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Conserved domains on  [gi|334185131|ref|NP_001189826|]
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chromatin-remodeling protein 11 [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11477522)

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 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
33-1052 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1956.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   33 AVARSSGSD-DDEVAAADESPVSDGEaapveddYEDEEDEEKAEISKREKARLKEMQKLKKQKIQEMLESQNASIDADMN 111
Cdd:PLN03142   20 AVARSAGSDsDDDEVPAEDEDEDEED-------DEEAESPAKAEISKREKARLKELKKQKKQEIQKILEQQNAAIDADMN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  112 NKGKGRLKYLLQQTELFAHFAKSDGSSSQKKAKGRGRHASKITEEEEDEEYLKEEEDGLTGSGNTRLLTQPSCIQGKMRD 191
Cdd:PLN03142   93 NKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 271
Cdd:PLN03142  173 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  272 NPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 351
Cdd:PLN03142  253 NPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  352 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 431
Cdd:PLN03142  333 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  432 YYKALLQKDLEAVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLITNAGKMVLLDKLLPKLKERDSRVLI 511
Cdd:PLN03142  413 YYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLI 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  512 FSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQ 591
Cdd:PLN03142  493 FSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQ 572
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  592 VDLQAQDRAHRIGQKKEVQVFRFCTESAIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 671
Cdd:PLN03142  573 VDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 652
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  672 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDskGADFYDFDD-DNKDENKLDFKKIVSDNWNDPPKRERKR 750
Cdd:PLN03142  653 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDD--TAELYDFDDeDDKDENKLDFKKIVSDNWIDPPKRERKR 730
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  751 NYSESEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQTHQKNQLKDTIDVEEPE-GGDPLTT 829
Cdd:PLN03142  731 NYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEePGDPLTA 810
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  830 EEVEEKEGLLEEGFSTWSRRDFNTFLRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFKERYKELNDYDRIIKNIERGE 909
Cdd:PLN03142  811 EEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGE 890
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  910 ARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMIHKLGYGNWDELKAAFRTSSVFRFDWFVKS 989
Cdd:PLN03142  891 ARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGNWDELKAAFRTSPLFRFDWFVKS 970
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  990 RTSQELARRCDTLIRLIEKENQEFDERERQARKEKKLAKSATPSKRPLGRQASESPSSTKKRK 1052
Cdd:PLN03142  971 RTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSSLKKRK 1033
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
33-1052 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1956.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   33 AVARSSGSD-DDEVAAADESPVSDGEaapveddYEDEEDEEKAEISKREKARLKEMQKLKKQKIQEMLESQNASIDADMN 111
Cdd:PLN03142   20 AVARSAGSDsDDDEVPAEDEDEDEED-------DEEAESPAKAEISKREKARLKELKKQKKQEIQKILEQQNAAIDADMN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  112 NKGKGRLKYLLQQTELFAHFAKSDGSSSQKKAKGRGRHASKITEEEEDEEYLKEEEDGLTGSGNTRLLTQPSCIQGKMRD 191
Cdd:PLN03142   93 NKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 271
Cdd:PLN03142  173 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  272 NPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 351
Cdd:PLN03142  253 NPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  352 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 431
Cdd:PLN03142  333 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  432 YYKALLQKDLEAVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLITNAGKMVLLDKLLPKLKERDSRVLI 511
Cdd:PLN03142  413 YYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLI 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  512 FSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQ 591
Cdd:PLN03142  493 FSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQ 572
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  592 VDLQAQDRAHRIGQKKEVQVFRFCTESAIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 671
Cdd:PLN03142  573 VDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 652
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  672 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDskGADFYDFDD-DNKDENKLDFKKIVSDNWNDPPKRERKR 750
Cdd:PLN03142  653 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDD--TAELYDFDDeDDKDENKLDFKKIVSDNWIDPPKRERKR 730
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  751 NYSESEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQTHQKNQLKDTIDVEEPE-GGDPLTT 829
Cdd:PLN03142  731 NYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEePGDPLTA 810
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  830 EEVEEKEGLLEEGFSTWSRRDFNTFLRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFKERYKELNDYDRIIKNIERGE 909
Cdd:PLN03142  811 EEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGE 890
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  910 ARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMIHKLGYGNWDELKAAFRTSSVFRFDWFVKS 989
Cdd:PLN03142  891 ARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGNWDELKAAFRTSPLFRFDWFVKS 970
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  990 RTSQELARRCDTLIRLIEKENQEFDERERQARKEKKLAKSATPSKRPLGRQASESPSSTKKRK 1052
Cdd:PLN03142  971 RTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSSLKKRK 1033
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
175-640 3.08e-144

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 447.75  E-value: 3.08e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  175 NTRLLTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWM 254
Cdd:COG0553   228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  255 NEIRRFCPVLRAVKFLGNPEERRHIREdllvAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMR 334
Cdd:COG0553   307 RELAKFAPGLRVLVLDGTRERAKGANP----FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  335 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 414
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLP 462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  415 PKKETILKVGMSQMQKQYYKALLQKDLEAVNAG-GERKRLLNIA--MQLRKCCNHPYLFqgAEPGPPYTTGDhlitnaGK 491
Cdd:COG0553   463 EKTEETLYVELTPEQRALYEAVLEYLRRELEGAeGIRRRGLILAalTRLRQICSHPALL--LEEGAELSGRS------AK 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  492 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKpGSEKFVFLLSTRAGGL 571
Cdd:COG0553   535 LEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGE 613
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185131  572 GINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTESAIEEKVIERAYKKLALDALVIQ 640
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
186-406 1.34e-137

