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Conserved domains on  [gi|1577429142|ref|NP_001010895|]
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DNA excision repair protein ERCC-6-like 2 isoform c [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 ...
123-371 5.73e-156

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: 450.68  E-value: 5.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                         250
                  ....*....|
gi 1577429142 362 KKMSGWFLRR 371
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-651 1.42e-130

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.53  E-value: 1.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429142 586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 651
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 6.41e-22

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: 89.31  E-value: 6.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142  18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
 
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 ...
123-371 5.73e-156

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: 450.68  E-value: 5.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                         250
                  ....*....|
gi 1577429142 362 KKMSGWFLRR 371
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-651 1.42e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.53  E-value: 1.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429142 586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 651
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
116-656 2.24e-74

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 259.73  E-value: 2.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  116 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 195
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  196 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 268
Cdd:PLN03142   220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 348
Cdd:PLN03142   295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  349 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 428
Cdd:PLN03142   369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  429 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 508
Cdd:PLN03142   426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  509 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 587
Cdd:PLN03142   472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQLHCVVV 656
Cdd:PLN03142   552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-462 5.21e-66

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: 219.48  E-value: 5.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 126 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 204
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 205 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:pfam00176  57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 358
Cdd:pfam00176 137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 359 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 438
Cdd:pfam00176 206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265
                         330       340
                  ....*....|....*....|....
gi 1577429142 439 ETVKTLYLSYLTVLQKVANHVALL 462
Cdd:pfam00176 266 REIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
506-632 1.43e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 188.45  E-value: 1.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 506 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1577429142 586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLI 632
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
508-621 5.29e-27

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 105.76  E-value: 5.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 508 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 587
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1577429142 588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 621
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
123-312 4.72e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.56  E-value: 4.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  123 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:smart00487   9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  203 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 275
Cdd:smart00487  60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1577429142  276 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 312
Cdd:smart00487 140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 6.41e-22

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: 89.31  E-value: 6.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142  18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
HELICc smart00490
helicase superfamily c-terminal domain;
538-621 6.99e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.96  E-value: 6.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  538 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 617
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 1577429142  618 YRIG 621
Cdd:smart00490  79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
80-302 2.28e-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: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  80 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 158
Cdd:COG1061    42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 159 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 237
Cdd:COG1061   117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 238 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 302
Cdd:COG1061   165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
 
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 ...
123-371 5.73e-156

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: 450.68  E-value: 5.73e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005    76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005   156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                         250
                  ....*....|
gi 1577429142 362 KKMSGWFLRR 371
Cdd:cd18005   236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-651 1.42e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.53  E-value: 1.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553   226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553   292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553   435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553   494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553   532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1577429142 586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQL 651
Cdd:COG0553   611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
116-656 2.24e-74

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 259.73  E-value: 2.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  116 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 195
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  196 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 268
Cdd:PLN03142   220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 348
Cdd:PLN03142   295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  349 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 428
Cdd:PLN03142   369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  429 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 508
Cdd:PLN03142   426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  509 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 587
Cdd:PLN03142   472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQIYKQQLHCVVV 656
Cdd:PLN03142   552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
123-320 6.04e-72

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: 231.30  E-value: 6.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrsmkkeplsstakKMFLI 202
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKER-------------------------GPVLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIRVK--QRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKN 279
Cdd:cd17919    56 VCPLSVLENWEREFEKWtPDLRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKN 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1577429142 280 PKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVP 320
Cdd:cd17919   136 PKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-462 5.21e-66

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: 219.48  E-value: 5.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 126 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 204
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 205 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:pfam00176  57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 358
Cdd:pfam00176 137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 359 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 438
Cdd:pfam00176 206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265
                         330       340
                  ....*....|....*....|....
gi 1577429142 439 ETVKTLYLSYLTVLQKVANHVALL 462
Cdd:pfam00176 266 REIKASLLNILMRLRKICNHPGLI 289
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
123-371 2.98e-59

