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Conserved domains on  [gi|91807128|ref|NP_075996|]
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DNA excision repair protein ERCC-6-like 2 isoform 2 [Mus musculus]

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 1.50e-152

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: 441.82  E-value: 1.50e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKKPPSTAKKMFLIV 201
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-LRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKA 280
Cdd:cd18005  77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 281 RVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005 157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                ....*....
gi 91807128 361 KMSGWFLRR 369
Cdd:cd18005 237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-649 9.90e-130

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 9.90e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553 172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 131 QFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmKKKPpstakkmFLIVAPLSVLYNW 210
Cdd:COG0553 251 AWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERG------------------LARP-------VLIVAPTSLVGNW 305
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 211 KDELDTWGY-FRVTVLHGSKKDNELLRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAV 289
Cdd:COG0553 306 QRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 290 KCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRR 369
Cdd:COG0553 385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRR 452
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 370 TKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTV 449
Cdd:COG0553 453 TKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTR 510
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 450 LQKVANHVALLQAastskhqetvikricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFS 529
Cdd:COG0553 511 LRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFS 556
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 530 FSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDL 609
Cdd:COG0553 557 QFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEE 636
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 91807128 610 QAVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553 637 QAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
17-72 1.03e-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: 77.37  E-value: 1.03e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 91807128  17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400   1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
 
Name Accession Description Interval E-value
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
122-369 1.50e-152

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: 441.82  E-value: 1.50e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKKPPSTAKKMFLIV 201
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-LRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKA 280
Cdd:cd18005  77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 281 RVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005 157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                ....*....
gi 91807128 361 KMSGWFLRR 369
Cdd:cd18005 237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-649 9.90e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 9.90e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553 172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 131 QFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmKKKPpstakkmFLIVAPLSVLYNW 210
Cdd:COG0553 251 AWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERG------------------LARP-------VLIVAPTSLVGNW 305
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 211 KDELDTWGY-FRVTVLHGSKKDNELLRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAV 289
Cdd:COG0553 306 QRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 290 KCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRR 369
Cdd:COG0553 385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRR 452
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 370 TKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTV 449
Cdd:COG0553 453 TKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTR 510
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 450 LQKVANHVALLQAastskhqetvikricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFS 529
Cdd:COG0553 511 LRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFS 556
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 530 FSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDL 609
Cdd:COG0553 557 QFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEE 636
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 91807128 610 QAVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553 637 QAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-654 4.53e-73

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 255.88  E-value: 4.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   115 PYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTrediennmpefllksmkkkppsTA 194
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI----------------------TG 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   195 KKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAI 267
Cdd:PLN03142  221 PHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkre 347
Cdd:PLN03142  296 IIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------- 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   348 latgrKAMHRLAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrk 427
Cdd:PLN03142  369 -----EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------- 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   428 ccyktNSRGDtvRTLCLSYLTVLQKVANHVALLQAASTSkhqetvikricdrvfsrfPDFVqkSKDAAFETlsdpkySGK 507
Cdd:PLN03142  426 -----NAGGE--RKRLLNIAMQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGK 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   508 MKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGL 586
Cdd:PLN03142  473 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGL 552
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91807128   587 GLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQLHCVVV 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 1.07e-68

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: 1.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   125 YQREGAQFLY-RHYIEGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpeflLKSMKKKPpstakkmFLIVAP 203
Cdd:pfam00176   1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP-------TLIVVP 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   204 LSVLYNWKDELDTW---GYFRVTVLHGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKN 277
Cdd:pfam00176  58 LSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   278 PKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHR 357
Cdd:pfam00176 138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSR 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   358 LAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVALILTSSQpctcgsgqkrrkccyktnsrGD 437
Cdd:pfam00176 207 LHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------GR 266
                         330       340
                  ....*....|....*....|...
gi 91807128   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 2.39e-55

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: 185.37  E-value: 2.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 504 YSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMA 583
Cdd:cd18793   9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 91807128 584 GGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLI 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 6.98e-27

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 105.37  E-value: 6.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   506 GKMKVLQQLLNhfRKQRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSqDVNIcLVSTMAGG 585
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 91807128   586 LGLNFVGANVVILFDPTWNPANDLQAVDRAYRIG 619
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
122-310 6.90e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.57  E-value: 6.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    122 LRDYQREGAQFLYRHYiegRGCILGDDMGLGKTIQVISFLAAVLHKKGtrediennmpefllksmkkkppstaKKMFLIV 201
Cdd:smart00487   9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-------------------------GGRVLVL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    202 APLSVL-YNWKDELDTWGYF----RVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHR 274
Cdd:smart00487  61 VPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHR 140
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 91807128    275 IKNPKAR--VTEVMKAV-KCKVRIGLTGTVLQNNMKELW 310
Cdd:smart00487 141 LLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
536-619 1.06e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.58  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    536 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSsqDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRA 615
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 91807128    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 1.03e-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: 77.37  E-value: 1.03e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 91807128  17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400   1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
79-300 1.88e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.44  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  79 RSLIFDDKDLEKPYFPDRKIPSLASAFQLSEDGDSIPYTinryLRDYQREGAQFLYRHYIEG--RGCILGDdMGLGKTIq 156
Cdd:COG1061  42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGggRGLVVAP-TGTGKTV- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 157 VISFLAAVLHKKGTrediennmpefllksmkkkppstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGSKKDNEll 235
Cdd:COG1061 116 LALALAAELLRGKR---------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91807128 236 rlkqrkCEIALTTYETL--RLCLEELNSlEWSAIIVDEAHRIknPKARVTEVMKAVKCKVRIGLTGT 300
Cdd:COG1061 165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
SWIM_PBPRA1643 TIGR04102
SWIM/SEC-C metal-binding motif protein, PBPRA1643 family; Members of this protein family have ...
416-429 7.93e-03

SWIM/SEC-C metal-binding motif protein, PBPRA1643 family; Members of this protein family have a SWIM, or SEC-C, domain (see pfam02810), a 21-amino acid putative Zn-binding domain that is shared with SecA, plant MuDR transposases, etc. This small protein family of unknown function occurs primarily in marine bacteria.


