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Conserved domains on  [gi|2462624628|ref|XP_054218906|]
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DNA excision repair protein ERCC-6-like 2 isoform X10 [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 7.03e-149

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 452.99  E-value: 7.03e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005     76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005    156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                          250
                   ....*....|
gi 2462624628  362 KKMSGWFLRR 371
Cdd:cd18005    236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-645 8.44e-124

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 402.30  E-value: 8.44e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553    226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553    292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553    359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553    435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553    494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553    532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQ 645
Cdd:COG0553    611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 8.11e-21

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


:

Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.38  E-value: 8.11e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462624628   18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
VIGSSK super family cl20696
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1067-1091 1.28e-03

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


The actual alignment was detected with superfamily member pfam14773:

Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.36  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*
gi 2462624628 1067 VAYIHSNQNVIGSSKAENHMSRWAA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
 
Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
123-371 7.03e-149

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 452.99  E-value: 7.03e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005     76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005    156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                          250
                   ....*....|
gi 2462624628  362 KKMSGWFLRR 371
Cdd:cd18005    236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-645 8.44e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 402.30  E-value: 8.44e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553    226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553    292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553    359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553    435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553    494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553    532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQ 645
Cdd:COG0553    611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
116-639 6.63e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 250.10  E-value: 6.63e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  116 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 195
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  196 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 268
Cdd:PLN03142   220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 348
Cdd:PLN03142   295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  349 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 428
Cdd:PLN03142   369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  429 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 508
Cdd:PLN03142   426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  509 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 587
Cdd:PLN03142   472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462624628  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEE 639
Cdd:PLN03142   552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-462 3.13e-65

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 223.33  E-value: 3.13e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  126 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 204
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  205 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:pfam00176   57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 358
Cdd:pfam00176  137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  359 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 438
Cdd:pfam00176  206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265
                          330       340
                   ....*....|....*....|....
gi 2462624628  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 3.92e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.77  E-value: 3.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  506 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462624628  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 1.91e-27

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 107.68  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  508 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 587
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462624628  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 621
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
123-312 1.85e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.87  E-value: 1.85e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   123 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   203 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 275
Cdd:smart00487   60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462624628   276 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 312
Cdd:smart00487  140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
538-621 8.69e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 8.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   538 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 617
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 2462624628   618 YRIG 621
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 8.11e-21

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


Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.38  E-value: 8.11e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462624628   18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
80-302 6.56e-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: 6.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   80 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 158
Cdd:COG1061     42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  159 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 237
Cdd:COG1061    117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  238 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 302
Cdd:COG1061    165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1067-1091 1.28e-03

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


Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.36  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*
gi 2462624628 1067 VAYIHSNQNVIGSSKAENHMSRWAA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
 
Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
123-371 7.03e-149

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 452.99  E-value: 7.03e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDIENNMPEFllrsmKKEPLSSTAKKMFLI 202
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF-----KKKPPASSAKKPVLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELI-RVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd18005     76 VAPLSVLYNWKDELDTWGHFEVGVYHGSRKDDELEgRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  282 ARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKAMQRLA 361
Cdd:cd18005    156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                          250
                   ....*....|
gi 2462624628  362 KKMSGWFLRR 371
Cdd:cd18005    236 VKLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
107-645 8.44e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 402.30  E-value: 8.44e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  107 KLSDNGDSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrs 186
Cdd:COG0553    226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------------- 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  187 mkkePlsstakkmFLIVAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVkQRKCEIALTTYETLRLCLDELNSLE 265
Cdd:COG0553    292 ----P--------VLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVD 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  266 WSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQrhta 345
Cdd:COG0553    359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  346 tkrelatgRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDvtlilqssepctcRSGQ 425
Cdd:COG0553    435 --------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLR-------------RELE 493
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  426 KRrnccyktnsHGETVKTLYLSYLTVLQKVANHVALLqaastSKQQETLIKRicdqvfsrfpdfvqkskdaafetlsdpk 505
Cdd:COG0553    494 GA---------EGIRRRGLILAALTRLRQICSHPALL-----LEEGAELSGR---------------------------- 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  506 ySGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:COG0553    532 -SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKA 610
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQ 645
Cdd:COG0553    611 GGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
123-320 1.11e-70

