-340 6.38e-70

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: 233.01  E-value: 6.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 104 ATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKST 183
Cdd:cd18062    5 AHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 184 LHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVrDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 263
Cdd:cd18062   85 LSNWVYEFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 264 SEIVR-EFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQK----------LVERLHMVLR 332
Cdd:cd18062  164 TQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLR 243

                 ....*...
gi 157817975 333 PFLLRRIK 340
Cdd:cd18062  244 PFLLRRLK 251
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
123-338 7.60e-70

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: 232.01  E-value: 7.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRAafvrdvLLPGEWD------------VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 270
Cdd:cd18002   81 YWGNPKDRK------VLRKFWDrknlytrdapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSF 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975 271 KTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDT-------NNCLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18002  155 HCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKdieshaeNKTGLNEHQLKRLHMILKPFMLRR 229
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
121-340 1.58e-67

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: 225.14  E-value: 1.58e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 121 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRS 200
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLIGDKEQRAAfVRDVllpGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 280
Cdd:cd18012   82 LVIHGTKRKREK-LRAL---EDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817975 281 TPLQNNLHELWSLLNFLLPDVFNSADDF-DSWFDTNNCLGDQKLVERLHMVLRPFLLRRIK 340
Cdd:cd18012  158 TPIENHLGELWSIFDFLNPGLLGSYKRFkKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
104-340 9.71e-67

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: 224.17  E-value: 9.71e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 104 ATNVCTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKST 183
Cdd:cd18063    5 AHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 184 LHNWMSEFKRWVPTLRSVCLIGDKEQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 263
Cdd:cd18063   85 LSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 264 SEIVR-EFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDQK----------LVERLHMVLR 332
Cdd:cd18063  164 TQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLR 243

                 ....*...
gi 157817975 333 PFLLRRIK 340
Cdd:cd18063  244 PFLLRRLK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
115-338 5.45e-66

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: 221.80  E-value: 5.45e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 115 PSYV--KWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFK 192
Cdd:cd18054   11 PSYIggENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 193 RWVPTLRSVCLIGDKEQRAAfVRDVllpgEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 262
Cdd:cd18054   91 IWAPEINVVVYIGDLMSRNT-IREY----EWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975 263 LSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSwfdtNNCLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18054  166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
123-302 1.34e-60

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: 204.54  E-value: 1.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRaAFVRDVLLPG--EWDVCVTSYEMLI---KEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLL 277
Cdd:cd17998   80 YYGSQEER-KHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                        170       180
                 ....*....|....*....|....*
gi 157817975 278 LTGTPLQNNLHELWSLLNFLLPDVF 302
Cdd:cd17998  159 LTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
425-551 5.26e-60

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: 200.78  E-value: 5.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 425 SGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPNStKFVFMLSTRA 504
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157817975 505 GGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKTVRVFRFI 551
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
841-955 4.56e-55

SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three alpha-helices. It has a role in DNA binding, contacting DNA target sites similar to c-Myb (pfam00249) repeats or homeodomains.


Pssm-ID: 462681 [Multi-domain]  Cd Length: 116  Bit Score: 186.19  E-value: 4.56e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  841 EKIMAQIERGEARIQRRISIKKALDTKIGRYKAPFHQLRISY-GTNKGKNYTEEEDRFLICMLHKLGFDKENVYDELRQC 919
Cdd:pfam09111   1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYpPNNKGKTYTEEEDRFLLCMLYKYGYGNEDLYEKIKQE 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 157817975  920 IRNSPQFRFDWFLKSRTAMELQRRCNTLITLIEREN 955
Cdd:pfam09111  81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
123-338 1.76e-54

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: 188.03  E-value: 1.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKeqraafvrdVLLpgewdvcvTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 282
Cdd:cd17994   81 YVGDH---------VLL--------TSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975 283 LQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
115-338 1.95e-53

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: 186.41  E-value: 1.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 115 PSYVKWGK---LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEF 191
Cdd:cd18053   10 PSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 192 KRWVPTLRSVCLIGDKEQRaafvrDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKS 261
Cdd:cd18053   90 QTWAPQMNAVVYLGDINSR-----NMIRTHEWmhpqtkrlkfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDS 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 262 KLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSwfdtNNCLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18053  165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
123-299 2.19e-53