Pssm-ID: 200353 [Multi-domain]  Cd Length: 108  Bit Score: 36.52  E-value: 7.93e-03
                          10
                  ....*....|....
gi 91807128   416 PCTCGSGQKRRKCC 429
Cdd:TIGR04102  94 PCPCGSGKKYKKCC 107
 
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 1.50e-152

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: 441.82  E-value: 1.50e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNMPEFllksMKKKPPSTAKKMFLIV 201
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRF----KKKPPASSAKKPVLIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNEL-LRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKA 280
Cdd:cd18005  77 APLSVLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 281 RVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAK 360
Cdd:cd18005 157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                ....*....
gi 91807128 361 KMSGWFLRR 369
Cdd:cd18005 237 KLSKFFLRR 245
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-649 9.90e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 399.21  E-value: 9.90e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553 172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 131 QFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmKKKPpstakkmFLIVAPLSVLYNW 210
Cdd:COG0553 251 AWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERG------------------LARP-------VLIVAPTSLVGNW 305
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 211 KDELDTWGY-FRVTVLHGSKKDNELLRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAV 289
Cdd:COG0553 306 QRELAKFAPgLRVLVLDGTRERAKGANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 290 KCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRR 369
Cdd:COG0553 385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRR 452
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 370 TKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTV 449
Cdd:COG0553 453 TKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTR 510
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 450 LQKVANHVALLQAastskhqetvikricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFS 529
Cdd:COG0553 511 LRQICSHPALLLE----------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFS 556
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 530 FSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDL 609
Cdd:COG0553 557 QFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEE 636
                       570       580       590       600
                ....*....|....*....|....*....|....*....|
gi 91807128 610 QAVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQL 649
Cdd:COG0553 637 QAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-654 4.53e-73

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 255.88  E-value: 4.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   115 PYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTrediennmpefllksmkkkppsTA 194
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGI----------------------TG 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   195 KKMflIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAI 267
Cdd:PLN03142  221 PHM--VVAPKSTLGNWMNEIRRFcPVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkre 347
Cdd:PLN03142  296 IIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQ------- 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   348 latgrKAMHRLAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrk 427
Cdd:PLN03142  369 -----EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------- 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   428 ccyktNSRGDtvRTLCLSYLTVLQKVANHVALLQAASTSkhqetvikricdrvfsrfPDFVqkSKDAAFETlsdpkySGK 507
Cdd:PLN03142  426 -----NAGGE--RKRLLNIAMQLRKCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGK 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   508 MKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGL 586
Cdd:PLN03142  473 MVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGL 552
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91807128   587 GLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQLHCVVV 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 5.24e-71

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


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 228.60  E-value: 5.24e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmpefllksmkkkppstakKMFLIV 201
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKER------------------------GPVLVV 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELLR--LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNP 278
Cdd:cd17919  57 CPLSVLENWEREFEKWtPDLRVVVYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNP 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 91807128 279 KARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVP 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 1.07e-68

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: 1.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   125 YQREGAQFLY-RHYIEGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpeflLKSMKKKPpstakkmFLIVAP 203
Cdd:pfam00176   1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTISLLLYLKH----------------VDKNWGGP-------TLIVVP 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   204 LSVLYNWKDELDTW---GYFRVTVLHGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKN 277
Cdd:pfam00176  58 LSLLHNWMNEFERWvspPALRVVVLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   278 PKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHR 357
Cdd:pfam00176 138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSR 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   358 LAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLETEDVALILTSSQpctcgsgqkrrkccyktnsrGD 437
Cdd:pfam00176 207 LHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------GR 266
                         330       340
                  ....*....|....*....|...
gi 91807128   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 2.91e-60

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: 202.22  E-value: 2.91e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefLLKSMkkkppstakkmfLIV 201
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-------------LIKSV------------LVV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGY-FRVTVLHGSKKD--NELLRLKQRKCEIALTTYETLRLCLEELNSLE-----WSAIIVDEAH 273
Cdd:cd18001  56 MPTSLIPHWVKEFAKWTPgLRVKVFHGTSKKerERNLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGH 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 274 RIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPG-LLGSRIHFKKQFSDPVEHGQRHTATKRELATGR 352
Cdd:cd18001 136 KIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGS 215
                       250
                ....*....|....*..
gi 91807128 353 KAMHRLAKKMSGWFLRR 369
Cdd:cd18001 216 EVAENLRQIIKPYFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
122-371 1.21e-56

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 192.01  E-value: 1.21e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLY--RHYieGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmpefllksmkkkpPStakkmfL 199
Cdd:cd18012   5 LRPYQKEGFNWLSflRHY--GLGGILADDMGLGKTLQTLALLLSRKEEGRKG-------------------PS------L 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 200 IVAPLSVLYNWKDELDTWG-YFRVTVLHGSK-KDNELLRLKQRkcEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKN 277
Cdd:cd18012  58 VVAPTSLIYNWEEEAAKFApELKVLVIHGTKrKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKN 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 278 PKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkrelatgRKAMHR 357
Cdd:cd18012 136 PQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEE 204
                       250
                ....*....|....
gi 91807128 358 LAKKMSGWFLRRTK 371
Cdd:cd18012 205 LKKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
504-630 2.39e-55

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: 185.37  E-value: 2.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 504 YSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMA 583
Cdd:cd18793   9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 91807128 584 GGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLI 630
Cdd:cd18793  89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
122-369 5.56e-54