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: 412.87  E-value: 1.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  186 QGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLR 265
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  266 AVKFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLIT 345
Cdd:cd17997    81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185131  346 GTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI-SGENDQQEVVQQLHKVLRPFLLRRLK 406
Cdd:cd17997   161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
192-470 3.18e-119

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: 367.78  E-value: 3.18e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   192 YQLAGLNWLIRLYEN-GINGILADEMGLGKTLQTISLLAYLHEYRGI-NGPHMVVAPKSTLGNWMNEIRRFC--PVLRAV 267
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   268 KFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGT 347
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   348 PLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEN-DQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMS 426
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 334185131   427 QMQKQYYKA-LLQKDLEAVNAGGE----RKRLLNIAMQLRKCCNHPYLF 470
Cdd:pfam00176  241 KLQRKLYQTfLLKKDLNAIKTGEGgreiKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
188-380 3.09e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.75  E-value: 3.09e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131    188 KMRDYQLAGLNWLIRLYENGIngiLADEMGLGKTLQ-TISLLAYLHeyRGINGPHMVVAP-KSTLGNWMNEIRRFCP--V 263
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGPslG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131    264 LRAVKFLGNPEERRHIREdlLVAGKFDICVTSFEMAIK--EKTALRRFSWRYIIIDEAHRIKNEN---SLLSKTMRLFST 338
Cdd:smart00487   83 LKVVGLYGGDSKREQLRK--LESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGfgdQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 334185131    339 NYRLLITGTPLQNNLHELWALLNflLPEIFSSAETFDEWFQI 380
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPIEQ 200
DpdE NF041062
protein DpdE;
212-374 3.31e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 48.04  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  212 LADEMGLGKTLQT-ISLLAYLHEYRGINGphMVVAPKSTLGNWMNEIR-RFcpvlravkFLGnpeerrhireDLLVAgkf 289
Cdd:NF041062  175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELRdKF--------FLD----------DFPGA--- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  290 DICVTSFEMAIKEKTALRRFSwrYIIIDEAHRI-KNENSLLSKTMRLF--------STNYRLLITGTPLQNNLHELWALL 360
Cdd:NF041062  232 RVRVLSHEEPERWEPLLDAPD--LLVVDEAHQLaRLAWSGDPPERARYrelaalahAAPRLLLLSATPVLGNEETFLALL 309
                         170
                  ....*....|....*.
gi 334185131  361 NFLLPEIF--SSAETF 374
Cdd:NF041062  310 HLLDPDLYplDDLEAF 325
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
33-1052 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1956.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   33 AVARSSGSD-DDEVAAADESPVSDGEaapveddYEDEEDEEKAEISKREKARLKEMQKLKKQKIQEMLESQNASIDADMN 111
Cdd:PLN03142   20 AVARSAGSDsDDDEVPAEDEDEDEED-------DEEAESPAKAEISKREKARLKELKKQKKQEIQKILEQQNAAIDADMN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  112 NKGKGRLKYLLQQTELFAHFAKSDGSSSQKKAKGRGRHASKITEEEEDEEYLKEEEDGLTGSGNTRLLTQPSCIQGKMRD 191
Cdd:PLN03142   93 NKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEEDGLGGSGGTRLLVQPSCIKGKMRD 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 271
Cdd:PLN03142  173 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  272 NPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 351
Cdd:PLN03142  253 NPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  352 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 431
Cdd:PLN03142  333 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQ 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  432 YYKALLQKDLEAVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLITNAGKMVLLDKLLPKLKERDSRVLI 511
Cdd:PLN03142  413 YYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLI 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  512 FSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKPGSEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQ 591
Cdd:PLN03142  493 FSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQ 572
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  592 VDLQAQDRAHRIGQKKEVQVFRFCTESAIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 671
Cdd:PLN03142  573 VDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVRYGAEMVFSSKD 652
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  672 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIQFKMDDskGADFYDFDD-DNKDENKLDFKKIVSDNWNDPPKRERKR 750
Cdd:PLN03142  653 STITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDD--TAELYDFDDeDDKDENKLDFKKIVSDNWIDPPKRERKR 730
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  751 NYSESEYFKQTLRQGAPAKPKEPRIPRMPQLHDFQFFNIQRLTELYEKEVRYLMQTHQKNQLKDTIDVEEPE-GGDPLTT 829
Cdd:PLN03142  731 NYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEePGDPLTA 810
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  830 EEVEEKEGLLEEGFSTWSRRDFNTFLRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFKERYKELNDYDRIIKNIERGE 909
Cdd:PLN03142  811 EEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGE 890
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  910 ARISRKDEIMKAIGKKLDRYRNPWLELKIQYGQNKGKLYNEECDRFMICMIHKLGYGNWDELKAAFRTSSVFRFDWFVKS 989
Cdd:PLN03142  891 ARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGNWDELKAAFRTSPLFRFDWFVKS 970
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  990 RTSQELARRCDTLIRLIEKENQEFDERERQARKEKKLAKSATPSKRPLGRQASESPSSTKKRK 1052
Cdd:PLN03142  971 RTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSSLKKRK 1033
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
175-640 3.08e-144