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: 2.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefLLRSMkkeplsstakkmfLI 202
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-------------LIKSV-------------LV 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRK---DNELIRVKQRKcEIALTTYETLRLCLDELNSLE-----WSAVIVDE 273
Cdd:cd18001    55 VMPTSLIPHWVKEFAKWTPgLRVKVFHGTSKkerERNLERIQRGG-GVLLTTYGMVLSNTEQLSADDhdefkWDYVILDE 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPG-LLGSGTYFKKQFSDPVEHGQRHTATKRELAT 352
Cdd:cd18001   134 GHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKAL 213
                         250
                  ....*....|....*....
gi 1577429142 353 GRKAMQRLAKKMSGWFLRR 371
Cdd:cd18001   214 GSEVAENLRQIIKPYFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
123-373 1.27e-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: 192.01  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:cd18012     5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR--------------------------KGPSLV 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHG-NRKDNELIRVKQRkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNP 280
Cdd:cd18012    59 VAPTSLIYNWEEEAAKFApELKVLVIHGtKRKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNP 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 281 KARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkrelatgRKAMQRL 360
Cdd:cd18012   137 QTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEEL 205
                         250
                  ....*....|...
gi 1577429142 361 AKKMSGWFLRRTK 373
Cdd:cd18012   206 KKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
506-632 1.43e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 188.45  E-value: 1.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 506 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1577429142 586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLI 632
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
123-371 1.84e-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: 178.63  E-value: 1.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkKGTREDiennmpefllrsmkkeplSSTAK 197
Cdd:cd18004     1 LRPHQREGVQFLYdcltGRRGYGGgGAILADEMGLGKTLQAIALVWTLL--KQGPYG------------------KPTAK 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 198 KmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLE-WSAVI 270
Cdd:cd18004    61 K-ALIVCPSSLVGNWKAEFDKWlglRRIKVVTADGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKIsIDLLI 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 271 VDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKREL 350
Cdd:cd18004   140 CDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDK 219
                         250       260
                  ....*....|....*....|.
gi 1577429142 351 ATGRKAMQRLAKKMSGWFLRR 371
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; ...
123-341 1.98e-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: 175.13  E-value: 1.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkePlsstakkmFLI 202
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRG-----------------P--------FLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd17995    56 IAPLSTIPNWQREFETWTDMNVVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRV 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQ 341
Cdd:cd17995   136 VVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQ 208
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
123-371 2.91e-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: 172.54  E-value: 2.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTR---FLYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPEFLLRSmkkeplsstakkm 199
Cdd:cd17999     1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLCILASDHHKR------ANSFNSENLPS------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 200 fLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHR 276
Cdd:cd17999    59 -LVVCPPTLVGHWVAEIKKYfpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 277 IKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKA 356
Cdd:cd17999   138 IKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALA 217
                         250
                  ....*....|....*
gi 1577429142 357 MQRLAKKMSGWFLRR 371
Cdd:cd17999   218 LEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
123-323 1.48e-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: 158.26  E-value: 1.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpefllrsmkkeplSSTAKKMFLI 202
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH-------------------------SKLGLGPSLI 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW-GYFRVTVLH----GNRKDNE---------LIRVKQRKCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18000    56 VCPATVLKQWVKEFHRWwPPFRVVVLHssgsGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQY 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLL 323
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 ...
123-355 1.45e-42

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 153.99  E-value: 1.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIH-------GGGCILGDDMGLGKTVQVISFLAAVL--HKKGTRediennmpefllrsmkkepls 193
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLaaAPRRSR--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 194 stakkmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNeliRVKQRKCEIA---------LTTYETLR--LCLD 259
Cdd:cd18007    60 ------PLVLCPASTLYNWEDEFKKWlppDLRPLLVLVSLSASK---RADARLRKINkwhkeggvlLIGYELFRnlASNA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 260 ELNSLEWSA------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGT 327
Cdd:cd18007   131 TTDPRLKQEfiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK 210
                         250       260
                  ....*....|....*....|....*...
gi 1577429142 328 YFKKQFSDPVEHGQRHTATKRELATGRK 355
Cdd:cd18007   211 EFKKKFVKPIEAGQCVDSTEEDVRLMLK 238
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
123-373 2.26e-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: 144.77  E-value: 2.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd17997     4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNI------NGP-------------------HLI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW-GYFRVTVLHGN-RKDNELIR--VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd17997    59 IVPKSTLDNWMREFKRWcPSLRVVVLIGDkEERADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHtatkrelatgrKAMQ 358
Cdd:cd17997   139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQ-----------EVVQ 207
                         250
                  ....*....|....*
gi 1577429142 359 RLAKKMSGWFLRRTK 373
Cdd:cd17997   208 RLHKVLRPFLLRRIK 222
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
123-321 7.50e-39