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: 185.57  E-value: 5.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLY-----RHYIEGRGCILGDDMGLGKTIQVISFLAAvlhkkgtrediennmpefLLKSMKKKPPsTAKK 196
Cdd:cd18004   1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVWT------------------LLKQGPYGKP-TAKK 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 197 mFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIV- 269
Cdd:cd18004  62 -ALIVCPSSLVGNWKAEFDKWlglRRIKVVTADGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKISIDLLIc 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 270 DEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELA 349
Cdd:cd18004 141 DEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKE 220
                       250       260
                ....*....|....*....|
gi 91807128 350 TGRKAMHRLAKKMSGWFLRR 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 3.10e-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: 180.14  E-value: 3.10e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmpefllksmkkkPPstakkmFLIV 201
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIR------------------GP------FLVI 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd17995  57 APLSTIPNWQREFETWTDMNVVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRVV 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 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 4.17e-48

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: 169.07  E-value: 4.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQ---FLYRHYIEGrgcILGDDMGLGKTIQVISFLAAVLHKKGTREDIENNmpefllksmkkkpPStakkmf 198
Cdd:cd17999   1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLCILASDHHKRANSFNSENL-------------PS------ 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 199 LIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRI 275
Cdd:cd17999  59 LVVCPPTLVGHWVAEIKKYfpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHII 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 276 KNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAM 355
Cdd:cd17999 139 KNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALAL 218
                       250
                ....*....|....
gi 91807128 356 HRLAKKMSGWFLRR 369
Cdd:cd17999 219 EALHKQVLPFLLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
122-353 1.76e-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: 1.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRH-------YIEGRGCILGDDMGLGKTIQVISFLAAVLhkkgtrediennmpefllksmkKKPPSTA 194
Cdd:cd18007   1 LKPHQVEGVRFLWSNlvgtdvgSDEGGGCILAHTMGLGKTLQVITFLHTYL----------------------AAAPRRS 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 195 KkmFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDN-ELLRLK-----QRKCEIALTTYETLRLCLEELNSLEWS 265
Cdd:cd18007  59 R--PLVLCPASTLYNWEDEFKKWlppDLRPLLVLVSLSASKrADARLRkinkwHKEGGVLLIGYELFRNLASNATTDPRL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 266 A--------------IIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQF 331
Cdd:cd18007 137 KqefiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
                       250       260
                ....*....|....*....|..
gi 91807128 332 SDPVEHGQRHTATKRELATGRK 353
Cdd:cd18007 217 VKPIEAGQCVDSTEEDVRLMLK 238
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
122-321 3.43e-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: 159.80  E-value: 3.43e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLH-KKGTRediennmpefllksmkkkpPStakkmfLI 200
Cdd:cd18000   1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHsKLGLG-------------------PS------LI 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 201 VAPLSVLYNWKDELDTW-GYFRVTVLH--------GSKKDNELLRLKQRKCE-----IALTTYETLRLCLEELNSLEWSA 266
Cdd:cd18000  56 VCPATVLKQWVKEFHRWwPPFRVVVLHssgsgtgsEEKLGSIERKSQLIRKVvgdggILITTYEGFRKHKDLLLNHNWQY 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 91807128 267 IIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLL 321
Cdd:cd18000 136 VILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
122-369 1.35e-40

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: 147.89  E-value: 1.35e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKKPPstakkmFLIV 201
Cdd:cd17993   2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS------------------YLFHSQQQYGP------FLVV 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd17993  58 VPLSTMPAWQREFAKWApDMNVIVYLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEA 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 273 HRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGllgsRIHFKKQFSDpvEHGQrhtatKRElatgr 352
Cdd:cd17993 138 HRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG----KFDIWEEFEE--EHDE-----EQE----- 201
                       250
                ....*....|....*..
gi 91807128 353 KAMHRLAKKMSGWFLRR 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 1.44e-40

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: 147.85  E-value: 1.44e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpefLLKSMKKKP-PstakkmFLI 200
Cdd:cd17997   4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG-------------------YLKHYKNINgP------HLI 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 201 VAPLSVLYNWKDELDTW-GYFRVTVLHGSKK-DNELLR--LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIK 276
Cdd:cd17997  59 IVPKSTLDNWMREFKRWcPSLRVVVLIGDKEeRADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 277 NPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKrelatgrkamh 356
Cdd:cd17997 139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQ----------- 207
                       250
                ....*....|....*
gi 91807128 357 RLAKKMSGWFLRRTK 371
Cdd:cd17997 208 RLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
122-371 9.18e-40

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: 146.38  E-value: 9.18e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpefLLKSMKKKPPstakkmFLIV 201
Cdd:cd18009   4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA-------------------HLRERGVWGP------FLVI 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLRLKQRK-------CEIALTTYETLRLCLEELNSLEWSAIIVDEAH 273
Cdd:cd18009  59 APLSTLPNWVNEFARFTpSVPVLLYHGTKEERERLRKKIMKregtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGH 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 274 RIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFsDPVEHGQRhTATKRELATGRK 353
Cdd:cd18009 139 RLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLSEERE 216
                       250       260
                ....*....|....*....|
gi 91807128 354 A--MHRLAKKMSGWFLRRTK 371
Cdd:cd18009 217 QniVHMLHAILKPFLLRRLK 236
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
122-369 1.15e-38

