|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
19-1043 |
0e+00 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 1992.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 19 SEEEQNHHINDQDDDDELQAVACSPSSGDDDNLPDVDLDADDNEPDEGNVVP---EISRREKARLREMQQIKKQKIQEML 95
Cdd:PLN03142 1 EEEQVNTQANEEEDEEELEAVARSAGSDSDDDEVPAEDEDEDEEDDEEAESPakaEISKREKARLKELKKQKKQEIQKIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 96 DAQNAAIDSDMNNKGKGRLKYLLQQTELFAHFAKGDQSSSQKKTKGRGRHASKVTEEEEDEEYLKEEEDGL---ASTRLL 172
Cdd:PLN03142 81 EQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHASKLTEEEEDEEYLKEEEDGLggsGGTRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 173 TQPSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRR 252
Cdd:PLN03142 161 VQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 253 FCPVLRAVKFLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTN 332
Cdd:PLN03142 241 FCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 333 YRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKET 412
Cdd:PLN03142 321 YRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 413 ILKVGMSQMQKQYYKALLQKDLEVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGDHLITNAGKMVLMDKLL 492
Cdd:PLN03142 401 ILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 493 PKLKERDSRVLIFSQMTRLLDILEDYLMFRGYQYCRIDGNTGGEDRDASIEAYNKPGSEKFVFLLSTRAGGLGINLATAD 572
Cdd:PLN03142 481 PKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATAD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 573 VVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMV 652
Cdd:PLN03142 561 IVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMV 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 653 RFGAEMVFSSKDNTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDD--EKDENKFDFKKIVSENW 730
Cdd:PLN03142 641 RYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDedDKDENKLDFKKIVSDNW 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 731 VEPPKRERKRNYSESEYFKQTLRQGGPTKPKEPRIPRMPQLHDFQFFNTQRLSELYEKEVRYLMQTHQKNQLQDSIDVDE 810
Cdd:PLN03142 721 IDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 811 PEEMGYPLTVEESEEKEHLLEKGFSSWTRKDFNTFIRACEKYGRNDIKGIASEMEGKAEEEVERYAKVFKERYKELSDYD 890
Cdd:PLN03142 801 PEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYD 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 891 RIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMICMVHKLGYGNWDELKAAFRTSP 970
Cdd:PLN03142 881 RIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGNWDELKAAFRTSP 960
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785442294 971 LFRFDWFVKSRTTQELTRRCDTLIRLVEKENQEYDERERQARKEKKLAKSMtTPSKRALPRQ-TESPSQKKRKQ 1043
Cdd:PLN03142 961 LFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKKLAKNA-TPSKRPSGRQaNESPSSLKKRK 1033
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
14-633 |
1.02e-149 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 462.00 E-value: 1.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 14 EPLSDSEEEQNHHINDQDDDDELQAVACSPSSGDDDNLPDVDLDADDNEPDEGNVVPEISRREKARLREMQQIKKQKIQE 93
Cdd:COG0553 70 LALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 94 MLDAQNAAIDSDMNNKGKGRLKYLLQQTELFAHFAKGDQSSSQKKTKGRGRHASKVTEEEEDEEYLKEEEDGLASTRLLT 173
Cdd:COG0553 150 LLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLRE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 174 Q----PSCIQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNE 249
Cdd:COG0553 230 AleslPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 250 IRRFCPVLRAVKFLGNPDERRHIREnllvAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLY 329
Cdd:COG0553 309 LAKFAPGLRVLVLDGTRERAKGANP----FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 330 NTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 409
Cdd:COG0553 385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEK 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 410 KETILKVGMSQMQKQYYKALLQK-DLEVVNAGGERKRLLNIA--MQLRKCCNHPYLFqgAEPGPPYTTGDhlitnaGKMV 486
Cdd:COG0553 465 TEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRGLILAalTRLRQICSHPALL--LEEGAELSGRS------AKLE 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 487 LMDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYQYCRIDGNTGGEDRDASIEAYNKpGSEKFVFLLSTRAGGLGI 566
Cdd:COG0553 537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGL 615
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 567 NLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 633
Cdd:COG0553 616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
179-399 |
2.73e-138 |
|
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: 414.80 E-value: 2.73e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 179 QGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLR 258
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 259 AVKFLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLIT 338
Cdd:cd17997 81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785442294 339 GTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQI-SGENDQQEVVQQLHKVLRPFLLRRLK 399
Cdd:cd17997 161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
185-463 |
2.40e-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: 2.40e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 185 YQLAGLNWLIRLYEN-GINGILADEMGLGKTLQTISLLGYLHEFRGITG-PHMVVAPKSTLGNWMNEIRRFC--PVLRAV 260
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 261 KFLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGT 340
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 341 PLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGEN-DQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMS 419
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785442294 420 QMQKQYYKA-LLQKDLEVVNAGGE----RKRLLNIAMQLRKCCNHPYLF 463
Cdd:pfam00176 241 KLQRKLYQTfLLKKDLNAIKTGEGgreiKASLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
169-410 |
4.11e-105 |
|
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: 328.55 E-value: 4.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 169 TRLLTQPSCIQ-GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWM 247
Cdd:cd18064 2 TRFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 248 NEIRRFCPVLRAVKFLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMR 327
Cdd:cd18064 82 AEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 328 LYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 407
Cdd:cd18064 162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLP 241
|
...
