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Conserved domains on  [gi|584059263|ref|XP_006774124|]
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PREDICTED: transcriptional regulator ATRX [Myotis davidii]

Protein Classification

DEXHc_ATRX and SF2_C_SNF domain-containing protein( domain architecture ID 12785140)

DEXHc_ATRX and SF2_C_SNF domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
5-248 1.31e-174

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: 506.35  E-value: 1.31e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKL-DFSTALVVCPLNTALNWMNEF 83
Cdd:cd18068    1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 162
Cdd:cd18068   81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 163 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 242
Cdd:cd18068  161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                 ....*.
gi 584059263 243 RVMKKR 248
Cdd:cd18068  241 RVMKKR 246
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
4-637 9.19e-89

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 9.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfsTALVVCPLNTALNWMNEF 83
Cdd:COG0553  241 TLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVVC 163
Cdd:COG0553  310 AKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE---------------LLAAVDWDLVIL 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 164 DEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvr 243
Cdd:COG0553  365 DEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---------- 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 244 vmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSSEGGRGKagAKLFQDFQM 323
Cdd:COG0553  435 --EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRR--GLILAALTR 510
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 324 LSRIWTHPwclqldyiskenkGYFDEDsmdefiasdsdetsmslssddyakkkktkgkkgkkdssssgsgsdndvevikv 403
Cdd:COG0553  511 LRQICSHP-------------ALLLEE----------------------------------------------------- 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 404 wnsrsrgggegnvdetgnnpsvsikteeskatsssnpsspapdwykdfvtdaDAEILEHSGKMVLLFEILRMAEEIGDKV 483
Cdd:COG0553  525 ----------------------------------------------------GAELSGRSAKLEALLELLEELLAEGEKV 552
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 484 LVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgRLFIIST 563
Cdd:COG0553  553 LVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRFQEGPEA--PVFLISL 608
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 564 KAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVD 637
Cdd:COG0553  609 KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
5-248 1.31e-174

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: 506.35  E-value: 1.31e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKL-DFSTALVVCPLNTALNWMNEF 83
Cdd:cd18068    1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 162
Cdd:cd18068   81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 163 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 242
Cdd:cd18068  161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                 ....*.
gi 584059263 243 RVMKKR 248
Cdd:cd18068  241 RVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
8-334 2.06e-108

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: 336.58  E-value: 2.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263    8 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDFSTALVVCPLNTALNWMNEFEKWQ 87
Cdd:pfam00176   1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   88 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 167
Cdd:pfam00176  73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  168 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 247
Cdd:pfam00176 134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  248 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQ-YYLDHLTGVGNSSEGGRGKAgAKLFQDFQMLSR 326
Cdd:pfam00176 203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                  ....*...
gi 584059263  327 IWTHPWCL 334
Cdd:pfam00176 282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
4-637 9.19e-89

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 9.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfsTALVVCPLNTALNWMNEF 83
Cdd:COG0553  241 TLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVVC 163
Cdd:COG0553  310 AKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE---------------LLAAVDWDLVIL 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 164 DEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvr 243
Cdd:COG0553  365 DEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---------- 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 244 vmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSSEGGRGKagAKLFQDFQM 323
Cdd:COG0553  435 --EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRR--GLILAALTR 510
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 324 LSRIWTHPwclqldyiskenkGYFDEDsmdefiasdsdetsmslssddyakkkktkgkkgkkdssssgsgsdndvevikv 403
Cdd:COG0553  511 LRQICSHP-------------ALLLEE----------------------------------------------------- 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 404 wnsrsrgggegnvdetgnnpsvsikteeskatsssnpsspapdwykdfvtdaDAEILEHSGKMVLLFEILRMAEEIGDKV 483
Cdd:COG0553  525 ----------------------------------------------------GAELSGRSAKLEALLELLEELLAEGEKV 552
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 484 LVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgRLFIIST 563
Cdd:COG0553  553 LVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRFQEGPEA--PVFLISL 608
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 564 KAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVD 637
Cdd:COG0553  609 KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
462-612 1.53e-51

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: 176.90  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 462 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 541
Cdd:cd18793    9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584059263 542 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 612
Cdd:cd18793   67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
36-661 4.68e-45

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 176.53  E-value: 4.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   36 ILAHCMGLGKTLQVVSFLhtVLLCEKLDFSTA-LVVCPLNTALNWMNEFEKWQEGLKddeklevselaTVK---RPQERS 111
Cdd:PLN03142  192 ILADEMGLGKTLQTISLL--GYLHEYRGITGPhMVVAPKSTLGNWMNEIRRFCPVLR-----------AVKfhgNPEERA 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  112 YMLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRI 189
Cdd:PLN03142  259 HQREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  190 ILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALT 269
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  270 KFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSseGGRGKagaKLFQDFQMLSRIWTHPWCLQldyiskenkgyfde 349
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA--GGERK---RLLNIAMQLRKCCNHPYLFQ-------------- 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  350 dsmdefiasdsdetsmslssddyakkkktkgkkgkkdssssgsgsdndvevikvwnsrsrgggegnvdetGNNPSVSIKT 429
Cdd:PLN03142  453 ----------------------------------------------------------------------GAEPGPPYTT 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  430 EEskatsssnpsspapdwykdfvtdadaEILEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrekte 509
Cdd:PLN03142  463 GE--------------------------HLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL--------- 507
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  510 dkdkplIYKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSY 589
Cdd:PLN03142  508 ------MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQV 573
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263  590 DIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMN--ELTELYTFEPDLL 661
Cdd:PLN03142  574 DLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNkdELLQMVRYGAEMV 647
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
464-601 4.25e-18