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 234.38  E-value: 1.11e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTRediennmpefllrsmkkeplsstakKMFLI 202
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKER-------------------------GPVLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIRVK--QRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKN 279
Cdd:cd17919     56 VCPLSVLENWEREFEKWtPDLRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKN 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462624628  280 PKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVP 320
Cdd:cd17919    136 PKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
116-639 6.63e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 250.10  E-value: 6.63e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  116 PYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTrediennmpefllrsmkkeplssT 195
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI-----------------------T 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  196 AKKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---VKQRKCEIALTTYEtlrLCLDELNSLE---WSA 268
Cdd:PLN03142   220 GPHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRY 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkr 348
Cdd:PLN03142   295 IIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  349 elatgrKAMQRLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVTLIlqssepctcrsgqkrr 428
Cdd:PLN03142   369 ------EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV---------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  429 nccyktNSHGETVKTLYLSylTVLQKVANHVALLQAASTSkqqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySG 508
Cdd:PLN03142   426 ------NAGGERKRLLNIA--MQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SG 471
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  509 KMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNIC-LVSTMAGG 587
Cdd:PLN03142   472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGG 551
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462624628  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLISLGTVEE 639
Cdd:PLN03142   552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
126-462 3.13e-65

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 223.33  E-value: 3.13e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  126 YQREGTRFLYGHYIHGG-GCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpeflLRSMKKEPlsstakkmFLIVA 204
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP--------TLIVV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  205 PLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:pfam00176   57 PLSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLK 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVehgQRHTATKRelatgrkaMQ 358
Cdd:pfam00176  137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VS 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  359 RLAKKMSGWFLRRTKTLIKDQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVTLILQSSEpctcrsgqkrrnccyktnshG 438
Cdd:pfam00176  206 RLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------G 265
                          330       340
                   ....*....|....*....|....
gi 2462624628  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 7.95e-58

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 199.52  E-value: 7.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefLLRSMkkeplsstakkmfLI 202
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-------------LIKSV-------------LV 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRK---DNELIRVKQRKcEIALTTYETLRLCLDELNSLE-----WSAVIVDE 273
Cdd:cd18001     55 VMPTSLIPHWVKEFAKWTPgLRVKVFHGTSKkerERNLERIQRGG-GVLLTTYGMVLSNTEQLSADDhdefkWDYVILDE 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPG-LLGSGTYFKKQFSDPVEHGQRHTATKRELAT 352
Cdd:cd18001    134 GHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKAL 213
                          250
                   ....*....|....*....
gi 2462624628  353 GRKAMQRLAKKMSGWFLRR 371
Cdd:cd18001    214 GSEVAENLRQIIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
506-632 3.92e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.77  E-value: 3.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  506 YSGKMKVLQQLLNHCRKNRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSTQDVNICLVSTMA 585
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462624628  586 GGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQCRDVKVLRLI 632
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
123-373 1.09e-55

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: 192.78  E-value: 1.09e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR--------------------------KGPSLV 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHG-NRKDNELIRVKQRkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNP 280
Cdd:cd18012     59 VAPTSLIYNWEEEAAKFApELKVLVIHGtKRKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNP 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  281 KARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRhtatkrelatgRKAMQRL 360
Cdd:cd18012    137 QTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEEL 205
                          250
                   ....*....|...
gi 2462624628  361 AKKMSGWFLRRTK 373
Cdd:cd18012    206 KKLISPFILRRLK 218
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
123-371 2.42e-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: 181.33  E-value: 2.42e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkKGTREDiennmpefllrsmkkeplSSTAK 197
Cdd:cd18004      1 LRPHQREGVQFLYdcltGRRGYGGgGAILADEMGLGKTLQAIALVWTLL--KQGPYG------------------KPTAK 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  198 KmFLIVAPLSVLYNWKDELDTW-GYFRVTVL--HGNRKDNELIRVKQ---RKCEIALTTYETLRLCLDELNSLE-WSAVI 270
Cdd:cd18004     61 K-ALIVCPSSLVGNWKAEFDKWlGLRRIKVVtaDGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKIsIDLLI 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  271 VDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKREL 350
Cdd:cd18004    140 CDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDK 219
                          250       260
                   ....*....|....*....|.
gi 2462624628  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 1.74e-50

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


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 178.21  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkePlsstakkmFLI 202
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRG-----------------P--------FLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd17995     56 IAPLSTIPNWQREFETWTDMNVVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRV 135
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462624628  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 6.38e-49

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 174.08  E-value: 6.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTR---FLYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPEFLLRSmkkeplsstakkm 199
Cdd:cd17999      1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLCILASDHHKR------ANSFNSENLPS------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  200 fLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHR 276
Cdd:cd17999     59 -LVVCPPTLVGHWVAEIKKYfpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHI 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  277 IKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGRKA 356
Cdd:cd17999    138 IKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALA 217
                          250
                   ....*....|....*
gi 2462624628  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 3.74e-44