gi 1785442294 408 PKK 410
Cdd:cd18064 242 PKK 244
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
180-399 |
3.64e-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: 315.09 E-value: 3.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 180 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 259
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 260 VKFLGNPDERRHIRENLL----VAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRL 335
Cdd:cd18009 81 LLYHGTKEERERLRKKIMkregTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785442294 336 LITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGEND------------QQEVVQQLHKVLRPFLLRRLK 399
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDnaadisnlseerEQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
180-399 |
6.65e-98 |
|
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: 308.91 E-value: 6.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 180 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 259
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 260 VKFLGNPDERRHIrENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTM-RLYNTNYRLLIT 338
Cdd:cd17996 82 IVYKGTPDVRKKL-QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 339 GTPLQNNLHELWALLNFLLPEVFSSAETFDEWF----QISGENDQQE--------VVQQLHKVLRPFLLRRLK 399
Cdd:cd17996 161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFntpfANTGEQVKIElneeetllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
170-399 |
1.58e-97 |
|
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: 308.10 E-value: 1.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 170 RLLTQPSCIQG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMN 248
Cdd:cd18065 3 RFEESPSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 249 EIRRFCPVLRAVKFLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRL 328
Cdd:cd18065 83 EFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785442294 329 YNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLK 399
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 ... |
182-397 |
1.83e-87 |
|
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350761 [Multi-domain] Cd Length: 223 Bit Score: 280.39 E-value: 1.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTP 341
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 342 LQNNLHELWALLNFLLPEVFSSAETFDEWFQ-------ISGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
182-361 |
2.73e-85 |
|
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: 272.90 E-value: 2.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLVaGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTP 341
Cdd:cd17919 81 YHGSQRERAQIRAKEKL-DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
170 180
....*....|....*....|
gi 1785442294 342 LQNNLHELWALLNFLLPEVF 361
Cdd:cd17919 160 LQNNLEELWALLDFLDPPFL 179
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
182-397 |
4.81e-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: 254.87 E-value: 4.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 261
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPD--ERRHIRENLLV---------AGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYN 330
Cdd:cd17995 80 YHGSGEsrQIIQQYEMYFKdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---GDLKTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
181-397 |
8.42e-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: 254.20 E-value: 8.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 181 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 260
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 261 KFLGNPDERRHIRENLLVAG-----KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRL 335
Cdd:cd17993 81 VYLGDIKSRDTIREYEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785442294 336 LITGTPLQNNLHELWALLNFLLPEVFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd17993 161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE----EHDEEQEKGIADLHKELEPFILRR 218
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
182-397 |
2.68e-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: 242.03 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENL------LVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRL 335
Cdd:cd18002 81 YWGNPKDRKVLRKFWdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785442294 336 LITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGEND-------QQEVVQQLHKVLRPFLLRR 397
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHaenktglNEHQLKRLHMILKPFMLRR 229
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
182-397 |
4.84e-70 |
|
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: 232.71 E-value: 4.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTP 341
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 342 LQNNLHELWALLNFLLPEVFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18006 161 IQNSLQELYALLSFIEPNVFPK-DKLDDFIKAYSEtDDESETVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
178-399 |
2.75e-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: 2.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 178 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 257
Cdd:cd18062 20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 258 RAVKFLGNPDERRHIREnLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMrlyNTNY---- 333
Cdd:cd18062 100 VKVSYKGSPAARRAFVP-QLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785442294 334 RLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQ----ISGE----NDQQE--VVQQLHKVLRPFLLRRLK 399
Cdd:cd18062 176 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGEkvdlNEEETilIIRRLHKVLRPFLLRRLK 251
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
178-399 |
4.16e-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: 230.14 E-value: 4.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 178 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 257
Cdd:cd18012 1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 258 RAVKFLGNPDERRHIREnllvAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLI 337