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: 143.27  E-value: 7.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtreDIENNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFH------SQQQYGP-------------------FLV 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd17993    57 VVPLSTMPAWQREFAKWApDMNVIVYLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDE 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1577429142 274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPG 321
Cdd:cd17993   137 AHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG 184
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
123-371 3.83e-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: 141.52  E-value: 3.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtREDIENNMPefllrsmkkeplssTAK 197
Cdd:cd18066     1 LRPHQREGIEFLYecvmGMRVNERfGAILADEMGLGKTLQCISLIWTLL-----RQGPYGGKP--------------VIK 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 198 KMfLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIrvKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEA 274
Cdd:cd18066    62 RA-LIVTPGSLVKNWKKEFQKWlgsERIKVFTVDQDHKVEEFI--ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 275 HRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGR 354
Cdd:cd18066   139 HRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGE 218
                         250
                  ....*....|....*..
gi 1577429142 355 KAMQRLAKKMSGWFLRR 371
Cdd:cd18066   219 ARAAELTRLTGLFILRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
123-371 2.31e-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: 139.91  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtrediennmpefllrsmKKEPLSSTAK 197
Cdd:cd18067     1 LRPHQREGVKFLYrcvtGRRIRGShGCIMADEMGLGKTLQCITLMWTLL---------------------RQSPQCKPEI 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 198 KMFLIVAPLSVLYNWKDELDTWGYFRVTVL--HGNRKDNELIRVKQRKCE--------IALTTYETLRLCLDELNSLEWS 267
Cdd:cd18067    60 DKAIVVSPSSLVKNWANELGKWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 268 AVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATK 347
Cdd:cd18067   140 LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASE 219
                         250       260
                  ....*....|....*....|....
gi 1577429142 348 RELATGRKAMQRLAKKMSGWFLRR 371
Cdd:cd18067   220 KERQLGEEKLQELISIVNRCIIRR 243
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
123-373 2.29e-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: 2.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGT---RFLYGHYIHGggcILGDDMGLGKTVQVISFLAavlhkkgtrediennmpefLLRSMKkeplsstAKKM 199
Cdd:cd18009     4 MRPYQLEGMewlRMLWENGING---ILADEMGLGKTIQTIALLA-------------------HLRERG-------VWGP 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 200 FLIVAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRVKQRK-------CEIALTTYETLRLCLDELNSLEWSAVIV 271
Cdd:cd18009    55 FLVIAPLSTLPNWVNEFARFTpSVPVLLYHGTKEERERLRKKIMKregtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIV 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 272 DEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFsDPVEHGQRhTATKRELA 351
Cdd:cd18009   135 DEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLS 212
                         250       260
                  ....*....|....*....|....
gi 1577429142 352 TGRKA--MQRLAKKMSGWFLRRTK 373
Cdd:cd18009   213 EEREQniVHMLHAILKPFLLRRLK 236
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
123-371 1.02e-34

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: 132.03  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLyghyIHGGGcILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTakkmfLI 202
Cdd:cd18008     1 LLPYQKQGLAWM----LPRGG-ILADEMGLGKTIQAL---ALILATRPQDPKIPEELEENSSDPKKLYLSKTT-----LI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDT---WGYFRVTVLHGNRKdNELIRVKQrKCEIALTTYETLR----------------LCLDELNS 263
Cdd:cd18008    68 VVPLSLLSQWKDEIEKhtkPGSLKVYVYHGSKR-IKSIEELS-DYDIVITTYGTLAsefpknkkgggrdskeKEASPLHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 264 LEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELW------CVMDWAVPGllgsgtYFKKQFSDPV 337
Cdd:cd18008   146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYsllrflRVEPFGDYP------WFNSDISKPF 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1577429142 338 EHGQRhtatkrelaTGRKAMQRLAKKMsgwFLRR 371
Cdd:cd18008   220 SKNDR---------KALERLQALLKPI---LLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
123-341 1.70e-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: 128.39  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSmkkepls 193
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIEslerykgssGFGCILAHSMGLGKTLQVISFL------------------DVLLRH------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 194 sTAKKMFLIVAPLSVLYNWKDELDTW------------GYFRVTVLHGNRKD----NELIRVKQRKCEIALTTYETLRLC 257
Cdd:cd18069    56 -TGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrpRPFKVFILNDEHKTtaarAKVIEDWVKDGGVLLMGYEMFRLR 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 258 LDElnslewSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPV 337
Cdd:cd18069   135 PGP------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI 208

