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Conserved domains on  [gi|767957351|ref|XP_011516948|]
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DNA excision repair protein ERCC-6-like 2 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 134-382 2.09e-151

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: 452.99  E-value: 2.09e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 213
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 292
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  293 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 372
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235

                         250
                  ....*....|
gi 767957351  373 KKMSGWFLRR 382
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 118-662 1.44e-126

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 1.44e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  118 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 197
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  198 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 276
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  277 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 356
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  357 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 436
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  437 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 516
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  517 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 596
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767957351  597 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 662
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
 29-84 3.97e-21

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.77  E-value: 3.97e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767957351   29 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 84
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
VIGSSK super family cl20696
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
 1129-1153 7.24e-04

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


The actual alignment was detected with superfamily member pfam14773:

Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.74  E-value: 7.24e-04
                           10        20
                   ....*....|....*....|....*
gi 767957351  1129 VAYIHSNQNVIGSSKAENHMSRWAA 1153
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
 
Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 134-382 2.09e-151

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: 452.99  E-value: 2.09e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 213
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 292
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  293 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 372
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235

                         250
                  ....*....|
gi 767957351  373 KKMSGWFLRR 382
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 118-662 1.44e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 1.44e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  118 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 197
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  198 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 276
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  277 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 356
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  357 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 436
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  437 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 516
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  517 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 596
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767957351  597 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 662
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 127-667 6.97e-70

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 254.73  E-value: 6.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  127 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 206
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  207 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 279
Cdd:PLN03142  220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 359
Cdd:PLN03142  295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  360 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 439
Cdd:PLN03142  369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  440 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 519
Cdd:PLN03142  426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  520 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 598
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767957351  599 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQLHCVVV 667
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 137-473 1.83e-65

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: 223.33  E-value: 1.83e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   137 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 215
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   216 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 289
Cdd:pfam00176   57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   290 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 369
Cdd:pfam00176  137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   370 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 449
Cdd:pfam00176  206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265

                          330       340
                   ....*....|....*....|....
gi 767957351   450 ETVKTLYLSYLTVLQKVANHVALL 473
Cdd:pfam00176  266 REIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 517-643 3.01e-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: 190.77  E-value: 3.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  517 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 596
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767957351  597 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLI 643
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 519-632 1.85e-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: 107.68  E-value: 1.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   519 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 598
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75

                           90       100       110
                   ....*....|....*....|....*....|....
gi 767957351   599 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 632
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
134-323 1.43e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.87  E-value: 1.43e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    134 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 213
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    214 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 286
Cdd:smart00487   60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 767957351    287 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 323
Cdd:smart00487  140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
549-632 6.83e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 6.83e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    549 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 628
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 767957351    629 YRIG 632
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
 29-84 3.97e-21

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.77  E-value: 3.97e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767957351   29 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 84
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
91-313 4.87e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.05  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   91 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 169
Cdd:COG1061    42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  170 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 248
Cdd:COG1061   117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  249 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 313
Cdd:COG1061   165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
 1129-1153 7.24e-04

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.74  E-value: 7.24e-04
                           10        20
                   ....*....|....*....|....*
gi 767957351  1129 VAYIHSNQNVIGSSKAENHMSRWAA 1153
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
 
Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 134-382 2.09e-151

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: 452.99  E-value: 2.09e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 213
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 292
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  293 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 372
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235

                         250
                  ....*....|
gi 767957351  373 KKMSGWFLRR 382
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 118-662 1.44e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 1.44e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  118 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 197
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  198 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 276
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  277 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 356
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  357 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 436
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  437 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 516
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  517 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 596
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767957351  597 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 662
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 134-331 6.28e-71

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: 234.38  E-value: 6.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrsmkkeplsstakKMFLI 213
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKER-------------------------GPVLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIRVK--QRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKN 290
Cdd:cd17919    56 VCPLSVLENWEREFEKWtPDLRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKN 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767957351  291 PKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVP 331
Cdd:cd17919   136 PKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 127-667 6.97e-70

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 254.73  E-value: 6.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  127 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 206
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  207 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 279
Cdd:PLN03142  220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 359
Cdd:PLN03142  295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  360 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 439
Cdd:PLN03142  369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  440 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 519
Cdd:PLN03142  426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  520 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 598
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767957351  599 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQLHCVVV 667
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 137-473 1.83e-65

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: 223.33  E-value: 1.83e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   137 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 215
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   216 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 289
Cdd:pfam00176   57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   290 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 369
Cdd:pfam00176  137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   370 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 449
Cdd:pfam00176  206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265