Cdd:cd18012 80 KVLVIHGTKRKREKLRA----LEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 338 TGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQ-QEVVQQLHKVLRPFLLRRLK 399
Cdd:cd18012 156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdEEALEELKKLISPFILRRLK 218
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
178-399 |
2.41e-68 |
|
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: 229.18 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 178 IQGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 257
Cdd:cd18063 20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 258 RAVKFLGNPDERRHIRENLLvAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMrlyNTNY---- 333
Cdd:cd18063 100 VKISYKGTPAMRRSLVPQLR-SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785442294 334 RLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQ----ISGE----NDQQE--VVQQLHKVLRPFLLRRLK 399
Cdd:cd18063 176 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfaMTGErvdlNEEETilIIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
171-397 |
1.31e-66 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350812 [Multi-domain] Cd Length: 237 Bit Score: 223.73 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 171 LLTQPSCIQGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWM 247
Cdd:cd18054 7 LKKQPSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 248 NEIRRFCPVLRAVKFLGNPDERRHIRENLLVAG-----KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLL 322
Cdd:cd18054 87 REFEIWAPEINVVVYIGDLMSRNTIREYEWIHSqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785442294 323 SKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDqqevVQQLHKVLRPFLLRR 397
Cdd:cd18054 167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRR 237
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
182-361 |
1.16e-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: 219.18 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLV-AGKFDVCVTSFEMVI---KEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLI 337
Cdd:cd17998 80 YYGSQEERKHLRYDILKgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
|
170 180
....*....|....*....|....
gi 1785442294 338 TGTPLQNNLHELWALLNFLLPEVF 361
Cdd:cd17998 160 TGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
174-397 |
3.87e-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: 202.97 E-value: 3.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 174 QPSCIQG----KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNE 249
Cdd:cd18053 9 QPSYIGGheglELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 250 IRRFCPVLRAVKFLGNPDERRHIRENLLVAG-----KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSK 324
Cdd:cd18053 89 IQTWAPQMNAVVYLGDINSRNMIRTHEWMHPqtkrlKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 325 TMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18053 169 TLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
483-608 |
3.70e-56 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 190.38 E-value: 3.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 483 GKMVLMDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMFRGYQYCRIDGNTGGEDRDASIEAYNKPGSEkFVFLLSTRAG 562
Cdd:cd18793 11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1785442294 563 GLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 608
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
185-397 |
4.39e-53 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350752 [Multi-domain] Cd Length: 196 Bit Score: 184.18 E-value: 4.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 185 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 264
Cdd:cd17994 4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 265 NpderrhirenllvagkfDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQN 344
Cdd:cd17994 84 D-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 345 NLHELWALLNFLLPEVFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 397
Cdd:cd17994 147 NLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 196
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
184-397 |
1.63e-52 |
|
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: 183.73 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 184 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEfRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFL 263
Cdd:cd18001 3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFD-SGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 264 G-NPDERRHIRENllVAGKFDVCVTSFEMVIKEKSAL-----RRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLI 337
Cdd:cd18001 82 GtSKKERERNLER--IQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785442294 338 TGTPLQNNLHELWALLNFLLP-EVFSSAETFDEWFQ--ISGENDQ----------QEVVQQLHKVLRPFLLRR 397
Cdd:cd18001 160 TGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFEnpITRGRDKdatqgekalgSEVAENLRQIIKPYFLRR 232
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
182-397 |
5.62e-52 |
|
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: 182.17 E-value: 5.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH-----EFRGITGPHMVVAPKSTLGNWMNEIRRFCP- 255
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHhkranSFNSENLPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 256 -VLRAVKFLGNPDERRHIRENLlvaGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYR 334
Cdd:cd17999 81 aFLKPLAYVGPPQERRRLREQG---EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785442294 335 LLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWF---------QISGENDQQEVVQ---QLHKVLRPFLLRR 397
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrdSKASAKEQEAGALaleALHKQVLPFLLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
182-397 |
1.94e-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: 177.54 E-value: 1.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 261
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLV-----------AGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYN 330
