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Conserved domains on  [gi|17136368|ref|NP_476661|]
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okra [Drosophila melanogaster]

Protein Classification

DEXHc_RAD54A and SF2_C_SNF domain-containing protein( domain architecture ID 13078943)

protein containing domains Rad54_N, DEXHc_RAD54A, and SF2_C_SNF

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
156-396 4.59e-158

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: 458.86  E-value: 4.59e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKR-GNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTK 234
Cdd:cd18067   1 LRPHQREGVKFLYRCVTGRRiRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEQF-SMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18067  81 WLGGRLQPLAIDGGSKKEIDRKLVQWaSQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCI 393
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                ...
gi 17136368 394 IRR 396
Cdd:cd18067 241 IRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
156-650 4.64e-123

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 384.58  E-value: 4.64e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECvegKRGNFNGCImADEMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:COG0553 242 LRPYQLEGAAWLLFL---RRLGLGGLL-ADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNWQRELAKF 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGrLLCLPMEGGTKENtiRALEQFSmtsarlGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:COG0553 313 APG-LRVLVLDGTRERA--KGANPFE------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAIlrgqntdstEQERQRAIEKTQELIGlvdQCIIR 395
Cdd:COG0553 384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRLLR---PFLLR 451
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 396 RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLksDQVRRSLADC-NEKASLTALADITTLKKICSHPDLIYEKLTARE 474
Cdd:COG0553 452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL--EYLRRELEGAeGIRRRGLILAALTRLRQICSHPALLLEEGAELS 529
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 475 KGfensqnvlpsnykpkdlnpelSGKFMLLDFMLAAIRAEGnDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKK 554
Cdd:COG0553 530 GR---------------------SAKLEALLELLEELLAEG-EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 555 RSKVVDRFNDpESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKI 634
Cdd:COG0553 588 RDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666
                       490
                ....*....|....*.
gi 17136368 635 LQRQTHKKSLSSTIID 650
Cdd:COG0553 667 LELLEEKRALAESVLG 682
Rad54_N super family cl07327
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
76-126 8.70e-04

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


The actual alignment was detected with superfamily member pfam08658:

Pssm-ID: 430137  Cd Length: 180  Bit Score: 41.09  E-value: 8.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368    76 IAKVLARKFKVPMDNYVP-DYGGKRV---LGVRRCIS--RRPLHDPMACNALVLFHP 126
Cdd:pfam08658  77 KETVFRKSFSVPLKNKKQgAYNPRRPpptLGTRRGAIfvPRPLHDPTGEFAIVLYDP 133
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
156-396 4.59e-158

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: 458.86  E-value: 4.59e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKR-GNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTK 234
Cdd:cd18067   1 LRPHQREGVKFLYRCVTGRRiRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEQF-SMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18067  81 WLGGRLQPLAIDGGSKKEIDRKLVQWaSQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCI 393
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                ...
gi 17136368 394 IRR 396
Cdd:cd18067 241 IRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
156-650 4.64e-123

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 384.58  E-value: 4.64e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECvegKRGNFNGCImADEMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:COG0553 242 LRPYQLEGAAWLLFL---RRLGLGGLL-ADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNWQRELAKF 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGrLLCLPMEGGTKENtiRALEQFSmtsarlGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:COG0553 313 APG-LRVLVLDGTRERA--KGANPFE------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAIlrgqntdstEQERQRAIEKTQELIGlvdQCIIR 395
Cdd:COG0553 384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRLLR---PFLLR 451
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 396 RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLksDQVRRSLADC-NEKASLTALADITTLKKICSHPDLIYEKLTARE 474
Cdd:COG0553 452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL--EYLRRELEGAeGIRRRGLILAALTRLRQICSHPALLLEEGAELS 529
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 475 KGfensqnvlpsnykpkdlnpelSGKFMLLDFMLAAIRAEGnDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKK 554
Cdd:COG0553 530 GR---------------------SAKLEALLELLEELLAEG-EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 555 RSKVVDRFNDpESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKI 634
Cdd:COG0553 588 RDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666
                       490
                ....*....|....*.
gi 17136368 635 LQRQTHKKSLSSTIID 650
Cdd:COG0553 667 LELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
159-466 4.36e-82

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: 263.78  E-value: 4.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   159 HQREGVRFMYECVEGKrgnFNGCIMADEMGLGKTLQCVTLVWTLLRQGPEckpTINKAIVVSPSSLVKNWEKEFTKWLHG 238
Cdd:pfam00176   1 YQIEGVNWMLSLENNL---GRGGILADEMGLGKTLQTISLLLYLKHVDKN---WGGPTLIVVPLSLLHNWMNEFERWVSP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   239 ---RLLCLpmeGGTKENTIRALEQFSMtsaRLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:pfam00176  75 palRVVVL---HGNKRPQERWKNDPNF---LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSteqerqraiekTQELIGLVDQCIIR 395
Cdd:pfam00176 149 LKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKG-----------VSRLHKLLKPFLLR 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136368   396 RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKS---DQVRRSLADCNEKASLtaLADITTLKKICSHPDLI 466
Cdd:pfam00176 218 RTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKkdlNAIKTGEGGREIKASL--LNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
156-680 2.52e-61

