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Conserved domains on  [gi|1958729531|ref|XP_038952188|]
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DNA excision repair protein ERCC-6-like 2 isoform X3 [Rattus norvegicus]

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 ...
122-369 7.95e-146

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: 440.66  E-value: 7.95e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKESSSTARKMFLIV 201
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-TRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNA 280
Cdd:cd18005     77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  281 RVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                   ....*....
gi 1958729531  361 KMSGYFLRR 369
Cdd:cd18005    237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
47-649 1.11e-126

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 406.53  E-value: 1.11e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   47 GEPFAVVLYPDFQEKKIPLQRLQEVKSTKDHSRSLIFDDEDLEKPYFPDQKIPSLVSAfQLSEDGDSIPYTINRYLRDYQ 126
Cdd:COG0553    168 LLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQ 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  127 REGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmPefllksmkkessstarkmFLIVAPLSV 206
Cdd:COG0553    247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------P------------------VLIVAPTSL 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  207 LYNWKDELDTWGY-FRVTVLHGSKKDNELTRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNARVTEV 285
Cdd:COG0553    302 VGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  286 MKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGY 365
Cdd:COG0553    381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPF 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  366 FLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSQGDTVRTLCLS 445
Cdd:COG0553    449 LLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILA 506
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  446 YLTVLQKVANHVALLQAastskhqetlikricdqvfsrfpdfvqkskdaafETLSDPKYSGKMKVLDQLLNHFRKHRDKV 525
Cdd:COG0553    507 ALTRLRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKV 552
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  526 LLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFIGANVVILFDPTWNP 605
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1958729531  606 ANDLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553    633 AVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
17-72 2.78e-17

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20400:

Pssm-ID: 470623  Cd Length: 59  Bit Score: 76.98  E-value: 2.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958729531   17 WCPGERCLAPSLDNKKLCEASIKSITVDENGEPFAVVL---YPDFQEKKIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
VIGSSK super family cl20696
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1132-1155 6.05e-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: 36.43  E-value: 6.05e-03
                           10        20
                   ....*....|....*....|....
gi 1958729531 1132 VAYIHSNQNVIGSSRAENHMSRWA 1155
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
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 ...
122-369 7.95e-146

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: 440.66  E-value: 7.95e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKESSSTARKMFLIV 201
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-TRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNA 280
Cdd:cd18005     77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  281 RVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                   ....*....
gi 1958729531  361 KMSGYFLRR 369
Cdd:cd18005    237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
47-649 1.11e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 406.53  E-value: 1.11e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   47 GEPFAVVLYPDFQEKKIPLQRLQEVKSTKDHSRSLIFDDEDLEKPYFPDQKIPSLVSAfQLSEDGDSIPYTINRYLRDYQ 126
Cdd:COG0553    168 LLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQ 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  127 REGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmPefllksmkkessstarkmFLIVAPLSV 206
Cdd:COG0553    247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------P------------------VLIVAPTSL 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  207 LYNWKDELDTWGY-FRVTVLHGSKKDNELTRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNARVTEV 285
Cdd:COG0553    302 VGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  286 MKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGY 365
Cdd:COG0553    381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPF 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  366 FLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSQGDTVRTLCLS 445
Cdd:COG0553    449 LLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILA 506
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  446 YLTVLQKVANHVALLQAastskhqetlikricdqvfsrfpdfvqkskdaafETLSDPKYSGKMKVLDQLLNHFRKHRDKV 525
Cdd:COG0553    507 ALTRLRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKV 552
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  526 LLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFIGANVVILFDPTWNP 605
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1958729531  606 ANDLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553    633 AVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-654 8.06e-72

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 261.27  E-value: 8.06e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  115 PYTINRYLRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTrediennmpefllksmkkesssTA 194
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI----------------------TG 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  195 RKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELTR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAI 267
Cdd:PLN03142   221 PHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYI 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkre 347
Cdd:PLN03142   296 IIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------- 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  348 latgrKAMHRLAKKMSGYFLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrk 427
Cdd:PLN03142   369 -----EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  428 ccyktNSQGDtvRTLCLSYLTVLQKVANHVALLQAASTSkhqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySGK 507
Cdd:PLN03142   426 -----NAGGE--RKRLLNIAMQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGK 472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  508 MKVLDQLLNHFRKHRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGL 586
Cdd:PLN03142   473 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGL 552
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958729531  587 GLNFIGANVVILFDPTWNPANDLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMYLRQVYKQQLHCVVV 654
Cdd:PLN03142   553 GINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
125-460 1.17e-66

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 226.80  E-value: 1.17e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  125 YQREGAQFLYRHYIK-GRGCILGDDMGLGKTIQVISFLAAVLHkkgtredIENNmpefllksmkkessstARKMFLIVAP 203
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKH-------VDKN----------------WGGPTLIVVP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  204 LSVLYNWKDELDTW---GYFRVTVLHGSKKDNELTRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:pfam00176   58 LSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  278 PNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHR 357
Cdd:pfam00176  138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSR 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  358 LAKKMSGYFLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLETEDVALILTSsqpctcgsgqkrrkccyktnSQGD 437
Cdd:pfam00176  207 LHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTG--------------------EGGR 266
                          330       340
                   ....*....|....*....|...
gi 1958729531  438 TVRTLCLSYLTVLQKVANHVALL 460
Cdd:pfam00176  267 EIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
504-630 9.72e-57

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: 192.31  E-value: 9.72e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  504 YSGKMKVLDQLLNHFRKHRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMA 583
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958729531  584 GGLGLNFIGANVVILFDPTWNPANDLQAIDRAYRIGQCRDVKVFRLI 630
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
506-619 4.36e-28