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: 184.45  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 L------------IGDKEQRAAFVRDVLLPGewDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 270
Cdd:cd18000   81 LhssgsgtgseekLGSIERKSQLIRKVVGDG--GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
                        170       180
                 ....*....|....*....|....*....
gi 157817975 271 KTTNRLLLTGTPLQNNLHELWSLLNFLLP 299
Cdd:cd18000  159 RTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
123-338 3.64e-51

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: 179.85  E-value: 3.64e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRN------IPGPHMVLVPKSTLHNWMSEFKRWVP 196
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 197 T--LRSVCLIGDKEQRAafvRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 274
Cdd:cd17999   80 NafLKPLAYVGPPQERR---RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975 275 RLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWF--------DTNNCLGDQKL----VERLHMVLRPFLLRR 338
Cdd:cd17999  157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrDSKASAKEQEAgalaLEALHKQVLPFLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
123-338 7.07e-49

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: 173.72  E-value: 7.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKH--------YRNIP------------GPHMVLVPKS 182
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPrfkkkppassakKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 183 TLHNWMSEFKRWvPTLRSVCLIGDKEQRAAFVRdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 262
Cdd:cd18005   81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGR--LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 263 LSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDT-------------NNCLGDQKLVErLHM 329
Cdd:cd18005  158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarELRLGRKRKQE-LAV 236

                 ....*....
gi 157817975 330 VLRPFLLRR 338
Cdd:cd18005  237 KLSKFFLRR 245
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
123-338 2.58e-46

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: 165.95  E-value: 2.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRA-------------------AFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 263
Cdd:cd18055   81 YTGDKDSRAiirenefsfddnavkggkkAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975 264 SEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
123-338 1.71e-45

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: 163.70  E-value: 1.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRA-------AFVRDVLLPGE------------WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 263
Cdd:cd18057   81 YTGDKESRSvirenefSFEDNAIRSGKkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975 264 SEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
123-338 2.55e-45

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: 163.31  E-value: 2.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPhMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIG-DKEQRAAFVRDVLLPGewDVCVTSYEMLIKEKSVF-----KKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL 276
Cdd:cd18001   80 FHGtSKKERERNLERIQRGG--GVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975 277 LLTGTPLQNNLHELWSLLNFLLP-DVFNSADDFDSWF--------DTNNCLGDQ----KLVERLHMVLRPFLLRR 338
Cdd:cd18001  158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFenpitrgrDKDATQGEKalgsEVAENLRQIIKPYFLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
123-338 9.80e-45

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: 161.69  E-value: 9.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISlyeNGinGILADEMGLGKTLQTISL-LGYMKHYRNIPGPHM----------------VLVPKSTLH 185
Cdd:cd18008    1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 186 NWMSEFKR--WVPTLRsVCLIGDKEQRaafvRDVLLPGEWDVCVTSYEML----------------IKEKSVFKKFNWRY 247
Cdd:cd18008   76 QWKDEIEKhtKPGSLK-VYVYHGSKRI----KSIEELSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 248 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSaddfDSWFDTNNCL----GDQKL 323
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGD----YPWFNSDISKpfskNDRKA 226
                        250
                 ....*....|....*
gi 157817975 324 VERLHMVLRPFLLRR 338
Cdd:cd18008  227 LERLQALLKPILLRR 241
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
123-338 1.01e-44

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: 160.98  E-value: 1.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVpTLRSVC 202
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFL-SEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDK------EQRAAFVRDV---LLPGEW--DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 271
Cdd:cd18058   79 YHGSQisrqmiQQYEMYYRDEqgnPLSGIFkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 272 TTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18058  159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
123-338 1.45e-44

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: 160.60  E-value: 1.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMSEFKRWVP------ 196
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWTEmntivy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 197 --TLRSVCLIGDKEQRAAFVRDVLLPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 272
Cdd:cd18060   80 hgSLASRQMIQQYEMYCKDSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817975 273 TNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18060  160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
123-338 3.14e-43