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 159.03  E-value: 3.74e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtrediennmpefllrsmkkeplSSTAKKMFLI 202
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH-------------------------SKLGLGPSLI 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW-GYFRVTVLH----GNRKDNE---------LIRVKQRKCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18000     56 VCPATVLKQWVKEFHRWwPPFRVVVLHssgsGTGSEEKlgsierksqLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQY 135
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462624628  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 1.27e-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: 156.30  E-value: 1.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIH-------GGGCILGDDMGLGKTVQVISFLAAVL--HKKGTRediennmpefllrsmkkepls 193
Cdd:cd18007      1 LKPHQVEGVRFLWSNLVGtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLaaAPRRSR--------------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  194 stakkmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNeliRVKQRKCEIA---------LTTYETLR--LCLD 259
Cdd:cd18007     60 ------PLVLCPASTLYNWEDEFKKWlppDLRPLLVLVSLSASK---RADARLRKINkwhkeggvlLIGYELFRnlASNA 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  260 ELNSLEWSA------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGT 327
Cdd:cd18007    131 TTDPRLKQEfiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK 210
                          250       260
                   ....*....|....*....|....*...
gi 2462624628  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 3.32e-39

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 145.93  E-value: 3.32e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd17997      4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNI------NGP-------------------HLI 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW-GYFRVTVLHGN-RKDNELIR--VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd17997     59 IVPKSTLDNWMREFKRWcPSLRVVVLIGDkEERADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHtatkrelatgrKAMQ 358
Cdd:cd17997    139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQ-----------EVVQ 207
                          250
                   ....*....|....*
gi 2462624628  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 2.04e-38

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 143.27  E-value: 2.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHkkgtreDIENNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFH------SQQQYGP-------------------FLV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd17993     57 VVPLSTMPAWQREFAKWApDMNVIVYLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDE 136
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462624628  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 6.52e-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: 142.68  E-value: 6.52e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtREDIENNMPefllrsmkkeplssTAK 197
Cdd:cd18066      1 LRPHQREGIEFLYecvmGMRVNERfGAILADEMGLGKTLQCISLIWTLL-----RQGPYGGKP--------------VIK 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  198 KMfLIVAPLSVLYNWKDELDTW---GYFRVTVLHGNRKDNELIrvKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEA 274
Cdd:cd18066     62 RA-LIVTPGSLVKNWKKEFQKWlgsERIKVFTVDQDHKVEEFI--ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEG 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  275 HRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATKRELATGR 354
Cdd:cd18066    139 HRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGE 218
                          250
                   ....*....|....*..
gi 2462624628  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 6.44e-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: 6.44e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLY----GHYIHGG-GCILGDDMGLGKTVQVISFLAAVLhkkgtrediennmpefllrsmKKEPLSSTAK 197
Cdd:cd18067      1 LRPHQREGVKFLYrcvtGRRIRGShGCIMADEMGLGKTLQCITLMWTLL---------------------RQSPQCKPEI 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  198 KMFLIVAPLSVLYNWKDELDTWGYFRVTVL--HGNRKDNELIRVKQRKCE--------IALTTYETLRLCLDELNSLEWS 267
Cdd:cd18067     60 DKAIVVSPSSLVKNWANELGKWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVG 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  268 AVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEHGQRHTATK 347
Cdd:cd18067    140 LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASE 219
                          250       260
                   ....*....|....*....|....
gi 2462624628  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 7.25e-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: 7.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGT---RFLYGHYIHGggcILGDDMGLGKTVQVISFLAavlhkkgtrediennmpefLLRSMKkeplsstAKKM 199
Cdd:cd18009      4 MRPYQLEGMewlRMLWENGING---ILADEMGLGKTIQTIALLA-------------------HLRERG-------VWGP 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  200 FLIVAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRVKQRK-------CEIALTTYETLRLCLDELNSLEWSAVIV 271
Cdd:cd18009     55 FLVIAPLSTLPNWVNEFARFTpSVPVLLYHGTKEERERLRKKIMKregtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIV 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  272 DEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFsDPVEHGQRhTATKRELA 351
Cdd:cd18009    135 DEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLS 212
                          250       260
                   ....*....|....*....|....
gi 2462624628  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 5.33e-35

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 134.34  E-value: 5.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLyghyIHGGGcILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTakkmfLI 202
Cdd:cd18008      1 LLPYQKQGLAWM----LPRGG-ILADEMGLGKTIQAL---ALILATRPQDPKIPEELEENSSDPKKLYLSKTT-----LI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDT---WGYFRVTVLHGNRKdNELIRVKQrKCEIALTTYETLR----------------LCLDELNS 263
Cdd:cd18008     68 VVPLSLLSQWKDEIEKhtkPGSLKVYVYHGSKR-IKSIEELS-DYDIVITTYGTLAsefpknkkgggrdskeKEASPLHR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  264 LEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELW------CVMDWAVPGllgsgtYFKKQFSDPV 337
Cdd:cd18008    146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYsllrflRVEPFGDYP------WFNSDISKPF 219
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462624628  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 2.08e-33