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: 109.61  E-value: 4.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  506 GKMKVLDQLLNhfRKHRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSqDVNIcLVSTMAGG 585
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958729531  586 LGLNFIGANVVILFDPTWNPANDLQAIDRAYRIG 619
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
122-310 1.15e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.04  E-value: 1.15e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   122 LRDYQREGAQFLYRHYikgRGCILGDDMGLGKTIQVISFLAAVLHKKGtrediennmpefllksmkkessstaRKMFLIV 201
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-------------------------GGRVLVL 60
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   202 APLSVL-YNWKDELDTWGYF----RVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHR 274
Cdd:smart00487   61 VPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHR 140
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1958729531   275 IRNPNAR--VTEVMKAV-KCKVRIGLTGTILQNNMKELW 310
Cdd:smart00487  141 LLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
536-619 3.25e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.89  E-value: 3.25e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   536 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSsqDVNICLVSTMAGGLGLNFIGANVVILFDPTWNPANDLQAIDRA 615
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1958729531   616 YRIG 619
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
17-72 2.78e-17

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: 76.98  E-value: 2.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958729531   17 WCPGERCLAPSLDNKKLCEASIKSITVDENGEPFAVVL---YPDFQEKKIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
122-300 1.59e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.59  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKG--RGCILGDdMGLGKTIqVISFLAAVLHKKGTrediennmpefllksmkkessstarkmFL 199
Cdd:COG1061     81 LRPYQQEALEALLAALERGggRGLVVAP-TGTGKTV-LALALAAELLRGKR---------------------------VL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  200 IVAPLSVLYN-WKDELDTWgyFRVTVLHGSKKDNEltrlkqrkCEIALTTYETL--RLCLEELNSlEWSAIIVDEAHRIr 276
Cdd:COG1061    132 VLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD--------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA- 199
                          170       180
                   ....*....|....*....|....
gi 1958729531  277 nPNARVTEVMKAVKCKVRIGLTGT 300
Cdd:COG1061    200 -GAPSYRRILEAFPAAYRLGLTAT 222
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1132-1155 6.05e-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: 36.43  E-value: 6.05e-03
                           10        20
                   ....*....|....*....|....
gi 1958729531 1132 VAYIHSNQNVIGSSRAENHMSRWA 1155
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
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 ...
122-369 7.95e-146

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: 440.66  E-value: 7.95e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKESSSTARKMFLIV 201
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-TRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNA 280
Cdd:cd18005     77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  281 RVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                   ....*....
gi 1958729531  361 KMSGYFLRR 369
Cdd:cd18005    237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
47-649 1.11e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 406.53  E-value: 1.11e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   47 GEPFAVVLYPDFQEKKIPLQRLQEVKSTKDHSRSLIFDDEDLEKPYFPDQKIPSLVSAfQLSEDGDSIPYTINRYLRDYQ 126
Cdd:COG0553    168 LLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQ 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  127 REGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmPefllksmkkessstarkmFLIVAPLSV 206
Cdd:COG0553    247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR-------P------------------VLIVAPTSL 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  207 LYNWKDELDTWGY-FRVTVLHGSKKDNELTRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNARVTEV 285
Cdd:COG0553    302 VGNWQRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKA 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  286 MKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGY 365
Cdd:COG0553    381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPF 448
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  366 FLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSQGDTVRTLCLS 445
Cdd:COG0553    449 LLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILA 506
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  446 YLTVLQKVANHVALLQAastskhqetlikricdqvfsrfpdfvqkskdaafETLSDPKYSGKMKVLDQLLNHFRKHRDKV 525
Cdd:COG0553    507 ALTRLRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKV 552
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  526 LLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFIGANVVILFDPTWNP 605
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 1958729531  606 ANDLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553    633 AVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-654 8.06e-72

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 261.27  E-value: 8.06e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  115 PYTINRYLRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTrediennmpefllksmkkesssTA 194
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI----------------------TG 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  195 RKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELTR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAI 267
Cdd:PLN03142   221 PHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYI 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkre 347
Cdd:PLN03142   296 IIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------- 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  348 latgrKAMHRLAKKMSGYFLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrk 427
Cdd:PLN03142   369 -----EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------- 425
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  428 ccyktNSQGDtvRTLCLSYLTVLQKVANHVALLQAASTSkhqetlikricdqvfsrfPDFVqkSKDAAFETlsdpkySGK 507
Cdd:PLN03142   426 -----NAGGE--RKRLLNIAMQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGK 472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  508 MKVLDQLLNHFRKHRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGL 586
Cdd:PLN03142   473 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGL 552
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958729531  587 GLNFIGANVVILFDPTWNPANDLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMYLRQVYKQQLHCVVV 654
Cdd:PLN03142   553 GINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
122-318 5.32e-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: 232.07  E-value: 5.32e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGtrediennmpefllksmkkessstARKMFLIV 201
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGK------------------------ERGPVLVV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNE--LTRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRNP 278
Cdd:cd17919     57 CPLSVLENWEREFEKWtPDLRVVVYHGSQRERAqiRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNP 136
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958729531  279 NARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVP 318
Cdd:cd17919    137 KSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
125-460 1.17e-66

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 226.80  E-value: 1.17e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  125 YQREGAQFLYRHYIK-GRGCILGDDMGLGKTIQVISFLAAVLHkkgtredIENNmpefllksmkkessstARKMFLIVAP 203
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKH-------VDKN----------------WGGPTLIVVP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  204 LSVLYNWKDELDTW---GYFRVTVLHGSKKDNELTRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:pfam00176   58 LSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  278 PNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHR 357
Cdd:pfam00176  138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSR 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  358 LAKKMSGYFLRRTKTLIKGQLPKKEDRMVYSSLTDFQKAVYQTVLETEDVALILTSsqpctcgsgqkrrkccyktnSQGD 437
Cdd:pfam00176  207 LHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTG--------------------EGGR 266
                          330       340
                   ....*....|....*....|...
gi 1958729531  438 TVRTLCLSYLTVLQKVANHVALL 460
Cdd:pfam00176  267 EIKASLLNILMRLRKICNHPGLI 289
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
122-369 2.51e-59