                          330       340
                   ....*....|....*....|....
gi 767957351   450 ETVKTLYLSYLTVLQKVANHVALL 473
Cdd:pfam00176  266 REIKASLLNILMRLRKICNHPGLI 289
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 134-382 5.89e-58

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: 199.52  E-value: 5.89e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefLLRSMkkeplsstakkmfLI 213
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-------------LIKSV-------------LV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRK---DNELIRVKQRKcEIALTTYETLRLCLDELNSLE-----WSAVIVDE 284
Cdd:cd18001    55 VMPTSLIPHWVKEFAKWTPgLRVKVFHGTSKkerERNLERIQRGG-GVLLTTYGMVLSNTEQLSADDhdefkWDYVILDE 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  285 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPG-LLGSGTYFKKQFSDPVEHGQRHTATKRELAT 363
Cdd:cd18001   134 GHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKAL 213

                         250
                  ....*....|....*....
gi 767957351  364 GRKAMQRLAKKMSGWFLRR 382
Cdd:cd18001   214 GSEVAENLRQIIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 517-643 3.01e-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: 190.77  E-value: 3.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  517 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 596
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767957351  597 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLI 643
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 134-384 5.44e-56

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: 193.55  E-value: 5.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 213
Cdd:cd18012     5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR--------------------------KGPSLV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHG-NRKDNELIRVKQRkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNP 291
Cdd:cd18012    59 VAPTSLIYNWEEEAAKFApELKVLVIHGtKRKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  292 KARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkrelatgRKAMQRL 371
Cdd:cd18012   137 QTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEEL 205

                         250
                  ....*....|...
gi 767957351  372 AKKMSGWFLRRTK 384
Cdd:cd18012   206 KKLISPFILRRLK 218
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 134-382 2.48e-51

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: 180.94  E-value: 2.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkKGTREDiennmpefllrsmkkeplSSTAK 208
Cdd:cd18004     1 LRPHQREGVQFLYdcltGRRGYGGgGAILADEMGLGKTLQAIALVWTLL--KQGPYG------------------KPTAK 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  209 KmFLIVAPLSVLYNWKDELDTW-GYFRVTVL--HGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLE-WSAVI 281
Cdd:cd18004    61 K-ALIVCPSSLVGNWKAEFDKWlGLRRIKVVtaDGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKIsIDLLI 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  282 VDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKREL 361
Cdd:cd18004   140 CDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDK 219

                         250       260
                  ....*....|....*....|.
gi 767957351  362 ATGRKAMQRLAKKMSGWFLRR 382
Cdd:cd18004   220 ELGAERSQELSELTSRFILRR 240
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 134-352 1.04e-50

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: 178.60  E-value: 1.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkePlsstakkmFLI 213
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRG-----------------P--------FLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd17995    56 IAPLSTIPNWQREFETWTDMNVVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRV 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQ 352
Cdd:cd17995   136 VVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQ 208
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 134-382 4.87e-49

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: 174.08  E-value: 4.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTR---FLYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPEFLLRSmkkeplsstakkm 210
Cdd:cd17999     1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLCILASDHHKR------ANSFNSENLPS------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  211 fLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHR 287
Cdd:cd17999    59 -LVVCPPTLVGHWVAEIKKYfpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHI 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  288 IKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKA 367
Cdd:cd17999   138 IKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALA 217

                         250
                  ....*....|....*
gi 767957351  368 MQRLAKKMSGWFLRR 382
Cdd:cd17999   218 LEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 134-334 2.88e-44

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: 159.03  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpefllrsmkkeplSSTAKKMFLI 213
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH-------------------------SKLGLGPSLI 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW-GYFRVTVLH----GNRKDNE---------LIRVKQRKCEIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18000    56 VCPATVLKQWVKEFHRWwPPFRVVVLHssgsGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQY 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLL 334
Cdd:cd18000   136 VILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 134-366 9.71e-43

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: 156.30  E-value: 9.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIH-------GGGCILGDDMGLGKTVQVISFLAAVL--HKKGTRediennmpefllrsmkkepls 204
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLaaAPRRSR--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  205 stakkmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNeliRVKQRKCEIA---------LTTYETLR--LCLD 270
Cdd:cd18007    60 ------PLVLCPASTLYNWEDEFKKWlppDLRPLLVLVSLSASK---RADARLRKINkwhkeggvlLIGYELFRnlASNA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  271 ELNSLEWSA------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGT 338
Cdd:cd18007   131 TTDPRLKQEfiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK 210