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: 80.72  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  464 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 543
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 584059263  544 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 601
Cdd:pfam00271  56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
525-601 1.90e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.64  E-value: 1.90e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263   525 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 601
Cdd:smart00490  10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
3-198 1.16e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 76.38  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263     3 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCEKldFSTALVVCPL-NTALNWMN 81
Cdd:smart00487   7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263    82 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 160
Cdd:smart00487  73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 584059263   161 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 198
Cdd:smart00487 133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
5-248 1.31e-174

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: 506.35  E-value: 1.31e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKL-DFSTALVVCPLNTALNWMNEF 83
Cdd:cd18068    1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 162
Cdd:cd18068   81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 163 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 242
Cdd:cd18068  161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                 ....*.
gi 584059263 243 RVMKKR 248
Cdd:cd18068  241 RVMKKR 246
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
5-248 8.24e-120

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: 364.31  E-value: 8.24e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESvkKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKlDFSTALVVCPLNTALNWMNEFE 84
Cdd:cd18007    1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-RRSRPLVLCPASTLYNWEDEFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLKDDEKLEVSeLATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNvKSRKLKEIFNKALVDPGPDFVVCD 164
Cdd:cd18007   78 KWLPPDLRPLLVLVS-LSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT-TDPRLKQEFIAALLDPGPDLLVLD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 165 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRV 244
Cdd:cd18007  156 EGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRL 235

                 ....
gi 584059263 245 MKKR 248
Cdd:cd18007  236 MLKR 239
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
8-334 2.06e-108

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: 336.58  E-value: 2.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263    8 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDFSTALVVCPLNTALNWMNEFEKWQ 87
Cdd:pfam00176   1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   88 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 167
Cdd:pfam00176  73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  168 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 247
Cdd:pfam00176 134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  248 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQ-YYLDHLTGVGNSSEGGRGKAgAKLFQDFQMLSR 326
Cdd:pfam00176 203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                  ....*...
gi 584059263  327 IWTHPWCL 334
Cdd:pfam00176 282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
4-637 9.19e-89

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 9.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfsTALVVCPLNTALNWMNEF 83
Cdd:COG0553  241 TLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVVC 163
Cdd:COG0553  310 AKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE---------------LLAAVDWDLVIL 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 164 DEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvr 243
Cdd:COG0553  365 DEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD---------- 434
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 244 vmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSSEGGRGKagAKLFQDFQM 323
Cdd:COG0553  435 --EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRR--GLILAALTR 510
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 324 LSRIWTHPwclqldyiskenkGYFDEDsmdefiasdsdetsmslssddyakkkktkgkkgkkdssssgsgsdndvevikv 403
Cdd:COG0553  511 LRQICSHP-------------ALLLEE----------------------------------------------------- 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 404 wnsrsrgggegnvdetgnnpsvsikteeskatsssnpsspapdwykdfvtdaDAEILEHSGKMVLLFEILRMAEEIGDKV 483
Cdd:COG0553  525 ----------------------------------------------------GAELSGRSAKLEALLELLEELLAEGEKV 552
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 484 LVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgRLFIIST 563
Cdd:COG0553  553 LVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRFQEGPEA--PVFLISL 608
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 564 KAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVD 637
Cdd:COG0553  609 KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
5-248 3.49e-86

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: 275.54  E-value: 3.49e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLdfSTALVVCPLNTALNWMNEFE 84
Cdd:cd18069    1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGA--KTVLAIVPVNTLQNWLSEFN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLKDDEKLEVSELAT------VKRPQERSYMLQRWQEDGGVMIIGYEMYRNlaqgrnvksrklkeifnkalvDPGP 158
Cdd:cd18069   79 KWLPPPEALPNVRPRPFKVfilndeHKTTAARAKVIEDWVKDGGVLLMGYEMFRL---------------------RPGP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 159 DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADST 238
Cdd:cd18069  138 DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDST 217
                        250
                 ....*....|
gi 584059263 239 MVDVRVMKKR 248
Cdd:cd18069  218 PQDVKLMRYR 227
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
5-263 4.86e-62

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: 210.22  E-value: 4.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVL--------LCEKldfstALVVCPLNTA 76
Cdd:cd18004    1 LRPHQREGVQFLYDC----LTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLkqgpygkpTAKK-----ALIVCPSSLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  77 LNWMNEFEKWqegLKDdEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRklkeifnkalvdp 156
Cdd:cd18004   72 GNWKAEFDKW---LGL-RRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKIS------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 157 gPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 236
Cdd:cd18004  135 -IDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPD 213
                        250       260
                 ....*....|....*....|....*..
gi 584059263 237 STMVDVRVMKKRAHILYEMLAGCVQRK 263
Cdd:cd18004  214 ASEEDKELGAERSQELSELTSRFILRR 240
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
5-210 4.10e-60