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: 157.15  E-value: 3.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVPTLRSVC 202
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRA-------AFVRDVLLPGE------------WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 263
Cdd:cd18056   81 YVGDKDSRAiirenefSFEDNAIRGGKkasrmkkeasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975 264 SEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD---IAKEDQIKKLHDMLGPHMLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
123-332 3.05e-42

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: 154.37  E-value: 3.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLIS-LYENGING------ILADEMGLGKTLQTISLL-GYMKHYRNIPGPhMVLVPKSTLHNWMSEFKRW 194
Cdd:cd18007    1 LKPHQVEGVRFLWSnLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 195 -----VPTLRSVCL--IGDKEQRAAFVRD------VLLPGewdvcVTSYEMLIKEKSVFKKFNWRY-----------LVI 250
Cdd:cd18007   80 lppdlRPLLVLVSLsaSKRADARLRKINKwhkeggVLLIG-----YELFRNLASNATTDPRLKQEFiaalldpgpdlLVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 251 DEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDT---NNCLGDQKLVERL 327
Cdd:cd18007  155 DEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKpieAGQCVDSTEEDVR 234

                 ....*
gi 157817975 328 HMVLR 332
Cdd:cd18007  235 LMLKR 239
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
123-338 3.21e-41

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: 150.95  E-value: 3.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVpTLRSVC 202
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDKEQRAA------FVRDV---LLPGEWD--VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 271
Cdd:cd18059   79 YHGSQASRRTiqlyemYFKDPqgrVIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 272 TTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18059  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
123-338 2.10e-39

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


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 146.28  E-value: 2.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWL----ISLYENGING-ILADEMGLGKTLQTISLLGYM-KHYRNIPGPH---MVLVPKSTLHNWMSEFKR 193
Cdd:cd18004    1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLlKQGPYGKPTAkkaLIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 194 WVP--TLRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVF---KKFNwrYLVIDEAHRIKNEKSKLSEIVR 268
Cdd:cd18004   81 WLGlrRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLskkISID--LLICDEGHRLKNSESKTTKALN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 269 EFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWF--------DTNNCLGDQKLVER----LHMVLRPFLL 336
Cdd:cd18004  159 SLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFeepilrsrDPDASEEDKELGAErsqeLSELTSRFIL 238

                 ..
gi 157817975 337 RR 338
Cdd:cd18004  239 RR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
123-338 1.15e-37

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: 140.91  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMSEFKRWVpTLRSVC 202
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 203 LIGDK------EQRAAFVRDV---LLPGEW--DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 271
Cdd:cd18061   79 YHGSLisrqmiQQYEMYFRDSqgrIIRGAYrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 272 TTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18061  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
123-338 2.18e-33

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: 128.09  E-value: 2.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLIslyENGINGILADEMGLGKTLQTISLlgyMKHYRNiPGPHMVLVPKSTLHNWMSEFKRWVPTL--RS 200
Cdd:cd18010    1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAI---AAYYRE-EWPLLIVCPSSLRLTWADEIERWLPSLppDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLIGDKeqraafvRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS-EIVREFKTTNR-LLL 278
Cdd:cd18010   74 IQVIVKS-------KDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTkAALPLLKRAKRvILL 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817975 279 TGTPLQNNLHELWSLLNFLLPDVFNSADDFDS-----------WFDTnnclGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18010  147 SGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfgWDYS----GSSNLEELHLLLLATIMIRR 213
DEXDc smart00487
DEAD-like helicases superfamily;
119-300 7.26e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.67  E-value: 7.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   119 KWGKLRDYQVRGLNWLISLYENGIngiLADEMGLGKTLQ-TISLLGYMKhyRNIPGPHMVLVP-KSTLHNWMSEFKRWVP 196
Cdd:smart00487   5 GFEPLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   197 --TLRSVCLIGDKEQRAafVRDVLLPGEWDVCVTSYEMLIK--EKSVFKKFNWRYLVIDEAHRIKNE--KSKLSEIVREF 270
Cdd:smart00487  80 slGLKVVGLYGGDSKRE--QLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....
gi 157817975   271 -KTTNRLLLTGTP---LQNNLHELWSLLNFLLPD 300
Cdd:smart00487 158 pKNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
139-338 4.01e-30