                         250       260
                  ....*....|....*....|....*...
gi 767957351  339 YFKKQFSDPVEHGQRHTATKRELATGRK 366
Cdd:cd18007   211 EFKKKFVKPIEAGQCVDSTEEDVRLMLK 238
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 134-384 1.32e-39

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: 146.70  E-value: 1.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakkmFLI 213
Cdd:cd17997     4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNI------NGP-------------------HLI 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW-GYFRVTVLHGN-RKDNELIR--VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 289
Cdd:cd17997    59 IVPKSTLDNWMREFKRWcPSLRVVVLIGDkEERADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  290 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHtatkrelatgrKAMQ 369
Cdd:cd17997   139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQ-----------EVVQ 207

                         250
                  ....*....|....*
gi 767957351  370 RLAKKMSGWFLRRTK 384
Cdd:cd17997   208 RLHKVLRPFLLRRIK 222
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 134-332 1.00e-38

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: 144.04  E-value: 1.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtreDIENNMPefllrsmkkeplsstakkmFLI 213
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFH------SQQQYGP-------------------FLV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 284
Cdd:cd17993    57 VVPLSTMPAWQREFAKWApDMNVIVYLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDE 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767957351  285 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPG 332
Cdd:cd17993   137 AHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG 184
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 134-382 3.23e-38

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: 143.06  E-value: 3.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtREDIENNMPefllrsmkkeplssTAK 208
Cdd:cd18066     1 LRPHQREGIEFLYecvmGMRVNERfGAILADEMGLGKTLQCISLIWTLL-----RQGPYGGKP--------------VIK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  209 KMfLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIrvKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEA 285
Cdd:cd18066    62 RA-LIVTPGSLVKNWKKEFQKWlgsERIKVFTVDQDHKVEEFI--ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  286 HRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGR 365
Cdd:cd18066   139 HRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGE 218

                         250
                  ....*....|....*..
gi 767957351  366 KAMQRLAKKMSGWFLRR 382
Cdd:cd18066   219 ARAAELTRLTGLFILRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 134-382 3.93e-37

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: 140.30  E-value: 3.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtrediennmpefllrsmKKEPLSSTAK 208
Cdd:cd18067     1 LRPHQREGVKFLYrcvtGRRIRGShGCIMADEMGLGKTLQCITLMWTLL---------------------RQSPQCKPEI 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  209 KMFLIVAPLSVLYNWKDELDTWGYFRVTVL--HGNRKDNELIRVKQRKCE--------IALTTYETLRLCLDELNSLEWS 278
Cdd:cd18067    60 DKAIVVSPSSLVKNWANELGKWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  279 AVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATK 358
Cdd:cd18067   140 LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASE 219

                         250       260
                  ....*....|....*....|....
gi 767957351  359 RELATGRKAMQRLAKKMSGWFLRR 382
Cdd:cd18067   220 KERQLGEEKLQELISIVNRCIIRR 243
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 134-384 5.54e-36

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: 136.75  E-value: 5.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGT---RFLYGHYIHGggcILGDDMGLGKTVQVISFLAavlhkkgtrediennmpefLLRSMKkeplsstAKKM 210
Cdd:cd18009     4 MRPYQLEGMewlRMLWENGING---ILADEMGLGKTIQTIALLA-------------------HLRERG-------VWGP 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  211 FLIVAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRVKQRK-------CEIALTTYETLRLCLDELNSLEWSAVIV 282
Cdd:cd18009    55 FLVIAPLSTLPNWVNEFARFTpSVPVLLYHGTKEERERLRKKIMKregtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIV 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  283 DEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFsDPVEHGQRhTATKRELA 362
Cdd:cd18009   135 DEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLS 212

                         250       260
                  ....*....|....*....|....
gi 767957351  363 TGRKA--MQRLAKKMSGWFLRRTK 384
Cdd:cd18009   213 EEREQniVHMLHAILKPFLLRRLK 236
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 134-382 4.10e-35

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: 134.34  E-value: 4.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLyghyIHGGGcILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTakkmfLI 213
Cdd:cd18008     1 LLPYQKQGLAWM----LPRGG-ILADEMGLGKTIQAL---ALILATRPQDPKIPEELEENSSDPKKLYLSKTT-----LI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDT---WGYFRVTVLHGNRKdNELIRVKQrKCEIALTTYETLR----------------LCLDELNS 274
Cdd:cd18008    68 VVPLSLLSQWKDEIEKhtkPGSLKVYVYHGSKR-IKSIEELS-DYDIVITTYGTLAsefpknkkgggrdskeKEASPLHR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  275 LEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELW------CVMDWAVPGllgsgtYFKKQFSDPV 348
Cdd:cd18008   146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYsllrflRVEPFGDYP------WFNSDISKPF 219