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: 202.80  E-value: 4.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCesvkktkksPGSGCILAHCMGLGKTLQVVSFLHTvLLCEKLDFSTALVVCPLNTALNWMNEFE 84
Cdd:cd17919    1 LRPYQLEGLNFLLELYE---------NGPGGILADEMGLGKTLQAIAFLAY-LLKEGKERGPVLVVCPLSVLENWEREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLKddeklevseLATVKRPQERSYMLQ--RWQEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVV 162
Cdd:cd17919   71 KWTPDLR---------VVVYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKA---------------SLRKFRWDLVV 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 584059263 163 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 210
Cdd:cd17919  127 VDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
462-612 1.53e-51

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: 176.90  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 462 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 541
Cdd:cd18793    9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584059263 542 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 612
Cdd:cd18793   67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
5-263 1.17e-47

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: 169.96  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCcesvkKTKKSPGS-GCILAHCMGLGKTLQVVSFLHTVL----LCeKLDFSTALVVCPLNTALNW 79
Cdd:cd18067    1 LRPHQREGVKFLYRCV-----TGRRIRGShGCIMADEMGLGKTLQCITLMWTLLrqspQC-KPEIDKAIVVSPSSLVKNW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  80 MNEFEKWQEGlkddeklEVSELATV-KRPQERSYMLQRWQEDGG------VMIIGYEMYRNLAqgrnvksrklkEIFNKA 152
Cdd:cd18067   75 ANELGKWLGG-------RLQPLAIDgGSKKEIDRKLVQWASQQGrrvstpVLIISYETFRLHV-----------EVLQKG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 153 LVDpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 232
Cdd:cd18067  137 EVG----LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKG 212
                        250       260       270
                 ....*....|....*....|....*....|.
gi 584059263 233 QCADSTMVDVRVMKKRAHILYEMLAGCVQRK 263
Cdd:cd18067  213 RDADASEKERQLGEEKLQELISIVNRCIIRR 243
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
36-661 4.68e-45

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 176.53  E-value: 4.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   36 ILAHCMGLGKTLQVVSFLhtVLLCEKLDFSTA-LVVCPLNTALNWMNEFEKWQEGLKddeklevselaTVK---RPQERS 111
Cdd:PLN03142  192 ILADEMGLGKTLQTISLL--GYLHEYRGITGPhMVVAPKSTLGNWMNEIRRFCPVLR-----------AVKfhgNPEERA 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  112 YMLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRI 189
Cdd:PLN03142  259 HQREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  190 ILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALT 269
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  270 KFLPPKHEYVLAVRMTPIQCKLYQYYLDHLTGVGNSseGGRGKagaKLFQDFQMLSRIWTHPWCLQldyiskenkgyfde 349
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA--GGERK---RLLNIAMQLRKCCNHPYLFQ-------------- 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  350 dsmdefiasdsdetsmslssddyakkkktkgkkgkkdssssgsgsdndvevikvwnsrsrgggegnvdetGNNPSVSIKT 429
Cdd:PLN03142  453 ----------------------------------------------------------------------GAEPGPPYTT 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  430 EEskatsssnpsspapdwykdfvtdadaEILEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrekte 509
Cdd:PLN03142  463 GE--------------------------HLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL--------- 507
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  510 dkdkplIYKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSY 589
Cdd:PLN03142  508 ------MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQV 573
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263  590 DIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMN--ELTELYTFEPDLL 661
Cdd:PLN03142  574 DLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNkdELLQMVRYGAEMV 647
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
5-238 9.17e-45

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: 161.39  E-value: 9.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfsTALVVCPLNTALNWMNEFE 84
Cdd:cd18001    1 LYPHQREGVAWLW---------SLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIK--SVLVVMPTSLIPHWVKEFA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLkddeklevselaTVK-----RPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEIFNKALVdpgPD 159
Cdd:cd18001   70 KWTPGL------------RVKvfhgtSKKERERNLERIQRGGGVLLTTYGMVLSNTE-------QLSADDHDEFK---WD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 160 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI-KENLLGSIKEFRNRFINPIQNGQCADST 238
Cdd:cd18001  128 YVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDAT 207
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
5-248 1.28e-42

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: 155.61  E-value: 1.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVL----------------LCEKLDFS--- 65
Cdd:cd18005    1 LRDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSakk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  66 TALVVCPLNTALNWMNEFEKWQEglkddekLEVSELATVKRPQERSYMLQRWQEDggVMIIGYEMYRNLAQGrnvksrkL 145
Cdd:cd18005   72 PVLIVAPLSVLYNWKDELDTWGH-------FEVGVYHGSRKDDELEGRLKAGRLE--VVVTTYDTLRRCIDS-------L 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 146 KEIfnkalvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18005  136 NSI--------NWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207
                        250       260
                 ....*....|....*....|...
gi 584059263 226 INPIQNGQCADSTMVDVRVMKKR 248
Cdd:cd18005  208 SEPIKRGQRHTATARELRLGRKR 230
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
5-263 1.53e-38