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 203.76  E-value: 2.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefLLKSMkkessstarkmfLIV 201
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-------------LIKSV------------LVV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGY-FRVTVLHGSKK---DNELTRLKQRKcEIALTTYETLRLCLEELNSLE-----WSAIIVDEA 272
Cdd:cd18001     56 MPTSLIPHWVKEFAKWTPgLRVKVFHGTSKkerERNLERIQRGG-GVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEG 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  273 HRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPG-LLGSRIHFKKQFSDPVEHGQRHTATKRELATG 351
Cdd:cd18001    135 HKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALG 214
                          250
                   ....*....|....*...
gi 1958729531  352 RKAMHRLAKKMSGYFLRR 369
Cdd:cd18001    215 SEVAENLRQIIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
504-630 9.72e-57

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: 192.31  E-value: 9.72e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  504 YSGKMKVLDQLLNHFRKHRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMA 583
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958729531  584 GGLGLNFIGANVVILFDPTWNPANDLQAIDRAYRIGQCRDVKVFRLI 630
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
122-371 1.15e-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: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLY--RHYikGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmPefllksmkkessstarkmFL 199
Cdd:cd18012      5 LRPYQKEGFNWLSflRHY--GLGGILADDMGLGKTLQTLALLLSRKEEGRKG-------P------------------SL 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  200 IVAPLSVLYNWKDELDTWG-YFRVTVLHGSK-KDNELTRLKQRkcEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:cd18012     58 VVAPTSLIYNWEEEAAKFApELKVLVIHGTKrKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKN 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  278 PNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkrelatgRKAMHR 357
Cdd:cd18012    136 PQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEE 204
                          250
                   ....*....|....
gi 1958729531  358 LAKKMSGYFLRRTK 371
Cdd:cd18012    205 LKKLISPFILRRLK 218
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
122-369 1.57e-53

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: 187.49  E-value: 1.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLY-----RHYIKGRGCILGDDMGLGKTIQVISFLAAVLhKKGtrediennmpefllksmkKESSSTARK 196
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVWTLL-KQG------------------PYGKPTAKK 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  197 mFLIVAPLSVLYNWKDELDTW-GYFRVTVL--HGSKKDNELTRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIV- 269
Cdd:cd18004     62 -ALIVCPSSLVGNWKAEFDKWlGLRRIKVVtaDGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKISIDLLIc 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  270 DEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELA 349
Cdd:cd18004    141 DEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKE 220
                          250       260
                   ....*....|....*....|
gi 1958729531  350 TGRKAMHRLAKKMSGYFLRR 369
Cdd:cd18004    221 LGAERSQELSELTSRFILRR 240
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
122-339 5.66e-52

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: 182.45  E-value: 5.66e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREdiennmPefllksmkkessstarkmFLIV 201
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRG------P------------------FLVI 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd17995     57 APLSTIPNWQREFETWTDMNVVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRVV 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 339
Cdd:cd17995    137 VVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQ 208
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
122-369 3.27e-46

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: 165.99  E-value: 3.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQ---FLYRHYIKGrgcILGDDMGLGKTIQVISFLAAVLHKKgtrediENNMPEFLLKSmkkessstarkmf 198
Cdd:cd17999      1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLCILASDHHKR------ANSFNSENLPS------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  199 LIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRI 275
Cdd:cd17999     59 LVVCPPTLVGHWVAEIKKYfpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHII 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  276 RNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAM 355
Cdd:cd17999    139 KNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALAL 218
                          250
                   ....*....|....
gi 1958729531  356 HRLAKKMSGYFLRR 369
Cdd:cd17999    219 EALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
122-321 1.03e-45

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: 163.26  E-value: 1.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkesSSTARKMFLIV 201
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH------------------------SKLGLGPSLIV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW-GYFRVTVLH--------GSKKDNELTRLKQRKCE-----IALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18000     57 CPATVLKQWVKEFHRWwPPFRVVVLHssgsgtgsEEKLGSIERKSQLIRKVvgdggILITTYEGFRKHKDLLLNHNWQYV 136
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLL 321
Cdd:cd18000    137 ILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
122-353 9.43e-45

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: 162.08  E-value: 9.43e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRH-------YIKGRGCILGDDMGLGKTIQVISFLAAVL--HKKGTRediennmpefllksmkkesss 192
Cdd:cd18007      1 LKPHQVEGVRFLWSNlvgtdvgSDEGGGCILAHTMGLGKTLQVITFLHTYLaaAPRRSR--------------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  193 tarkmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDN-ELTRLK-----QRKCEIALTTYETLRLCLEELNSLE 263
Cdd:cd18007     60 -----PLVLCPASTLYNWEDEFKKWlppDLRPLLVLVSLSASKrADARLRkinkwHKEGGVLLIGYELFRNLASNATTDP 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  264 WSA--------------IIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKK 329
Cdd:cd18007    135 RLKqefiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKK 214
                          250       260
                   ....*....|....*....|....
gi 1958729531  330 QFSDPVEHGQRHTATKRELATGRK 353
Cdd:cd18007    215 KFVKPIEAGQCVDSTEEDVRLMLK 238
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
122-369 1.42e-39

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


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 146.35  E-value: 1.42e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKESSstarkmFLIV 201
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS------------------YLFHSQQQYGP------FLVV 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELTR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd17993     58 VPLSTMPAWQREFAKWApDMNVIVYLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEA 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  273 HRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGllgsRIHFKKQFSDpvEHGQrhtatKRElatgr 352
Cdd:cd17993    138 HRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG----KFDIWEEFEE--EHDE-----EQE----- 201
                          250
                   ....*....|....*..
gi 1958729531  353 KAMHRLAKKMSGYFLRR 369
Cdd:cd17993    202 KGIADLHKELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
122-371 5.70e-39

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


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 144.77  E-value: 5.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTredienNMPefllksmkkessstarkmFLIV 201
Cdd:cd17997      4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNI------NGP------------------HLII 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW-GYFRVTVLHGSKK-DNELTR--LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:cd17997     60 VPKSTLDNWMREFKRWcPSLRVVVLIGDKEeRADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKN 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  278 PNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKrelatgrkamhR 357
Cdd:cd17997    140 EKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQ-----------R 208
                          250
                   ....*....|....
gi 1958729531  358 LAKKMSGYFLRRTK 371
Cdd:cd17997    209 LHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
122-371 2.70e-37