                         250       260       270
                  ....*....|....*....|....*....|....
gi 767957351  349 EHGQRhtatkrelaTGRKAMQRLAKKMsgwFLRR 382
Cdd:cd18008   220 SKNDR---------KALERLQALLKPI---LLRR 241
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 134-384 7.88e-34

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: 130.18  E-value: 7.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRF---LYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPefllrsmkkeplsstakkm 210
Cdd:cd17996     4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTISLITYLMEKKK------NNGP------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  211 FLIVAPLSVLYNWKDELDTWGYFRVTVLH-GNRKDNELIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHR 287
Cdd:cd17996    56 YLVIVPLSTLSNWVSEFEKWAPSVSKIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  288 IKNPKARVTEVMKALKCN-VRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHtatKRELATGR 365
Cdd:cd17996   136 MKNAQSKLTQTLNTYYHArYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEE 212

                         250       260
                  ....*....|....*....|.
gi 767957351  366 KAM--QRLAKKMSGWFLRRTK 384
Cdd:cd17996   213 TLLiiRRLHKVLRPFLLRRLK 233
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 134-352 1.59e-33

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: 129.16  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSmkkepls 204
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIEslerykgssGFGCILAHSMGLGKTLQVISFL------------------DVLLRH------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  205 sTAKKMFLIVAPLSVLYNWKDELDTW------------GYFRVTVLHGNRKD----NELIRVKQRKCEIALTTYETLRLC 268
Cdd:cd18069    56 -TGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrpRPFKVFILNDEHKTtaarAKVIEDWVKDGGVLLMGYEMFRLR 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  269 LDElnslewSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPV 348
Cdd:cd18069   135 PGP------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI 208


                  ....
gi 767957351  349 EHGQ 352
Cdd:cd18069   209 LNGQ 212
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 134-346 2.28e-33

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: 128.62  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 213
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----------------EIFLMGIRGP---------FLI 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18058    55 IAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSC 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd18058   135 VIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD 201
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 134-382 5.91e-32

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: 124.77  E-value: 5.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPEfllrsmkkeplsstakkmfLI 213
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPH-------------------LI 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW--GyFRVTVLHGNRKDNELIRV---KQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRI 288
Cdd:cd18003    56 VVPTSVMLNWEMEFKRWcpG-FKILTYYGSAKERKLKRQgwmKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  289 KNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP----VEHGQRHTatkrelatg 364
Cdd:cd18003   135 KNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN--------- 205

                         250
                  ....*....|....*...
gi 767957351  365 RKAMQRLAKKMSGWFLRR 382
Cdd:cd18003   206 EELVRRLHKVLRPFLLRR 223
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 134-346 2.60e-31

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: 122.81  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSMKKEPlsstakkmFLI 213
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL------------------YEILLTGIRGP--------FLI 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18061    55 IAPLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRC 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd18061   135 VIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 134-382 3.26e-31

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: 122.81  E-value: 3.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsMKKEPlsstakkmFLI 213
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH-----------------QLYGP--------FLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 284
Cdd:cd18054    76 VVPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  285 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQfsdpveHGQrhtatkrelatG 364
Cdd:cd18054   156 AHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEED------HGK-----------G 218

                         250
                  ....*....|....*....
gi 767957351  365 RK-AMQRLAKKMSGWFLRR 382
Cdd:cd18054   219 REnGYQSLHKVLEPFLLRR 237
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 134-346 8.30e-31

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: 121.31  E-value: 8.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllrsmkKEPLSSTAKKMFLI 213
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------------------------QEVYNVGIHGPFLV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18060    55 IAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRC 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd18060   135 VIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 134-361 1.90e-30

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: 120.92  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsmkkeplssTAKKMFLI 213
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEH-------------------------QLYGPFLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 284
Cdd:cd18053    76 VVPLSTLTSWQREIQTWApQMNAVVYLGDINSRNMIRthewmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  285 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGqrHTATKREL 361
Cdd:cd18053   156 AHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG--YASLHKEL 230
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 134-382 1.98e-30

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: 119.85  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVlhkKGTREDiennmpefllrsmkkeplsstaKKMFLI 213
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYL---AGRLKL----------------------LGPFLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE----IALTTYEtlrLCLDE---LNSLEWSAVIVDEAH 286
Cdd:cd18006    56 LCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAH 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  287 RIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTY--FKKQFSDpvehgqrhtaTKRELATg 364
Cdd:cd18006   133 RLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSE----------TDDESET- 201