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 223.91  E-value: 2.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   156 LRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVWTLlrqgPECKPTINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYEN---GING-ILADEMGLGKTLQTISLLGYL----HEYRGITGPHMVVAPKSTLGNWMNEIRRF 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   236 lhgrllClPMeggtkentIRAL------EQFSMTSARLGTP----VLLISYETFRIYAEILCKYEVGMVICDEGHRLKNS 305
Cdd:PLN03142  242 ------C-PV--------LRAVkfhgnpEERAHQREELLVAgkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   306 DNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESailrgqntdSTEQERQraiEKTQEL 385
Cdd:PLN03142  307 NSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQL 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   386 IGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDqvrrsLADCNEKASLTALADITT-LKKICSHPD 464
Cdd:PLN03142  375 HKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKD-----LDVVNAGGERKRLLNIAMqLRKCCNHPY 449
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   465 LiyekltarekgFENSQNVLPsnYKPKDLNPELSGKFMLLDFMLAAIRaEGNDKVVLISNYTQTLDLFEQLARKRKYGFV 544
Cdd:PLN03142  450 L-----------FQGAEPGPP--YTTGEHLVENSGKMVLLDKLLPKLK-ERDSRVLIFSQMTRLLDILEDYLMYRGYQYC 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   545 RLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRL 624
Cdd:PLN03142  516 RIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRF 595
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368   625 VASGSIEEKILQRQTHKKSLSSTIIDNNESAE-KHFTRDDLKDLFTFDANILSDTHD 680
Cdd:PLN03142  596 CTEYTIEEKVIERAYKKLALDALVIQQGRLAEqKTVNKDELLQMVRYGAEMVFSSKD 652
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
497-625 8.28e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.38  E-value: 8.28e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 497 LSGKFMLLDFMLAAIRAEGnDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsFLFMLSS 576
Cdd:cd18793   9 VSGKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLST 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17136368 577 KAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLV 625
Cdd:cd18793  87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
156-346 4.19e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 4.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    156 LRPHQREGVRFMYEcvegkrgNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECkptinKAIVVSP-SSLVKNWEKEFTK 234
Cdd:smart00487   9 LRPYQKEAIEALLS-------GLRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    235 WL-HGRLLCLPMEGG-TKENTIRALEqfsmtsaRLGTPVLLISYETFRIYAE--ILCKYEVGMVICDEGHRLKNSDNltY 310
Cdd:smart00487  77 LGpSLGLKVVGLYGGdSKREQLRKLE-------SGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGF--G 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 17136368    311 QALMGL-----KTKRRVLLSGTP---IQNDLTEYYSLVNFVNPE 346
Cdd:smart00487 148 DQLEKLlkllpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
504-614 4.89e-25

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: 99.98  E-value: 4.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   504 LDFMLAAIRAEGNDKVVLISNYTQTLDLfEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsflFMLSSKAGGCGL 583
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 17136368   584 NLIGANRLFMFDPDWNPANDEQAMARVWRDG 614
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
530-614 3.69e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.26  E-value: 3.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    530 DLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsflFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMAR 609
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 17136368    610 VWRDG 614
Cdd:smart00490  78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
156-415 8.14e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.96  E-value: 8.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYEcvEGKRGNFNGCIMADeMGLGKTlqcVTLVWTLLRQGpeckpTINKAIVVSPS-SLVKNWEKEFTK 234
Cdd:COG1061  81 LRPYQQEALEALLA--ALERGGGRGLVVAP-TGTGKT---VLALALAAELL-----RGKRVLVLVPRrELLEQWAEELRR 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLclpmEGGTKENtiraleqfsmtsarlGTPVLLISYETFRIYAEI-LCKYEVGMVICDEGHRLKNSdnlTYQAL 313
Cdd:COG1061 150 FLGDPLA----GGGKKDS---------------DAPITVATYQSLARRAHLdELGDRFGLVIIDEAHHAGAP---SYRRI 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MG-LKTKRRVLLSGTPIQNDLTEYYsLVNFVNPemlgtaaVFKRNFESAILRG--------QNTDSTEQERQRAIEKTQE 384
Cdd:COG1061 208 LEaFPAAYRLGLTATPFRSDGREIL-LFLFDGI-------VYEYSLKEAIEDGylappeyyGIRVDLTDERAEYDALSER 279
                       250       260       270
                ....*....|....*....|....*....|....
gi 17136368 385 LIGLVDQC---IIRRTNQILTKYLPVKFEMVICA 415
Cdd:COG1061 280 LREALAADaerKDKILRELLREHPDDRKTLVFCS 313
DpdE NF041062
protein DpdE;
184-627 2.36e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 61.14  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   184 ADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEftkwLHGRLlclpmeggtkentirALEQFsmt 263
Cdd:NF041062  176 ADEVGLGKTIEAGLVIRQHLLDNPD-----ARVLVLVPDALVRQWRRE----LRDKF---------------FLDDF--- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   264 sarLGTPVLLISYETFRIYAEILCKYevGMVICDEGHRL-------KNSDNLTYQALMGL--KTKRRVLLSGTPIQNDLT 334
Cdd:NF041062  229 ---PGARVRVLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLLLLSATPVLGNEE 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   335 EYYSLVNFVNPEM--LGTAAVFKRN-----------------FESAILRGQ---------------------------NT 368
Cdd:NF041062  304 TFLALLHLLDPDLypLDDLEAFRERleereelgrlvlgldpdNPNFLLRQAldelralfpedeelqelaeellplldeFD 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   369 DSTEQERQRAIEKTQELIG---LVDQCIIR--RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCN- 442
Cdd:NF041062  384 DEEPEERARAVSALRAHISetyRLHRRMIRnrRSSVLGADYLVPGRAGPRVLVWESPAREAADEALEDWREEAALLDAEs 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   443 EKASLTALA-DITTLKKICSHPDLIYEKLTAREKG-------------FENSQNVLPSNYKPKDLNPELSGkfMLLDFMl 508
Cdd:NF041062  464 DPAARAAYArALAWLVARLGGPDDLAALLRWRLRGdaasadlagerelLEALIAALEDEAKDADLLAALAD--WLLPLL- 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   509 aairaEGNDKVVLISNYTQTLD-LFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSkaGGCGLNLIG 587
Cdd:NF041062  541 -----RGSGKAVVFCGDGSLADhLAAALARLGAGSVERHLSGQGADQAERAVRAFRQDPSARVLVCDRS--GEEGLNLQG 613
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 17136368   588 ANRLFMFDPDWNPANDEQAMARV---WRDGQKKPCYIYRLVAS 627
Cdd:NF041062  614 ADRLVHLDLPWSPNRLEQRIGRLdryASLRGGRPVESYVLAPS 656
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
76-126 8.70e-04