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 447.75  E-value: 3.08e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  175 NTRLLTQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWM 254
Cdd:COG0553   228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  255 NEIRRFCPVLRAVKFLGNPEERRHIREdllvAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMR 334
Cdd:COG0553   307 RELAKFAPGLRVLVLDGTRERAKGANP----FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  335 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 414
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLP 462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  415 PKKETILKVGMSQMQKQYYKALLQKDLEAVNAG-GERKRLLNIA--MQLRKCCNHPYLFqgAEPGPPYTTGDhlitnaGK 491
Cdd:COG0553   463 EKTEETLYVELTPEQRALYEAVLEYLRRELEGAeGIRRRGLILAalTRLRQICSHPALL--LEEGAELSGRS------AK 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  492 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKpGSEKFVFLLSTRAGGL 571
Cdd:COG0553   535 LEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGE 613
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185131  572 GINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTESAIEEKVIERAYKKLALDALVIQ 640
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
186-406 1.34e-137

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: 412.87  E-value: 1.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  186 QGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLR 265
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  266 AVKFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLIT 345
Cdd:cd17997    81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185131  346 GTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI-SGENDQQEVVQQLHKVLRPFLLRRLK 406
Cdd:cd17997   161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
192-470 3.18e-119

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: 367.78  E-value: 3.18e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   192 YQLAGLNWLIRLYEN-GINGILADEMGLGKTLQTISLLAYLHEYRGI-NGPHMVVAPKSTLGNWMNEIRRFC--PVLRAV 267
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   268 KFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGT 347
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   348 PLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEN-DQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMS 426
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 334185131   427 QMQKQYYKA-LLQKDLEAVNAGGE----RKRLLNIAMQLRKCCNHPYLF 470
Cdd:pfam00176  241 KLQRKLYQTfLLKKDLNAIKTGEGgreiKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
176-417 8.87e-106

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: 330.47  E-value: 8.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  176 TRLLTQPSCIQ-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWM 254
Cdd:cd18064     2 TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  255 NEIRRFCPVLRAVKFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMR 334
Cdd:cd18064    82 AEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  335 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 414
Cdd:cd18064   162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLP 241

                  ...
gi 334185131  415 PKK 417
Cdd:cd18064   242 PKK 244
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
187-406 1.16e-100

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: 316.64  E-value: 1.16e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  187 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRA 266
Cdd:cd18009     2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  267 VKFLGNPEERRHIREDLL----VAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 342
Cdd:cd18009    81 LLYHGTKEERERLRKKIMkregTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185131  343 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEND------------QQEVVQQLHKVLRPFLLRRLK 406
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDnaadisnlseerEQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
187-406 2.67e-97

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: 307.37  E-value: 2.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  187 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRA 266
Cdd:cd17996     2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  267 VKFLGNPEERRHIrEDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTM-RLFSTNYRLLIT 345
Cdd:cd17996    82 IVYKGTPDVRKKL-QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLLT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  346 GTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGENDQQE--------VVQQLHKVLRPFLLRRLK 406
Cdd:cd17996   161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFntpfANTGEQVKIElneeetllIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
177-406 1.32e-96

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: 305.40  E-value: 1.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  177 RLLTQPSCIQG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMN 255
Cdd:cd18065     3 RFEESPSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  256 EIRRFCPVLRAVKFLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRL 335
Cdd:cd18065    83 EFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334185131  336 FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLK 406
Cdd:cd18065   163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
189-404 3.25e-89

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: 285.40  E-value: 3.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 348
Cdd:cd18003    81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  349 LQNNLHELWALLNFLLPEIFSSAETFDEWFQ-------ISGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18003   161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
189-365 3.45e-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: 275.21  E-value: 3.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLVaGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 348
Cdd:cd17919    81 YHGSQRERAQIRAKEKL-DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                         170
                  ....*....|....*..
gi 334185131  349 LQNNLHELWALLNFLLP 365
Cdd:cd17919   160 LQNNLEELWALLDFLDP 176
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
188-404 1.95e-78

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: 255.74  E-value: 1.95e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  188 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 267
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  268 KFLGNPEERRHIREDLLVAG-----KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 342
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185131  343 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE----EHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
189-404 6.51e-78

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 254.48  E-value: 6.51e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 268
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPE--ERRHIREDLLV---------AGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 337
Cdd:cd17995    80 YHGSGEsrQIIQQYEMYFKdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---GDLKTAEQVEKLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
189-404 1.19e-73

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: 243.18  E-value: 1.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIR----------EDllvaGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 338
Cdd:cd18002    81 YWGNPKDRKVLRkfwdrknlytRD----APFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHC 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  339 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEND-------QQEVVQQLHKVLRPFLLRR 404
Cdd:cd18002   157 RNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHaenktglNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
189-404 4.93e-73