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: 119.50  E-value: 4.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 139 ENGINGILADEMGLGKTLQTISLLgymkhyrnIPGPHMVLVPKSTLHNWMSEFKRWVptlRSVCLIGDKEQRAAFVRDVL 218
Cdd:cd18071   46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHV---KPGQLKVYTYHGGERNRDPK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 219 LPGEWDVCVTSYEMLIKEKSV-----FKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSL 293
Cdd:cd18071  115 LLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157817975 294 LNFLLPDVFNSADDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRR 338
Cdd:cd18071  195 LSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
426-540 8.88e-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: 108.45  E-value: 8.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  426 GKMVVLDKLLPKlkEQGSRVLIFSQMTRVLDIlEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPnstKFVFMLSTRAG 505
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 157817975  506 GLGINLATADVVILYDSDWNPQVDLQAMDRAHRIG 540
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
123-313 1.21e-27

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: 112.22  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLislYEN------------GINGILADEMGLGKTLQTISLLG-YMKHyrniPGPHMVL--VPKSTLHNW 187
Cdd:cd18069    1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDvLLRH----TGAKTVLaiVPVNTLQNW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 188 MSEFKRWVPTLRS----------VCLIGDKEQRAAFVRDVLLpgEWD----VCVTSYEMlikeksvfkkFNWR----YLV 249
Cdd:cd18069   74 LSEFNKWLPPPEAlpnvrprpfkVFILNDEHKTTAARAKVIE--DWVkdggVLLMGYEM----------FRLRpgpdVVI 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817975 250 IDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFD 313
Cdd:cd18069  142 CDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
144-338 1.44e-27

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: 112.19  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 144 GILADEMGLGKTLQTISLLGYMKHYRN---------------------IP-GPHMVLVPKSTLHNWMSEFKRWVPTLR-S 200
Cdd:cd18072   23 GILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASNKlR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLI--GDKEQRAAFVRDvllpgeWDVCVTSYEMLIKE---------KSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 269
Cdd:cd18072  103 VCLYhgPNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817975 270 FKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWFDTNNCLGDqklvERLHMVLRPFLLRR 338
Cdd:cd18072  177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
123-308 1.19e-26

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: 109.55  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLnwlISLYE--------NGINGILADEMGLGKTLQTISLLGYM---KHYRNIP--GPHMVLVPKSTLHNWMS 189
Cdd:cd18066    1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLlrqGPYGGKPviKRALIVTPGSLVKNWKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 190 EFKRWVPTLRSVCLIGDKEQRaafVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 269
Cdd:cd18066   78 EFQKWLGSERIKVFTVDQDHK---VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTS 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157817975 270 FKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDF 308
Cdd:cd18066  155 LSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
123-338 3.49e-26

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: 108.33  E-value: 3.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWL----ISLYENGING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPH----MVLVPKSTLHNWMSEFKR 193
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 194 WVPTlRSVCLIGD----KEQRAAFVRDVLLPGE---WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEI 266
Cdd:cd18067   81 WLGG-RLQPLAIDggskKEIDRKLVQWASQQGRrvsTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 267 VREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWF-------------DTNNCLGDQKLVERLHMVLRp 333
Cdd:cd18067  160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadasEKERQLGEEKLQELISIVNR- 238

                 ....*
gi 157817975 334 FLLRR 338
Cdd:cd18067  239 CIIRR 243
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
123-312 2.78e-25

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: 105.74  E-value: 2.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWL---------ISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLV--PKSTLHNWMSEF 191
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVvcPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 192 KRWVPTLR--------SVCLIGDKEQRAafvrdvLLPGEWD----VCVTSYEM---LIKEKSVFKKFNWR---------- 246
Cdd:cd18068   81 EKWQEGLKdeekievnELATYKRPQERS------YKLQRWQeeggVMIIGYDMyriLAQERNVKSREKLKeifnkalvdp 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817975 247 ---YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDSWF 312
Cdd:cd18068  155 gpdFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
123-337 3.67e-24