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 143.83  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTvLLCEKLD-----FSTALVVCPLNTALNW 79
Cdd:cd18066    1 LRPHQREGIEFLYEC----VMGMRVNERFGAILADEMGLGKTLQCISLIWT-LLRQGPYggkpvIKRALIVTPGSLVKNW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  80 MNEFEKWQeglkDDEKLEVSELATVKRPQE--RSYMLQrwqedggVMIIGYEMY-RNLAQGRNVKSrklkeifnkalvdp 156
Cdd:cd18066   76 KKEFQKWL----GSERIKVFTVDQDHKVEEfiASPLYS-------VLIISYEMLlRSLDQISKLNF-------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 157 gpDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 236
Cdd:cd18066  131 --DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPT 208
                        250       260
                 ....*....|....*....|....*..
gi 584059263 237 STMVDVRVMKKRAHILYEMLAGCVQRK 263
Cdd:cd18066  209 ATPEEKKLGEARAAELTRLTGLFILRR 235
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
5-237 1.33e-33

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: 128.84  E-value: 1.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGV---QFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLlcEKLDFSTALVVCPLNTALNWMN 81
Cdd:cd18012    5 LRPYQKEGFnwlSFLRHY------------GLGGILADDMGLGKTLQTLALLLSRK--EEGRKGPSLVVAPTSLIYNWEE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  82 EFEKWQEGLKddeklevselATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpdF 160
Cdd:cd18012   71 EAAKFAPELK----------VLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIE-------LLKEVkFH---------Y 124
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263 161 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADS 237
Cdd:cd18012  125 LVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA 201
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
5-211 5.58e-32

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: 123.20  E-value: 5.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVkktkkspgsGCILAHCMGLGKTLQVVSFLhTVLLCEKLDFSTALVVCPLNTALNWMNEFE 84
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRV---------GGILGDEMGLGKTIQIIAFL-AALHHSKLGLGPSLIVCPATVLKQWVKEFH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KW------------QEGLKDDEKLEVSELATVKRPQERsymlqrwqEDGGVMIIGYEMYRnlaqgrnvksrklkeIFNKA 152
Cdd:cd18000   71 RWwppfrvvvlhssGSGTGSEEKLGSIERKSQLIRKVV--------GDGGILITTYEGFR---------------KHKDL 127
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 584059263 153 LVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 211
Cdd:cd18000  128 LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVF 186
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
4-225 1.39e-28

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: 114.79  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMwdcccesvkKTKKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCEKLDFSTALVVCPLNTALNWMNEF 83
Cdd:cd18009    3 VMRPYQLEGMEWL---------RMLWENGINGILADEMGLGKTIQTIALL--AHLRERGVWGPFLVIAPLSTLPNWVNEF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQ--------EGLKDDEKlevsELATVKRPQERSYMlqrwqeDGGVMIIGYEMYRNLAqgrnvksrklkeifnKALVD 155
Cdd:cd18009   72 ARFTpsvpvllyHGTKEERE----RLRKKIMKREGTLQ------DFPVVVTSYEIAMRDR---------------KALQH 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 156 PGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18009  127 YAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF 196
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
5-229 3.48e-28

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: 113.60  E-value: 3.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWdcccesvkKTKKSPGSGcILAHCMGLGKTLQ----VVSFLHTVLLCEKLDFSTALVVCPLNTALNWM 80
Cdd:cd17999    1 LRPYQQEGINWLA--------FLNKYNLHG-ILCDDMGLGKTLQtlciLASDHHKRANSFNSENLPSLVVCPPTLVGHWV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  81 NEFEKWqeglKDDEKLEVseLATVKRPQERSyMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpd 159
Cdd:cd17999   72 AEIKKY----FPNAFLKP--LAYVGPPQERR-RLREQGEKHNVIVASYDVLRNDIE-------VLTKIeWN--------- 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 160 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 229
Cdd:cd17999  129 YCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPI 198
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
5-225 2.07e-27

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: 111.19  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFE 84
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYN---------RRNCILADEMGLGKTIQSIAFLEHLYQVEGIR-GPFLVIAPLSTIPNWQREFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWqeglkddeklevSELATVkrpqersymLQRWQEDGGVMIIGYEMYRNLAQGRnVKSRKLK--------EIFNK---AL 153
Cdd:cd17995   71 TW------------TDMNVV---------VYHGSGESRQIIQQYEMYFKDAQGR-KKKGVYKfdvlittyEMVIAdaeEL 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584059263 154 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd17995  129 RKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
4-231 4.68e-26

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: 107.45  E-value: 4.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWdccceSVKKTKKSPgsgcILAHCMGLGKTLQVVSFLhTVLLCEKLDFSTALVVCPLNTALNWMNEF 83
Cdd:cd17996    3 TLKEYQLKGLQWMV-----SLYNNNLNG----ILADEMGLGKTIQTISLI-TYLMEKKKNNGPYLVIVPLSTLSNWVSEF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEglkddeklEVSELATVKRPQERSyMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSR-KLKEIFNKalvdpgpdF 160
Cdd:cd17996   73 EKWAP--------SVSKIVYKGTPDVRK-KLQSQIRAGkfNVLLTTYEYI--------IKDKpLLSKIKWK--------Y 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584059263 161 VVCDEGHILKNEASAVSKAMNS-IRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 231
Cdd:cd17996  128 MIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFAN 199
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
5-210 1.20e-25