                  ....
gi 1577429142 338 EHGQ 341
Cdd:cd18069   209 LNGQ 212
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
123-373 1.99e-33

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: 128.26  E-value: 1.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRF---LYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPefllrsmkkeplsstakkm 199
Cdd:cd17996     4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTISLITYLMEKKK------NNGP------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 200 FLIVAPLSVLYNWKDELDTWGYFRVTVLH-GNRKDNELIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHR 276
Cdd:cd17996    56 YLVIVPLSTLSNWVSEFEKWAPSVSKIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 277 IKNPKARVTEVMKALKCN-VRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHtatKRELATGR 354
Cdd:cd17996   136 MKNAQSKLTQTLNTYYHArYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEE 212
                         250       260
                  ....*....|....*....|.
gi 1577429142 355 KAM--QRLAKKMSGWFLRRTK 373
Cdd:cd17996   213 TLLiiRRLHKVLRPFLLRRLK 233
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
123-335 2.57e-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: 127.47  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 202
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----------------EIFLMGIRGP---------FLI 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18058    55 IAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSC 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
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 ...
123-371 7.93e-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: 123.23  E-value: 7.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPEfllrsmkkeplsstakkmfLI 202
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPH-------------------LI 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW--GyFRVTVLHGNRKDNELIRV---KQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRI 277
Cdd:cd18003    56 VVPTSVMLNWEMEFKRWcpG-FKILTYYGSAKERKLKRQgwmKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNI 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 278 KNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP----VEHGQRHTatkrelatg 353
Cdd:cd18003   135 KNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN--------- 205
                         250
                  ....*....|....*...
gi 1577429142 354 RKAMQRLAKKMSGWFLRR 371
Cdd:cd18003   206 EELVRRLHKVLRPFLLRR 223
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
123-371 1.60e-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: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsMKKEPlsstakkmFLI 202
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH-----------------QLYGP--------FLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd18054    76 VVPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQfsdpveHGQrhtatkrelatG 353
Cdd:cd18054   156 AHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEED------HGK-----------G 218
                         250
                  ....*....|....*....
gi 1577429142 354 RK-AMQRLAKKMSGWFLRR 371
Cdd:cd18054   219 REnGYQSLHKVLEPFLLRR 237
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
123-335 5.90e-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: 120.93  E-value: 5.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllrsmkKEPLSSTAKKMFLI 202
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------------------------QEVYNVGIHGPFLV 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18060    55 IAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRC 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18060   135 VIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
123-335 8.32e-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: 120.50  E-value: 8.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSMKKEPlsstakkmFLI 202
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL------------------YEILLTGIRGP--------FLI 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18061    55 IAPLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRC 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18061   135 VIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
123-350 1.78e-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: 120.15  E-value: 1.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsmkkeplssTAKKMFLI 202
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEH-------------------------QLYGPFLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd18053    76 VVPLSTLTSWQREIQTWApQMNAVVYLGDINSRNMIRthewmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGqrHTATKREL 350
Cdd:cd18053   156 AHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG--YASLHKEL 230
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
123-335 7.42e-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: 117.83  E-value: 7.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 202
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLY-----------------EIYLKGIHGP---------FLV 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18059    55 IAPLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRC 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18059   135 VVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
123-371 8.45e-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: 117.54  E-value: 8.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVlhkKGTREDiennmpefllrsmkkeplsstaKKMFLI 202
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYL---AGRLKL----------------------LGPFLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE----IALTTYEtlrLCLDE---LNSLEWSAVIVDEAH 275
Cdd:cd18006    56 LCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAH 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 276 RIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTY--FKKQFSDpvehgqrhtaTKRELATg 353
Cdd:cd18006   133 RLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSE----------TDDESET- 201
                         250
                  ....*....|....*...
gi 1577429142 354 rkaMQRLAKKMSGWFLRR 371
Cdd:cd18006   202 ---VEELHLLLQPFLLRR 216
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
123-335 3.87e-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: 114.84  E-value: 3.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllRSMKKEplsSTAKKMFLI 202
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------------------YSLYKE---GHSKGPFLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNrkdnelirvkqrkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd17994    56 SAPLSTIINWEREFEMWApDFYVVTYVGD--------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQ 121
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1577429142 282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd17994   122 SKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
123-371 1.45e-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: 114.14  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDiennmpefllrsmkkeplsstakkmFLI 202
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGP-------------------------FLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVD 272
Cdd:cd18002    56 IAPASTLHNWQQEISRFvPQFKVLPYWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 273 EAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVE-HGQRHTATKREla 351
Cdd:cd18002   136 EAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH-- 213
                         250       260
                  ....*....|....*....|
gi 1577429142 352 tgrkAMQRLAKKMSGWFLRR 371
Cdd:cd18002   214 ----QLKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
113-384 3.37e-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: 113.61  E-value: 3.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 113 DSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkepl 192
Cdd:cd18064     6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYR--------NIP------------ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 193 sstakKMFLIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIR--VKQRKCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18064    66 -----GPHMVLVPKSTLHNWMAEFKRWvPTLRAVCLIGDKDQRAaFVRdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtatKR 348
Cdd:cd18064   141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TN 208
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1577429142 349 ELATGRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKE 384
Cdd:cd18064   209 NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
123-341 2.33e-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: 2.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-LYKEGH------------------------SKGPYLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVK----------------------QRKCEIALTTYETLRLCLD 259
Cdd:cd18057    56 SAPLSTIINWEREFEMWAPdFYVVTYTGDKESRSVIRENefsfednairsgkkvfrmkkeaQIKFHVLLTSYELITIDQA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18057   136 ILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKE 215