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: 102.81  E-value: 3.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLyengiNGILADEMGLGKTLQTISLLgyMKHYRN--------IPGPHMVLVP-----------KST 183
Cdd:cd18070    1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPdndldaadDDSDEMVCCPdclvaetpvssKAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 184 L--------HNWMSEFKRWVPT-LRSVCLIGDKEQRAAFVRDVLLPGEWDVCVTSYEMLIKE------------KSVFKK 242
Cdd:cd18070   74 LivcpsailAQWLDEINRHVPSsLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTElhyaeanrsnrrRRRQKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 243 F----------NWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFdsWF 312
Cdd:cd18070  154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWW--AR 231
                        250       260
                 ....*....|....*....|....*
gi 157817975 313 DTNNCLGDQKLVERLHMVLRPFLLR 337
Cdd:cd18070  232 VLIRPQGRNKAREPLAALLKELLWR 256
HELICc smart00490
helicase superfamily c-terminal domain;
456-540 2.91e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 2.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975   456 DILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEPnstKFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDR 535
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 157817975   536 AHRIG 540
Cdd:smart00490  78 AGRAG 82
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
686-771 3.61e-23

HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of which (H2, H3, H4) form an L-like configuration. Helix H2 runs antiparallel to helices H3 and H4, packing closely against helix H4, whilst helix H1 reposes in the concave surface formed by these three helices and runs perpendicular to them. The domain confers DNA and nucleosome binding properties to the protein.


Pssm-ID: 430414  Cd Length: 110  Bit Score: 95.32  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  686 AVDAYFREALRVSEPKAPKAPRPPK---QPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRSP--------DLPNAAQ 754
Cdd:pfam09110   1 SVDNYYKDVLGTGGKKSTTKPKAPRapkQINIQDHQFFPPRLKELQEKEQLYYKKKIGYKVTLDDgkeedgeeFEEEREA 80
                          90
                  ....*....|....*..
gi 157817975  755 AQKEEQLKIDEAGPLND 771
Cdd:pfam09110  81 KRKLEQEEIDNAEPLTE 97
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
123-310 8.39e-23

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 97.36  E-value: 8.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGIngILADEMGLGKTlqtISLLGYMKHY--RNIPGPHMVLVPKSTLHNWMSEF--KRWVPTL 198
Cdd:cd18011    1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKT---IEAGLIIKELllRGDAKRVLILCPASLVEQWQDELqdKFGLPFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 199 RSVCLIGDKEQRaafvRDVLLPGEWDVCVTSYEML---IKEKSVFKKFNWRYLVIDEAHRIKN----EKSKLSEIVREF- 270
Cdd:cd18011   76 ILDRETAAQLRR----LIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLa 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157817975 271 -KTTNRLLLTGTPLQNNLHELWSLLNFLLPDVFNSADDFDS 310
Cdd:cd18011  152 kRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
123-297 1.10e-16

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: 80.09  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLIslyENGINGILADeMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTL-HNWMSEFKRW--VPTLR 199
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 200 SVCLIGDKEQRAAfvrdvLLPGEWDVCVTSYEMLIK-EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF-KTTNRLL 277
Cdd:cd18013   76 VSVAVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                        170       180
                 ....*....|....*....|.
gi 157817975 278 -LTGTPLQNNLHELWSLLNFL 297
Cdd:cd18013  151 gLTGTPSPNGLMDLWAQIALL 171
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
123-282 9.86e-11

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: 60.78  E-value: 9.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGL-NWLISLYENGinGILADEMGLGKTLQTISLlgyMKHYRNipGPHMVLVP-KSTLHNWMSEFKRWVPTlRS 200
Cdd:cd17926    1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALAL---IAYLKE--LRTLIVVPtDALLDQWKERFEDFLGD-SS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 201 VCLIGDKEQRAAFVRDVLlpgewdvcVTSYEMLIK-EKSVFKKFN-WRYLVIDEAHRIKNEKskLSEIVREFKTTNRLLL 278
Cdd:cd17926   73 IGLIGGGKKKDFDDANVV--------VATYQSLSNlAEEEKDLFDqFGLLIVDEAHHLPAKT--FSEILKELNAKYRLGL 142