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 104.77  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMwdcccESVKKTKKSpgsgCILAHCMGLGKTLQVVSFLhtVLLCEKLDFSTALVVCPLNTALNWMNEFE 84
Cdd:cd17998    1 LKDYQLIGLNWL-----NLLYQKKLS----GILADEMGLGKTIQVIAFL--AYLKEIGIPGPHLVVVPSSTLDNWLREFK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLKddekLEVSELATVKRPQERsYMLQRWQEDGGVMIIGYemyrNLAQGrNVKSRKLKEIFNKalvdpgpDFVVCD 164
Cdd:cd17998   70 RWCPSLK----VEPYYGSQEERKHLR-YDILKGLEDFDVIVTTY----NLATS-NPDDRSFFKRLKL-------NYVVYD 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 584059263 165 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 210
Cdd:cd17998  133 EGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
36-229 7.58e-25

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: 103.59  E-value: 7.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  36 ILAHCMGLGKTLQVVSFL-HtvLLCEKLDFSTALVVCPLNTALNWMNEFEKWQEGLKddeklevsELATVKRPQERSYML 114
Cdd:cd18003   23 ILADEMGLGKTIQTIALLaH--LACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFK--------ILTYYGSAKERKLKR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 115 QRWQEDGG--VMIIGYEMyrnLAQGRNV-KSRKLKeifnkalvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIIL 191
Cdd:cd18003   93 QGWMKPNSfhVCITSYQL---VVQDHQVfKRKKWK-------------YLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 584059263 192 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 229
Cdd:cd18003  157 TGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL 194
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
36-221 5.63e-23

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: 98.16  E-value: 5.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  36 ILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddekleVSELATVKrpQERSYMLQ 115
Cdd:cd17997   26 ILADEMGLGKTLQTISLLGYLKHYKNIN-GPHLIIVPKSTLDNWMREFKRWCPSLR------VVVLIGDK--EERADIIR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 116 RWQEDG--GVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTG 193
Cdd:cd17997   97 DVLLPGkfDVCITSYEMVI-----------KEKTVLKKF----NWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
                        170       180
                 ....*....|....*....|....*...
gi 584059263 194 TPLQNNLIEYHCMVNFIKENLLGSIKEF 221
Cdd:cd17997  162 TPLQNNLHELWALLNFLLPDVFTSSEDF 189
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
4-221 2.62e-22

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: 96.27  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLdFSTALVVCPLNTALNWMNEF 83
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCK---------GNNGILADEMGLGKTVQTISFLSYLFHSQQQ-YGPFLVVVPLSTMPAWQREF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKddeklEVSELATVKRPQersymlqrwqedggvMIIGYEMYRNlaqgrnvKSRKLK--------EIFNKALVD 155
Cdd:cd17993   71 AKWAPDMN-----VIVYLGDIKSRD---------------TIREYEFYFS-------QTKKLKfnvllttyEIILKDKAF 123
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584059263 156 PGP---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 221
Cdd:cd17993  124 LGSikwQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF 192
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
5-227 1.06e-21

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: 94.43  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFE 84
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAE---------QHGCILGDEMGLGKTCQTISLLWYLAGRLKLL-GPFLVLCPLSVLDNWKEELN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWQEGLK----DDEKLEVSELatvkrpQERSYMLQRWQedggVMIIGYEMYrnLAQGRNVKSRKLKeifnkalvdpgpdF 160
Cdd:cd18006   71 RFAPDLSvityMGDKEKRLDL------QQDIKSTNRFH----VLLTTYEIC--LKDASFLKSFPWA-------------S 125
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263 161 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGsiKEFRNRFIN 227
Cdd:cd18006  126 LVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP--KDKLDDFIK 190
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
5-233 1.83e-21

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: 94.28  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMwdCCCesvkktkkspgsGCILAHCMGLGKTLQVVSFLHT---------------VLLCEKLDFSTA-L 68
Cdd:cd18008    1 LLPYQKQGLAWM--LPR------------GGILADEMGLGKTIQALALILAtrpqdpkipeeleenSSDPKKLYLSKTtL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  69 VVCPLNTALNWMNEFEK-------------WQEGLKDDEKLEvselatvkrpqerSYMlqrwqedggVMIIGYEMYRNLA 135
Cdd:cd18008   67 IVVPLSLLSQWKDEIEKhtkpgslkvyvyhGSKRIKSIEELS-------------DYD---------IVITTYGTLASEF 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 136 QGRNVKSRKLKEifnkaLVDPGPDF------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNF 209
Cdd:cd18008  125 PKNKKGGGRDSK-----EKEASPLHrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRF 199
                        250       260
                 ....*....|....*....|....
gi 584059263 210 IKENLLGSIKEFRNRFINPIQNGQ 233
Cdd:cd18008  200 LRVEPFGDYPWFNSDISKPFSKND 223
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
5-236 3.85e-21