                         250
                  ....*....|....*...
gi 767957351  365 rkaMQRLAKKMSGWFLRR 382
Cdd:cd18006   202 ---VEELHLLLQPFLLRR 216
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 134-346 5.23e-30

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: 118.98  E-value: 5.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 213
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLY-----------------EIYLKGIHGP---------FLV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18059    55 IAPLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRC 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd18059   135 VVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 134-346 2.10e-29

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: 116.38  E-value: 2.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllRSMKKEplsSTAKKMFLI 213
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------------------YSLYKE---GHSKGPFLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHGNrkdnelirvkqrkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 292
Cdd:cd17994    56 SAPLSTIINWEREFEMWApDFYVVTYVGD--------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQ 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767957351  293 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd17994   122 SKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 134-382 1.29e-28

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: 115.29  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDiennmpefllrsmkkeplsstakkmFLI 213
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGP-------------------------FLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVD 283
Cdd:cd18002    56 IAPASTLHNWQQEISRFvPQFKVLPYWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLD 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  284 EAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVE-HGQRHTATKREla 362
Cdd:cd18002   136 EAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH-- 213

                         250       260
                  ....*....|....*....|
gi 767957351  363 tgrkAMQRLAKKMSGWFLRR 382
Cdd:cd18002   214 ----QLKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 124-395 3.83e-28

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: 114.38  E-value: 3.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  124 DSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkepl 203
Cdd:cd18064     6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYR--------NIP------------ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  204 sstakKMFLIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIR--VKQRKCEIALTTYETLRLCLDELNSLEWSA 279
Cdd:cd18064    66 -----GPHMVLVPKSTLHNWMAEFKRWvPTLRAVCLIGDKDQRAaFVRdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  280 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtatKR 359
Cdd:cd18064   141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TN 208

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767957351  360 ELATGRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKE 395
Cdd:cd18064   209 NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 519-632 1.85e-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: 107.68  E-value: 1.85e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   519 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 598
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75

                           90       100       110
                   ....*....|....*....|....*....|....
gi 767957351   599 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 632
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 134-352 4.52e-27

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: 110.92  E-value: 4.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 213
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-LYKEGH------------------------SKGPYLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVK----------------------QRKCEIALTTYETLRLCLD 270
Cdd:cd18057    56 SAPLSTIINWEREFEMWAPdFYVVTYTGDKESRSVIRENefsfednairsgkkvfrmkkeaQIKFHVLLTSYELITIDQA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  271 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 350
Cdd:cd18057   136 ILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKE 215


                  ..
gi 767957351  351 GQ 352
Cdd:cd18057   216 DQ 217
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 134-347 1.49e-26

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: 108.83  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHyihGGGCILGDDMGLGKTVQVISFLAAVlhkkgtrediENNMPefllrsmkkeplsstakkmFLI 213
Cdd:cd18010     1 LLPFQREGVCFALRR---GGRVLIADEMGLGKTVQAIAIAAYY----------REEWP-------------------LLI 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW----GYFRVTVLHGNRkdnELIRVKQRKceIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 289
Cdd:cd18010    49 VCPSSLRLTWADEIERWlpslPPDDIQVIVKSK---DGLRDGDAK--VVIVSYDLLRRLEKQLLARKFKVVICDESHYLK 123

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  290 NPKA-RVTEVMKALK-CNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP 347
Cdd:cd18010   124 NSKAkRTKAALPLLKrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 134-346 2.03e-26

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: 108.95  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 213
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH------------------------TKGPFLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 270
Cdd:cd18055    56 SAPLSTIINWEREFQMWApdfyvvtytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767957351  271 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 346
Cdd:cd18055   136 ALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 130-384 1.50e-25

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: 107.07  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  130 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPefllrsmkkeplsstakk 209
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK------RLNGP------------------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  210 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 286
Cdd:cd18063    76 -YLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTpamRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  287 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 364
Cdd:cd18063   155 RMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETIL- 233

                         250       260
                  ....*....|....*....|
gi 767957351  365 rkAMQRLAKKMSGWFLRRTK 384
Cdd:cd18063   234 --IIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 134-384 1.77e-25

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 106.26  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkeplsstakKMFLI 213
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYR--------NIP-----------------GPHMV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 289
Cdd:cd18065    71 LVPKSTLHNWMNEFKRWvPSLRAVCLIGDKDARAaFIRDVMMPGEwdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  290 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtaTKRELATgRKAMQ 369
Cdd:cd18065   151 NEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVE 218