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: 240.80  E-value: 4.93e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 348
Cdd:cd18006    81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  349 LQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18006   161 IQNSLQELYALLSFIEPNVFPK-DKLDDFIKAYSEtDDESETVEELHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
185-406 1.13e-69

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 231.69  E-value: 1.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  185 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWMNEIRRFCPVL 264
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  265 RAVKFLGNPEERRHIREdllvAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 344
Cdd:cd18012    80 KVLVIHGTKRKREKLRA----LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  345 TGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ-QEVVQQLHKVLRPFLLRRLK 406
Cdd:cd18012   156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
185-406 3.14e-69

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: 231.86  E-value: 3.14e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  185 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVL 264
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  265 RAVKFLGNPEERRHIREdLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 340
Cdd:cd18062   100 VKVSYKGSPAARRAFVP-QLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185131  341 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----ISGE----NDQQE--VVQQLHKVLRPFLLRRLK 406
Cdd:cd18062   176 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGEkvdlNEEETilIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
185-406 3.39e-69

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 231.49  E-value: 3.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  185 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVL 264
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  265 RAVKFLGNPEERRHIREDLLvAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 340
Cdd:cd18063   100 VKISYKGTPAMRRSLVPQLR-SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185131  341 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----ISGE----NDQQE--VVQQLHKVLRPFLLRRLK 406
Cdd:cd18063   176 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGErvdlNEEETilIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
178-404 6.75e-67

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: 224.88  E-value: 6.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  178 LLTQPSCIQGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWM 254
Cdd:cd18054     7 LKKQPSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  255 NEIRRFCPVLRAVKFLGNPEERRHIREDLLVAG-----KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLL 329
Cdd:cd18054    87 REFEIWAPEINVVVYIGDLMSRNTIREYEWIHSqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185131  330 SKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDqqevVQQLHKVLRPFLLRR 404
Cdd:cd18054   167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
189-368 2.26e-65

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: 218.41  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLV-AGKFDICVTSFEMAI---KEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 344
Cdd:cd17998    80 YYGSQEERKHLRYDILKgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                         170       180
                  ....*....|....*....|....
gi 334185131  345 TGTPLQNNLHELWALLNFLLPEIF 368
Cdd:cd17998   160 TGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
181-404 5.17e-59

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: 202.59  E-value: 5.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  181 QPSCIQG----KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNE 256
Cdd:cd18053     9 QPSYIGGheglELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  257 IRRFCPVLRAVKFLGNPEERRHIREDLLVAG-----KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSK 331
Cdd:cd18053    89 IQTWAPQMNAVVYLGDINSRNMIRTHEWMHPqtkrlKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYK 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  332 TMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18053   169 TLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
189-404 1.94e-53

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: 186.40  E-value: 1.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLH-----EYRGINGPHMVVAPKSTLGNWMNEIRRFCP- 262
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHhkranSFNSENLPSLVVCPPTLVGHWVAEIKKYFPn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  263 -VLRAVKFLGNPEERRHIREDLlvaGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 341
Cdd:cd17999    81 aFLKPLAYVGPPQERRRLREQG---EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185131  342 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF---------QISGENDQQEVVQ---QLHKVLRPFLLRR 404
Cdd:cd17999   158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrdSKASAKEQEAGALaleALHKQVLPFLLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
490-615 2.33e-51

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: 176.90  E-value: 2.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  490 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKPGSEkFVFLLSTRAG 569
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 334185131  570 GLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 615
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
191-404 2.73e-51

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 180.26  E-value: 2.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  191 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPhMVVAPKSTLGNWMNEIRRFCPVLRAVKFL 270
Cdd:cd18001     3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKVFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  271 G-NPEERRHIREDllVAGKFDICVTSFEMAIKEKTAL-----RRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 344
Cdd:cd18001    82 GtSKKERERNLER--IQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  345 TGTPLQNNLHELWALLNFLLP-EIFSSAETFDEWFQ--ISGENDQ----------QEVVQQLHKVLRPFLLRR 404
Cdd:cd18001   160 TGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFEnpITRGRDKdatqgekalgSEVAENLRQIIKPYFLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
192-404 7.37e-51

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: 177.63  E-value: 7.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 271
Cdd:cd17994     4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  272 NpeerrHIredLLvagkfdicvTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQN 351
Cdd:cd17994    84 D-----HV---LL---------TSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQN 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 334185131  352 NLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 404
Cdd:cd17994   147 NLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
189-404 4.83e-50

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: 176.39  E-value: 4.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHeYRGINGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 268
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLV-----------AGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 337
Cdd:cd18058    79 YHGSQISRQMIQQYEMYyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF---GDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
189-404 3.29e-49

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: 174.09  E-value: 3.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYrGINGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 268
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIRE---------DLLVAG--KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 337
Cdd:cd18060    79 YHGSLASRQMIQQyemyckdsrGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
191-365 6.61e-49

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: 172.12  E-value: 6.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  191 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAV--- 267
Cdd:cd18000     3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVvlh 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  268 ---KFLGNPEERRHIREDLL----VAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNY 340
Cdd:cd18000    83 ssgSGTGSEEKLGSIERKSQlirkVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
                         170       180
                  ....*....|....*....|....*
gi 334185131  341 RLLITGTPLQNNLHELWALLNFLLP 365
Cdd:cd18000   163 RLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
189-404 3.94e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 170.98  E-value: 3.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHeYRGINGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 268
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIY-LKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIR---------EDLLVAG--KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 337
Cdd:cd18059    79 YHGSQASRRTIQlyemyfkdpQGRVIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
899-1010 4.74e-48