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 41.09  E-value: 8.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368    76 IAKVLARKFKVPMDNYVP-DYGGKRV---LGVRRCIS--RRPLHDPMACNALVLFHP 126
Cdd:pfam08658  77 KETVFRKSFSVPLKNKKQgAYNPRRPpptLGTRRGAIfvPRPLHDPTGEFAIVLYDP 133
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
156-396 4.59e-158

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: 458.86  E-value: 4.59e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKR-GNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTK 234
Cdd:cd18067   1 LRPHQREGVKFLYRCVTGRRiRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEQF-SMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18067  81 WLGGRLQPLAIDGGSKKEIDRKLVQWaSQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCI 393
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                ...
gi 17136368 394 IRR 396
Cdd:cd18067 241 IRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
156-650 4.64e-123

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 384.58  E-value: 4.64e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECvegKRGNFNGCImADEMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:COG0553 242 LRPYQLEGAAWLLFL---RRLGLGGLL-ADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNWQRELAKF 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGrLLCLPMEGGTKENtiRALEQFSmtsarlGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:COG0553 313 APG-LRVLVLDGTRERA--KGANPFE------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAIlrgqntdstEQERQRAIEKTQELIGlvdQCIIR 395
Cdd:COG0553 384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRLLR---PFLLR 451
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 396 RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLksDQVRRSLADC-NEKASLTALADITTLKKICSHPDLIYEKLTARE 474
Cdd:COG0553 452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL--EYLRRELEGAeGIRRRGLILAALTRLRQICSHPALLLEEGAELS 529
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 475 KGfensqnvlpsnykpkdlnpelSGKFMLLDFMLAAIRAEGnDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKK 554
Cdd:COG0553 530 GR---------------------SAKLEALLELLEELLAEG-EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 555 RSKVVDRFNDpESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLVASGSIEEKI 634
Cdd:COG0553 588 RDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666
                       490
                ....*....|....*.
gi 17136368 635 LQRQTHKKSLSSTIID 650
Cdd:COG0553 667 LELLEEKRALAESVLG 682
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
156-396 1.45e-113

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: 344.27  E-value: 1.45e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRG-NFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTK 234
Cdd:cd18004   1 LRPHQREGVQFLYDCLTGRRGyGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEQFSMTSARlgtPVLLISYETFRIYAE-ILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18004  81 WLGLRRIKVVTADGNAKDVKASLDFFSSASTY---PVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVDQCI 393
Cdd:cd18004 158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFI 237

                ...
gi 17136368 394 IRR 396
Cdd:cd18004 238 LRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
159-466 4.36e-82

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: 263.78  E-value: 4.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   159 HQREGVRFMYECVEGKrgnFNGCIMADEMGLGKTLQCVTLVWTLLRQGPEckpTINKAIVVSPSSLVKNWEKEFTKWLHG 238
Cdd:pfam00176   1 YQIEGVNWMLSLENNL---GRGGILADEMGLGKTLQTISLLLYLKHVDKN---WGGPTLIVVPLSLLHNWMNEFERWVSP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   239 ---RLLCLpmeGGTKENTIRALEQFSMtsaRLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:pfam00176  75 palRVVVL---HGNKRPQERWKNDPNF---LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSteqerqraiekTQELIGLVDQCIIR 395
Cdd:pfam00176 149 LKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKG-----------VSRLHKLLKPFLLR 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136368   396 RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKS---DQVRRSLADCNEKASLtaLADITTLKKICSHPDLI 466
Cdd:pfam00176 218 RTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKkdlNAIKTGEGGREIKASL--LNILMRLRKICNHPGLI 289
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
156-396 4.33e-75

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: 243.21  E-value: 4.33e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGNFN-GCIMADEMGLGKTLQCVTLVWTLLRQGPE-CKPTINKAIVVSPSSLVKNWEKEFT 233
Cdd:cd18066   1 LRPHQREGIEFLYECVMGMRVNERfGAILADEMGLGKTLQCISLIWTLLRQGPYgGKPVIKRALIVTPGSLVKNWKKEFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 234 KWLhgrllclpmegGTKENTIRALEQFSMTSARLGTP---VLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTY 310
Cdd:cd18066  81 KWL-----------GSERIKVFTVDQDHKVEEFIASPlysVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLVD 390
Cdd:cd18066 150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTG 229

                ....*.
gi 17136368 391 QCIIRR 396
Cdd:cd18066 230 LFILRR 235
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
156-381 1.51e-64

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: 215.23  E-value: 1.51e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYE-CVEGKRGNFN--GCIMADEMGLGKTLQCVTLVWTLLRqgpeCKPTINKAIVVSPSSLVKNWEKEF 232
Cdd:cd18007   1 LKPHQVEGVRFLWSnLVGTDVGSDEggGCILAHTMGLGKTLQVITFLHTYLA----AAPRRSRPLVLCPASTLYNWEDEF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 233 TKWLHGRLLCLPME-----GGTKENTIRALEQFSmtsARLGtpVLLISYETFR---------------IYAEILCKYeVG 292
Cdd:cd18007  77 KKWLPPDLRPLLVLvslsaSKRADARLRKINKWH---KEGG--VLLIGYELFRnlasnattdprlkqeFIAALLDPG-PD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 293 MVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTE 372
Cdd:cd18007 151 LLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTE 230

                ....*....
gi 17136368 373 QERQRAIEK 381
Cdd:cd18007 231 EDVRLMLKR 239
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
156-345 7.69e-63