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: 143.38  E-value: 1.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRhYIEGR------GCILGDDMGLGKTIQVISFLAAvlhkkgtrediennmpefLLKSMKKKPPSTAK 195
Cdd:cd18067   1 LRPHQREGVKFLYR-CVTGRrirgshGCIMADEMGLGKTLQCITLMWT------------------LLRQSPQCKPEIDK 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 196 KMflIVAPLSVLYNWKDELDTWGYFRVTVL--HGSKKDNELLRLKQRKCE--------IALTTYETLRLCLEELNSLEWS 265
Cdd:cd18067  62 AI--VVSPSSLVKNWANELGKWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 266 AIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATK 345
Cdd:cd18067 140 LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASE 219
                       250       260
                ....*....|....*....|....
gi 91807128 346 RELATGRKAMHRLAKKMSGWFLRR 369
Cdd:cd18067 220 KERQLGEEKLQELISIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
122-369 1.14e-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: 140.37  E-value: 1.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLY-----RHYIEGRGCILGDDMGLGKTIQVISflaavlhkkgtrediennmpefLLKSMKKKPPSTAK- 195
Cdd:cd18066   1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCIS----------------------LIWTLLRQGPYGGKp 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 196 --KMFLIVAPLSVLYNWKDELDTW---GYFRVTVLHGSKKDNELLrlKQRKCEIALTTYETLRLCLEELNSLEWSAIIVD 270
Cdd:cd18066  59 viKRALIVTPGSLVKNWKKEFQKWlgsERIKVFTVDQDHKVEEFI--ASPLYSVLIISYEMLLRSLDQISKLNFDLVICD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 271 EAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELAT 350
Cdd:cd18066 137 EGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKL 216
                       250
                ....*....|....*....
gi 91807128 351 GRKAMHRLAKKMSGWFLRR 369
Cdd:cd18066 217 GEARAAELTRLTGLFILRR 235
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
122-371 2.30e-37

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: 139.43  E-value: 2.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQF---LYRHYIEGrgcILGDDMGLGKTIQVISFLAAVLHKKGtredieNNMPefllksmkkkppstakkmF 198
Cdd:cd17996   4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTISLITYLMEKKK------NNGP------------------Y 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 199 LIVAPLSVLYNWKDELDTWGYFRVTVLH-GSKKDNELLRLKQRKCE--IALTTYETLRLCLEELNSLEWSAIIVDEAHRI 275
Cdd:cd17996  57 LVIVPLSTLSNWVSEFEKWAPSVSKIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRM 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 276 KNPKARVTEVMKAVKC-KVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHtatKRELATGRK 353
Cdd:cd17996 137 KNAQSKLTQTLNTYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEET 213
                       250       260
                ....*....|....*....|
gi 91807128 354 AM--HRLAKKMSGWFLRRTK 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 ...
122-310 7.80e-35

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


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 132.41  E-value: 7.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRhyiegRGCILGDDMGLGKTIQVIsflAAVLHKKGTREDIENNMPEFLLKSMKKKPPSTakkmFLIV 201
Cdd:cd18008   1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQAL---ALILATRPQDPKIPEELEENSSDPKKLYLSKT----TLIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDT---WGYFRVTVLHGSKKDNELLRLKQrkCEIALTTYETLR------------LCLEE----LNSL 262
Cdd:cd18008  69 VPLSLLSQWKDEIEKhtkPGSLKVYVYHGSKRIKSIEELSD--YDIVITTYGTLAsefpknkkgggrDSKEKeaspLHRI 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 91807128 263 EWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELW 310
Cdd:cd18008 147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLY 194
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
122-339 1.76e-34

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: 131.09  E-value: 1.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIE---------GRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkkppS 192
Cdd:cd18069   1 LKPHQIGGIRFLYDNIIEslerykgssGFGCILAHSMGLGKTLQVISFLDVLLR-------------------------H 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 193 TAKKMFLIVAPLSVLYNWKDELDTW------------GYFRVTVLHGSKKD----NELLRLKQRKCEIALTTYETLRLcl 256
Cdd:cd18069  56 TGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrpRPFKVFILNDEHKTtaarAKVIEDWVKDGGVLLMGYEMFRL-- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 257 EELNSLewsaIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVE 336
Cdd:cd18069 134 RPGPDV----VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209

                ...
gi 91807128 337 HGQ 339
Cdd:cd18069 210 NGQ 212
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
122-333 1.88e-33

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 127.85  E-value: 1.88e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpEFLLKSMKKKppstakkmFLIV 201
Cdd:cd18058   1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----------------EIFLMGIRGP--------FLII 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18058  56 APLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSCV 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 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 1.92e-33

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: 127.85  E-value: 1.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGtredieNNMPEfllksmkkkppstakkmfLIV 201
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPH------------------LIV 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTW--GyFRVTVLHGSKKDNELLR---LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIK 276
Cdd:cd18003  57 VPTSVMLNWEMEFKRWcpG-FKILTYYGSAKERKLKRqgwMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 277 NPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDP----VEHGQRHTatkrelatgR 352
Cdd:cd18003 136 NFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN---------E 206
                       250
                ....*....|....*..
gi 91807128 353 KAMHRLAKKMSGWFLRR 369
Cdd:cd18003 207 ELVRRLHKVLRPFLLRR 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
122-333 5.15e-32

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: 124.01  E-value: 5.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLhkkgtrediennmpefllkSMKKKPPstakkmFLIV 201
Cdd:cd18060   1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-------------------NVGIHGP------FLVI 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18060  56 APLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCV 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18060 136 IIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
122-333 6.28e-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: 123.58  E-value: 6.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHkkgtrediennmpefllksmkkkppSTAKKMFLIV 201
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILL-------------------------TGIRGPFLII 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18061  56 APLSTIANWEREFRTWTDLNVVVYHGSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCV 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18061 136 IIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
122-369 9.91e-32