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 129.16  E-value: 2.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSmkkepls 193
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIEslerykgssGFGCILAHSMGLGKTLQVISFL------------------DVLLRH------- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  194 sTAKKMFLIVAPLSVLYNWKDELDTW------------GYFRVTVLHGNRKD----NELIRVKQRKCEIALTTYETLRLC 257
Cdd:cd18069     56 -TGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrpRPFKVFILNDEHKTtaarAKVIEDWVKDGGVLLMGYEMFRLR 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  258 LDElnslewSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPV 337
Cdd:cd18069    135 PGP------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI 208

                   ....
gi 2462624628  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 2.60e-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: 129.03  E-value: 2.60e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRF---LYGHYIHGggcILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPefllrsmkkeplsstakkm 199
Cdd:cd17996      4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTISLITYLMEKKK------NNGP------------------- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  200 FLIVAPLSVLYNWKDELDTWGYFRVTVLH-GNRKDNELIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHR 276
Cdd:cd17996     56 YLVIVPLSTLSNWVSEFEKWAPSVSKIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHR 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  277 IKNPKARVTEVMKALKCN-VRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHtatKRELATGR 354
Cdd:cd17996    136 MKNAQSKLTQTLNTYYHArYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEE 212
                          250       260
                   ....*....|....*....|.
gi 2462624628  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 6.30e-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: 127.85  E-value: 6.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 202
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----------------EIFLMGIRGP---------FLI 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18058     55 IAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSC 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  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 7.72e-32

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 124.77  E-value: 7.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGtredieNNMPEfllrsmkkeplsstakkmfLI 202
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPH-------------------LI 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW--GyFRVTVLHGNRKDNELIRV---KQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAHRI 277
Cdd:cd18003     56 VVPTSVMLNWEMEFKRWcpG-FKILTYYGSAKERKLKRQgwmKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNI 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  278 KNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP----VEHGQRHTatkrelatg 353
Cdd:cd18003    135 KNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN--------- 205
                          250
                   ....*....|....*...
gi 2462624628  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 4.28e-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: 4.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsMKKEPlsstakkmFLI 202
Cdd:cd18054     21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH-----------------QLYGP--------FLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd18054     76 VVPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  274 AHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQfsdpveHGQrhtatkrelatG 353
Cdd:cd18054    156 AHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEED------HGK-----------G 218
                          250
                   ....*....|....*....
gi 2462624628  354 RK-AMQRLAKKMSGWFLRR 371
Cdd:cd18054    219 REnGYQSLHKVLEPFLLRR 237
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
123-335 4.41e-31

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 122.42  E-value: 4.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpEFLLRSMKKEPlsstakkmFLI 202
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL------------------YEILLTGIRGP--------FLI 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18061     55 IAPLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRC 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18061    135 VIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
123-335 2.06e-30

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: 120.54  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllrsmkKEPLSSTAKKMFLI 202
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------------------------QEVYNVGIHGPFLV 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKC--------------EIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18060     55 IAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRC 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18060    135 VIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
123-371 3.45e-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: 119.46  E-value: 3.45e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVlhkKGTREDiennmpefllrsmkkeplsstaKKMFLI 202
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYL---AGRLKL----------------------LGPFLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE----IALTTYEtlrLCLDE---LNSLEWSAVIVDEAH 275
Cdd:cd18006     56 LCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAH 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  276 RIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTY--FKKQFSDpvehgqrhtaTKRELATg 353
Cdd:cd18006    133 RLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSE----------TDDESET- 201
                          250
                   ....*....|....*...
gi 2462624628  354 rkaMQRLAKKMSGWFLRR 371
Cdd:cd18006    202 ---VEELHLLLQPFLLRR 216
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
123-350 4.48e-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: 4.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediennmpefllrsmkkeplssTAKKMFLI 202
Cdd:cd18053     21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEH-------------------------QLYGPFLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIR--------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDE 273
Cdd:cd18053     76 VVPLSTLTSWQREIQTWApQMNAVVYLGDINSRNMIRthewmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDE 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  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 1.18e-29

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


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 118.21  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpEFLLRSMKKEplsstakkmFLI 202
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLY-----------------EIYLKGIHGP---------FLV 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQR--------------KCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18059     55 IAPLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRC 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSD 335
Cdd:cd18059    135 VVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
123-335 4.63e-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: 115.61  E-value: 4.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLaavlhkkgtrediennmpefllRSMKKEplsSTAKKMFLI 202
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------------------YSLYKE---GHSKGPFLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNrkdnelirvkqrkcEIALTTYETLRLCLDELNSLEWSAVIVDEAHRIKNPK 281
Cdd:cd17994     56 SAPLSTIINWEREFEMWApDFYVVTYVGD--------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQ 121
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462624628  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 2.87e-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: 114.52  E-value: 2.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTREDiennmpefllrsmkkeplsstakkmFLI 202
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGP-------------------------FLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNELIR---------VKQRKCEIALTTYETLRLCLDELNSLEWSAVIVD 272
Cdd:cd18002     56 IAPASTLHNWQQEISRFvPQFKVLPYWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  273 EAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVE-HGQRHTATKREla 351
Cdd:cd18002    136 EAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH-- 213
                          250       260
                   ....*....|....*....|
gi 2462624628  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 1.36e-27