Cdd:cd18058 79 YHGSQISRQMIQQYEMYyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF---GDLKTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
182-397 |
3.22e-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: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFrGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 261
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRE---------NLLVAG--KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYN 330
Cdd:cd18060 79 YHGSLASRQMIQQyemyckdsrGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRR 222
|
|
| SLIDE |
pfam09111 |
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ... |
890-1001 |
4.60e-49 |
|
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: 169.24 E-value: 4.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 890 DRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQY-GQNKGKLYNEECDRFMICMVHKLGYGN---WDELKAA 965
Cdd:pfam09111 1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYpPNNKGKTYTEEEDRFLLCMLYKYGYGNedlYEKIKQE 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1785442294 966 FRTSPLFRFDWFVKSRTTQELTRRCDTLIRLVEKEN 1001
Cdd:pfam09111 81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
182-397 |
3.97e-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: 3.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLgYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 261
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIR---------ENLLVAG--KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYN 330
Cdd:cd18059 79 YHGSQASRRTIQlyemyfkdpQGRVIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
185-397 |
7.48e-48 |
|
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: 170.58 E-value: 7.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 185 YQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFLG 264
Cdd:cd18055 4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 265 NPDERRHIRENLL------VAG-------------KFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKT 325
Cdd:cd18055 84 DKDSRAIIRENEFsfddnaVKGgkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785442294 326 MRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 397
Cdd:cd18055 164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
184-358 |
7.09e-47 |
|
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: 166.35 E-value: 7.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 184 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV--- 260
Cdd:cd18000 3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVvlh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 261 ---KFLGNPDERRHIRENLL----VAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNY 333
Cdd:cd18000 83 ssgSGTGSEEKLGSIERKSQlirkVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
|
170 180
....*....|....*....|....*
gi 1785442294 334 RLLITGTPLQNNLHELWALLNFLLP 358
Cdd:cd18000 163 RLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
183-397 |
9.17e-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: 9.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 183 RDYQLAGLNWLIrlyENGinGILADEMGLGKTLQTISL-LGYLHEFRGITGPHM----------------VVAPKSTLGN 245
Cdd:cd18008 2 LPYQKQGLAWML---PRG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 246 WMNEIRRFC--PVLRAVKFLGNpdeRRHIRENLLVagKFDVCVTSFEMV----------------IKEKSALRRFSWRYI 307
Cdd:cd18008 77 WKDEIEKHTkpGSLKVYVYHGS---KRIKSIEELS--DYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 308 VIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLH 387
Cdd:cd18008 152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERLQ 231
|
250
....*....|
gi 1785442294 388 KVLRPFLLRR 397
Cdd:cd18008 232 ALLKPILLRR 241
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
182-397 |
1.40e-46 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350815 [Multi-domain] Cd Length: 232 Bit Score: 166.78 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIREN-------LLVAGK------------FDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLL 322
Cdd:cd18057 81 YTGDKESRSVIRENefsfednAIRSGKkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785442294 323 SKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 397
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
182-397 |
9.40e-45 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350814 [Multi-domain] Cd Length: 232 Bit Score: 161.77 E-value: 9.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 261
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLL-------------------VAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLL 322
Cdd:cd18056 81 YVGDKDSRAIIRENEFsfednairggkkasrmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785442294 323 SKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRR 397
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ---IKKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
182-397 |
2.76e-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: 159.79 E-value: 2.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAVK 261
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEIL-LTGIRGPFLIIAPLSTIANWEREFRTWTD-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 262 FLGNPDERRHIRENLLV-----------AGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYN 330
Cdd:cd18061 79 YHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
182-397 |
1.48e-40 |
|
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: 149.84 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLG------------YLHEFRGITGPH--------MVVAPKS 241
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrENNRPRFKKKPPassakkpvLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 242 TLGNWMNEIRRFCPvLRAVKFLGNPDERrhIRENLLVAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSL 321
Cdd:cd18005 81 VLYNWKDELDTWGH-FEVGVYHGSRKDD--ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 322 LSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQ------------QEVVQQLHKV 389
Cdd:cd18005 158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQrhtatarelrlgRKRKQELAVK 237
|
....*...