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: 92.65  E-value: 3.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFmwdccceSVKKtkkspGSGCILAHCMGLGKTLQVVsflhTVLLCEKLDFStALVVCPLNTALNWMNEFE 84
Cdd:cd18010    1 LLPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAI----AIAAYYREEWP-LLIVCPSSLRLTWADEIE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KWqegLKDDEKLEVSELATVKRPQERSymlqrwqeDGGVMIIGYEMyrnlaqgrnvkSRKLKEIFNKAlvdpGPDFVVCD 164
Cdd:cd18010   64 RW---LPSLPPDDIQVIVKSKDGLRDG--------DAKVVIVSYDL-----------LRRLEKQLLAR----KFKVVICD 117
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 165 EGHILKNEASAVSKAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 236
Cdd:cd18010  118 ESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWD 191
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
3-232 6.16e-20

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: 90.06  E-value: 6.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   3 IKLKPHQVDGVQFM---WdCCCESVkktkkspgsgcILAHCMGLGKTLQVVSFLhTVLLCEKLDFSTALVVCPLNTALNW 79
Cdd:cd18054   19 LELRDYQLEGLNWLahsW-CKNNSV-----------ILADEMGLGKTIQTISFL-SYLFHQHQLYGPFLLVVPLSTLTSW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  80 MNEFEKWQEGLkdDEKLEVSELATVKRPQERSYMLQRWQE-DGGVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 158
Cdd:cd18054   86 QREFEIWAPEI--NVVVYIGDLMSRNTIREYEWIHSQTKRlKFNALITTYEIL--------LKDKTVLGSINWA------ 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 159 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 232
Cdd:cd18054  150 -FLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
464-601 4.25e-18

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: 80.72  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  464 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 543
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 584059263  544 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 601
Cdd:pfam00271  56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
4-275 8.31e-18

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: 83.95  E-value: 8.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   4 KLKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEF 83
Cdd:cd18064   15 KLRDYQVRGLNWLI---------SLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIP-GPHMVLVPKSTLHNWMAEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKD-----DEKLEVSELATVKRPQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 158
Cdd:cd18064   85 KRWVPTLRAvcligDKDQRAAFVRDVLLPGE-------WD----VCVTSYEML--------IKEKSVFKKFNWR------ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 159 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINpiqNGQCADST 238
Cdd:cd18064  140 -YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT---NNCLGDQK 215
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 584059263 239 MVDVRVMKKRAHILyemlagcvqRKDYTALTKFLPPK 275
Cdd:cd18064  216 LVERLHMVLRPFLL---------RRIKADVEKSLPPK 243
HELICc smart00490
helicase superfamily c-terminal domain;
525-601 1.90e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.64  E-value: 1.90e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263   525 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 601
Cdd:smart00490  10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
5-221 3.45e-17

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: 81.65  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCEKLDFSTALVVCPLNTALNWMN 81
Cdd:cd18057    1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTIVFLYS-LYKEGHSKGPYLVSAPLSTIINWER 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  82 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMIiGYEMYRnLAQGRNVKSRKLKEIFNKALVDPGP--- 158
Cdd:cd18057   68 EFEMWAPDFYVVTYTGDKESRSVIRENEFSF------EDNAIRS-GKKVFR-MKKEAQIKFHVLLTSYELITIDQAIlgs 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 159 ---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 221
Cdd:cd18057  140 iewACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTperfNNLEGFLEEF 209
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
32-225 4.48e-17

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: 81.60  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  32 GSGCILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFEKWQEGLK-----DDEKLEVSELATVKR 106
Cdd:cd18065   34 GVNGILADEMGLGKTLQTIALLGYLKHYRNIP-GPHMVLVPKSTLHNWMNEFKRWVPSLRavcliGDKDARAAFIRDVMM 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 107 PQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSR 186
Cdd:cd18065  113 PGE-------WD----VCVTSYEMV--------IKEKSVFKKFNWR-------YLVIDEAHRIKNEKSKLSEIVREFKTT 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 584059263 187 RRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18065  167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 205
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
5-225 8.94e-17

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: 79.79  E-value: 8.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCEKLDFSTALVVCPLNTALNWMN 81
Cdd:cd17994    1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTIQTIVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  82 EFEKWqeglkddekleVSELATVkrpqerSYMLQRwqedggVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALvdpgpdfv 161
Cdd:cd17994   68 EFEMW-----------APDFYVV------TYVGDH------VLLTSYELI-------SIDQAILGSIDWAVL-------- 109
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584059263 162 VCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd17994  110 VVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF 173
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
5-230 3.40e-16

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 78.55  E-value: 3.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMwdcccesvkktKKSPGSGCILAhcMGLGKTLQVVSFLHTVLLcekLDF-STALVVCPLNTALN-WMNE 82
Cdd:cd18013    1 PHPYQKVAINFI-----------IEHPYCGLFLD--MGLGKTVTTLTALSDLQL---DDFtRRVLVIAPLRVARStWPDE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  83 FEKWqEGLKDdekLEVSelATVKRPQERSYMLQRwqeDGGVMIIGYEmyrnlaqgrNVKsrKLKEIFNkalvDPGP-DFV 161
Cdd:cd18013   65 VEKW-NHLRN---LTVS--VAVGTERQRSKAANT---PADLYVINRE---------NLK--WLVNKSG----DPWPfDMV 120
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584059263 162 VCDEGHILKNEASAVSKAMNSIRSR-RRII-LTGTPLQNNLIEYHCMVNFIK--ENLLGSIKEFRNRFINPIQ 230
Cdd:cd18013  121 VIDELSSFKSPRSKRFKALRKVRPViKRLIgLTGTPSPNGLMDLWAQIALLDqgERLGRSITAYRERWFDPDK 193
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
3-221 4.82e-16