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: 113.22  E-value: 1.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  113 DSIPYTINRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkepl 192
Cdd:cd18064      6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYR--------NIP------------ 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  193 sstakKMFLIVAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIR--VKQRKCEIALTTYETLRLCLDELNSLEWSA 268
Cdd:cd18064     66 -----GPHMVLVPKSTLHNWMAEFKRWvPTLRAVCLIGDKDQRAaFVRdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRY 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  269 VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtatKR 348
Cdd:cd18064    141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TN 208
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462624628  349 ELATGRKAMQRLAKKMSGWFLRRTKTLIKDQLPKKE 384
Cdd:cd18064    209 NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
508-621 1.91e-27

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 107.68  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  508 GKMKVLQQLLNhcRKNRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStQDVNIcLVSTMAGG 587
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK-GKIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462624628  588 LGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIG 621
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
123-336 1.94e-26

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 108.83  E-value: 1.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHyihGGGCILGDDMGLGKTVQVISFLAAVlhkkgtrediENNMPefllrsmkkeplsstakkmFLI 202
Cdd:cd18010      1 LLPFQREGVCFALRR---GGRVLIADEMGLGKTVQAIAIAAYY----------REEWP-------------------LLI 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW----GYFRVTVLHGNRkdnELIRVKQRKceIALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd18010     49 VCPSSLRLTWADEIERWlpslPPDDIQVIVKSK---DGLRDGDAK--VVIVSYDLLRRLEKQLLARKFKVVICDESHYLK 123
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  279 NPKA-RVTEVMKALK-CNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDP 336
Cdd:cd18010    124 NSKAkRTKAALPLLKrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
123-341 2.47e-26

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: 109.00  E-value: 2.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-LYKEGH------------------------SKGPYLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWGY-FRVTVLHGNRKDNELIRVK----------------------QRKCEIALTTYETLRLCLD 259
Cdd:cd18057     56 SAPLSTIINWEREFEMWAPdFYVVTYTGDKESRSVIRENefsfednairsgkkvfrmkkeaQIKFHVLLTSYELITIDQA 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18057    136 ILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKE 215

                   ..
gi 2462624628  340 GQ 341
Cdd:cd18057    216 DQ 217
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
123-341 7.20e-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: 107.79  E-value: 7.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH------------------------TKGPFLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 259
Cdd:cd18055     56 SAPLSTIINWEREFQMWApdfyvvtytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQA 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18055    136 ALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKE 215

                   ..
gi 2462624628  340 GQ 341
Cdd:cd18055    216 DQ 217
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
123-320 3.02e-25

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 104.39  E-value: 3.02e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAavlhkkgtrediennmpeFLLRSMKKEPlsstakkmFLI 202
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA------------------YLKEIGIPGP--------HLV 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-YFRVTVLHGNRKDNELIRV----KQRKCEIALTTYETLRLCLDE---LNSLEWSAVIVDEA 274
Cdd:cd17998     55 VVPSSTLDNWLREFKRWCpSLKVEPYYGSQEERKHLRYdilkGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEG 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462624628  275 HRIKNPKA-RVTEVMKaLKCNVRIGLTGTILQNNMKELWCVMDWAVP 320
Cdd:cd17998    135 HMLKNMTSeRYRHLMT-INANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
123-373 3.40e-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: 105.87  E-value: 3.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtredienNMPefllrsmkkeplsstakKMFLI 202
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYR--------NIP-----------------GPHMV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTW-GYFRVTVLHGNRKDNE-LIRVKQRKCE--IALTTYETLRLCLDELNSLEWSAVIVDEAHRIK 278
Cdd:cd18065     71 LVPKSTLHNWMNEFKRWvPSLRAVCLIGDKDARAaFIRDVMMPGEwdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  279 NPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSdpvehgqrhtaTKRELATgRKAMQ 358
Cdd:cd18065    151 NEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVE 218
                          250
                   ....*....|....*
gi 2462624628  359 RLAKKMSGWFLRRTK 373
Cdd:cd18065    219 RLHAVLKPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
119-373 3.81e-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: 106.30  E-value: 3.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  119 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKgtrediENNMPefllrsmkkeplsstakk 198
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK------RLNGP------------------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  199 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 275
Cdd:cd18063     76 -YLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTpamRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGH 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  276 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 353
Cdd:cd18063    155 RMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETIL- 233
                          250       260
                   ....*....|....*....|
gi 2462624628  354 rkAMQRLAKKMSGWFLRRTK 373
Cdd:cd18063    234 --IIRRLHKVLRPFLLRRLK 251
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
123-341 5.23e-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: 105.15  E-value: 5.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAvLHKKGTrediennmpefllrsmkkeplsstAKKMFLI 202
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS-LYKEGH------------------------SKGPFLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYNWKDELDTWG-----------------------YFRVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLD 259
Cdd:cd18056     56 SAPLSTIINWEREFEMWApdmyvvtyvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMA 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  260 ELNSLEWSAVIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH 339
Cdd:cd18056    136 ILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKE 215