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: 166.55  E-value: 4.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   899 DRIIKNIERGEARISRKDEIMKAIGKKLDRYRNPWLELKIQY-GQNKGKLYNEECDRFMICMIHKLGYGN---WDELKAA 974
Cdd:pfam09111    1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYpPNNKGKTYTEEEDRFLLCMLYKYGYGNedlYEKIKQE 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 334185131   975 FRTSSVFRFDWFVKSRTSQELARRCDTLIRLIEKEN 1010
Cdd:pfam09111   81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
190-404 7.95e-47

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: 167.85  E-value: 7.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  190 RDYQLAGLNWLIrlyENGinGILADEMGLGKTLQTISL-LAYLHEYRGINGPHM----------------VVAPKSTLGN 252
Cdd:cd18008     2 LPYQKQGLAWML---PRG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLSQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  253 WMNEIRRFC--PVLRAVKFLGNpeERRHIREDLLvagKFDICVTSFEM----------------AIKEKTALRRFSWRYI 314
Cdd:cd18008    77 WKDEIEKHTkpGSLKVYVYHGS--KRIKSIEELS---DYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  315 IIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLH 394
Cdd:cd18008   152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERLQ 231
                         250
                  ....*....|
gi 334185131  395 KVLRPFLLRR 404
Cdd:cd18008   232 ALLKPILLRR 241
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
192-404 3.54e-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: 165.57  E-value: 3.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 271
Cdd:cd18055     4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  272 NPEERRHIRE------DLLVAG-------------KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKT 332
Cdd:cd18055    84 DKDSRAIIREnefsfdDNAVKGgkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185131  333 MRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 404
Cdd:cd18055   164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
189-404 1.36e-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: 164.08  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIRED-------LLVAGK------------FDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLL 329
Cdd:cd18057    81 YTGDKESRSVIRENefsfednAIRSGKkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185131  330 SKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 404
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
189-404 3.92e-44

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: 159.40  E-value: 3.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 268
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILL-TGIRGPFLIIAPLSTIANWEREFRTWTD-LNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIREDLLV-----------AGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFS 337
Cdd:cd18061    79 YHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
189-404 2.06e-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: 157.92  E-value: 2.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 268
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  269 FLGNPEERRHIRE------DLLVAG-------------KFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLL 329
Cdd:cd18056    81 YVGDKDSRAIIREnefsfeDNAIRGgkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334185131  330 SKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 404
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ---IKKLHDMLGPHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
189-404 2.78e-41

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: 152.15  E-value: 2.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLA------------YLHEYRGINGPH--------MVVAPKS 248
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrENNRPRFKKKPPassakkpvLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  249 TLGNWMNEIRRFCPvLRAVKFLGNPEERrhIREDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSL 328
Cdd:cd18005    81 VLYNWKDELDTWGH-FEVGVYHGSRKDD--ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  329 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ------------QEVVQQLHKV 396
Cdd:cd18005   158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQrhtatarelrlgRKRKQELAVK 237

                  ....*...
gi 334185131  397 LRPFLLRR 404
Cdd:cd18005   238 LSKFFLRR 245
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
189-404 2.86e-37

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: 140.50  E-value: 2.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWL----IRLYENGING-ILADEMGLGKTLQTISLLAYLHEYRGINGPH----MVVAPKSTLGNWMNEIRR 259
Cdd:cd18004     1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  260 FCPvLRAVKFL---GNPEERRHIREDLLVAGKFDICVTSFEMaikektaLRRFSWRYI--------IIDEAHRIKNENSL 328
Cdd:cd18004    81 WLG-LRRIKVVtadGNAKDVKASLDFFSSASTYPVLIISYET-------LRRHAEKLSkkisidllICDEGHRLKNSESK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  329 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQ---QEVVQQLHKV 396
Cdd:cd18004   153 TTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdpdASEEDKelgAERSQELSEL 232

                  ....*...
gi 334185131  397 LRPFLLRR 404
Cdd:cd18004   233 TSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
211-378 2.62e-34

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: 131.64  E-value: 2.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  211 ILADEMGLGKTLQTISLL-AYLHEYRGINGPhMVVAPKSTLGNWMNEIRRFCPVlRAVKFLGNPEERRHIRED------- 282
Cdd:cd18007    30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKWLPP-DLRPLLVLVSLSASKRADarlrkin 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  283 -------LLVAGkfdicVTSFEMAIKEKTALRRFSWRY-----------IIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 344
Cdd:cd18007   108 kwhkeggVLLIG-----YELFRNLASNATTDPRLKQEFiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILL 182
                         170       180       190
                  ....*....|....*....|....*....|....
gi 334185131  345 TGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF 378
Cdd:cd18007   183 TGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
188-380 3.09e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.75  E-value: 3.09e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131    188 KMRDYQLAGLNWLIRLYENGIngiLADEMGLGKTLQ-TISLLAYLHeyRGINGPHMVVAP-KSTLGNWMNEIRRFCP--V 263
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGPslG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131    264 LRAVKFLGNPEERRHIREdlLVAGKFDICVTSFEMAIK--EKTALRRFSWRYIIIDEAHRIKNEN---SLLSKTMRLFST 338
Cdd:smart00487   83 LKVVGLYGGDSKREQLRK--LESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGfgdQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 334185131    339 NYRLLITGTPLQNNLHELWALLNflLPEIFSSAETFDEWFQI 380
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPIEQ 200
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
191-374 3.70e-28