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: 78.55  E-value: 4.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   3 IKLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHtVLLCEKLDFSTALVVCPLNTALNWMNE 82
Cdd:cd18053   19 LELRDYQLNGLNWLAHSWCK---------GNSCILADEMGLGKTIQTISFLN-YLFHEHQLYGPFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  83 FEKWQEG------LKDDEKLEVSELATVKRPQERSYMLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdp 156
Cdd:cd18053   89 IQTWAPQmnavvyLGDINSRNMIRTHEWMHPQTKRLKFN-------ILLTTYEIL--------LKDKSFLGGLNWA---- 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584059263 157 gpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 221
Cdd:cd18053  150 ---FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF 211
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
32-225 1.12e-15

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: 77.36  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  32 GSGCILAHCMGLGKTLQVVSFLHTvLLCEKLDFSTALVVCPLNTALNWMNEFEKWQ--------EGLKDDEKL----EVS 99
Cdd:cd18055   19 GTDTILADEMGLGKTIQTIVFLYS-LYKEGHTKGPFLVSAPLSTIINWEREFQMWApdfyvvtyTGDKDSRAIirenEFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 100 ELATVKRPQERSYMLQRW-QEDGGVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSK 178
Cdd:cd18055   98 FDDNAVKGGKKAFKMKREaQVKFHVLLTSYELV-------TIDQAALGSIRWACL--------VVDEAHRLKNNQSKFFR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 584059263 179 AMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18055  163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXDc smart00487
DEAD-like helicases superfamily;
3-198 1.16e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 76.38  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263     3 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCEKldFSTALVVCPL-NTALNWMN 81
Cdd:smart00487   7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263    82 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 160
Cdd:smart00487  73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 584059263   161 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 198
Cdd:smart00487 133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
5-221 1.71e-15

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: 77.03  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCEKLDFSTALVVCPLNTALNWMN 81
Cdd:cd18056    1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTAVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  82 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMiiGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGP--- 158
Cdd:cd18056   68 EFEMWAPDMYVVTYVGDKDSRAIIRENEFSF------EDNAIR--GGKKASRMKKEASVKFHVLLTSYELITIDMAIlgs 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 159 -DF--VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 221
Cdd:cd18056  140 iDWacLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTperfHNLEGFLEEF 209
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
35-225 2.08e-15

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: 76.23  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  35 CILAHCMGLGKTLQVVSFLHTVLLceKLDFSTALVVCPLNTALNWMNEFEKWQEglkddEKLEVSELATVKRPqersyml 114
Cdd:cd18058   22 CILADEMGLGKTIQSITFLSEIFL--MGIRGPFLIIAPLSTITNWEREFRTWTE-----MNAIVYHGSQISRQ------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 115 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 183
Cdd:cd18058   88 ---------MIQQYEMYYRDEQGNPLsgifKFQVVITTFEMILAD-CPELkkinwscVIIDEAHRLKNRNCKLLEGLKLM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 584059263 184 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18058  158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
35-225 2.46e-15

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: 76.22  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  35 CILAHCMGLGKTLQVVSFLHTVLLceKLDFSTALVVCPLNTALNWMNEFEKWQEglkddeklevselatvkrpqeRSYML 114
Cdd:cd18059   22 CILADEMGLGKTIQSITFLYEIYL--KGIHGPFLVIAPLSTIPNWEREFRTWTE---------------------LNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 115 QRWQEDGGVMIIGYEMYRNLAQGRNVK-SRKLKEI---FNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 183
Cdd:cd18059   79 YHGSQASRRTIQLYEMYFKDPQGRVIKgSYKFHAIittFEMILTD-CPELrnipwrcVVIDEAHRLKNRNCKLLEGLKMM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 584059263 184 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18059  158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
5-231 4.47e-15

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: 75.62  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCEKLD-FSTALVVCPLNTALNWMNEF 83
Cdd:cd18002    1 LKEYQLKGLNWLANL---------YEQGINGILADEMGLGKTVQSIAVL--AHLAEEHNiWGPFLVIAPASTLHNWQQEI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  84 EKWQEGLKddeklevsELATVKRPQERSYMLQRWQ------EDGG--VMIIGYEM-YRNLAQGRNVKSRklkeifnkalv 154
Cdd:cd18002   70 SRFVPQFK--------VLPYWGNPKDRKVLRKFWDrknlytRDAPfhVVITSYQLvVQDEKYFQRVKWQ----------- 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263 155 dpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 231
Cdd:cd18002  131 -----YMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIES 202
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
36-250 7.75e-15