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: 123.58  E-value: 9.91e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksMKKKPpstakkmFLIV 201
Cdd:cd18054  21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH-----------------QLYGP-------FLLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd18054  77 VPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 273 HRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPgllgSRIHFKKQFSDpvEHGQrhtatKRElaTGR 352
Cdd:cd18054 157 HRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP----EKFEFWEDFEE--DHGK-----GRE--NGY 223
                       250
                ....*....|....*..
gi 91807128 353 KAMHRLakkMSGWFLRR 369
Cdd:cd18054 224 QSLHKV---LEPFLLRR 237
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
122-333 1.30e-31

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: 122.83  E-value: 1.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpEFLLKSMKKKppstakkmFLIV 201
Cdd:cd18059   1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLY-----------------EIYLKGIHGP--------FLVI 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18059  56 APLSTIPNWEREFRTWTELNVVVYHGSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCV 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18059 136 VIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
122-322 1.92e-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: 122.16  E-value: 1.92e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKKPPstakkmFLIV 201
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW------------------YLAGRLKLLGP------FLVL 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLRlKQRKCE----IALTTYEtlrLCLEE---LNSLEWSAIIVDEAH 273
Cdd:cd18006  57 CPLSVLDNWKEELNRFApDLSVITYMGDKEKRLDLQ-QDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAH 132
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 91807128 274 RIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLG 322
Cdd:cd18006 133 RLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP 181
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
122-333 2.16e-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: 118.31  E-value: 2.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkkppstAKKMFLIV 201
Cdd:cd17994   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH-----------------------SKGPFLVS 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGskkDNELLrlkqrkceialTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKA 280
Cdd:cd17994  57 APLSTIINWEREFEMWApDFYVVTYVG---DHVLL-----------TSYELISIDQAILGSIDWAVLVVDEAHRLKNNQS 122
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 91807128 281 RVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 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 5.17e-30

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: 118.38  E-value: 5.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmpefllksmkkKPpstakkmFLIV 201
Cdd:cd18002   1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIW-----------------GP-------FLVI 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELLR---------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDE 271
Cdd:cd18002  57 APASTLHNWQQEISRFvPQFKVLPYWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 272 AHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVE-HGQRHTATKRElat 350
Cdd:cd18002 137 AQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH--- 213
                       250
                ....*....|....*....
gi 91807128 351 grkAMHRLAKKMSGWFLRR 369
Cdd:cd18002 214 ---QLKRLHMILKPFMLRR 229
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
122-348 1.23e-29

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: 117.46  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtrediennmpefllksmkkkppsTAKKMFLIV 201
Cdd:cd18053  21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEH------------------------QLYGPFLLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLRL--------KQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEA 272
Cdd:cd18053  77 VPLSTLTSWQREIQTWApQMNAVVYLGDINSRNMIRThewmhpqtKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91807128 273 HRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGqrHTATKREL 348
Cdd:cd18053 157 HRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG--YASLHKEL 230
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
112-382 6.97e-28

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 112.84  E-value: 6.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 112 DSIPYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtredienNMPefllksmkkkpp 191
Cdd:cd18064   6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYR--------NIP------------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 192 stakKMFLIVAPLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYETLRLCLEELNSLEWSAI 267
Cdd:cd18064  66 ----GPHMVLVPKSTLHNWMAEFKRWvPTLRAVCLIGDKDQRAAFVrdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 268 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtatKRE 347
Cdd:cd18064 142 VIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TNN 209
                       250       260       270
                ....*....|....*....|....*....|....*
gi 91807128 348 LATGRKAMHRLAKKMSGWFLRRTKTLIKGQLPKKE 382
Cdd:cd18064 210 CLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
122-339 1.07e-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: 111.70  E-value: 1.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkkppstAKKMFLIV 201
Cdd:cd18057   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-LYKEGH-----------------------SKGPYLVS 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGY-FRVTVLHGSK------KDNE-------------LLRLK---QRKCEIALTTYETLRLCLEE 258
Cdd:cd18057  57 APLSTIINWEREFEMWAPdFYVVTYTGDKesrsviRENEfsfednairsgkkVFRMKkeaQIKFHVLLTSYELITIDQAI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 259 LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHG 338
Cdd:cd18057 137 LGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKED 216

                .
gi 91807128 339 Q 339
Cdd:cd18057 217 Q 217
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
122-333 1.30e-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: 111.64  E-value: 1.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkkppstAKKMFLIV 201
Cdd:cd18055   1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS-LYKEGH-----------------------TKGPFLVS 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-----------------------YFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE 258
Cdd:cd18055  57 APLSTIINWEREFQMWApdfyvvtytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAA 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91807128 259 LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 333
Cdd:cd18055 137 LGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
122-348 3.02e-27

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: 111.13  E-value: 3.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLY---------RHYIEGRGCILGDDMGLGKTIQVISFLAAVL-HKKgtREDIennmpefllksmkkkpp 191
Cdd:cd18068   1 LKPHQVDGVQFMWdccceslkkTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLlCEK--LENF----------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 192 stakKMFLIVAPLSVLYNWKDELDTWGYF-------RVTVLhGSKKDNELLRLK----QRKCEIALTTYETLRLCLEELN 260
Cdd:cd18068  62 ----SRVLVVCPLNTVLNWLNEFEKWQEGlkdeekiEVNEL-ATYKRPQERSYKlqrwQEEGGVMIIGYDMYRILAQERN 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 261 -SLEWSA---------------IIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSR 324
Cdd:cd18068 137 vKSREKLkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTI 216
                       250       260
                ....*....|....*....|....
gi 91807128 325 IHFKKQFSDPVEHGQRHTATKREL 348
Cdd:cd18068 217 KEFRNRFVNPIQNGQCADSTLVDV 240
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
122-334 4.85e-27