                   ..
gi 2462624628  340 GQ 341
Cdd:cd18056    216 DQ 217
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
139-371 9.52e-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: 9.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  139 IHGGgcILGDDMGLGKTVQVISFLAAvlhkkgtrediennmpefllrsmkkeplsstakKMFLIVAPLSVLYNWKDELD- 217
Cdd:cd18071     48 VRGG--ILADDMGLGKTLTTISLILA---------------------------------NFTLIVCPLSVLSNWETQFEe 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  218 --TWGYFRVTVLHG---NRKDNELIrvkqrKCEIALTTYETLrlCLDE-------LNSLEWSAVIVDEAHRIKNPKARVT 285
Cdd:cd18071     93 hvKPGQLKVYTYHGgerNRDPKLLS-----KYDIVLTTYNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  286 EVMKALKCNVRIGLTGTILQNNMKELWCVMdwavpgllgsgTYFK-KQFSDPvEHGQRhtATKRELATG-RKAMQRLAKK 363
Cdd:cd18071    166 KAVLNLSSERRWVLTGTPIQNSPKDLGSLL-----------SFLHlKPFSNP-EYWRR--LIQRPLTMGdPTGLKRLQVL 231

                   ....*...
gi 2462624628  364 MSGWFLRR 371
Cdd:cd18071    232 MKQITLRR 239
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
123-350 1.25e-24

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: 104.58  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIH---------GGGCILGDDMGLGKTVQVISFLAAVL-HKKgtREDIennmpefllrsmkkepl 192
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCEslkktkkspGSGCILAHCMGLGKTLQVVTFLHTVLlCEK--LENF----------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  193 sstakKMFLIVAPLSVLYNWKDELDTWgyfrvtvLHGNRKDN-----ELIRVK------------QRKCEIALTTYETLR 255
Cdd:cd18068     62 -----SRVLVVCPLNTVLNWLNEFEKW-------QEGLKDEEkievnELATYKrpqersyklqrwQEEGGVMIIGYDMYR 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  256 LCLDELN-SLEWSA---------------VIVDEAHRIKNPKARVTEVMKALKCNVRIGLTGTILQNNMKELWCVMDWAV 319
Cdd:cd18068    130 ILAQERNvKSREKLkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462624628  320 PGLLGSGTYFKKQFSDPVEHGQRHTATKREL 350
Cdd:cd18068    210 PNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
119-373 4.14e-24

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


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 103.20  E-value: 4.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  119 INRYLRDYQREGTRFLYGHYIHGGGCILGDDMGLGKTVQVISFLAAVLHKKGTredienNMPefllrsmkkeplsstakk 198
Cdd:cd18062     20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRI------NGP------------------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  199 mFLIVAPLSVLYNWKDELDTWGYFRVTVLHGNR---KDNELIRVKQRKCEIALTTYETLRLCLDELNSLEWSAVIVDEAH 275
Cdd:cd18062     76 -FLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSpaaRRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGH 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  276 RIKNPKARVTEVMKA-LKCNVRIGLTGTILQNNMKELWCVMDWAVPGLLGSGTYFKKQFSDPVEH-GQRHTATKRELATg 353
Cdd:cd18062    155 RMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL- 233
                          250       260
                   ....*....|....*....|
gi 2462624628  354 rkAMQRLAKKMSGWFLRRTK 373
Cdd:cd18062    234 --IIRRLHKVLRPFLLRRLK 251
DEXDc smart00487
DEAD-like helicases superfamily;
123-312 1.85e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.87  E-value: 1.85e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   123 LRDYQREGTRFLYGHYihgGGCILGDDMGLGKTVQVISFLAAVLHKKGtrediennmpefllrsmkkeplsstaKKMFLI 202
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK--------------------------GGRVLV 59
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   203 VAPLSVL-YNWKDELDTWGYF----RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCL--DELNSLEWSAVIVDEAH 275
Cdd:smart00487   60 LVPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAH 139
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462624628   276 RIKNPKAR--VTEVMKAL-KCNVRIGLTGTILQNNMKELW 312
Cdd:smart00487  140 RLLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
538-621 8.69e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 8.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   538 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNStqDVNICLVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRA 617
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 2462624628   618 YRIG 621
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
18-73 8.11e-21