                  ..
gi 1577429142 340 GQ 341
Cdd:cd18057   216 DQ 217
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
508-621 5.29e-27

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 105.76  E-value: 5.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 508 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 587
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1577429142 588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 621
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
123-341 1.50e-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: 108.56  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH------------------------TKGPFLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 259
Cdd:cd18055    56 SAPLSTIINWEREFQMWApdfyvvtytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18055   136 ALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKE 215

                  ..
gi 1577429142 340 GQ 341
Cdd:cd18055   216 DQ 217
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
123-336 5.30e-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: 106.14  E-value: 5.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHyihGGGCILGDDMGLGKTVQVISFLAAVlhkkgtrediENNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd18010     1 LLPFQREGVCFALRR---GGRVLIADEMGLGKTVQAIAIAAYY----------REEWP-------------------LLI 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW----GYFRVTVLHGNRkdnELIRVKQRKceIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd18010    49 VCPSSLRLTWADEIERWlpslPPDDIQVIVKSK---DGLRDGDAK--VVIVSYDLLRRLEKQLLARKFKVVICDESHYLK 123
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 279 NPKA-RVTEVMKALK-CNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP 336
Cdd:cd18010   124 NSKAkRTKAALPLLKrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
123-341 1.08e-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: 105.92  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS-LYKEGH------------------------SKGPFLV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 259
Cdd:cd18056    56 SAPLSTIINWEREFEMWApdmyvvtyvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18056   136 ILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKE 215