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: 113.07  E-value: 3.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  191 DYQLAGLNWLIRlyeNGINGILADEMGLGKTLQTISLLAYLHEyrgiNGPHMVVAPKSTLGNWMNEIRRFCPVLravkfl 270
Cdd:cd18010     3 PFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPSL------ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  271 gNPEERRHIR--EDLLVAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSK-TMRLF-STNYRLLITG 346
Cdd:cd18010    70 -PPDDIQVIVksKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKaALPLLkRAKRVILLSG 148
                         170       180
                  ....*....|....*....|....*...
gi 334185131  347 TPLQNNLHELWALLNFLLPEIFSSAETF 374
Cdd:cd18010   149 TPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
205-404 1.43e-26

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: 109.48  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  205 ENGINGILADEMGLGKTLQTISLLAYlheyrginGPHMVVAPKSTLGNWMNEIRRFC-PVLRAVKFLGNPEERRHIREdl 283
Cdd:cd18071    46 ELVRGGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVkPGQLKVYTYHGGERNRDPKL-- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  284 lvAGKFDICVTSF-----EMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWA 358
Cdd:cd18071   116 --LSKYDIVLTTYntlasDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 334185131  359 LLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRR 404
Cdd:cd18071   194 LLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
504-604 4.92e-25

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: 100.36  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   504 ERDSRVLIFSQMTRLLDilEDYLMYR-GYLYCRIDGNTGGDERDASIEAYNKpgsEKFVFLLSTRAGGLGINLATADVVI 582
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDVAERGLDLPDVDLVI 87
                           90       100
                   ....*....|....*....|..
gi 334185131   583 LYDSDWNPQVDLQAQDRAHRIG 604
Cdd:pfam00271   88 NYDLPWNPASYIQRIGRAGRAG 109
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
192-404 5.45e-23

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: 99.09  E-value: 5.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISLLAY--------------------LHEYRGI--NGPHMVVAPKS 248
Cdd:cd18072     4 HQKQALAWLLwRERQKPRGGILADDMGLGKTLTMIALILAqkntqnrkeeekekalteweSKKDSTLvpSAGTLVVCPAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  249 TLGNWMNEIRRFCP--VLRAVKFLGNPEERRHiredlLVAGKFDICVTSFEMAIKE---------KTALRRFSWRYIIID 317
Cdd:cd18072    84 LVHQWKNEVESRVAsnKLRVCLYHGPNRERIG-----EVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  318 EAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisgENDQQEVVQQLHKVL 397
Cdd:cd18072   159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV----DNKSRKGGERLNILT 234

                  ....*..
gi 334185131  398 RPFLLRR 404
Cdd:cd18072   235 KSLLLRR 241
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
189-404 6.38e-23

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: 99.08  E-value: 6.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYEN----GING-ILADEMGLGKTLQTISLLAYLHEYRGINGPH----MVVAPKSTLGNWMNEIrr 259
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGrrirGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANEL-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  260 fcpvlraVKFLGN-----PEERRHIREDLLVAGKF----------DICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKN 324
Cdd:cd18067    79 -------GKWLGGrlqplAIDGGSKKEIDRKLVQWasqqgrrvstPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  325 ENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQ 392
Cdd:cd18067   152 SDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpilkgrdadASEKERQlgeEKLQE 231
                         250
                  ....*....|..
gi 334185131  393 LHKVLRPFLLRR 404
Cdd:cd18067   232 LISIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
211-379 1.06e-22

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 97.99  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  211 ILADEMGLGKTLQTISLLAYLHEyRGINGPH------MVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPEerrHIREDLL 284
Cdd:cd18066    28 ILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQD---HKVEEFI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  285 VAGKFDICVTSFEMAIKEKTALRRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLL 364
Cdd:cd18066   104 ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVN 183
                         170
                  ....*....|....*
gi 334185131  365 PEIFSSAETFDEWFQ 379
Cdd:cd18066   184 PGILGSLSTYRKVYE 198
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
207-378 2.14e-22

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 97.65  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  207 GINGILADEMGLGKTLQTISLL--AYLHEYRGINGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFL--------GNPEER 276
Cdd:cd18068    28 GSGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDEEKIevnelatyKRPQER 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  277 RHIREDLLVAGkfDICVTSFEM--------AIKEKTALRRFSWRY--------IIIDEAHRIKNENSLLSKTMRLFSTNY 340
Cdd:cd18068   108 SYKLQRWQEEG--GVMIIGYDMyrilaqerNVKSREKLKEIFNKAlvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKR 185
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 334185131  341 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF 378
Cdd:cd18068   186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
189-376 3.45e-22