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


Pssm-ID: 410471  Cd Length: 59  Bit Score: 87.38  E-value: 8.11e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462624628   18 WHPGERCLAPSPDNGKLCEASIKSITVDENGKSFAVVLYADF---QERKIPLKQLQEVK 73
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYesdEDEKVPVSKLQKVK 59
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
143-312 1.89e-19

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: 89.46  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  143 GCILGDDMGLGKTVQVIsflAAVLHKKGTREDIENNMPEFLLRSMKKEPLSSTAKKMFLIVAPLSVLYNWKDELDT---W 219
Cdd:cd18072     22 GGILADDMGLGKTLTMI---ALILAQKNTQNRKEEEKEKALTEWESKKDSTLVPSAGTLVVCPASLVHQWKNEVESrvaS 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  220 GYFRVTVLHGNRKDNelIRVKQRKCEIALTTYETL---------RLCLDELNSLEWSAVIVDEAHRIKNPKARVTEVMKA 290
Cdd:cd18072     99 NKLRVCLYHGPNRER--IGEVLRDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                          170       180
                   ....*....|....*....|..
gi 2462624628  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 1.25e-17

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: 1.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYghyIHGGgcILGDDMGLGKTVQVISFLAAvlHkkgTREDIENNMPEFLLRSMKKEPLSSTAKKMF-- 200
Cdd:cd18070      1 LLPYQRRAVNWML---VPGG--ILADEMGLGKTVEVLALILL--H---PRPDNDLDAADDDSDEMVCCPDCLVAETPVss 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  201 ---LIVAPLSVLYNWKDELD--TWGYFRVTVLHGNRKDNELIRVKQRK---CEIALTTYETLRLCLDE------------ 260
Cdd:cd18070     71 katLIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALASPAPEIlaeYDIVVTTYDVLRTELHYaeanrsnrrrrr 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462624628  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 6.58e-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: 6.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHyiHGGGCILgdDMGLGKTVQVISFLAAVLHKKGTREdiennmpefllrsmkkeplsstakkmFLI 202
Cdd:cd18013      1 PHPYQKVAINFIIEH--PYCGLFL--DMGLGKTVTTLTALSDLQLDDFTRR--------------------------VLV 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  203 VAPLSVLYN-WKDELDTWGYFR---VTVLHGNRKdnELIRVKQRKCEIALTTYETLR-LCLDELNSLEWSAVIVDEAHRI 277
Cdd:cd18013     51 IAPLRVARStWPDEVEKWNHLRnltVSVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSF 128
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462624628  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 3.99e-14

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 72.71  E-value: 3.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREgtrFLYGHYIHG-GGCILGDDMGLGKTVQVisflAAVLHkkgtrediennmpEFLLRSMKKEplsstakkmFL 201
Cdd:cd18011      1 PLPHQID---AVLRALRKPpVRLLLADEVGLGKTIEA----GLIIK-------------ELLLRGDAKR---------VL 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  202 IVAPLSVLYNWKDELDTWGYFRVTVLHGNRKDNELIRVKQRKCE--IALTTYETLR---LCLDELNSLEWSAVIVDEAHR 276
Cdd:cd18011     52 ILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHK 131
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462624628  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 6.56e-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: 6.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628   80 RNLIFDDEDLEKPYFPNRKFPSSSVAFKLSDNGDSIPYTinryLRDYQREGTRFLYGHYIHGGG-CILGDDMGLGKTVqV 158
Cdd:COG1061     42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGGGrGLVVAPTGTGKTV-L 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  159 ISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGNRKDNEli 237
Cdd:COG1061    117 ALALAAELLRGKR----------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462624628  238 rvkqrkCEIALTTYETL--RLCLDELNSlEWSAVIVDEAHRIknPKARVTEVMKALKCNVRIGLTGT 302
Cdd:COG1061    165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
ResIII pfam04851
Type III restriction enzyme, res subunit;
123-302 8.05e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 59.22  E-value: 8.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHG--GGCIlgdDM--GLGKTVqVISFLAAVLHKKGTrediennmpefllrsmkkeplsstaKK 198
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTL-TAAKLIARLFKKGP-------------------------IK 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  199 MFLIVAP-LSVLYNWKDELDTWG---YFRVTVLHGNRKDNElirvkQRKCEIALTTYETL----RLCLDELNSLEWSAVI 270
Cdd:pfam04851   55 KVLFLVPrKDLLEQALEEFKKFLpnyVEIGEIISGDKKDES-----VDDNKIVVTTIQSLykalELASLELLPDFFDVII 129
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462624628  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 9.09e-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: 9.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  123 LRDYQREGTRFLYGHYIHGGGCIlgdDM--GLGKTVqvISFLAAVLHKKGTrediennmpefllrsmkkeplsstakkmF 200
Cdd:cd17926      1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTL--TALALIAYLKELR----------------------------T 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  201 LIVAP-LSVLYNWKDELDTWGYFR-VTVLHGNRKDnelirvKQRKCEIALTTYETLRLCLDELNSL--EWSAVIVDEAHR 276
Cdd:cd17926     48 LIVVPtDALLDQWKERFEDFLGDSsIGLIGGGKKK------DFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHH 121
                          170       180
                   ....*....|....*....|....*.
gi 2462624628  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 1.11e-08