                  ..
gi 1577429142 340 GQ 341
Cdd:cd18056   216 DQ 217
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
123-373 2.20e-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: 105.10  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkeplsstakKMFLI 202
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYR--------NIP-----------------GPHMV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd18065    71 LVPKSTLHNWMNEFKRWvPSLRAVCLIGDKDARAaFIRDVMMPGEwdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtaTKRELATgRKAMQ 358
Cdd:cd18065   151 NEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVE 218
                         250
                  ....*....|....*
gi 1577429142 359 RLAKKMSGWFLRRTK 373
Cdd:cd18065   219 RLHAVLKPFLLRRIK 233
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
123-350 2.58e-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: 2.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLAAVL-HKKgtREDIennmpefllrsmkkepl 192
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCEslkktkkspGSGCILAHCMGLGKTLQVVTFLHTVLlCEK--LENF----------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 193 sstakKMFLIVAPLSVLYNWKDELDTWgyfrvtvLHGNRKDN-----ELIRVK------------QRKCEIALTTYETLR 255
Cdd:cd18068    62 -----SRVLVVCPLNTVLNWLNEFEKW-------QEGLKDEEkievnELATYKrpqersyklqrwQEEGGVMIIGYDMYR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 256 LCLDELN-SLEWSA---------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAV 319
Cdd:cd18068   130 ILAQERNvKSREKLkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1577429142 320 PGLLGSGTYFKKQFSDPVEHGQRHTATKREL 350
Cdd:cd18068   210 PNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
119-373 2.95e-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: 105.53  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 119 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPefllrsmkkeplsstakk 198
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK------RLNGP------------------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 199 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 275
Cdd:cd18063    76 -YLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTpamRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 276 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 353
Cdd:cd18063   155 RMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETIL- 233
                         250       260
                  ....*....|....*....|
gi 1577429142 354 rkAMQRLAKKMSGWFLRRTK 373
Cdd:cd18063   234 --IIRRLHKVLRPFLLRRLK 251
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
139-371 3.79e-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: 3.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 139 IHGGgcILGDDMGLGKTVQVISFLAAvlhkkgtrediennmpefllrsmkkeplsstakKMFLIVAPLSVLYNWKDELD- 217
Cdd:cd18071    48 VRGG--ILADDMGLGKTLTTISLILA---------------------------------NFTLIVCPLSVLSNWETQFEe 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 218 --TWGYFRVTVLHG---NRKDNELIrvkqrKCEIALTTYETLrlCLDE-------LNSLEWSAVIVDEAHRIKNPKARVT 285
Cdd:cd18071    93 hvKPGQLKVYTYHGgerNRDPKLLS-----KYDIVLTTYNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 286 EVMKALKCNVRIGLTGTILQNNMKELWCVMdwavpgllgsgTYFK-KQFSDPvEHGQRhtATKRELATG-RKAMQRLAKK 363
Cdd:cd18071   166 KAVLNLSSERRWVLTGTPIQNSPKDLGSLL-----------SFLHlKPFSNP-EYWRR--LIQRPLTMGdPTGLKRLQVL 231

                  ....*...
gi 1577429142 364 MSGWFLRR 371
Cdd:cd18071   232 MKQITLRR 239
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
123-320 4.05e-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: 102.85  E-value: 4.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpeFLLRSMKKEPlsstakkmFLI 202
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA------------------YLKEIGIPGP--------HLV 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRV----KQRKCEIALTTYETLRLCLDE---LNSLEWSAVIVDEA 274
Cdd:cd17998    55 VVPSSTLDNWLREFKRWCpSLKVEPYYGSQEERKHLRYdilkGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEG 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1577429142 275 HRIKNPKA-RVTEVMKaLKCNVRIGLTGTILQNNMKELWCVMDWAVP 320
Cdd:cd17998   135 HMLKNMTSeRYRHLMT-INANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
119-373 3.50e-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: 102.04  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 119 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakk 198
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRI------NGP------------------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 199 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 275
Cdd:cd18062    76 -FLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSpaaRRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 276 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 353
Cdd:cd18062   155 RMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL- 233
                         250       260
                  ....*....|....*....|
gi 1577429142 354 rkAMQRLAKKMSGWFLRRTK 373
Cdd:cd18062   234 --IIRRLHKVLRPFLLRRLK 251
DEXDc smart00487
DEAD-like helicases superfamily;
123-312 4.72e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.56  E-value: 4.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  123 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:smart00487   9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  203 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 275
Cdd:smart00487  60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1577429142  276 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 312
Cdd:smart00487 140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 6.41e-22