                 ....
gi 157817975 279 TGTP 282
Cdd:cd17926  143 TATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
121-696 1.03e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 65.43  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 121 GKLRDYQVRGLN-WLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIpgphMVLVPKSTL-HNWMSEFKRWVPTL 198
Cdd:COG1061   79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELlEQWAEELRRFLGDP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 199 RSVcliGDKEQRaafvrdvllpgEWDVCVTSYEMLIKEKSvFKKF--NWRYLVIDEAHRIKNEksKLSEIVREFKTTNRL 276
Cdd:COG1061  155 LAG---GGKKDS-----------DAPITVATYQSLARRAH-LDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRL 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 277 LLTGTPL-QNNLHELWSLLNFLLPDVfnsaddfdSWfdtnnclgdQKLVERLHmvLRPFLLRRIKADVEkslppkKEVKI 355
Cdd:COG1061  218 GLTATPFrSDGREILLFLFDGIVYEY--------SL---------KEAIEDGY--LAPPEYYGIRVDLT------DERAE 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 356 YVGLSKMQREWYTRilmkdidilnsagkmDKMRLLNILMQLRKccNHPylfdgaepgppyttdmhlvtnsgkmvvldkll 435
Cdd:COG1061  273 YDALSERLREALAA---------------DAERKDKILRELLR--EHP-------------------------------- 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 436 pklkeQGSRVLIFSQMTRVLDILEDYCMWRNYEYCRLDGQTPHDERQDSINAYNEpnsTKFVFMLSTRAGGLGINLATAD 515
Cdd:COG1061  304 -----DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLD 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 516 VVILYDSDWNPQVDLQAMDRAHRIGQTK-TVRVFRFITDNTVEERIVERAEMKLRLDSIVIQQGRLVDQNLNKIGKDEML 594
Cdd:COG1061  376 VAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPAL 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 595 QMIRHGATHVFASKESEITDEDIDGILERGAKKTAEMNEKLSKMGESSLRNFTMDTESSVYNFEGEDYREKQKIAFTEWI 674
Cdd:COG1061  456 EVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLL 535
                        570       580
                 ....*....|....*....|..
gi 157817975 675 EPPKRERKANYAVDAYFREALR 696
Cdd:COG1061  536 LELLELLAALLRLEELAALLLK 557
ResIII pfam04851
Type III restriction enzyme, res subunit;
122-282 4.92e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 59.22  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  122 KLRDYQVRGL-NWLISLYENGINGILADEMGLGKTLQTISLlgyMKHYRNIPGPH--MVLVP-KSTLHNWMSEFKRWVPT 197
Cdd:pfam04851   3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKL---IARLFKKGPIKkvLFLVPrKDLLEQALEEFKKFLPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  198 LRSVCLI--GDKEQRAAfvrdvllpGEWDVCVTSYEML----IKEKSVFKKFNWRYLVIDEAHRIKNEKSKlsEIVREFK 271
Cdd:pfam04851  80 YVEIGEIisGDKKDESV--------DDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYFK 149
                         170
                  ....*....|.
gi 157817975  272 TTNRLLLTGTP 282
Cdd:pfam04851 150 PAFLLGLTATP 160
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
143-281 6.76e-09

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: 55.49  E-value: 6.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 143 NGILADEMGLGKTLQ-TISLLGYMKHYRnipGPHMVLVPKSTL-HNWMSEFKRWVPTLRSVCLIG---DKEQRAAFVRDv 217
Cdd:cd00046    3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLRELFGPGIRVAVLVggsSAEEREKNKLG- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817975 218 llpgEWDVCVTSYEMLIKEKSVFKKF---NWRYLVIDEAHRI-KNEKS----KLSEIVREFKTTNRLLLTGT 281
Cdd:cd00046   79 ----DADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlIDSRGalilDLAVRKAGLKNAQVILLSAT 146
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
787-826 4.54e-06