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


Pssm-ID: 410549  Cd Length: 50  Bit Score: 52.25  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462624628   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 8.92e-08

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 53.46  E-value: 8.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  194 STAKKMFLIVAPLSV-LYNWKDELDTWGYF---RVTVLHGNRKDnelirvKQRKCEIALTTYETLR----------LCLD 259
Cdd:cd18029     48 CTIKKSTLVLCTSAVsVEQWRRQFLDWTTIddeQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFME 121
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462624628  260 ELNSLEWSAVIVDEAHRIKNPKARvtEVMKALKCNVRIGLTGTIL 304
Cdd:cd18029    122 FITEREWGLIILDEVHVVPAPMFR--RVLTLQKAHCKLGLTATLV 164
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
504-676 1.15e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.66  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  504 PKYSGKMKVLQQLLNhcrKNRD-KVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEFnSTQ 574
Cdd:COG1111    335 PKLSKLREILKEQLG---TNPDsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERF-RAG 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  575 DVNIcLVSTMAGGLGLNFVGANVVVLFDPTWNPandLQAIDRAYRIGQCRDVKVLRLISLGTVEEIMYlrQIYKQREGQV 654
Cdd:COG1111    411 EFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRDEAYY--WSSRRKEKKM 484
                          170       180
                   ....*....|....*....|..
gi 2462624628  655 EAGIMTATTWLKEGPPAHKLEM 676
Cdd:COG1111    485 KSILKKLKKLLDKQEKEKLKES 506
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
141-302 3.47e-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: 3.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  141 GGGCILGDDMGLGKTvqVISFLAAVLHkkgtrediennmpefllrsmkkepLSSTAKKmFLIVAPLSVL-YNWKDELDTW 219
Cdd:cd00046      1 GENVLITAPTGSGKT--LAALLAALLL------------------------LLKKGKK-VLVLVPTKALaLQTAERLREL 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  220 GYF--RVTVLHGNRKDNELIRVKQRKCEIALTTYETLRLCLDELNSL---EWSAVIVDEAHRIKnPKARVTEVMKALKCN 294
Cdd:cd00046     54 FGPgiRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALL-IDSRGALILDLAVRK 132
                          170
                   ....*....|....
gi 2462624628  295 V------RIGLTGT 302
Cdd:cd00046    133 AglknaqVILLSAT 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
580-622 6.46e-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: 6.46e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462624628  580 LVSTMAGGLGLNFVGANVVVLFDPTWNPANDLQAIDRAYRIGQ 622
Cdd:cd18785     26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1067-1091 1.28e-03

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


Pssm-ID: 464308  Cd Length: 62  Bit Score: 38.36  E-value: 1.28e-03
                           10        20
                   ....*....|....*....|....*
gi 2462624628 1067 VAYIHSNQNVIGSSKAENHMSRWAA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRAE 62
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
197-303 1.95e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  197 KKMFLIVAPLSVL-YNWKDELDTWGYF---RVTVLHGNRKDNELIRvKQRKCEIALTTYETLRLCLDE---LNSLEWsaV 269
Cdd:pfam00270   45 GPQALVLAPTRELaEQIYEELKKLGKGlglKVASLLGGDSRKEQLE-KLKGPDILVGTPGRLLDLLQErklLKNLKL--L 121
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462624628  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 2.77e-03

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 40.40  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624628  198 KMFLIVAPLSVLYNWK-DELDTWGY--FRVTVLHG--NRKDNELirvkqRKCEIALTTYETLrlclDEL--NSLEW---- 266
Cdd:cd18028     46 GKALYLVPLRALASEKyEEFKKLEEigLKVGISTGdyDEDDEWL-----GDYDIIVATYEKF----DSLlrHSPSWlrdv 116
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462624628  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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