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: 208.57  E-value: 7.69e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEgkrgNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTKW 235
Cdd:cd17919   1 LRPYQLEGLNFLLELYE----NGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVL----VVCPLSVLENWEREFEKW 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHG-RLLCLPmegGTKENTIRALEQFSMTSArlgtPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALM 314
Cdd:cd17919  73 TPDlRVVVYH---GSQRERAQIRAKEKLDKF----DVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALK 145
                       170       180       190
                ....*....|....*....|....*....|.
gi 17136368 315 GLKTKRRVLLSGTPIQNDLTEYYSLVNFVNP 345
Cdd:cd17919 146 ALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
156-680 2.52e-61

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 223.91  E-value: 2.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   156 LRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVWTLlrqgPECKPTINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYEN---GING-ILADEMGLGKTLQTISLLGYL----HEYRGITGPHMVVAPKSTLGNWMNEIRRF 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   236 lhgrllClPMeggtkentIRAL------EQFSMTSARLGTP----VLLISYETFRIYAEILCKYEVGMVICDEGHRLKNS 305
Cdd:PLN03142  242 ------C-PV--------LRAVkfhgnpEERAHQREELLVAgkfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   306 DNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESailrgqntdSTEQERQraiEKTQEL 385
Cdd:PLN03142  307 NSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQL 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   386 IGLVDQCIIRRTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDqvrrsLADCNEKASLTALADITT-LKKICSHPD 464
Cdd:PLN03142  375 HKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKD-----LDVVNAGGERKRLLNIAMqLRKCCNHPY 449
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   465 LiyekltarekgFENSQNVLPsnYKPKDLNPELSGKFMLLDFMLAAIRaEGNDKVVLISNYTQTLDLFEQLARKRKYGFV 544
Cdd:PLN03142  450 L-----------FQGAEPGPP--YTTGEHLVENSGKMVLLDKLLPKLK-ERDSRVLIFSQMTRLLDILEDYLMYRGYQYC 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   545 RLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRL 624
Cdd:PLN03142  516 RIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRF 595
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368   625 VASGSIEEKILQRQTHKKSLSSTIIDNNESAE-KHFTRDDLKDLFTFDANILSDTHD 680
Cdd:PLN03142  596 CTEYTIEEKVIERAYKKLALDALVIQQGRLAEqKTVNKDELLQMVRYGAEMVFSSKD 652
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
156-396 5.93e-59

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: 200.30  E-value: 5.93e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGnfngCIMADEMGLGKTLQCVTLVWTLL------------RQGPECKPTINKA----IVV 219
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRG----GILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennRPRFKKKPPASSAkkpvLIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 220 SPSSLVKNWEKEFTKWLHGRLLCLpmEGGTKENTIraleQFSMTSARLgtPVLLISYETFRIYAEILCKYEVGMVICDEG 299
Cdd:cd18005  77 APLSVLYNWKDELDTWGHFEVGVY--HGSRKDDEL----EGRLKAGRL--EVVVTTYDTLRRCIDSLNSINWSAVIADEA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 300 HRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAI 379
Cdd:cd18005 149 HRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGR 228
                       250
                ....*....|....*..
gi 17136368 380 EKTQELIGLVDQCIIRR 396
Cdd:cd18005 229 KRKQELAVKLSKFFLRR 245
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
497-625 8.28e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.38  E-value: 8.28e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 497 LSGKFMLLDFMLAAIRAEGnDKVVLISNYTQTLDLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsFLFMLSS 576
Cdd:cd18793   9 VSGKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLST 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17136368 577 KAGGCGLNLIGANRLFMFDPDWNPANDEQAMARVWRDGQKKPCYIYRLV 625
Cdd:cd18793  87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
156-374 7.31e-50

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: 175.46  E-value: 7.31e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECV-----EGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQgpECKPTINKAIVVSPSSLVKNWEK 230
Cdd:cd18068   1 LKPHQVDGVQFMWDCCceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLC--EKLENFSRVLVVCPLNTVLNWLN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWlhgrllclpMEGGTKENTIRALE----------QFSMTSARLGTPVLLISYETFRIYA------------EILCK 288
Cdd:cd18068  79 EFEKW---------QEGLKDEEKIEVNElatykrpqerSYKLQRWQEEGGVMIIGYDMYRILAqernvksreklkEIFNK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 289 YEVG----MVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILR 364
Cdd:cd18068 150 ALVDpgpdFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQN 229
                       250
                ....*....|
gi 17136368 365 GQNTDSTEQE 374
Cdd:cd18068 230 GQCADSTLVD 239
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
156-377 1.67e-47

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: 168.07  E-value: 1.67e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGNFN-----GCIMADEMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKNWEK 230
Cdd:cd18069   1 LKPHQIGGIRFLYDNIIESLERYKgssgfGCILAHSMGLGKTLQVISFLDVLLRHTG-----AKTVLAIVPVNTLQNWLS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWLhgrllclPMEGGTKENTIRALEQFSM------TSARLGT--------PVLLISYETFRIyaeilcKYEVGMVIC 296
Cdd:cd18069  76 EFNKWL-------PPPEALPNVRPRPFKVFILndehktTAARAKViedwvkdgGVLLMGYEMFRL------RPGPDVVIC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 297 DEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQE-- 374
Cdd:cd18069 143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDvk 222

                ....*
gi 17136368 375 --RQR 377
Cdd:cd18069 223 lmRYR 227
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
156-396 1.74e-43

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: 157.15  E-value: 1.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGNfngcIMADEMGLGKTLQCVTLVWTLLRQGpeckpTINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGGKGG----ILADDMGLGKTVQICAFLSGMFDSG-----LIKSVLVVMPTSLIPHWVKEFAKW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGrLLCLPMEGGTKENTIRALEqfsmtSARLGTPVLLISYETFRIYAEILCKYEVG-----MVICDEGHRLKNSDNLTY 310
Cdd:cd18001  72 TPG-LRVKVFHGTSKKERERNLE-----RIQRGGGVLLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNSKTKSA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFV-NPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLV 389
Cdd:cd18001 146 KSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQII 225