                         250
                  ....*....|....*
gi 767957351  370 RLAKKMSGWFLRRTK 384
Cdd:cd18065   219 RLHAVLKPFLLRRIK 233
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 134-352 1.91e-25

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: 106.30  E-value: 1.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 213
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS-LYKEGH------------------------SKGPFLV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 270
Cdd:cd18056    56 SAPLSTIINWEREFEMWApdmyvvtyvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  271 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 350
Cdd:cd18056   136 ILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKE 215


                  ..
gi 767957351  351 GQ 352
Cdd:cd18056   216 DQ 217
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 134-331 2.33e-25

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: 104.39  E-value: 2.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpeFLLRSMKKEPlsstakkmFLI 213
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA------------------YLKEIGIPGP--------HLV 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRV----KQRKCEIALTTYETLRLCLDE---LNSLEWSAVIVDEA 285
Cdd:cd17998    55 VVPSSTLDNWLREFKRWCpSLKVEPYYGSQEERKHLRYdilkGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEG 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767957351  286 HRIKNPKA-RVTEVMKaLKCNVRIGLTGTILQNNMKELWCVMDWAVP 331
Cdd:cd17998   135 HMLKNMTSeRYRHLMT-INANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 134-361 5.26e-25

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 105.36  E-value: 5.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLAAVL-HKKgtREDIennmpefllrsmkkepl 203
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCEslkktkkspGSGCILAHCMGLGKTLQVVTFLHTVLlCEK--LENF----------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  204 sstakKMFLIVAPLSVLYNWKDELDTWgyfrvtvLHGNRKDN-----ELIRVK------------QRKCEIALTTYETLR 266
Cdd:cd18068    62 -----SRVLVVCPLNTVLNWLNEFEKW-------QEGLKDEEkievnELATYKrpqersyklqrwQEEGGVMIIGYDMYR 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  267 LCLDELN-SLEWSA---------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAV 330
Cdd:cd18068   130 ILAQERNvKSREKLkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209

                         250       260       270
                  ....*....|....*....|....*....|.
gi 767957351  331 PGLLGSGTYFKKQFSDPVEHGQRHTATKREL 361
Cdd:cd18068   210 PNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 150-382 7.27e-25

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 104.47  E-value: 7.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  150 IHGGgcILGDDMGLGKTVQVISFLAAvlhkkgtrediennmpefllrsmkkeplsstakKMFLIVAPLSVLYNWKDELD- 228
Cdd:cd18071    48 VRGG--ILADDMGLGKTLTTISLILA---------------------------------NFTLIVCPLSVLSNWETQFEe 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  229 --TWGYFRVTVLHG---NRKDNELIrvkqrKCEIALTTYETLrlCLDE-------LNSLEWSAVIVDEAHRIKNPKARVT 296
Cdd:cd18071    93 hvKPGQLKVYTYHGgerNRDPKLLS-----KYDIVLTTYNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  297 EVMKALKCNVRIGLTGTILQNNMKELWCVMdwavpgllgsgTYFK-KQFSDPvEHGQRhtATKRELATG-RKAMQRLAKK 374
Cdd:cd18071   166 KAVLNLSSERRWVLTGTPIQNSPKDLGSLL-----------SFLHlKPFSNP-EYWRR--LIQRPLTMGdPTGLKRLQVL 231


                  ....*...
gi 767957351  375 MSGWFLRR 382
Cdd:cd18071   232 MKQITLRR 239
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 130-384 1.63e-24

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 103.97  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  130 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakk 209
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRI------NGP------------------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  210 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 286
Cdd:cd18062    76 -FLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSpaaRRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  287 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 364
Cdd:cd18062   155 RMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL- 233

                         250       260
                  ....*....|....*....|
gi 767957351  365 rkAMQRLAKKMSGWFLRRTK 384
Cdd:cd18062   234 --IIRRLHKVLRPFLLRRLK 251
DEXDc smart00487
DEAD-like helicases superfamily;
134-323 1.43e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.87  E-value: 1.43e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    134 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 213
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    214 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 286
Cdd:smart00487   60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 767957351    287 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 323
Cdd:smart00487  140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
549-632 6.83e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 6.83e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351    549 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 628
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 767957351    629 YRIG 632
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
 29-84 3.97e-21

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.77  E-value: 3.97e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767957351   29 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 84
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 154-323 8.42e-20