gi 1785442294 390 LRPFLLRR 397
Cdd:cd18005 238 LSKFFLRR 245
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
182-397 |
1.72e-36 |
|
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: 138.19 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWL----IRLYENGING-ILADEMGLGKTLQTISLLGYLHEFRGITGPH----MVVAPKSTLGNWMNEIRR 252
Cdd:cd18004 1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 253 FCPvLRAVKFL---GNPDERRHIRENLLVAGKFDVCVTSFEMvikeksaLRRFSWRYI--------VIDEAHRIKNENSL 321
Cdd:cd18004 81 WLG-LRRIKVVtadGNAKDVKASLDFFSSASTYPVLIISYET-------LRRHAEKLSkkisidllICDEGHRLKNSESK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 322 LSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQI---------SGENDQ---QEVVQQLHKV 389
Cdd:cd18004 153 TTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdpdASEEDKelgAERSQELSEL 232
|
....*...
gi 1785442294 390 LRPFLLRR 397
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 ... |
204-371 |
3.37e-33 |
|
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: 128.56 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 204 ILADEMGLGKTLQTISLL-GYLHEFRGITGPhMVVAPKSTLGNWMNEIRRFCPvlravkflgnPDERR-HIRENLLVAGK 281
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKWLP----------PDLRPlLVLVSLSASKR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 282 FDVCV-----------------TSFEMVIKEKSALRRFSWRY-----------IVIDEAHRIKNENSLLSKTMRLYNTNY 333
Cdd:cd18007 99 ADARLrkinkwhkeggvlligyELFRNLASNATTDPRLKQEFiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785442294 334 RLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWF 371
Cdd:cd18007 179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
181-373 |
8.72e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 117.59 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 181 KMRDYQLAGLNWLIRLYENGIngiLADEMGLGKTLQ-TISLLGYLHEFRGitGPHMVVAP-KSTLGNWMNEIRRFCP--V 256
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRDVI---LAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPtRELAEQWAEELKKLGPslG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 257 LRAVKFLGNPDERRHIREnlLVAGKFDVCVTSFEMVIK--EKSALRRFSWRYIVIDEAHRIKNEN---SLLSKTMRLYNT 331
Cdd:smart00487 83 LKVVGLYGGDSKREQLRK--LESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGfgdQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785442294 332 NYRLLITGTPLQNNLHELWALLNflLPEVFSSAETFDEWFQI 373
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPIEQ 200
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
198-397 |
1.98e-27 |
|
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: 111.79 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 198 ENGINGILADEMGLGKTLQTISLLgylhefrgITGPHMVVAPKSTLGNWMNEIRRFC-PVlrAVKFLGNPDERRHIRENL 276
Cdd:cd18071 46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVkPG--QLKVYTYHGGERNRDPKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 277 LvaGKFDVCVTSFEMVIKEKSA-----LRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWA 351
Cdd:cd18071 116 L--SKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1785442294 352 LLNFLLPEVFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRR 397
Cdd:cd18071 194 LLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
483-597 |
8.23e-27 |
|
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: 105.76 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 483 GKMVLMDKLLPKlkERDSRVLIFSQMTRLLDilEDYLMFR-GYQYCRIDGNTGGEDRDASIEAYNKpgsEKFVFLLSTRA 561
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1785442294 562 GGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIG 597
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
184-367 |
1.68e-25 |
|
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: 105.36 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 184 DYQLAGLNWLIRlyeNGINGILADEMGLGKTLQTISLLGYLHEfrgiTGPHMVVAPKSTLGNWMNEIRRFCPVLravkfl 263
Cdd:cd18010 3 PFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPSL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 264 gNPDErrhirENLLVAGK-------FDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSK-TMRLY-NTNYR 334
Cdd:cd18010 70 -PPDD-----IQVIVKSKdglrdgdAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKaALPLLkRAKRV 143
|
170 180 190
....*....|....*....|....*....|...
gi 1785442294 335 LLITGTPLQNNLHELWALLNFLLPEVFSSAETF 367
Cdd:cd18010 144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
185-397 |
3.61e-24 |
|
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: 102.56 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 185 YQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISLL--------------------GYLHEFRGITGPH--MVVAPKS 241
Cdd:cd18072 4 HQKQALAWLLwRERQKPRGGILADDMGLGKTLTMIALIlaqkntqnrkeeekekalteWESKKDSTLVPSAgtLVVCPAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 242 TLGNWMNEIRRFCP--VLRAVKFLGNPDERrhIRENLlvaGKFDVCVTSFEMVIKE---------KSALRRFSWRYIVID 310
Cdd:cd18072 84 LVHQWKNEVESRVAsnKLRVCLYHGPNRER--IGEVL---RDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 311 EAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFqisgENDQQEVVQQLHKVL 390
Cdd:cd18072 159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV----DNKSRKGGERLNILT 234
|
....*..