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: 75.48  E-value: 7.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  36 ILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddeKLEVSELATVKR---PQERSY 112
Cdd:cd18063   46 ILADEMGLGKTIQTIALITYLMEHKRLN-GPYLIIVPLSTLSNWTYEFDKWAPSVV---KISYKGTPAMRRslvPQLRSG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 113 MLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIIL 191
Cdd:cd18063  122 KFN-------VLLTTYEYI--------IKDKHI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILL 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 192 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 250
Cdd:cd18063  180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLH 239
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
36-250 6.30e-14

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: 72.77  E-value: 6.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  36 ILAHCMGLGKTLQVVSFLHTVLLCEKLDfSTALVVCPLNTALNWMNEFEKWQEglkddeklEVSELATVKRPQ-ERSYML 114
Cdd:cd18062   46 ILADEMGLGKTIQTIALITYLMEHKRIN-GPFLIIVPLSTLSNWVYEFDKWAP--------SVVKVSYKGSPAaRRAFVP 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 115 QRWQEDGGVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIILTG 193
Cdd:cd18062  117 QLRSGKFNVLLTTYEYI--------IKDKQI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTG 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 584059263 194 TPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 250
Cdd:cd18062  182 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLH 239
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
5-232 1.21e-13

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: 71.73  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTvllceklDFStaLVVCPLNTALNWMNEFE 84
Cdd:cd18071   21 LPPFWEEAVGLFLNTITNFSQKKRPELVRGGILADDMGLGKTLTTISLILA-------NFT--LIVCPLSVLSNWETQFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  85 KwqeglkddeklevselaTVKRPQERSYMlqrwqedggvmiigyemYRNLAQGRNVKSRKLKEI----FNKALVDPG--P 158
Cdd:cd18071   92 E-----------------HVKPGQLKVYT-----------------YHGGERNRDPKLLSKYDIvlttYNTLASDFGakG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 159 DF---------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLgSIKEFRNRFI-NP 228
Cdd:cd18071  138 DSplhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPF-SNPEYWRRLIqRP 216

                 ....
gi 584059263 229 IQNG 232
Cdd:cd18071  217 LTMG 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
35-225 1.45e-13

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: 70.85  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  35 CILAHCMGLGKTLQVVSFLHTVllcekldFSTA-----LVVCPLNTALNWMNEFEKWQEGlkdDEKLEVSELATVKrpqe 109
Cdd:cd18060   22 CILADEMGLGKTIQSIAFLQEV-------YNVGihgpfLVIAPLSTITNWEREFNTWTEM---NTIVYHGSLASRQ---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 110 rsymlqrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSK 178
Cdd:cd18060   88 --------------MIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 584059263 179 AMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18060  153 SLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
35-225 5.63e-13

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: 69.26  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  35 CILAHCMGLGKTLQVVSFLHTVLLCE-KLDFstaLVVCPLNTALNWMNEFEKWQeglkdDEKLEVSELATVKRPqersyM 113
Cdd:cd18061   22 CILADEMGLGKTIQSITFLYEILLTGiRGPF---LIIAPLSTIANWEREFRTWT-----DLNVVVYHGSLISRQ-----M 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263 114 LQRwqedggvmiigYEMYRNLAQGRNVK-SRKLKEIFN--KALVDPGPDF-------VVCDEGHILKNEASAVSKAMNSI 183
Cdd:cd18061   89 IQQ-----------YEMYFRDSQGRIIRgAYRFQAIITtfEMILGGCPELnaidwrcVIIDEAHRLKNKNCKLLEGLKLM 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 584059263 184 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 225
Cdd:cd18061  158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
5-222 2.43e-10

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: 61.15  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFMWDcccesvkktKKSPGsgCILAHCMGLGKTLQVVSFLHTVLL---CEKLdfstaLVVCPlnTALNwmn 81
Cdd:cd18011    1 PLPHQIDAVLRALR---------KPPVR--LLLADEVGLGKTIEAGLIIKELLLrgdAKRV-----LILCP--ASLV--- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  82 efEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEdGGVMIIGYEMYRnlaqgRNVKSRKLkeifnkaLVDPGPDFV 161
Cdd:cd18011   60 --EQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEE-FPIVIVSLDLLK-----RSEERRGL-------LLSEEWDLV 124
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584059263 162 VCDEGHILKNEASAVS----KAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFR 222
Cdd:cd18011  125 VVDEAHKLRNSGGGKEtkryKLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
5-211 3.21e-09

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: 58.65  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263   5 LKPHQVDGVQFM-WdcccesvkKTKKSPgSGCILAHCMGLGKTLQVVSF------------------LHTVLLCE-KLDF 64
Cdd:cd18072    1 LLLHQKQALAWLlW--------RERQKP-RGGILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKdSTLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584059263  65 STA--LVVCPLNTALNWMNEFEKWQEGlkddEKLEVSELATVKRpQERSYMLQRWQedggVMIIGYemyrnlaqgrNVKS 142
Cdd:cd18072   72 PSAgtLVVCPASLVHQWKNEVESRVAS----NKLRVCLYHGPNR-ERIGEVLRDYD----IVITTY----------SLVA 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584059263 143 RKLKEIFNKALVDPGPDF----VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 211
Cdd:cd18072  133 KEIPTYKEESRSSPLFRIawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
559-611 1.04e-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: 44.23  E-value: 1.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 584059263 559 FIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQtKPVYVYRF 611
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILF 76
 
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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