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 95.82  E-value: 3.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLYENGIngILADEMGLGKTLQTISLLAYLhEYRGINGPHMVVAPKSTLGNWMNEIRRF--CPVLRA 266
Cdd:cd18011     1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQDKfgLPFLIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  267 VKFLGNPEERRHIRedllVAGKFDICVTSFEMA---IKEKTALRRFSWRYIIIDEAHRIKNEN----SLLSKTMRLFS-- 337
Cdd:cd18011    78 DRETAAQLRRLIGN----PFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLAkr 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 334185131  338 TNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDE 376
Cdd:cd18011   154 ARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
HELICc smart00490
helicase superfamily c-terminal domain;
520-604 3.63e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 3.63e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131    520 DILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNKPgseKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDR 599
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 334185131    600 AHRIG 604
Cdd:smart00490   78 AGRAG 82
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
189-403 1.01e-21

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: 95.87  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIRLyengiNGILADEMGLGKTLQTISLL------------AYLHEYRGINGPHM-------------V 243
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDClvaetpvsskatlI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  244 VAPKSTLGNWMNEIRRFCPV-LRAVKFLG---NPEERRHIREDLLVAgkfDICVTSFE---------MAIKEKTALRRFS 310
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSsLKVLTYQGvkkDGALASPAPEILAEY---DIVVTTYDvlrtelhyaEANRSNRRRRRQK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  311 -------------WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDE- 376
Cdd:cd18070   153 ryeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARv 232
                         250       260
                  ....*....|....*....|....*..
gi 334185131  377 WFQISGENDQQEvvqQLHKVLRPFLLR 403
Cdd:cd18070   233 LIRPQGRNKARE---PLAALLKELLWR 256
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
192-386 9.37e-20

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: 89.49  E-value: 9.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  192 YQLAGLNWLirlYEN------------GINGILADEMGLGKTLQTISLLAYLHEYRGINGPhMVVAPKSTLGNWMNEIRR 259
Cdd:cd18069     4 HQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTV-LAIVPVNTLQNWLSEFNK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  260 FCPVLRA----------VKFLGNPEERRHIREDLLV--AGKFDICVTSFEMaikektalrrFSWR----YIIIDEAHRIK 323
Cdd:cd18069    80 WLPPPEAlpnvrprpfkVFILNDEHKTTAARAKVIEdwVKDGGVLLMGYEM----------FRLRpgpdVVICDEGHRIK 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185131  324 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ 386
Cdd:cd18069   150 NCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQ 212
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
189-363 2.61e-13

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 70.46  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGLNWLIrlyENGINGILADeMGLGKTLQTISLLAYLHEyRGINGPHMVVAPKSTLGN-WMNEIRRFcPVLRAV 267
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKW-NHLRNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  268 KF---LGNPEERRHiredlLVAGKFDICVTSFEMA---IKEKtaLRRFSWRYIIIDEAHRIKNENSllSKTMRLFSTNYR 341
Cdd:cd18013    75 TVsvaVGTERQRSK-----AANTPADLYVINRENLkwlVNKS--GDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRPV 145
                         170       180
                  ....*....|....*....|....*.
gi 334185131  342 ----LLITGTPLQNNLHELWALLNFL 363
Cdd:cd18013   146 ikrlIGLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
187-704 1.45e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.59  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  187 GKMRDYQLAGLN-WLIRLYENGINGILADEMGLGKTLqtISLLAYLHEYRGinGPHMVVAPKSTLGN-WMNEIRRFcpvL 264
Cdd:COG1061    79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV--LALALAAELLRG--KRVLVLVPRRELLEqWAEELRRF---L 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  265 RAVKFLGNPEERRhiredllvagkFDICVTSFEMAIKEKTaLRRFS--WRYIIIDEAHRIKNENslLSKTMRLFSTNYRL 342
Cdd:COG1061   152 GDPLAGGGKKDSD-----------APITVATYQSLARRAH-LDELGdrFGLVIIDEAHHAGAPS--YRRILEAFPAAYRL 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  343 LITGTPL-QNNLHELWALLNFLLPEIfssaetfdewfqisGENDQQEvvqqlHKVLRPFLLRRLKSDVEKglppkketil 421
Cdd:COG1061   218 GLTATPFrSDGREILLFLFDGIVYEY--------------SLKEAIE-----DGYLAPPEYYGIRVDLTD---------- 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  422 kvgmsqmQKQYYKALLQKDLEAVNAGGERKRLlnIAMQLRKccNHPylfqgaepgppyttgdhlitnagkmvlldkllpk 501
Cdd:COG1061   269 -------ERAEYDALSERLREALAADAERKDK--ILRELLR--EHP---------------------------------- 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  502 lkeRDSRVLIFSQMTRLLDILEDYLMYRGYLYCRIDGNTGGDERDASIEAYNkpgSEKFVFLLSTRAGGLGINLATADVV 581
Cdd:COG1061   304 ---DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDVA 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  582 ILYDSDWNPQVDLQAQDRAHRIGQKKE-VQVFRFCTESAIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVR 660
Cdd:COG1061   378 ILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEV 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 334185131  661 YGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDA 704
Cdd:COG1061   458 KGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKA 501
ResIII pfam04851
Type III restriction enzyme, res subunit;
188-348 3.51e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 53.83  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   188 KMRDYQLAGL-NWLIRLYENGINGILADEMGLGKTLQTISLLAYLHEYRGINgPHMVVAPKSTLGN-WMNEIRRFCPVLR 265
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRKDLLEqALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   266 AVKFLGNPEERRHIREDllvagkFDICVTSFEMAIKE-KTALRRFS---WRYIIIDEAHRiknensLLSKTMR----LFS 337
Cdd:pfam04851   82 EIGEIISGDKKDESVDD------NKIVVTTIQSLYKAlELASLELLpdfFDVIIIDEAHR------SGASSYRnileYFK 149
                          170
                   ....*....|.
gi 334185131   338 TNYRLLITGTP 348
Cdd:pfam04851  150 PAFLLGLTATP 160
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
845-889 1.48e-07