gi 1785442294 391 RPFLLRR 397
Cdd:cd18072 235 KSLLLRR 241
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
204-372 |
6.93e-23 |
|
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: 98.76 E-value: 6.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 204 ILADEMGLGKTLQTISLLGYLHEfRGITGPH------MVVAPKSTLGNWMNEIRRFCPVLRAVKFLGNPDerrHIRENLL 277
Cdd:cd18066 28 ILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQD---HKVEEFI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 278 VAGKFDVCVTSFEMVIKEKSALRRFSWRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLL 357
Cdd:cd18066 104 ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVN 183
|
170
....*....|....*
gi 1785442294 358 PEVFSSAETFDEWFQ 372
Cdd:cd18066 184 PGILGSLSTYRKVYE 198
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
182-397 |
1.68e-22 |
|
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: 97.93 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYEN----GING-ILADEMGLGKTLQTISLLGYLHEFRGITGPH----MVVAPKSTLGNWMNEI-- 250
Cdd:cd18067 1 LRPHQREGVKFLYRCVTGrrirGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELgk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 251 ---RRFCPV----------LRAVKFLGNPDERRHIRENLLVagkfdvcvtSFEMVIKEKSALRRFSWRYIVIDEAHRIKN 317
Cdd:cd18067 81 wlgGRLQPLaidggskkeiDRKLVQWASQQGRRVSTPVLII---------SYETFRLHVEVLQKGEVGLVICDEGHRLKN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 318 ENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQI---------SGENDQQ---EVVQQ 385
Cdd:cd18067 152 SDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpilkgrdadASEKERQlgeEKLQE 231
|
250
....*....|..
gi 1785442294 386 LHKVLRPFLLRR 397
Cdd:cd18067 232 LISIVNRCIIRR 243
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
513-597 |
1.73e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.27 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 513 DILEDYLMFRGYQYCRIDGNTGGEDRDASIEAYNKPgseKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDR 592
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 1785442294 593 AHRIG 597
Cdd:smart00490 78 AGRAG 82
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
182-369 |
1.36e-21 |
|
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: 93.89 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLYENGIngILADEMGLGKTLQTISLLGYLhEFRGITGPHMVVAPKSTLGNWMNEIRRF--CPVLRA 259
Cdd:cd18011 1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQDKfgLPFLIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 260 VKFLGNPDERRHIRenllVAGKFDVCVTSFEMV---IKEKSALRRFSWRYIVIDEAHRIKNEN----SLLSKTMRLY--N 330
Cdd:cd18011 78 DRETAAQLRRLIGN----PFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLakR 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785442294 331 TNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDE 369
Cdd:cd18011 154 ARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
200-371 |
1.85e-21 |
|
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: 94.95 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 200 GINGILADEMGLGKTLQTISLLG--YLHEFRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFL--------GNPDER 269
Cdd:cd18068 28 GSGCILAHCMGLGKTLQVVTFLHtvLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDEEKIevnelatyKRPQER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 270 RHIRENLLVAGkfDVCVTSFEMV--------IKEKSALRRFSWRY--------IVIDEAHRIKNENSLLSKTMRLYNTNY 333
Cdd:cd18068 108 SYKLQRWQEEG--GVMIIGYDMYrilaqernVKSREKLKEIFNKAlvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKR 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785442294 334 RLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWF 371
Cdd:cd18068 186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
185-379 |
8.75e-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: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 185 YQLAGLNWLirlYEN------------GINGILADEMGLGKTLQTISLLGYLheFRGITGPH-MVVAPKSTLGNWMNEIR 251
Cdd:cd18069 4 HQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLSEFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 252 RFCPVLRA----------VKFLGNPDERRHIRENLLV--AGKFDVCVTSFEMvikeksalrrFSWR----YIVIDEAHRI 315
Cdd:cd18069 79 KWLPPPEAlpnvrprpfkVFILNDEHKTTAARAKVIEdwVKDGGVLLMGYEM----------FRLRpgpdVVICDEGHRI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785442294 316 KNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDEWFQISGENDQ 379
Cdd:cd18069 149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQ 212
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
182-396 |
5.71e-19 |
|
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: 87.78 E-value: 5.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIRLyengiNGILADEMGLGKTLQTISLL------------GYLHEFRGITGPHM-------------V 236
Cdd:cd18070 1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDClvaetpvsskatlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 237 VAPKSTLGNWMNEIRRFCPV-LRAVKFLGNPDE---RRHIRENLLVAgkfDVCVTSFEMVIKE---------KSALRRFS 303
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDgalASPAPEILAEY---DIVVTTYDVLRTElhyaeanrsNRRRRRQK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 304 -------------WRYIVIDEAHRIKNENSLLSKTMRLYNTNYRLLITGTPLQNNLHELWALLNFLLPEVFSSAETFDE- 369
Cdd:cd18070 153 ryeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARv 232
|
250 260
....*....|....*....|....*..