                ....*..
gi 17136368 390 DQCIIRR 396
Cdd:cd18001 226 KPYFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
152-377 7.78e-43

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: 154.65  E-value: 7.78e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 152 LSNILRPHQREGVRFMYECvegKRGNFNGCiMADEMGLGKTLQCVTLVWTLLRQGPEcKPtinkAIVVSPSSLVKNWEKE 231
Cdd:cd18012   1 LKATLRPYQKEGFNWLSFL---RHYGLGGI-LADDMGLGKTLQTLALLLSRKEEGRK-GP----SLVVAPTSLIYNWEEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 232 FTKWLHGrLLCLPMEG-GTKENTIRALEQFSmtsarlgtpVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTY 310
Cdd:cd18012  72 AAKFAPE-LKVLVIHGtKRKREKLRALEDYD---------LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTA 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQR 377
Cdd:cd18012 142 KAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKL 208
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
156-358 3.00e-38

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: 142.00  E-value: 3.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGnfngCIMADEMGLGKTLQCVTLVWTLLRQGPECKPtinkAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRN----CILADEMGLGKTIQSIAFLEHLYQVEGIRGP----FLVIAPLSTIPNWQREFETW 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGRLLCLPMEGGTKEnTIRALEQFSMTSARLGTP------VLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd17995  73 TDMNVVVYHGSGESRQ-IIQQYEMYFKDAQGRKKKgvykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKL 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17136368 310 YQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd17995 152 LQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
156-396 1.10e-35

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: 135.17  E-value: 1.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVR---FMyecvegKRGNFNGcIMADEMGLGKTLQCVTLVWT---LLRQGPECKPtiNKAIVVSPSSLVKNWE 229
Cdd:cd17999   1 LRPYQQEGINwlaFL------NKYNLHG-ILCDDMGLGKTLQTLCILASdhhKRANSFNSEN--LPSLVVCPPTLVGHWV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 230 KEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSarlgtpVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd17999  72 AEIKKYFPNAFLKPLAYVGPPQERRRLREQGEKHN------VIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 310 YQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQERQRAIEKTQELIGLV 389
Cdd:cd17999 146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQV 225

                ....*..
gi 17136368 390 DQCIIRR 396
Cdd:cd17999 226 LPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
156-345 1.67e-35

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: 133.22  E-value: 1.67e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGNfngcIMADEMGLGKTLQCVTLVWTL----LRQGPeckptinkAIVVSPSSLVKNWEKE 231
Cdd:cd18000   1 LFKYQQTGVQWLWELHCQRVGG----ILGDEMGLGKTIQIIAFLAALhhskLGLGP--------SLIVCPATVLKQWVKE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 232 FTKW---LHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTP--VLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSD 306
Cdd:cd18000  69 FHRWwppFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVVGDggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPD 148
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 17136368 307 NLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNP 345
Cdd:cd18000 149 AEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
155-405 8.85e-34

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: 129.81  E-value: 8.85e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 155 ILRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVwTLLRQ----GPeckptinkAIVVSPSSLVKNWEK 230
Cdd:cd18009   3 VMRPYQLEGMEWLRMLWEN---GING-ILADEMGLGKTIQTIALL-AHLRErgvwGP--------FLVIAPLSTLPNWVN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWL--------HGrllclpmeggTKE--NTIRALEQFSMTSARlGTPVLLISYETFRIYAEILCKYEVGMVICDEGH 300
Cdd:cd18009  70 EFARFTpsvpvllyHG----------TKEerERLRKKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGH 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 301 RLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFE-SAILRGQNTDSTEQERQRai 379
Cdd:cd18009 139 RLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfSSLSDNAADISNLSEERE-- 216
                       250       260
                ....*....|....*....|....*.
gi 17136368 380 ektqeliglvdQCIIRRTNQILTKYL 405
Cdd:cd18009 217 -----------QNIVHMLHAILKPFL 231
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
156-353 4.27e-33

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: 127.17  E-value: 4.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECvegkRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTKW 235
Cdd:cd18006   1 LRPYQLEGVNWLLQC----RAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFL----VLCPLSVLDNWKEELNRF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LhGRLLCLPMEGGTKEntiRALEQFSMTSArLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMG 315
Cdd:cd18006  73 A-PDLSVITYMGDKEK---RLDLQQDIKST-NRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSE 147
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17136368 316 LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAV 353
Cdd:cd18006 148 FSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKL 185
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
156-396 5.35e-33

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: 127.40  E-value: 5.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYecvegkrgnFNGCIMADEMGLGKTLQCVTLV-----------------WTLLRQGPECKPTinkaIV 218
Cdd:cd18008   1 LLPYQKQGLAWML---------PRGGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTT----LI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 219 VSPSSLVKNWEKEF-TKWLHGRLLCLPMEGGTKENTIRALEQFSmtsarlgtpVLLISYETFRI-YAEILCKYEVGM--- 293
Cdd:cd18008  68 VVPLSLLSQWKDEIeKHTKPGSLKVYVYHGSKRIKSIEELSDYD---------IVITTYGTLASeFPKNKKGGGRDSkek 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 294 ------------VICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFesa 361
Cdd:cd18008 139 easplhrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDI--- 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 17136368 362 ilrgqnTDSTEQERQRAIEKTQELIGlvdQCIIRR 396
Cdd:cd18008 216 ------SKPFSKNDRKALERLQALLK---PILLRR 241
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
156-346 2.31e-31