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: 89.85  E-value: 8.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  154 GCILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTAKKMFLIVAPLSVLYNWKDELDT---W 230
Cdd:cd18072    22 GGILADDMGLGKTLTMI---ALILAQKNTQNRKEEEKEKALTEWESKKDSTLVPSAGTLVVCPASLVHQWKNEVESrvaS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  231 GYFRVTVLHGNRKDNelIRVKQRKCEIALTTYETL---------RLCLDELNSLEWSAVIVDEAHRIKNPKARVTEVMKA 301
Cdd:cd18072    99 NKLRVCLYHGPNRER--IGEVLRDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176

                         170       180
                  ....*....|....*....|..
gi 767957351  302 LKCNVRIGLTGTILQNNMKELW 323
Cdd:cd18072   177 LRAHARWALTGTPIQNNLLDMY 198
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 134-322 9.50e-18

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: 84.32  E-value: 9.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYghyIHGGgcILGDDMGLGKTVQVISFLAAvlHkkgTREDIENNMPEFLLRSMKKEPLSSTAKKMF-- 211
Cdd:cd18070     1 LLPYQRRAVNWML---VPGG--ILADEMGLGKTVEVLALILL--H---PRPDNDLDAADDDSDEMVCCPDCLVAETPVss 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  212 ---LIVAPLSVLYNWKDELD--TWGYFRVTVLHGNRKDNELIRVKQRK---CEIALTTYETLRLCLDE------------ 271
Cdd:cd18070    71 katLIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALASPAPEIlaeYDIVVTTYDVLRTELHYaeanrsnrrrrr 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767957351  272 ----------LNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKEL 322
Cdd:cd18070   151 qkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDL 211
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 134-323 5.05e-16

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 78.55  E-value: 5.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHyiHGGGCILgdDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkeplsstakkmFLI 213
Cdd:cd18013     1 PHPYQKVAINFIIEH--PYCGLFL--DMGLGKTVTTLTALSDLQLDDFTRR--------------------------VLV 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  214 VAPLSVLYN-WKDELDTWGYFR---VTVLHGNRKdnELIRVKQRKCEIALTTYETLR-LCLDELNSLEWSAVIVDEAHRI 288
Cdd:cd18013    51 IAPLRVARStWPDEVEKWNHLRnltVSVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSF 128

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767957351  289 KNPKARVTEVMKALKCNVR--IGLTGTILQNNMKELW 323
Cdd:cd18013   129 KSPRSKRFKALRKVRPVIKrlIGLTGTPSPNGLMDLW 165
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 134-333 3.06e-14

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: 72.71  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREgtrFLYGHYIHG-GGCILGDDMGLGKTVQVisflAAVLHkkgtrediennmpEFLLRSMKKEplsstakkmFL 212
Cdd:cd18011     1 PLPHQID---AVLRALRKPpVRLLLADEVGLGKTIEA----GLIIK-------------ELLLRGDAKR---------VL 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  213 IVAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE--IALTTYETLR---LCLDELNSLEWSAVIVDEAHR 287
Cdd:cd18011    52 ILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHK 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767957351  288 IKN----PKARVTEVMKALKCNVR--IGLTGTILQNNMKELWCVMDWAVPGL 333
Cdd:cd18011   132 LRNsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPGR 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
91-313 4.87e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.05  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   91 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 169
Cdd:COG1061    42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  170 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 248
Cdd:COG1061   117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767957351  249 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 313
Cdd:COG1061   165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
ResIII pfam04851
Type III restriction enzyme, res subunit;
134-313 2.90e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 59.99  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   134 LRDYQREGTRFLYGHYIHG--GGCIlgdDM--GLGKTVqVISFLAAVLHKKGTrediennmpefllrsmkkeplsstaKK 209
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTL-TAAKLIARLFKKGP-------------------------IK 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   210 MFLIVAP-LSVLYNWKDELDTWG---YFRVTVLHGNRKDNElirvkQRKCEIALTTYETL----RLCLDELNSLEWSAVI 281
Cdd:pfam04851   55 KVLFLVPrKDLLEQALEEFKKFLpnyVEIGEIISGDKKDES-----VDDNKIVVTTIQSLykalELASLELLPDFFDVII 129

                          170       180       190
                   ....*....|....*....|....*....|..
gi 767957351   282 VDEAHRIKNPKARvtEVMKALKCNVRIGLTGT 313
Cdd:pfam04851  130 IDEAHRSGASSYR--NILEYFKPAFLLGLTAT 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 134-313 7.06e-09