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: 109.22  E-value: 4.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHyiEGRgCILGDDMGLGKTIQVISFLAAVlhkkgtrediENNMPefllksmkkkppstakkmFLIV 201
Cdd:cd18010   1 LLPFQREGVCFALRR--GGR-VLIADEMGLGKTVQAIAIAAYY----------REEWP------------------LLIV 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTW----GYFRVTVLHGSKkdnELLRLKQRKceIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKN 277
Cdd:cd18010  50 CPSSLRLTWADEIERWlpslPPDDIQVIVKSK---DGLRDGDAK--VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKN 124
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 91807128 278 PKA-RVTEVMKAVK-CKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDP 334
Cdd:cd18010 125 SKAkRTKAALPLLKrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
506-619 6.98e-27

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 105.37  E-value: 6.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   506 GKMKVLQQLLNhfRKQRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSqDVNIcLVSTMAGG 585
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 91807128   586 LGLNFVGANVVILFDPTWNPANDLQAVDRAYRIG 619
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
122-339 7.62e-27

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: 109.38  E-value: 7.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAvLHKKGTrediennmpefllksmkkkppstAKKMFLIV 201
Cdd:cd18056   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS-LYKEGH-----------------------SKGPFLVS 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-----------------------YFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE 258
Cdd:cd18056  57 APLSTIINWEREFEMWApdmyvvtyvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 259 LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHG 338
Cdd:cd18056 137 LGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKED 216

                .
gi 91807128 339 Q 339
Cdd:cd18056 217 Q 217
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
118-371 3.87e-26

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 107.84  E-value: 3.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 118 INRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKKPPstakkm 197
Cdd:cd18063  20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT------------------YLMEHKRLNGP------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 198 FLIVAPLSVLYNWKDELDTWGyfrVTVLHGSKKDNELLR------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDE 271
Cdd:cd18063  76 YLIIVPLSTLSNWTYEFDKWA---PSVVKISYKGTPAMRrslvpqLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 272 AHRIKNPKARVTEVMKA-VKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELA 349
Cdd:cd18063 153 GHRMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETI 232
                       250       260
                ....*....|....*....|..
gi 91807128 350 TgrkAMHRLAKKMSGWFLRRTK 371
Cdd:cd18063 233 L---IIRRLHKVLRPFLLRRLK 251
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
140-369 4.68e-26

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: 107.17  E-value: 4.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 140 GRGCILGDDMGLGKTIQVISFLAAvlhkkgtrediennmpefllksmkkkppstakKMFLIVAPLSVLYNWKDELD---T 216
Cdd:cd18071  48 VRGGILADDMGLGKTLTTISLILA--------------------------------NFTLIVCPLSVLSNWETQFEehvK 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 217 WGYFRVTVLHGSKKDNELLRLKqrKCEIALTTYETLrlCLEE-------LNSLEWSAIIVDEAHRIKNPKARVTEVMKAV 289
Cdd:cd18071  96 PGQLKVYTYHGGERNRDPKLLS--KYDIVLTTYNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 290 KCKVRIGLTGTVLQNNMKELWCVMdwavpgllgSRIHFKKqFSDPvEHGQRhtATKRELATG-RKAMHRLAKKMSGWFLR 368
Cdd:cd18071 172 SSERRWVLTGTPIQNSPKDLGSLL---------SFLHLKP-FSNP-EYWRR--LIQRPLTMGdPTGLKRLQVLMKQITLR 238

                .
gi 91807128 369 R 369
Cdd:cd18071 239 R 239
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
122-318 3.27e-25

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 103.23  E-value: 3.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKKPpstakkmFLIV 201
Cdd:cd17998   1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA------------------YLKEIGIPGP-------HLVV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWG-YFRVTVLHGSKKDNELLR---LKQR-KCEIALTTYETLRLCLEE---LNSLEWSAIIVDEAH 273
Cdd:cd17998  56 VPSSTLDNWLREFKRWCpSLKVEPYYGSQEERKHLRydiLKGLeDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGH 135
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 91807128 274 RIKNPKA-RVTEVMKaVKCKVRIGLTGTVLQNNMKELWCVMDWAVP 318
Cdd:cd17998 136 MLKNMTSeRYRHLMT-INANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
118-371 3.92e-25

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: 105.13  E-value: 3.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 118 INRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAavlhkkgtrediennmpeFLLKSMKKKPPstakkm 197
Cdd:cd18062  20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT------------------YLMEHKRINGP------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 198 FLIVAPLSVLYNWKDELDTWGYFRVTVLH-GSKKDNE--LLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHR 274
Cdd:cd18062  76 FLIIVPLSTLSNWVYEFDKWAPSVVKVSYkGSPAARRafVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 275 IKNPKARVTEVMKA-VKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELATgr 352
Cdd:cd18062 156 MKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL-- 233
                       250
                ....*....|....*....
gi 91807128 353 kAMHRLAKKMSGWFLRRTK 371
Cdd:cd18062 234 -IIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
122-371 6.16e-25

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


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 103.94  E-value: 6.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQVISFLAAVLHKKgtredienNMPefllksmkkkppstakKMFLIV 201
Cdd:cd18065  16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYR--------NIP----------------GPHMVL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTW-GYFRVTVLHGSKKDNELL---RLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKN 277
Cdd:cd18065  72 VPKSTLHNWMNEFKRWvPSLRAVCLIGDKDARAAFirdVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 278 PKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtaTKRELATgRKAMHR 357
Cdd:cd18065 152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVER 219
                       250
                ....*....|....
gi 91807128 358 LAKKMSGWFLRRTK 371
Cdd:cd18065 220 LHAVLKPFLLRRIK 233
DEXDc smart00487
DEAD-like helicases superfamily;
122-310 6.90e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.57  E-value: 6.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    122 LRDYQREGAQFLYRHYiegRGCILGDDMGLGKTIQVISFLAAVLHKKGtrediennmpefllksmkkkppstaKKMFLIV 201
Cdd:smart00487   9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-------------------------GGRVLVL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    202 APLSVL-YNWKDELDTWGYF----RVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHR 274
Cdd:smart00487  61 VPTRELaEQWAEELKKLGPSlglkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHR 140
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 91807128    275 IKNPKAR--VTEVMKAV-KCKVRIGLTGTVLQNNMKELW 310
Cdd:smart00487 141 LLDGGFGdqLEKLLKLLpKNVQLLLLSATPPEEIENLLE 179
HELICc smart00490
helicase superfamily c-terminal domain;
536-619 1.06e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.58  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128    536 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSsqDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRA 615
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 91807128    616 YRIG 619
Cdd:smart00490  79 GRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
130-310 3.10e-20