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: 122.08  E-value: 2.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFM-YECVEGkrgnfNGCIMADEMGLGKTLQCVTLVWTLLRQ----GPeckptinkAIVVSPSSLVKNWEK 230
Cdd:cd17993   2 LRDYQLTGLNWLaHSWCKG-----NNGILADEMGLGKTVQTISFLSYLFHSqqqyGP--------FLVVVPLSTMPAWQR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTY 310
Cdd:cd17993  69 EFAKWAPDMNVIVYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLY 148
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPE 346
Cdd:cd17993 149 EALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG 184
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
156-373 2.10e-30

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: 119.35  E-value: 2.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKrgnFNGcIMADEMGLGKTLQCVTLVwTLLRQ-----GPEckptinkaIVVSPSSLVKNWEK 230
Cdd:cd17997   4 MRDYQIRGLNWLISLFENG---ING-ILADEMGLGKTLQTISLL-GYLKHykninGPH--------LIIVPKSTLDNWMR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWLHG-RLLCLPmegGTKENTIRALEQFSMTSArlgTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd17997  71 EFKRWCPSlRVVVLI---GDKEERADIIRDVLLPGK---FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKL 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136368 310 YQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQNTDSTEQ 373
Cdd:cd17997 145 SQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQR 208
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
156-346 1.61e-29

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: 115.95  E-value: 1.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRF---MYEcvegKRGNfngCIMADEMGLGKTLQCVTLVWTLL---RQGPEckptinkaIVVSPSSLVKNWE 229
Cdd:cd17998   1 LKDYQLIGLNWlnlLYQ----KKLS---GILADEMGLGKTIQVIAFLAYLKeigIPGPH--------LVVVPSSTLDNWL 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 230 KEFTKWLHGrLLCLPMEGGTKEntiRALEQFSMTSARLGTPVLLISYE---TFRIYAEILCKYEVGMVICDEGHRLKNSD 306
Cdd:cd17998  66 REFKRWCPS-LKVEPYYGSQEE---RKHLRYDILKGLEDFDVIVTTYNlatSNPDDRSFFKRLKLNYVVYDEGHMLKNMT 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17136368 307 NLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPE 346
Cdd:cd17998 142 SERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
156-405 1.99e-29

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: 116.68  E-value: 1.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMyecVEGKRGNFNGcIMADEMGLGKTLQCVTL---------VWtllrqGPEckptinkaIVVSPSSLVK 226
Cdd:cd18003   1 LREYQHIGLDWL---ATLYEKNLNG-ILADEMGLGKTIQTIALlahlacekgNW-----GPH--------LIVVPTSVML 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 227 NWEKEFTKWLHGrLLCLPMEGGTKEntiRALEqfsmtsaRLG--TP----VLLISYETFRIYAEILCKYEVGMVICDEGH 300
Cdd:cd18003  64 NWEMEFKRWCPG-FKILTYYGSAKE---RKLK-------RQGwmKPnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAH 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 301 RLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFeSAILRGqntdsteqerqrAIE 380
Cdd:cd18003 133 NIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWF-SNPLTA------------MSE 199
                       250       260
                ....*....|....*....|....*
gi 17136368 381 KTQEliglVDQCIIRRTNQILTKYL 405
Cdd:cd18003 200 GSQE----ENEELVRRLHKVLRPFL 220
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
156-405 3.13e-29

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: 116.31  E-value: 3.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMyecVEGKRGNFNGcIMADEMGLGKTLQCVTLVWTLLrqgpECKPTINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd17996   4 LKEYQLKGLQWM---VSLYNNNLNG-ILADEMGLGKTIQTISLITYLM----EKKKNNGPYLVIVPLSTLSNWVSEFEKW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LhGRLLCL-----PMEGGTKENTIRAlEQFSmtsarlgtpVLLISYEtFRIYAE-ILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd17996  76 A-PSVSKIvykgtPDVRKKLQSQIRA-GKFN---------VLLTTYE-YIIKDKpLLSKIKWKYMIIDEGHRMKNAQSKL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 310 YQALMG-LKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFES--AILRGQNTDSTEQERQraiektqeLI 386
Cdd:cd17996 144 TQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfANTGEQVKIELNEEET--------LL 215
                       250
                ....*....|....*....
gi 17136368 387 glvdqcIIRRTNQILTKYL 405
Cdd:cd17996 216 ------IIRRLHKVLRPFL 228
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
156-380 8.14e-29

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: 115.49  E-value: 8.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYE--CvegkrgNFNGCIMADEMGLGKTLQCVTLVWTLLRQ----GPeckptinkAIVVSPSSLVKNWE 229
Cdd:cd18054  21 LRDYQLEGLNWLAHswC------KNNSVILADEMGLGKTIQTISFLSYLFHQhqlyGP--------FLLVVPLSTLTSWQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 230 KEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd18054  87 REFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136368 310 YQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGtaavFKRNFESAilRGQNTDSTEQERQRAIE 380
Cdd:cd18054 167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFE----FWEDFEED--HGKGRENGYQSLHKVLE 231
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
156-356 7.82e-28

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: 111.91  E-value: 7.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYEcvegkrgnFNG-CIMADEMGLGKTLQCVTLVWTLLRQGPeckptinkAIVVSPSSLVKNWEKEFTK 234
Cdd:cd18010   1 LLPFQREGVCFALR--------RGGrVLIADEMGLGKTVQAIAIAAYYREEWP--------LLIVCPSSLRLTWADEIER 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGrllcLPMEGgtkENTIR-ALEQFSMTSARlgtpVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18010  65 WLPS----LPPDD---IQVIVkSKDGLRDGDAK----VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAA 133
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17136368 314 MGL--KTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKR 356
Cdd:cd18010 134 LPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGR 178
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
156-359 2.11e-27