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: 55.77  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  134 LRDYQREGTRFLYGHYIHGGGCIlgdDM--GLGKTVqvISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmF 211
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTL--TALALIAYLKELR----------------------------T 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  212 LIVAP-LSVLYNWKDELDTWGYFR-VTVLHGNRKDnelirvKQRKCEIALTTYETLRLCLDELNSL--EWSAVIVDEAHR 287
Cdd:cd17926    48 LIVVPtDALLDQWKERFEDFLGDSsIGLIGGGKKK------DFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHH 121

                         170       180
                  ....*....|....*....|....*.
gi 767957351  288 IKNPKARvtEVMKALKCNVRIGLTGT 313
Cdd:cd17926   122 LPAKTFS--EILKELNAKYRLGLTAT 145
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 32-83 8.79e-09

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 52.25  E-value: 8.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767957351   32 GERCLAPSPDNGKLCEASIKSITVDENGksfAVVLYADF-QERKIPLKQLQEV 83
Cdd:cd21182     1 GDKCLAPYSDDGKYYEATIEEITEESDT---ATVVFDGYgNSEEVPLSDLKPL 50
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
 205-315 6.59e-08

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 53.46  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  205 STAKKMFLIVAPLSV-LYNWKDELDTWGYF---RVTVLHGNRKDnelirvKQRKCEIALTTYETLR----------LCLD 270
Cdd:cd18029    48 CTIKKSTLVLCTSAVsVEQWRRQFLDWTTIddeQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFME 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767957351  271 ELNSLEWSAVIVDEAHRIKNPKARvtEVMKALKCNVRIGLTGTIL 315
Cdd:cd18029   122 FITEREWGLIILDEVHVVPAPMFR--RVLTLQKAHCKLGLTATLV 164
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 152-313 2.70e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 51.25  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  152 GGGCILGDDMGLGKTvqVISFLAAVLHkkgtrediennmpefllrsmkkepLSSTAKKmFLIVAPLSVL-YNWKDELDTW 230
Cdd:cd00046     1 GENVLITAPTGSGKT--LAALLAALLL------------------------LLKKGKK-VLVLVPTKALaLQTAERLREL 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  231 GYF--RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSL---EWSAVIVDEAHRIKnPKARVTEVMKALKCN 305
Cdd:cd00046    54 FGPgiRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALL-IDSRGALILDLAVRK 132

                         170
                  ....*....|....
gi 767957351  306 V------RIGLTGT 313
Cdd:cd00046   133 AglknaqVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
515-653 9.73e-07

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 53.20  E-value: 9.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  515 PKYSGKMKVLQQLLNhcrKNRD-KVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEFnSTQ 585
Cdd:COG1111   335 PKLSKLREILKEQLG---TNPDsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERF-RAG 410

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767957351  586 DVNIcLVSTMAGGLGLNFVGANVVVLFDPTWNPandLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMY 653
Cdd:COG1111   411 EFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRDEAYY 474
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 591-633 5.07e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 42.69  E-value: 5.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767957351  591 LVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQ 633
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
 1129-1153 7.24e-04

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.74  E-value: 7.24e-04
                           10        20
                   ....*....|....*....|....*
gi 767957351  1129 VAYIHSNQNVIGSSKAENHMSRWAA 1153
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 208-314 1.52e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351   208 KKMFLIVAPLSVL-YNWKDELDTWGYF---RVTVLHGNRKDNELIRvKQRKCEIALTTYETLRLCLDE---LNSLEWsaV 280
Cdd:pfam00270   45 GPQALVLAPTRELaEQIYEELKKLGKGlglKVASLLGGDSRKEQLE-KLKGPDILVGTPGRLLDLLQErklLKNLKL--L 121

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767957351   281 IVDEAHRI--KNPKARVTEVMKALKCNVRI-GLTGTI 314
Cdd:pfam00270  122 VLDEAHRLldMGFGPDLEEILRRLPKKRQIlLLSATL 158
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 209-322 2.15e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 40.40  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767957351  209 KMFLIVAPLSVLYNWK-DELDTWGY--FRVTVLHG--NRKDNELirvkqRKCEIALTTYETLrlclDEL--NSLEW---- 277
Cdd:cd18028    46 GKALYLVPLRALASEKyEEFKKLEEigLKVGISTGdyDEDDEWL-----GDYDIIVATYEKF----DSLlrHSPSWlrdv 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767957351  278 SAVIVDEAHRIKNPK-ARVTEV----MKALKCNVR-IGLTGTIlqNNMKEL 322
Cdd:cd18028   117 GVVVVDEIHLISDEErGPTLESivarLRRLNPNTQiIGLSATI--GNPDEL 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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