gi 1785442294 370 WFQISGENDQQEvvqQLHKVLRPFLLR 396
Cdd:cd18070 233 LIRPQGRNKARE---PLAALLKELLWR 256
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
182-356 |
4.02e-14 |
|
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: 72.77 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGLNWLIrlyENGINGILADeMGLGKTLQTISLLGYLHeFRGITGPHMVVAPKSTLGN-WMNEIRRFcPVLRAV 260
Cdd:cd18013 1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKW-NHLRNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 261 KF---LGNPDERRHirenlLVAGKFDVCVTSFEMVIK-EKSALRRFSWRYIVIDEAHRIKNENSLLSK-TMRLYNTNYRL 335
Cdd:cd18013 75 TVsvaVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKaLRKVRPVIKRL 149
|
170 180
....*....|....*....|..
gi 1785442294 336 L-ITGTPLQNNLHELWALLNFL 356
Cdd:cd18013 150 IgLTGTPSPNGLMDLWAQIALL 171
|
|
| HAND |
pfam09110 |
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ... |
747-833 |
1.97e-13 |
|
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: 67.58 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 747 YFKQTLRQGGPTKPKEPRIPRMP---QLHDFQFFNTqRLSELYEKEvryLMQTHQKNQLQ---DSIDVDEPEEMGY---- 816
Cdd:pfam09110 5 YYKDVLGTGGKKSTTKPKAPRAPkqiNIQDHQFFPP-RLKELQEKE---QLYYKKKIGYKvtlDDGKEEDGEEFEEerea 80
|
90 100 110
....*....|....*....|....*....|
gi 1785442294 817 -------------PLTVEESEEKEHLLEKG 833
Cdd:pfam09110 81 krkleqeeidnaePLTEEEEAEKEELLSEG 110
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
180-754 |
1.52e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 65.05 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 180 GKMRDYQLAGLN-WLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITgphmVVAPKSTLGN-WMNEIRRFcpvL 257
Cdd:COG1061 79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVL----VLVPRRELLEqWAEELRRF---L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 258 RAVKFLGNPDERRhirenllvagkFDVCVTSFEMVIKEKSaLRRFS--WRYIVIDEAHRIKNENslLSKTMRLYNTNYRL 335
Cdd:COG1061 152 GDPLAGGGKKDSD-----------APITVATYQSLARRAH-LDELGdrFGLVIIDEAHHAGAPS--YRRILEAFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 336 LITGTPL-QNNLHELWALLnfllpevfssaetfdewFQISGENDQQEVVQQlhKVLRPFLLRRLKSDVEKglppkketil 414
Cdd:COG1061 218 GLTATPFrSDGREILLFLF-----------------DGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTD---------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 415 kvgmsqmQKQYYKALLQKDLEVVNAGGERKRLlnIAMQLRKccNHPylfqgaepgppyttgdhlitnagkmvlmdkllpk 494
Cdd:COG1061 269 -------ERAEYDALSERLREALAADAERKDK--ILRELLR--EHP---------------------------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 495 lkeRDSRVLIFSQMTRLLDILEDYLMFRGYQYCRIDGNTGGEDRDASIEAYNkpgSEKFVFLLSTRAGGLGINLATADVV 574
Cdd:COG1061 304 ---DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDVA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 575 ILYDSDWNPQVDLQAQDRAHRIGQKKE-VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELLQMVR 653
Cdd:COG1061 378 ILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 654 FGAEMVFSSKDNTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDEKDENKFDFKKIVSENWVEP 733
Cdd:COG1061 458 KGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
|
570 580
....*....|....*....|.