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: 109.84  E-value: 2.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGV---RFMYecvegkrGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGpECKPTInkaIVVSPSSLVKNWEKEF 232
Cdd:cd17994   1 LHPYQLEGLnwlRFSW-------AQGTDTILADEMGLGKTIQTIVFLYSLYKEG-HSKGPF---LVSAPLSTIINWEREF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 233 TKWlhgrllclpmeggtkentirALEQFSMTSArlGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQA 312
Cdd:cd17994  70 EMW--------------------APDFYVVTYV--GDHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRI 127
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17136368 313 LMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFE 359
Cdd:cd17994 128 LNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA 174
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
156-358 1.35e-26

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


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 109.00  E-value: 1.35e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFM-YECVEGkrgnfNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTK 234
Cdd:cd18057   1 LHPYQLEGLNWLrFSWAQG-----TDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYL----VSAPLSTIINWEREFEM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WL------------HGRLLCLPMEGGTKENTIRALEQ-FSMT-SARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGH 300
Cdd:cd18057  72 WApdfyvvtytgdkESRSVIRENEFSFEDNAIRSGKKvFRMKkEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAH 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136368 301 RLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18057 152 RLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
156-358 4.46e-26

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 107.46  E-value: 4.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFM-YECVEGkrgnfNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTK 234
Cdd:cd18056   1 LHPYQLEGLNWLrFSWAQG-----TDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFL----VSAPLSTIINWEREFEM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WL------------HGRLLCLPMEGGTKENTIRALEQFS--MTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGH 300
Cdd:cd18056  72 WApdmyvvtyvgdkDSRAIIRENEFSFEDNAIRGGKKASrmKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAH 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136368 301 RLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18056 152 RLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF 209
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
156-355 9.38e-26

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: 106.67  E-value: 9.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFM-YECVEGkrgnfNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTK 234
Cdd:cd18053  21 LRDYQLNGLNWLaHSWCKG-----NSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFL----LVVPLSTLTSWQREIQT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALM 314
Cdd:cd18053  92 WAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLI 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17136368 315 GLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFK 355
Cdd:cd18053 172 DFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFE 212
DEXDc smart00487
DEAD-like helicases superfamily;
156-346 4.19e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.73  E-value: 4.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    156 LRPHQREGVRFMYEcvegkrgNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECkptinKAIVVSP-SSLVKNWEKEFTK 234
Cdd:smart00487   9 LRPYQKEAIEALLS-------GLRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    235 WL-HGRLLCLPMEGG-TKENTIRALEqfsmtsaRLGTPVLLISYETFRIYAE--ILCKYEVGMVICDEGHRLKNSDNltY 310
Cdd:smart00487  77 LGpSLGLKVVGLYGGdSKREQLRKLE-------SGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGF--G 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 17136368    311 QALMGL-----KTKRRVLLSGTP---IQNDLTEYYSLVNFVNPE 346
Cdd:smart00487 148 DQLEKLlkllpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
504-614 4.89e-25

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: 99.98  E-value: 4.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   504 LDFMLAAIRAEGNDKVVLISNYTQTLDLfEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsflFMLSSKAGGCGL 583
Cdd:pfam00271   3 LEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 17136368   584 NLIGANRLFMFDPDWNPANDEQAMARVWRDG 614
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
156-381 3.28e-24

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: 101.81  E-value: 3.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVWTLlrqgPECKPTINKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18002   1 LKEYQLKGLNWLANLYEQ---GING-ILADEMGLGKTVQSIAVLAHL----AEEHNIWGPFLVIAPASTLHNWQQEISRF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LhGRLLCLPMEGGTKENTI--RALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQAL 313
Cdd:cd18002  73 V-PQFKVLPYWGNPKDRKVlrKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136368 314 MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGT----AAVFKRNFESAILRGQNTDSTEQERQRAIEK 381
Cdd:cd18002 152 LSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDShdefNEWFSKDIESHAENKTGLNEHQLKRLHMILK 223
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
182-358 1.30e-23

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: 100.09  E-value: 1.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 182 IMADEMGLGKTLQCVTLVWTLLRQGPECKPTInkaiVVSPSSLVKNWEKEFTKWL------------HGRLLCLPMEGGT 249
Cdd:cd18055  23 ILADEMGLGKTIQTIVFLYSLYKEGHTKGPFL----VSAPLSTIINWEREFQMWApdfyvvtytgdkDSRAIIRENEFSF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 250 KENTIRALEQ-FSMTS-ARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGT 327
Cdd:cd18055  99 DDNAVKGGKKaFKMKReAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGT 178
                       170       180       190
                ....*....|....*....|....*....|.
gi 17136368 328 PIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18055 179 PLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
151-405 1.43e-23

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: 100.52  E-value: 1.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 151 LLSNILRPHQREGVRFMyecVEGKRGNFNGcIMADEMGLGKTLQCVTLVWTLLrqgpECKPTINKAIVVSPSSLVKNWEK 230
Cdd:cd18063  19 LINGTLKHYQLQGLEWM---VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EHKRLNGPYLIIVPLSTLSNWTY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWLhgrllclPMEGGTKENTIRALEQFSMTSARLGT-PVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd18063  91 EFDKWA-------PSVVKISYKGTPAMRRSLVPQLRSGKfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 310 YQAL-MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAI-LRGQNTDSTEQErqraiektqelig 387
Cdd:cd18063 164 TQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEE------------- 230
                       250
                ....*....|....*...
gi 17136368 388 lvDQCIIRRTNQILTKYL 405
Cdd:cd18063 231 --TILIIRRLHKVLRPFL 246
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
156-358 6.28e-23

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: 97.82  E-value: 6.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYecveGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18060   1 LREYQLEGVNWLL----FNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIH-----GPFLVIAPLSTITNWEREFNTW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 -------LHGRLLCLPMeggtkentIRALEQFSMTSARLGTP------VLLISYETFRIYAEILCKYEVGMVICDEGHRL 302
Cdd:cd18060  72 temntivYHGSLASRQM--------IQQYEMYCKDSRGRLIPgaykfdALITTFEMILSDCPELREIEWRCVIIDEAHRL 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17136368 303 KNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18060 144 KNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
156-358 1.36e-22