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: 140.60  E-value: 2.70e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVlhkkgtredIENNMPefllksmkkessstarKMFLIV 201
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL---------RERGVW----------------GPFLVI 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKD-NELTRLKQRK------CEIALTTYETLRLCLEELNSLEWSAIIVDEAH 273
Cdd:cd18009     59 APLSTLPNWVNEFARFTpSVPVLLYHGTKEErERLRKKIMKRegtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGH 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  274 RIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFsDPVEHGQRhTATKRELATGRK 353
Cdd:cd18009    139 RLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLSEERE 216
                          250       260
                   ....*....|....*....|
gi 1958729531  354 A--MHRLAKKMSGYFLRRTK 371
Cdd:cd18009    217 QniVHMLHAILKPFLLRRLK 236
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
122-369 7.79e-37

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: 139.21  E-value: 7.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLY-----RHYIKGRGCILGDDMGLGKTIQVISFLAAVLhkkgtREDIENNMPefllksmkkessstARK 196
Cdd:cd18066      1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLL-----RQGPYGGKP--------------VIK 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  197 MFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDNELtrLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAH 273
Cdd:cd18066     62 RALIVTPGSLVKNWKKEFQKWlgsERIKVFTVDQDHKVEEF--IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGH 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  274 RIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRK 353
Cdd:cd18066    140 RLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEA 219
                          250
                   ....*....|....*.
gi 1958729531  354 AMHRLAKKMSGYFLRR 369
Cdd:cd18066    220 RAAELTRLTGLFILRR 235
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
122-371 1.48e-36

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: 138.27  E-value: 1.48e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQF---LYRHYIKGrgcILGDDMGLGKTIQVISFLAAVLHKKGtredieNNMPefllksmkkessstarkmF 198
Cdd:cd17996      4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTISLITYLMEKKK------NNGP------------------Y 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  199 LIVAPLSVLYNWKDELDTWGYFRVTVLH-GSKKDNELTRLKQRKCE--IALTTYETLRLCLEELNSLEWSAIIVDEAHRI 275
Cdd:cd17996     57 LVIVPLSTLSNWVSEFEKWAPSVSKIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRM 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  276 RNPNARVTEVMKAVKC-KVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHtatKRELATGRK 353
Cdd:cd17996    137 KNAQSKLTQTLNTYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEET 213
                          250       260
                   ....*....|....*....|
gi 1958729531  354 AM--HRLAKKMSGYFLRRTK 371
Cdd:cd17996    214 LLiiRRLHKVLRPFLLRRLK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
122-369 2.04e-36

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: 138.19  E-value: 2.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRhyikgRGCILGDDMGLGKTIQVIsflAAVLHKKGTREDIENNMPEFLLKSMKKESSSTarkmFLIV 201
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQAL---ALILATRPQDPKIPEELEENSSDPKKLYLSKT----TLIV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDT---WGYFRVTVLHGSKKDNELTRLKQrkCEIALTTYETLR------------LCLEE----LNSL 262
Cdd:cd18008     69 VPLSLLSQWKDEIEKhtkPGSLKVYVYHGSKRIKSIEELSD--YDIVITTYGTLAsefpknkkgggrDSKEKeaspLHRI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  263 EWSAIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWcvmdwavPGLLGSRIHFKKQFSdpvehGQRHT 342
Cdd:cd18008    147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLY-------SLLRFLRVEPFGDYP-----WFNSD 214
                          250       260
                   ....*....|....*....|....*..
gi 1958729531  343 ATKRELATGRKAMHRLAKKMSGYFLRR 369
Cdd:cd18008    215 ISKPFSKNDRKALERLQALLKPILLRR 241
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
122-369 2.40e-36

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: 137.99  E-value: 2.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRhYIKGR------GCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmkKESSSTAR 195
Cdd:cd18067      1 LRPHQREGVKFLYR-CVTGRrirgshGCIMADEMGLGKTLQCITLMWTLLRQS-------------------PQCKPEID 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  196 KMfLIVAPLSVLYNWKDELDTWGYFRVTVL--HGSKKDNELTRLKQRKCE--------IALTTYETLRLCLEELNSLEWS 265
Cdd:cd18067     61 KA-IVVSPSSLVKNWANELGKWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVG 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  266 AIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATK 345
Cdd:cd18067    140 LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASE 219
                          250       260
                   ....*....|....*....|....
gi 1958729531  346 RELATGRKAMHRLAKKMSGYFLRR 369
Cdd:cd18067    220 KERQLGEEKLQELISIVNRCIIRR 243
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
122-333 5.75e-34

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: 130.55  E-value: 5.75e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpEFLLKSMkkessstaRKMFLIV 201
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----------------EIFLMGI--------RGPFLII 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18058     56 APLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSCV 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18058    136 IIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD 201
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
122-369 9.33e-34

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: 129.78  E-value: 9.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGtredieNNMPEfllksmkkessstarkmfLIV 201
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPH------------------LIV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW--GyFRVTVLHGSKKDNELTR---LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIR 276
Cdd:cd18003     57 VPTSVMLNWEMEFKRWcpG-FKILTYYGSAKERKLKRqgwMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIK 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  277 NPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDP----VEHGQRHTatkrelatgR 352
Cdd:cd18003    136 NFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN---------E 206
                          250
                   ....*....|....*..
gi 1958729531  353 KAMHRLAKKMSGYFLRR 369
Cdd:cd18003    207 ELVRRLHKVLRPFLLRR 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
122-333 6.26e-33

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: 127.48  E-value: 6.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLhkkgtrediennmpefllksmkkesSSTARKMFLIV 201
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-------------------------NVGIHGPFLVI 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18060     56 APLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCV 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18060    136 IIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
122-339 1.27e-32