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: 89.31  E-value: 6.41e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142  18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400     1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
HELICc smart00490
helicase superfamily c-terminal domain;
538-621 6.99e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.96  E-value: 6.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  538 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 617
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 1577429142  618 YRIG 621
Cdd:smart00490  79 GRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
143-312 4.77e-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: 4.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 143 GCILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTAKKMFLIVAPLSVLYNWKDELDT---W 219
Cdd:cd18072    22 GGILADDMGLGKTLTMI---ALILAQKNTQNRKEEEKEKALTEWESKKDSTLVPSAGTLVVCPASLVHQWKNEVESrvaS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 220 GYFRVTVLHGNRKDNelIRVKQRKCEIALTTYETL---------RLCLDELNSLEWSAVIVDEAHRIKNPKARVTEVMKA 290
Cdd:cd18072    99 NKLRVCLYHGPNRER--IGEVLRDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                         170       180
                  ....*....|....*....|..
gi 1577429142 291 LKCNVRIGLTGTILQNNMKELW 312
Cdd:cd18072   177 LRAHARWALTGTPIQNNLLDMY 198
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
123-311 4.94e-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: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYghyIHGGgcILGDDMGLGKTVQVISFLAAvlHkkgTREDIENNMPEFLLRSMKKEPLSSTAKKMF-- 200
Cdd:cd18070     1 LLPYQRRAVNWML---VPGG--ILADEMGLGKTVEVLALILL--H---PRPDNDLDAADDDSDEMVCCPDCLVAETPVss 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 201 ---LIVAPLSVLYNWKDELD--TWGYFRVTVLHGNRKDNELIRVKQRK---CEIALTTYETLRLCLDE------------ 260
Cdd:cd18070    71 katLIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALASPAPEIlaeYDIVVTTYDVLRTELHYaeanrsnrrrrr 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1577429142 261 ----------LNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKEL 311
Cdd:cd18070   151 qkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDL 211
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
123-312 2.70e-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: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHyiHGGGCILgdDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkeplsstakkmFLI 202
Cdd:cd18013     1 PHPYQKVAINFIIEH--PYCGLFL--DMGLGKTVTTLTALSDLQLDDFTRR--------------------------VLV 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 203 VAPLSVLYN-WKDELDTWGYFR---VTVLHGNRKdnELIRVKQRKCEIALTTYETLR-LCLDELNSLEWSAVIVDEAHRI 277
Cdd:cd18013    51 IAPLRVARStWPDEVEKWNHLRnltVSVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSF 128
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1577429142 278 KNPKARVTEVMKALKCNVR--IGLTGTILQNNMKELW 312
Cdd:cd18013   129 KSPRSKRFKALRKVRPVIKrlIGLTGTPSPNGLMDLW 165
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
123-322 4.36e-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: 71.55  E-value: 4.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREgtrFLYGHYIHG-GGCILGDDMGLGKTVQVisflAAVLHkkgtrediennmpEFLLRSMKKEplsstakkmFL 201
Cdd:cd18011     1 PLPHQID---AVLRALRKPpVRLLLADEVGLGKTIEA----GLIIK-------------ELLLRGDAKR---------VL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 202 IVAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE--IALTTYETLR---LCLDELNSLEWSAVIVDEAHR 276
Cdd:cd18011    52 ILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHK 131
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1577429142 277 IKN----PKARVTEVMKALKCNVR--IGLTGTILQNNMKELWCVMDWAVPGL 322
Cdd:cd18011   132 LRNsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPGR 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
80-302 2.28e-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: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142  80 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 158
Cdd:COG1061    42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 159 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 237
Cdd:COG1061   117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1577429142 238 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 302
Cdd:COG1061   165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
ResIII pfam04851
Type III restriction enzyme, res subunit;
123-302 2.05e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 59.99  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHG--GGCIlgdDM--GLGKTVqVISFLAAVLHKKGTrediennmpefllrsmkkeplsstaKK 198
Cdd:pfam04851   4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTL-TAAKLIARLFKKGP-------------------------IK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 199 MFLIVAP-LSVLYNWKDELDTWG---YFRVTVLHGNRKDNElirvkQRKCEIALTTYETL----RLCLDELNSLEWSAVI 270