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 44.49  E-value: 4.54e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157817975 787 NWNKRDFNQFIKANEKWGRDDIENIAREVEGKTPEEVIEY 826
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRER 40
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
785-826 1.41e-05

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 42.98  E-value: 1.41e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 157817975   785 FTNWNKRDFNQFIKANEKWGRDDIENIAREVEGKTPEEVIEY 826
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRER 42
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
495-551 3.92e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 42.69  E-value: 3.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157817975 495 KFVFMLSTRAGGLGINLATADVVILYDSDWNPQVDLQAMDRAHRIGQTKtVRVFRFI 551
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE-GEVILFV 77
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
151-282 1.48e-04

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: 43.39  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975  151 GLGKTLqtISLLGYMKH-YRNIPGPH-MVLVPKSTL-HNWMSEFKRW--VPTLRSVCLIGDKEQR--AAFVRDVllpgew 223
Cdd:pfam00270  24 GSGKTL--AFLLPALEAlDKLDNGPQaLVLAPTRELaEQIYEELKKLgkGLGLKVASLLGGDSRKeqLEKLKGP------ 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817975  224 DVCVTSYEML---IKEKSVFKKFnwRYLVIDEAHRIKNE--KSKLSEIVREFKTTNR-LLLTGTP 282
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMgfGPDLEEILRRLPKKRQiLLLSATL 158
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
146-308 4.11e-04

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 44.44  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 146 LADEMGLGKTLQTisllGYMKHYRNIPGPH---MVLVPKSTLHNWMSEFkrwvptLRSVCL---IGDKEQRAAFVRDVLL 219
Cdd:PRK04914 174 LADEVGLGKTIEA----GMIIHQQLLTGRAervLILVPETLQHQWLVEM------LRRFNLrfsLFDEERYAEAQHDADN 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 220 PGEWDVCV-TSYEMLIKEKSVFKKF---NWRYLVIDEAHRIKNEKSKLSeivREF--------KTTNRLLLTGTPLQNNL 287
Cdd:PRK04914 244 PFETEQLViCSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHLVWSEEAPS---REYqvveqlaeVIPGVLLLTATPEQLGQ 320
                        170       180
                 ....*....|....*....|.
gi 157817975 288 HELWSLLNFLLPDVFNSADDF 308
Cdd:PRK04914 321 ESHFARLRLLDPDRFHDYEAF 341
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
123-282 1.81e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 40.24  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 123 LRDYQVRGLNWLISLYENGINGILAdEM--GLGKTLqTISLLGYmKHYRNIPGPH-MVLVPKSTL-HNWMSEFKRWVPTL 198
Cdd:cd18032    1 PRYYQQEAIEALEEAREKGQRRALL-VMatGTGKTY-TAAFLIK-RLLEANRKKRiLFLAHREELlEQAERSFKEVLPDG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 199 RSVCLIGDKEQraafvrdvllPGEWDVCVTSYEMLIKEK--SVFKKFNWRYLVIDEAHRikNEKSKLSEIVREFKTTNRL 276
Cdd:cd18032   78 SFGNLKGGKKK----------PDDARVVFATVQTLNKRKrlEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLL 145

                 ....*.
gi 157817975 277 LLTGTP 282
Cdd:cd18032  146 GLTATP 151
PTZ00110 PTZ00110
helicase; Provisional
421-542 8.54e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 39.76  E-value: 8.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817975 421 LVTNSGKMVVLDKLLPKLKEQGSRVLIFSQMTRVLDILEdycmwrnyEYCRLDGQTP---H-DERQDSIN-AYNEPNSTK 495
Cdd:PTZ00110 356 VVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLT--------KELRLDGWPAlciHgDKKQEERTwVLNEFKTGK 427
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157817975 496 FVFMLSTRAGGLGINLATADVVILYDSdwnPQvdlQAMDRAHRIGQT 542
Cdd:PTZ00110 428 SPIMIATDVASRGLDVKDVKYVINFDF---PN---QIEDYVHRIGRT 468
 
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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