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: 126.85  E-value: 1.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYI---------KGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkessS 192
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIeslerykgsSGFGCILAHSMGLGKTLQVISFLDVLLR-------------------------H 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  193 TARKMFLIVAPLSVLYNWKDELDTW------------GYFRVTVLHGSKKDNElTRLK-----QRKCEIALTTYETLRLc 255
Cdd:cd18069     56 TGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrpRPFKVFILNDEHKTTA-ARAKviedwVKDGGVLLMGYEMFRL- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  256 lEELNSLewsaIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPV 335
Cdd:cd18069    134 -RPGPDV----VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI 208

                   ....
gi 1958729531  336 EHGQ 339
Cdd:cd18069    209 LNGQ 212
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
122-333 1.71e-32

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: 126.27  E-value: 1.71e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkessSTARKMFLIV 201
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILL-------------------------TGIRGPFLII 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18061     56 APLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCV 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18061    136 IIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
122-333 4.84e-32

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: 125.14  E-value: 4.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpEFLLKSMKKEssstarkmFLIV 201
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLY-----------------EIYLKGIHGP--------FLVI 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18059     56 APLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCV 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18059    136 VIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
122-369 1.15e-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: 124.35  E-value: 1.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmkkesssTARKMFLIV 201
Cdd:cd18054     21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH------------------------QLYGPFLLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELTR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd18054     77 VPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  273 HRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPgllgSRIHFKKQFSDpvEHGQrhtatKRElaTGR 352
Cdd:cd18054    157 HRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP----EKFEFWEDFEE--DHGK-----GRE--NGY 223
                          250
                   ....*....|....*..
gi 1958729531  353 KAMHRLakkMSGYFLRR 369
Cdd:cd18054    224 QSLHKV---LEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
122-369 1.84e-31

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: 122.93  E-value: 1.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKESSstarkmFLIV 201
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW------------------YLAGRLKLLGP------FLVL 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQRKCE----IALTTYEtlrLCLEE---LNSLEWSAIIVDEAHR 274
Cdd:cd18006     57 CPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAHR 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  275 IRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRI--HFKKQFSDpvehgqrhtaTKRELATGr 352
Cdd:cd18006    134 LKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAYSE----------TDDESETV- 202
                          250
                   ....*....|....*..
gi 1958729531  353 KAMHRLAKKmsgYFLRR 369
Cdd:cd18006    203 EELHLLLQP---FLLRR 216
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
122-369 5.57e-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: 119.38  E-value: 5.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmkkesssTARKMFLIV 201
Cdd:cd18053     21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEH------------------------QLYGPFLLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELTR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd18053     77 VPLSTLTSWQREIQTWApQMNAVVYLGDINSRNMIRthewmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  273 HRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPgllgSRIHFKKQFSDpvEHGQrhtatKRElaTGR 352
Cdd:cd18053    157 HRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP----EKFSSWEDFEE--EHGK-----GRE--YGY 223
                          250
                   ....*....|....*..
gi 1958729531  353 KAMHrlaKKMSGYFLRR 369
Cdd:cd18053    224 ASLH---KELEPFLLRR 237
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
122-333 7.10e-30

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: 117.93  E-value: 7.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLaavlhkkgtrediennmpefllKSMKKESSStaRKMFLIV 201
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------------------YSLYKEGHS--KGPFLVS 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGskkDNELtrlkqrkceiaLTTYETLRLCLEELNSLEWSAIIVDEAHRIRNPNA 280
Cdd:cd17994     57 APLSTIINWEREFEMWApDFYVVTYVG---DHVL-----------LTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQS 122
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958729531  281 RVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd17994    123 KFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
122-369 7.99e-29

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: 116.06  E-value: 7.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDiennmpefllksmkkessstarkmFLIV 201
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGP------------------------FLVI 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELTR---------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDE 271
Cdd:cd18002     57 APASTLHNWQQEISRFvPQFKVLPYWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDE 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  272 AHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVE-HGQRHTATKRElat 350
Cdd:cd18002    137 AQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH--- 213
                          250
                   ....*....|....*....
gi 1958729531  351 grkAMHRLAKKMSGYFLRR 369
Cdd:cd18002    214 ---QLKRLHMILKPFMLRR 229
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
506-619 4.36e-28

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: 109.61  E-value: 4.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  506 GKMKVLDQLLNhfRKHRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSqDVNIcLVSTMAGG 585
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958729531  586 LGLNFIGANVVILFDPTWNPANDLQAIDRAYRIG 619
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
139-369 2.34e-27

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 112.18  E-value: 2.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  139 KGRGCILGDDMGLGKTIQVISFLAAvlhkkgtrediennmpefllksmkkessstarKMFLIVAPLSVLYNWKDELD--- 215
Cdd:cd18071     47 LVRGGILADDMGLGKTLTTISLILA--------------------------------NFTLIVCPLSVLSNWETQFEehv 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  216 TWGYFRVTVLHGSKKDNELTRLKqrKCEIALTTYETLrlCLEE-------LNSLEWSAIIVDEAHRIRNPNARVTEVMKA 288
Cdd:cd18071     95 KPGQLKVYTYHGGERNRDPKLLS--KYDIVLTTYNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  289 VKCKVRIGLTGTILQNNMKELWCVMdwavpgllgSRIHFKKqFSDPvEHGQRhtATKRELATG-RKAMHRLAKKMSGYFL 367
Cdd:cd18071    171 LSSERRWVLTGTPIQNSPKDLGSLL---------SFLHLKP-FSNP-EYWRR--LIQRPLTMGdPTGLKRLQVLMKQITL 237

                   ..
gi 1958729531  368 RR 369
Cdd:cd18071    238 RR 239
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
112-382 3.59e-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: 111.68  E-value: 3.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  112 DSIPYTINRYLRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtredienNMPefllksmkkess 191
Cdd:cd18064      6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYR--------NIP------------ 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  192 starKMFLIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNE-LTR--LKQRKCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18064     66 ----GPHMVLVPKSTLHNWMAEFKRWvPTLRAVCLIGDKDQRAaFVRdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  268 IVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtatKRE 347
Cdd:cd18064    142 VIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TNN 209
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958729531  348 LATGRKAMHRLAKKMSGYFLRRTKTLIKGQLPKKE 382
Cdd:cd18064    210 CLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
122-339 6.62e-27