'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: 48.73  E-value: 1.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 334185131  845 TWSRRDFNTFLRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFK 889
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNLL 45
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
757-831 1.89e-07

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: 50.25  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   757 YFKQTLRQGAPAKPKEPRIPRMP---QLHDFQFFNiQRLTELYEKEvryLMQTHQKNQLKDTI-DVEEPEGGD------- 825
Cdd:pfam09110    5 YYKDVLGTGGKKSTTKPKAPRAPkqiNIQDHQFFP-PRLKELQEKE---QLYYKKKIGYKVTLdDGKEEDGEEfeeerea 80
                           90
                   ....*....|....*....
gi 334185131   826 -------------PLTTEE 831
Cdd:pfam09110   81 krkleqeeidnaePLTEEE 99
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
209-347 2.46e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 51.25  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  209 NGILADEMGLGKTLQ-TISLLAYLHEYRGingPHMVVAPKSTLGN-WMNEIR-RFCPVLRAVKFLG--NPEERRHIREDL 283
Cdd:cd00046     3 NVLITAPTGSGKTLAaLLAALLLLLKKGK---KVLVLVPTKALALqTAERLReLFGPGIRVAVLVGgsSAEEREKNKLGD 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334185131  284 LvagkfDICVTSFEMAIKEKTALRRFS---WRYIIIDEAHRI-KNENSLLSKTMRL----FSTNYRLLITGT 347
Cdd:cd00046    80 A-----DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGALILDLAVrkagLKNAQVILLSAT 146
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
843-891 4.73e-07

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 47.22  E-value: 4.73e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 334185131    843 FSTWSRRDFNTFLRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFKER 891
Cdd:smart00717    1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNLLKP 49
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
189-348 7.55e-07

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: 49.61  E-value: 7.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  189 MRDYQLAGL-NWLIRLYENGinGILADEMGLGKTLQTISLLAYLHEYRGIngphmVVAPKSTLGN-WMNEIRRFCPVlRA 266
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKELRTL-----IVVPTDALLDqWKERFEDFLGD-SS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  267 VKFLGNPEERRHIREDLLVAgkfdiCVTSFEMAIKE-KTALRRFSwrYIIIDEAHRIKNENslLSKTMRLFSTNYRLLIT 345
Cdd:cd17926    73 IGLIGGGKKKDFDDANVVVA-----TYQSLSNLAEEeKDLFDQFG--LLIVDEAHHLPAKT--FSEILKELNAKYRLGLT 143

                  ...
gi 334185131  346 GTP 348
Cdd:cd17926   144 ATP 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
557-615 9.70e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.62  E-value: 9.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 334185131  557 SEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQkKEVQVFRFC 615
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DpdE NF041062
protein DpdE;
212-374 3.31e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 48.04  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  212 LADEMGLGKTLQT-ISLLAYLHEYRGINGphMVVAPKSTLGNWMNEIR-RFcpvlravkFLGnpeerrhireDLLVAgkf 289
Cdd:NF041062  175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELRdKF--------FLD----------DFPGA--- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131  290 DICVTSFEMAIKEKTALRRFSwrYIIIDEAHRI-KNENSLLSKTMRLF--------STNYRLLITGTPLQNNLHELWALL 360
Cdd:NF041062  232 RVRVLSHEEPERWEPLLDAPD--LLVVDEAHQLaRLAWSGDPPERARYrelaalahAAPRLLLLSATPVLGNEETFLALL 309
                         170
                  ....*....|....*.
gi 334185131  361 NFLLPEIF--SSAETF 374
Cdd:NF041062  310 HLLDPDLYplDDLEAF 325
AAA_22 pfam13401
AAA domain;
217-348 1.98e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185131   217 GLGKTLqTISLLAYLHEYRGINGPHMVVAPKSTLgnwmneiRRFCPVLraVKFLGNPEERRHIREDLlvagkfdicvtsf 296
Cdd:pfam13401   15 GTGKTT-LLRRLLEQLPEVRDSVVFVDLPSGTSP-------KDLLRAL--LRALGLPLSGRLSKEEL------------- 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334185131   297 eMAIKEKTALRRFSWRYIIIDEAHRIKNEN-SLLSKTMRLFSTNYRLLITGTP 348
Cdd:pfam13401   72 -LAALQQLLLALAVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLILVGTP 123
 
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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