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 90.62  E-value: 3.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 130 AQFLYRHYIEGRGCILGDDMGLGKTIQVIsflAAVLHKKGTREDIENNMPEFLLKSMKKKPPS-TAKKMFLIVAPLSVLY 208
Cdd:cd18072  10 AWLLWRERQKPRGGILADDMGLGKTLTMI---ALILAQKNTQNRKEEEKEKALTEWESKKDSTlVPSAGTLVVCPASLVH 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 209 NWKDELDT---WGYFRVTVLHGSKKDNELLRLkqRKCEIALTTYETL---------RLCLEELNSLEWSAIIVDEAHRIK 276
Cdd:cd18072  87 QWKNEVESrvaSNKLRVCLYHGPNRERIGEVL--RDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIK 164
                       170       180       190
                ....*....|....*....|....*....|....
gi 91807128 277 NPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELW 310
Cdd:cd18072 165 NPKVQASIAVCKLRAHARWALTGTPIQNNLLDMY 198
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
17-72 1.03e-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: 77.37  E-value: 1.03e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 91807128  17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400   1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
122-310 1.89e-17

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: 81.63  E-value: 1.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLyrhyIEGRGCILGDDMGLGKTIQVISFLAAVlhkkgtrediennmpefllksmkkKPPSTAKKMfLIV 201
Cdd:cd18013   1 PHPYQKVAINFI----IEHPYCGLFLDMGLGKTVTTLTALSDL------------------------QLDDFTRRV-LVI 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYN-WKDELDTWGYFR---VTVLHGSKKdnELLRLKQRKCEIALTTYETLR-LCLEELNSLEWSAIIVDEAHRIK 276
Cdd:cd18013  52 APLRVARStWPDEVEKWNHLRnltVSVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFK 129
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 91807128 277 NPKARVTEVMKAVKCKVR--IGLTGTVLQNNMKELW 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 2.55e-14

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 72.32  E-value: 2.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIegRGCILGDDMGLGKTIQVisflAAVLHkkgtrediennmpEFLLKSMKKKppstakkmFLIV 201
Cdd:cd18011   1 PLPHQIDAVLRALRKPP--VRLLLADEVGLGKTIEA----GLIIK-------------ELLLRGDAKR--------VLIL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 202 APLSVLYNWKDELDTWGYFRVTVLHGSKKDNELLRLKQRKCE--IALTTYETLR---LCLEELNSLEWSAIIVDEAHRIK 276
Cdd:cd18011  54 CPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLR 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91807128 277 N----PKARVTEVMKAVKCKVR--IGLTGTVLQNNMKELWCVMDWAVPGllgsRIHFKKQFSDPVEHGQRH 341
Cdd:cd18011 134 NsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPG----RFAVLGRFLRLDGLREVL 200
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
122-309 5.50e-14

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: 72.38  E-value: 5.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRhyiegRGCILGDDMGLGKTIQVISFLAAvlHkkgTREDIENNMPEFLLKSMK-------KKPPSTA 194
Cdd:cd18070   1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILL--H---PRPDNDLDAADDDSDEMVccpdclvAETPVSS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 195 KKMfLIVAPLSVLYNWKDELD--TWGYFRVTVLHGSKKDNELL-----RLKQrkCEIALTTYETLR-------------- 253
Cdd:cd18070  71 KAT-LIVCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALAspapeILAE--YDIVVTTYDVLRtelhyaeanrsnrr 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91807128 254 LCLEE--------LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKEL 309
Cdd:cd18070 148 RRRQKryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDL 211
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
79-300 1.88e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.44  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  79 RSLIFDDKDLEKPYFPDRKIPSLASAFQLSEDGDSIPYTinryLRDYQREGAQFLYRHYIEG--RGCILGDdMGLGKTIq 156
Cdd:COG1061  42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGggRGLVVAP-TGTGKTV- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 157 VISFLAAVLHKKGTrediennmpefllksmkkkppstakkmFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGSKKDNEll 235
Cdd:COG1061 116 LALALAAELLRGKR---------------------------VLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD-- 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91807128 236 rlkqrkCEIALTTYETL--RLCLEELNSlEWSAIIVDEAHRIknPKARVTEVMKAVKCKVRIGLTGT 300
Cdd:COG1061 165 ------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
122-300 3.88e-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: 61.55  E-value: 3.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 122 LRDYQREGAQFLYRHYIEGRGCIlgdDM--GLGKTiqVISFLAAVLHKKGTrediennmpefllksmkkkppstakkmFL 199
Cdd:cd17926   1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKT--LTALALIAYLKELR---------------------------TL 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 200 IVAP-LSVLYNWKDELDTWGYFRVTVLHGSKKDNellrlKQRKCEIALTTYETLRLCLEELNSL--EWSAIIVDEAHRIK 276
Cdd:cd17926  49 IVVPtDALLDQWKERFEDFLGDSSIGLIGGGKKK-----DFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLP 123
                       170       180
                ....*....|....*....|....
gi 91807128 277 NPKARvtEVMKAVKCKVRIGLTGT 300
Cdd:cd17926 124 AKTFS--EILKELNAKYRLGLTAT 145
ResIII pfam04851
Type III restriction enzyme, res subunit;
122-300 4.15e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 61.92  E-value: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   122 LRDYQREGAQFLYRHYIEG--RGCIlgdDM--GLGKTIqVISFLAAVLHKKGTrediennmpefllksmkkkppstaKKM 197
Cdd:pfam04851   4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTL-TAAKLIARLFKKGP------------------------IKK 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   198 FLIVAP-LSVLYNWKDELDtwGYFRVTVLHGSKKDNELLRLKQRKCEIALTTYETL----RLCLEELNSLEWSAIIVDEA 272
Cdd:pfam04851  56 VLFLVPrKDLLEQALEEFK--KFLPNYVEIGEIISGDKKDESVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEA 133
                         170       180
                  ....*....|....*....|....*...
gi 91807128   273 HRIKNPKARvtEVMKAVKCKVRIGLTGT 300
Cdd:pfam04851 134 HRSGASSYR--NILEYFKPAFLLGLTAT 159
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
140-300 7.67e-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: 54.72  E-value: 7.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 140 GRGCILGDDMGLGKTIQVISFLAAVLHKKGTRediennmpefllksmkkkppstakkmFLIVAPLSVL-YNWKDELDTWG 218
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK--------------------------VLVLVPTKALaLQTAERLRELF 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 219 YF--RVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEELNSL---EWSAIIVDEAHRIKnPKARVTEVMKAVKCKV 293
Cdd:cd00046  55 GPgiRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALL-IDSRGALILDLAVRKA 133
                       170
                ....*....|...
gi 91807128 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 2.93e-08