Cdd:pfam04851  55 KVLFLVPrKDLLEQALEEFKKFLpnyVEIGEIISGDKKDES-----VDDNKIVVTTIQSLykalELASLELLPDFFDVII 129
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1577429142 271 VDEAHRIKNPKARvtEVMKALKCNVRIGLTGT 302
Cdd:pfam04851 130 IDEAHRSGASSYR--NILEYFKPAFLLGLTAT 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
123-302 3.96e-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: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 123 LRDYQREGTRFLYGHYIHGGGCIlgdDM--GLGKTVqvISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmF 200
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTL--TALALIAYLKELR----------------------------T 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 201 LIVAP-LSVLYNWKDELDTWGYFR-VTVLHGNRKDnelirvKQRKCEIALTTYETLRLCLDELNSL--EWSAVIVDEAHR 276
Cdd:cd17926    48 LIVVPtDALLDQWKERFEDFLGDSsIGLIGGGKKK------DFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHH 121
                         170       180
                  ....*....|....*....|....*.
gi 1577429142 277 IKNPKARvtEVMKALKCNVRIGLTGT 302
Cdd:cd17926   122 LPAKTFS--EILKELNAKYRLGLTAT 145
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
21-72 8.07e-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: 51.87  E-value: 8.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1577429142  21 GERCLAPSPDNGKLCEASIKSITVDENGksfAVVLYADF-QERKIPLKQLQEV 72
Cdd:cd21182     1 GDKCLAPYSDDGKYYEATIEEITEESDT---ATVVFDGYgNSEEVPLSDLKPL 50
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
194-304 6.99e-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: 52.69  E-value: 6.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 194 STAKKMFLIVAPLSV-LYNWKDELDTWGYF---RVTVLHGNRKDnelirvKQRKCEIALTTYETLR----------LCLD 259
Cdd:cd18029    48 CTIKKSTLVLCTSAVsVEQWRRQFLDWTTIddeQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFME 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1577429142 260 ELNSLEWSAVIVDEAHRIKNPKARvtEVMKALKCNVRIGLTGTIL 304
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 ...
141-302 1.51e-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: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 141 GGGCILGDDMGLGKTvqVISFLAAVLHkkgtrediennmpefllrsmkkepLSSTAKKmFLIVAPLSVL-YNWKDELDTW 219
Cdd:cd00046     1 GENVLITAPTGSGKT--LAALLAALLL------------------------LLKKGKK-VLVLVPTKALaLQTAERLREL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 220 GYF--RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSL---EWSAVIVDEAHRIKnPKARVTEVMKALKCN 294
Cdd:cd00046    54 FGPgiRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALL-IDSRGALILDLAVRK 132
                         170
                  ....*....|....
gi 1577429142 295 V------RIGLTGT 302
Cdd:cd00046   133 AglknaqVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
504-642 4.18e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 53.20  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 504 PKYSGKMKVLQQLLNhcrKNRD-KVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEF-NST 573
Cdd:COG1111   335 PKLSKLREILKEQLG---TNPDsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERFrAGE 411
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1577429142 574 QDVnicLVSTMAGGLGLNFVGANVVVLFDPTWNPandLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMY 642
Cdd:COG1111   412 FNV---LVATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRDEAYY 474
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
580-622 2.95e-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: 2.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1577429142 580 LVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQ 622
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
197-303 8.49e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 197 KKMFLIVAPLSVL-YNWKDELDTWGYF---RVTVLHGNRKDNELIRvKQRKCEIALTTYETLRLCLDE---LNSLEWsaV 269
Cdd:pfam00270  45 GPQALVLAPTRELaEQIYEELKKLGKGlglKVASLLGGDSRKEQLE-KLKGPDILVGTPGRLLDLLQErklLKNLKL--L 121
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1577429142 270 IVDEAHRI--KNPKARVTEVMKALKCNVRI-GLTGTI 303
Cdd:pfam00270 122 VLDEAHRLldMGFGPDLEEILRRLPKKRQIlLLSATL 158
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
198-311 1.20e-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: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1577429142 198 KMFLIVAPLSVLYNWK-DELDTWGY--FRVTVLHG--NRKDNELirvkqRKCEIALTTYETLrlclDEL--NSLEW---- 266
Cdd:cd18028    46 GKALYLVPLRALASEKyEEFKKLEEigLKVGISTGdyDEDDEWL-----GDYDIIVATYEKF----DSLlrHSPSWlrdv 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1577429142 267 SAVIVDEAHRIKNPK-ARVTEV----MKALKCNVR-IGLTGTIlqNNMKEL 311
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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