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: 110.49  E-value: 6.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkessstARKMFLIV 201
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH-----------------------TKGPFLVS 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-----------------------YFRVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEE 258
Cdd:cd18055     57 APLSTIINWEREFQMWApdfyvvtytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAA 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  259 LNSLEWSAIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHG 338
Cdd:cd18055    137 LGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKED 216

                   .
gi 1958729531  339 Q 339
Cdd:cd18055    217 Q 217
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
122-339 6.76e-27

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 110.54  E-value: 6.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkessstARKMFLIV 201
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-LYKEGH-----------------------SKGPYLVS 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGY-FRVTVLHGSK------KDNELT-------------RLK---QRKCEIALTTYETLRLCLEE 258
Cdd:cd18057     57 APLSTIINWEREFEMWAPdFYVVTYTGDKesrsviRENEFSfednairsgkkvfRMKkeaQIKFHVLLTSYELITIDQAI 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  259 LNSLEWSAIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHG 338
Cdd:cd18057    137 LGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKED 216

                   .
gi 1958729531  339 Q 339
Cdd:cd18057    217 Q 217
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
118-371 8.09e-27

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: 110.92  E-value: 8.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  118 INRYLRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediENNMPefllksmkkessstarkm 197
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHK------RLNGP------------------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  198 FLIVAPLSVLYNWKDELDTWGYFRVTVLHG---SKKDNELTRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHR 274
Cdd:cd18063     76 YLIIVPLSTLSNWTYEFDKWAPSVVKISYKgtpAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  275 IRNPNARVTEVMKA-VKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELATgr 352
Cdd:cd18063    156 MKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETIL-- 233
                          250
                   ....*....|....*....
gi 1958729531  353 kAMHRLAKKMSGYFLRRTK 371
Cdd:cd18063    234 -IIRRLHKVLRPFLLRRLK 251
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
122-348 1.95e-26

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: 109.59  E-value: 1.95e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLY---------RHYIKGRGCILGDDMGLGKTIQVISFLAAVLhkkgtrediennMPEfllksmKKESSS 192
Cdd:cd18068      1 LKPHQVDGVQFMWdccceslkkTKKSPGSGCILAHCMGLGKTLQVVTFLHTVL------------LCE------KLENFS 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  193 TArkmfLIVAPLSVLYNWKDELDTWgyfrvtvLHGSKKDN-----ELTRLK------------QRKCEIALTTYETLRLC 255
Cdd:cd18068     63 RV----LVVCPLNTVLNWLNEFEKW-------QEGLKDEEkievnELATYKrpqersyklqrwQEEGGVMIIGYDMYRIL 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  256 LEELN-SLEWSA---------------IIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPG 319
Cdd:cd18068    132 AQERNvKSREKLkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPN 211
                          250       260
                   ....*....|....*....|....*....
gi 1958729531  320 LLGSRIHFKKQFSDPVEHGQRHTATKREL 348
Cdd:cd18068    212 LLGTIKEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
118-371 4.00e-26

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: 108.98  E-value: 4.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  118 INRYLRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKGTredienNMPefllksmkkessstarkm 197
Cdd:cd18062     20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRI------NGP------------------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  198 FLIVAPLSVLYNWKDELDTWGYFRVTVLH-GSKKDNE--LTRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHR 274
Cdd:cd18062     76 FLIIVPLSTLSNWVYEFDKWAPSVVKVSYkGSPAARRafVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  275 IRNPNARVTEVMKA-VKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELATgr 352
Cdd:cd18062    156 MKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL-- 233
                          250
                   ....*....|....*....
gi 1958729531  353 kAMHRLAKKMSGYFLRRTK 371
Cdd:cd18062    234 -IIRRLHKVLRPFLLRRLK 251
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
122-339 4.25e-26

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: 108.23  E-value: 4.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkessstARKMFLIV 201
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS-LYKEGH-----------------------SKGPFLVS 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-----------------------YFRVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEE 258
Cdd:cd18056     57 APLSTIINWEREFEMWApdmyvvtyvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAI 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  259 LNSLEWSAIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHG 338
Cdd:cd18056    137 LGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKED 216

                   .
gi 1958729531  339 Q 339
Cdd:cd18056    217 Q 217
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
122-334 6.53e-26

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 106.91  E-value: 6.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHyiKGRgCILGDDMGLGKTIQVISFLAAVlhkkgtrediENNMPefllksmkkessstarkmFLIV 201
Cdd:cd18010      1 LLPFQREGVCFALRR--GGR-VLIADEMGLGKTVQAIAIAAYY----------REEWP------------------LLIV 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW----GYFRVTVLHGSKkdNELTRLKQRkceIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:cd18010     50 CPSSLRLTWADEIERWlpslPPDDIQVIVKSK--DGLRDGDAK---VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKN 124
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958729531  278 PNA-RVTEVMKAVK-CKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDP 334
Cdd:cd18010    125 SKAkRTKAALPLLKrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
DEXDc smart00487
DEAD-like helicases superfamily;
122-310 1.15e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.04  E-value: 1.15e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   122 LRDYQREGAQFLYRHYikgRGCILGDDMGLGKTIQVISFLAAVLHKKGtrediennmpefllksmkkessstaRKMFLIV 201
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-------------------------GGRVLVL 60
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   202 APLSVL-YNWKDELDTWGYF----RVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHR 274
Cdd:smart00487   61 VPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHR 140
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1958729531   275 IRNPNAR--VTEVMKAV-KCKVRIGLTGTILQNNMKELW 310
Cdd:smart00487  141 LLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
122-371 4.04e-24