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


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 53.84  E-value: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 192 STAKKMFLIVAPLSV-LYNWKDELDTWGYF---RVTVLHGSKKDnellrlKQRKCEIALTTYETLR----------LCLE 257
Cdd:cd18029  48 CTIKKSTLVLCTSAVsVEQWRRQFLDWTTIddeQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFME 121
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 91807128 258 ELNSLEWSAIIVDEAHRIKNPKARvtEVMKAVKCKVRIGLTGTVL 302
Cdd:cd18029 122 FITEREWGLIILDEVHVVPAPMFR--RVLTLQKAHCKLGLTATLV 164
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
502-640 2.02e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 51.27  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128 502 PKYSGKMKVLQQLLNHFRKqrDKVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEFnSSQD 573
Cdd:COG1111 335 PKLSKLREILKEQLGTNPD--SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERF-RAGE 411
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91807128 574 VNIcLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQavdRAYRIGQCRDVKVLRLISLGTVEEIMY 640
Cdd:COG1111 412 FNV-LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEAYY 474
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
20-71 2.22e-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: 42.24  E-value: 2.22e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 91807128  20 GERCLAPSLDNKKLCEASIKSITVDGNGkpfAVVLYPDF-QEKTIPLQRLQEV 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 ...
578-620 2.44e-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: 43.08  E-value: 2.44e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 91807128 578 LVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQ 620
Cdd:cd18785  26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
138-301 6.43e-05

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: 43.77  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   138 IEGRGCILGDDMGLGKTiqvisfLAAVLhkkgtrediennmpeFLLKSMKKKPPstaKKMFLIVAPLSVL----Y-NWKD 212
Cdd:pfam00270  12 LEGRDVLVQAPTGSGKT------LAFLL---------------PALEALDKLDN---GPQALVLAPTRELaeqiYeELKK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128   213 ELDTWGYFRVTVLHGSKKDNELLRLKqrKCEIALTTYETLRLCLEE---LNSLEWsaIIVDEAHRI--KNPKARVTEVMK 287
Cdd:pfam00270  68 LGKGLGLKVASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQErklLKNLKL--LVLDEAHRLldMGFGPDLEEILR 143
                         170
                  ....*....|....*
gi 91807128   288 AVKCKVRI-GLTGTV 301
Cdd:pfam00270 144 RLPKKRQIlLLSATL 158
PRK02250 PRK02250
hypothetical protein; Provisional
325-429 8.65e-04

hypothetical protein; Provisional


Pssm-ID: 179393 [Multi-domain]  Cd Length: 166  Bit Score: 40.63  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91807128  325 IHFKKQFSdpvEHGQRHTATKRElatgrkamhRLAKKMSGWFLrrtktlIKGQLPKKEdrmvycslTDFQKAVYQTVlet 404
Cdd:PRK02250  92 VEFKAYFD---EEGKRYCLEERS---------RFLKENGLWYY------IDGTFPEEE--------PEQDPRLNQSV--- 142
                         90       100
                 ....*....|....*....|....*
gi 91807128  405 edVALILTSSQPCTCGSGQKRRKCC 429
Cdd:PRK02250 143 --SSLKQGRNDPCICGSGKKFKKCC 165
SWIM_PBPRA1643 TIGR04102
SWIM/SEC-C metal-binding motif protein, PBPRA1643 family; Members of this protein family have ...
416-429 7.93e-03

SWIM/SEC-C metal-binding motif protein, PBPRA1643 family; Members of this protein family have a SWIM, or SEC-C, domain (see pfam02810), a 21-amino acid putative Zn-binding domain that is shared with SecA, plant MuDR transposases, etc. This small protein family of unknown function occurs primarily in marine bacteria.


Pssm-ID: 200353 [Multi-domain]  Cd Length: 108  Bit Score: 36.52  E-value: 7.93e-03
                          10
                  ....*....|....
gi 91807128   416 PCTCGSGQKRRKCC 429
Cdd:TIGR04102  94 PCPCGSGKKYKKCC 107
 
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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