gi 1785442294 734 PKRERKRNYSESEYFKQTLRQ 754
Cdd:COG1061 538 LLELLAALLRLEELAALLLKE 558
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
181-341 |
1.08e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 49.59 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 181 KMRDYQLAGL-NWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEFRGITgPHMVVAPKSTLGN-WMNEIRRFCPVLR 258
Cdd:pfam04851 3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 259 AVKFLGNPDERRHIRENllvagkFDVCVTSFEMVIKE-KSALRRFS---WRYIVIDEAHRiknensLLSKTMR---LYNT 331
Cdd:pfam04851 82 EIGEIISGDKKDESVDD------NKIVVTTIQSLYKAlELASLELLpdfFDVIIIDEAHR------SGASSYRnilEYFK 149
|
170
....*....|.
gi 1785442294 332 NYRLL-ITGTP 341
Cdd:pfam04851 150 PAFLLgLTATP 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
182-341 |
3.00e-06 |
|
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: 48.07 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 182 MRDYQLAGL-NWLIRLYENGinGILADEMGLGKTLQTISLLGYLHEFRGItgphmVVAPKSTLGN-WMNEIRRFCPVlRA 259
Cdd:cd17926 1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKELRTL-----IVVPTDALLDqWKERFEDFLGD-SS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 260 VKFLGNPDERRHIRENLLVAgkfdvCVTSFEMVIKE-KSALRRFSwrYIVIDEAHRIKNENslLSKTMRLYNTNYRLLIT 338
Cdd:cd17926 73 IGLIGGGKKKDFDDANVVVA-----TYQSLSNLAEEeKDLFDQFG--LLIVDEAHHLPAKT--FSEILKELNAKYRLGLT 143
|
...
gi 1785442294 339 GTP 341
Cdd:cd17926 144 ATP 146
|
|
| DpdE |
NF041062 |
protein DpdE; |
205-367 |
7.74e-06 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 50.36 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 205 LADEMGLGKTLQT-ISLLGYLHEFRGITGphMVVAPKSTLGNWMNEIR-RFcpvlravkFLGN-PDERrhirenllvagk 281
Cdd:NF041062 175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELRdKF--------FLDDfPGAR------------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 282 fdVCVTSFEMVIKEKSALRRFSwrYIVIDEAHRI-KNENSLLSKTMRLYN--------TNYRLLITGTPLQNNLHELWAL 352
Cdd:NF041062 233 --VRVLSHEEPERWEPLLDAPD--LLVVDEAHQLaRLAWSGDPPERARYRelaalahaAPRLLLLSATPVLGNEETFLAL 308
|
170
....*....|....*..
gi 1785442294 353 LNFLLPEVF--SSAETF 367
Cdd:NF041062 309 LHLLDPDLYplDDLEAF 325
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
202-340 |
8.67e-06 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 46.63 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785442294 202 NGILADEMGLGKTLqtISLLGYLHEFRGITGPHMVVAPKSTLGN-WMNEIR-RFCPVLRAVKFLG--NPDERRHIRENLL 277
Cdd:cd00046 3 NVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPTKALALqTAERLReLFGPGIRVAVLVGgsSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785442294 278 vagkfDVCVTSFEMVIKEKSALRRFS---WRYIVIDEAHRI-KNENSLLSKTMRLYN----TNYRLLITGT 340
Cdd:cd00046 81 -----DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGALILDLAVRKaglkNAQVILLSAT 146
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
836-880 |
9.19e-06 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 43.72 E-value: 9.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1785442294 836 SWTRKDFNTFIRACEKYGRNDIKGIASEMEGKAEEEVERYAKVFK 880
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRERWRNLL 45
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
550-608 |
9.68e-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: 9.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785442294 550 SEKFVFLLSTRAGGLGINLATADVVILYDSDWNPQVDLQAQDRAHRIGQkKEVQVFRFC 608
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
836-882 |
2.70e-05 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 42.21 E-value: 2.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1785442294 836 SWTRKDFNTFIRACEKYGRNDIKGIASEMEGKAEEEVERYAKVFKER 882
Cdd:smart00717 3 EWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRERWRNLLKP 49
|
|
| |