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: 102.40  E-value: 4.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVLHKKgtredienNMPefllksmkkessstarKMFLIV 201
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYR--------NIP----------------GPHMVL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNEL---TRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIRN 277
Cdd:cd18065     72 VPKSTLHNWMNEFKRWvPSLRAVCLIGDKDARAAfirDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  278 PNARVTEVMKAVKCKVRIGLTGTILQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtaTKRELATgRKAMHR 357
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVER 219
                          250
                   ....*....|....
gi 1958729531  358 LAKKMSGYFLRRTK 371
Cdd:cd18065    220 LHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
122-318 7.44e-24

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: 100.15  E-value: 7.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCILGDDMGLGKTIQVISFLAAVlhkkgtrediennmpefllksmkKESSSTARKmfLIV 201
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYL-----------------------KEIGIPGPH--LVV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELTR---LKQR-KCEIALTTYETLRLCLEE---LNSLEWSAIIVDEAH 273
Cdd:cd17998     56 VPSSTLDNWLREFKRWCpSLKVEPYYGSQEERKHLRydiLKGLeDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGH 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958729531  274 RIRNPNA-RVTEVMKaVKCKVRIGLTGTILQNNMKELWCVMDWAVP 318
Cdd:cd17998    136 MLKNMTSeRYRHLMT-INANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
130-310 2.86e-22

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: 97.17  E-value: 2.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  130 AQFLYRHYIKGRGCILGDDMGLGKTIQVIsflAAVLHKKGTREDIENNMPEFLLKSMKKESSS-TARKMFLIVAPLSVLY 208
Cdd:cd18072     10 AWLLWRERQKPRGGILADDMGLGKTLTMI---ALILAQKNTQNRKEEEKEKALTEWESKKDSTlVPSAGTLVVCPASLVH 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  209 NWKDELDT---WGYFRVTVLHGSKKDNELTRLkqRKCEIALTTYETL---------RLCLEELNSLEWSAIIVDEAHRIR 276
Cdd:cd18072     87 QWKNEVESrvaSNKLRVCLYHGPNRERIGEVL--RDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIK 164
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958729531  277 NPNARVTEVMKAVKCKVRIGLTGTILQNNMKELW 310
Cdd:cd18072    165 NPKVQASIAVCKLRAHARWALTGTPIQNNLLDMY 198
HELICc smart00490
helicase superfamily c-terminal domain;
536-619 3.25e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.89  E-value: 3.25e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531   536 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSsqDVNICLVSTMAGGLGLNFIGANVVILFDPTWNPANDLQAIDRA 615
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1958729531   616 YRIG 619
Cdd:smart00490   79 GRAG 82
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
17-72 2.78e-17

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: 76.98  E-value: 2.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958729531   17 WCPGERCLAPSLDNKKLCEASIKSITVDENGEPFAVVL---YPDFQEKKIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
122-368 7.65e-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: 82.01  E-value: 7.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLyrhyiKGRGCILGDDMGLGKTIQVISFLAAvlHKKG--------TREDIENNMPEFLLKSMKKESSST 193
Cdd:cd18070      1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALILL--HPRPdndldaadDDSDEMVCCPDCLVAETPVSSKAT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  194 arkmfLIVAPLSVLYNWKDELD--TWGYFRVTVLHGSKKDNEL-----TRLKQrkCEIALTTYETLR------------- 253
Cdd:cd18070     74 -----LIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALaspapEILAE--YDIVVTTYDVLRtelhyaeanrsnr 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  254 -LCLEE--------LNSLEWSAIIVDEAHRIRNPNARVTEVMKAVKCKVRIGLTGTILQNNMKELwcvmdWAVPGLLGsr 324
Cdd:cd18070    147 rRRRQKryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDL-----FGLLSFLG-- 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958729531  325 ihfkkqfSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGYFLR 368
Cdd:cd18070    220 -------VEPFCDSDWWARVLIRPQGRNKAREPLAALLKELLWR 256
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
122-310 4.24e-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: 4.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHyikgRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkesSSTARKMfLIV 201
Cdd:cd18013      1 PHPYQKVAINFIIEH----PYCGLFLDMGLGKTVTTLTALSDLQL------------------------DDFTRRV-LVI 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYN-WKDELDTWGYFR---VTVLHGSKKdnELTRLKQRKCEIALTTYETLR-LCLEELNSLEWSAIIVDEAHRIR 276
Cdd:cd18013     52 APLRVARStWPDEVEKWNHLRnltVSVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFK 129
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958729531  277 NPNARVTEVMKAVKCKVR--IGLTGTILQNNMKELW 310
Cdd:cd18013    130 SPRSKRFKALRKVRPVIKrlIGLTGTPSPNGLMDLW 165
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
122-341 7.12e-15

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: 74.63  E-value: 7.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIkgRGCILGDDMGLGKTIQVisflAAVLHkkgtrediennmpEFLLksmkkessSTARKMFLIV 201
Cdd:cd18011      1 PLPHQIDAVLRALRKPP--VRLLLADEVGLGKTIEA----GLIIK-------------ELLL--------RGDAKRVLIL 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELTRLKQRKCE--IALTTYETLR---LCLEELNSLEWSAIIVDEAHRIR 276
Cdd:cd18011     54 CPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLR 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958729531  277 N-----PNARvTEVMKAVKCKVR--IGLTGTILQNNMKELWCVMDWAVPGllgsRIHFKKQFSDPVEHGQRH 341
Cdd:cd18011    134 NsgggkETKR-YKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPG----RFAVLGRFLRLDGLREVL 200
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
122-300 1.59e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.59  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKG--RGCILGDdMGLGKTIqVISFLAAVLHKKGTrediennmpefllksmkkessstarkmFL 199
Cdd:COG1061     81 LRPYQQEALEALLAALERGggRGLVVAP-TGTGKTV-LALALAAELLRGKR---------------------------VL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  200 IVAPLSVLYN-WKDELDTWgyFRVTVLHGSKKDNEltrlkqrkCEIALTTYETL--RLCLEELNSlEWSAIIVDEAHRIr 276
Cdd:COG1061    132 VLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD--------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA- 199
                          170       180
                   ....*....|....*....|....
gi 1958729531  277 nPNARVTEVMKAVKCKVRIGLTGT 300
Cdd:COG1061    200 -GAPSYRRILEAFPAAYRLGLTAT 222
ResIII pfam04851
Type III restriction enzyme, res subunit;
122-300 1.04e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 64.23  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKG--RGCIlgdDM--GLGKTIqVISFLAAVLHKKGtreDIENnmpefllksmkkessstarkm 197
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTL-TAAKLIARLFKKG---PIKK--------------------- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  198 FLIVAP-LSVLYNWKDELDTWG---YFRVTVLHGSKKDNELTrlkqrKCEIALTTYETL----RLCLEELNSLEWSAIIV 269
Cdd:pfam04851   56 VLFLVPrKDLLEQALEEFKKFLpnyVEIGEIISGDKKDESVD-----DNKIVVTTIQSLykalELASLELLPDFFDVIII 130
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958729531  270 DEAHRIRNPNARvtEVMKAVKCKVRIGLTGT 300
Cdd:pfam04851  131 DEAHRSGASSYR--NILEYFKPAFLLGLTAT 159
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
122-300 4.34e-11

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: 62.32  E-value: 4.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  122 LRDYQREGAQFLYRHYIKGRGCIlgdDM--GLGKTiqVISFLAAVLHKKGTrediennmpefllksmkkessstarkmFL 199
Cdd:cd17926      1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKT--LTALALIAYLKELR---------------------------TL 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  200 IVAP-LSVLYNWKDELDTWGYFRVTVLHGSKKDNELTrlkqrKCEIALTTYETLRLCLEELNSL--EWSAIIVDEAHRIR 276
Cdd:cd17926     49 IVVPtDALLDQWKERFEDFLGDSSIGLIGGGKKKDFD-----DANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLP 123
                          170       180
                   ....*....|....*....|....
gi 1958729531  277 NPNARvtEVMKAVKCKVRIGLTGT 300
Cdd:cd17926    124 AKTFS--EILKELNAKYRLGLTAT 145
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
140-300 6.68e-09

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: 55.87  E-value: 6.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  140 GRGCILGDDMGLGKTIqvISFLAAVLHkkgtrediennmpefllksmkkesSSTARKMFLIVAPLSVL-YNWKDELDTWG 218
Cdd:cd00046      1 GENVLITAPTGSGKTL--AALLAALLL------------------------LLKKGKKVLVLVPTKALaLQTAERLRELF 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  219 YF--RVTVLHGSKKDNELTRLKQRKCEIALTTYETLRLCLEELNSL---EWSAIIVDEAHRIrNPNARVTEVMKAVKCKV 293
Cdd:cd00046     55 GPgiRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHAL-LIDSRGALILDLAVRKA 133
                          170
                   ....*....|...
gi 1958729531  294 ------RIGLTGT 300
Cdd:cd00046    134 glknaqVILLSAT 146
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
192-302 4.57e-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: 54.23  E-value: 4.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  192 STARKMFLIVAPLSV-LYNWKDELDTWGYF---RVTVLHGSKKDneltrlKQRKCEIALTTYETLR----------LCLE 257
Cdd:cd18029     48 CTIKKSTLVLCTSAVsVEQWRRQFLDWTTIddeQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFME 121
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958729531  258 ELNSLEWSAIIVDEAHRIRNPNARvtEVMKAVKCKVRIGLTGTIL 302
Cdd:cd18029    122 FITEREWGLIILDEVHVVPAPMFR--RVLTLQKAHCKLGLTATLV 164
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
502-640 8.77e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.66  E-value: 8.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  502 PKYSGKMKVLDQLLNhfrKHRD-KVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEFnSSQ 572
Cdd:COG1111    335 PKLSKLREILKEQLG---TNPDsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERF-RAG 410
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958729531  573 DVNIcLVSTMAGGLGLNFIGANVVILFDPTWNPandLQAIDRAYRIGQCRDVKVFRLISLGTVEEIMY 640
Cdd:COG1111    411 EFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSE---IRSIQRKGRTGRKREGRVVVLIAKGTRDEAYY 474
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
20-71 2.33e-05

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: 43.01  E-value: 2.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958729531   20 GERCLAPSLDNKKLCEASIKSITVDENGepfAVVLYPDF-QEKKIPLQRLQEV 71
Cdd:cd21182      1 GDKCLAPYSDDGKYYEATIEEITEESDT---ATVVFDGYgNSEEVPLSDLKPL 50
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
578-630 2.73e-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: 43.46  E-value: 2.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958729531  578 LVSTMAGGLGLNFIGANVVILFDPTWNPANDLQAIDRAYRIGQcRDVKVFRLI 630
Cdd:cd18785     26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
138-301 1.88e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 43.39  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  138 IKGRGCILGDDMGLGKTiqvisfLAAVLhkkgtrediennmpeFLLKSMKKESSStarKMFLIVAPLSVL----Y-NWKD 212
Cdd:pfam00270   12 LEGRDVLVQAPTGSGKT------LAFLL---------------PALEALDKLDNG---PQALVLAPTRELaeqiYeELKK 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729531  213 ELDTWGYFRVTVLHGSKKDNELTRLKqrKCEIALTTYETLRLCLEE---LNSLEWsaIIVDEAHRIRNPNAR--VTEVMK 287
Cdd:pfam00270   68 LGKGLGLKVASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQErklLKNLKL--LVLDEAHRLLDMGFGpdLEEILR 143
                          170
                   ....*....|....*
gi 1958729531  288 AVKCKVRI-GLTGTI 301
Cdd:pfam00270  144 RLPKKRQIlLLSATL 158
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1132-1155 6.05e-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: 36.43  E-value: 6.05e-03
                           10        20
                   ....*....|....*....|....
gi 1958729531 1132 VAYIHSNQNVIGSSRAENHMSRWA 1155
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
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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