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: 97.03  E-value: 1.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYecveGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18058   1 LREYQLEGMNWLL----FNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIR-----GPFLIIAPLSTITNWEREFRTW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 -------LHGRLLCLPMEggTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNL 308
Cdd:cd18058  72 temnaivYHGSQISRQMI--QQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17136368 309 TYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18058 150 LLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
151-405 5.28e-22

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: 96.27  E-value: 5.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 151 LLSNILRPHQREGVRFMyecVEGKRGNFNGcIMADEMGLGKTLQCVTLVWTLLrqgpECKPTINKAIVVSPSSLVKNWEK 230
Cdd:cd18062  19 LVNGVLKQYQIKGLEWL---VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EHKRINGPFLIIVPLSTLSNWVY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 231 EFTKWlhgrllclpmeggtKENTIRALEQFSMTSARLGTP--------VLLISYETFRIYAEILCKYEVGMVICDEGHRL 302
Cdd:cd18062  91 EFDKW--------------APSVVKVSYKGSPAARRAFVPqlrsgkfnVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 303 KNSDNLTYQAL-MGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAI-LRGQNTDSTEQErqraie 380
Cdd:cd18062 157 KNHHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEE------ 230
                       250       260
                ....*....|....*....|....*
gi 17136368 381 ktqeliglvDQCIIRRTNQILTKYL 405
Cdd:cd18062 231 ---------TILIIRRLHKVLRPFL 246
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
156-346 1.89e-21

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: 93.12  E-value: 1.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFmyeCVEGKRgnfNGCIMADEMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKNWEKE-FTK 234
Cdd:cd18011   1 PLPHQIDAVLR---ALRKPP---VRLLLADEVGLGKTIEAGLIIKELLLRGD-----AKRVLILCPASLVEQWQDElQDK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPmeggtkeNTIRALEQfSMTSARLGTPVLLISYETFR---IYAEILCKYEVGMVICDEGHRLKNSDNLTYQ 311
Cdd:cd18011  70 FGLPFLILDR-------ETAAQLRR-LIGNPFEEFPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGGGKET 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17136368 312 ALMGL------KTKRRVLLSGTPIQNDLTEYYSLVNFVNPE 346
Cdd:cd18011 142 KRYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPG 182
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
156-396 4.86e-21

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: 92.40  E-value: 4.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYecveGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18059   1 LREYQLEGVNWLL----FNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIH-----GPFLVIAPLSTIPNWEREFRTW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGRLLCLPMEGGTKEnTIRALEQ-FSMTSARL-----GTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLT 309
Cdd:cd18059  72 TELNVVVYHGSQASRR-TIQLYEMyFKDPQGRVikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 310 YQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAilrgqntdSTEqerqraiEKTQELIGLV 389
Cdd:cd18059 151 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDL--------KTE-------EQVQKLQAIL 215

                ....*..
gi 17136368 390 DQCIIRR 396
Cdd:cd18059 216 KPMMLRR 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
156-360 2.44e-20

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: 90.88  E-value: 2.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVWTLLR----QGPEckptinkaIVVSPSSLVKNWEKE 231
Cdd:cd18064  16 LRDYQVRGLNWLISLYEN---GING-ILADEMGLGKTLQTISLLGYMKHyrniPGPH--------MVLVPKSTLHNWMAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 232 FTKWLHG-RLLCLPmegGTKENTIRALEQFSMTSArlgTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTY 310
Cdd:cd18064  84 FKRWVPTlRAVCLI---GDKDQRAAFVRDVLLPGE---WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFES 360
Cdd:cd18064 158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT 207
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
156-358 3.04e-20

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: 90.06  E-value: 3.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGnfngCIMADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEFTKW 235
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRN----CILADEMGLGKTIQSITFLYEILLTGIR-----GPFLIIAPLSTIANWEREFRTW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 -------LHGRLLCLPMeggtkentiraLEQFSMTSARLGTPVLLISYEtfriYAEILCKYEVGM-------------VI 295
Cdd:cd18061  72 tdlnvvvYHGSLISRQM-----------IQQYEMYFRDSQGRIIRGAYR----FQAIITTFEMILggcpelnaidwrcVI 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136368 296 CDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNF 358
Cdd:cd18061 137 IDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
156-381 5.39e-20

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: 89.69  E-value: 5.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGkrgNFNGcIMADEMGLGKTLQCVTLVWTLLR----QGPEckptinkaIVVSPSSLVKNWEKE 231
Cdd:cd18065  16 LRDYQVRGLNWMISLYEN---GVNG-ILADEMGLGKTLQTIALLGYLKHyrniPGPH--------MVLVPKSTLHNWMNE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 232 FTKWLHG-RLLCLPMEGGTKENTIRALeqfsMTSARLGtpVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTY 310
Cdd:cd18065  84 FKRWVPSlRAVCLIGDKDARAAFIRDV----MMPGEWD--VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136368 311 QALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGqntDSTEQERQRAIEK 381
Cdd:cd18065 158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG---DQKLVERLHAVLK 225
HELICc smart00490
helicase superfamily c-terminal domain;
530-614 3.69e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.26  E-value: 3.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368    530 DLFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDsflFMLSSKAGGCGLNLIGANRLFMFDPDWNPANDEQAMAR 609
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 17136368    610 VWRDG 614
Cdd:smart00490  78 AGRAG 82
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
180-382 5.15e-17

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: 81.36  E-value: 5.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 180 GCIMADEMGLGKTLQCVTLVWTllrqgpeckptiNKAIVVSPSSLVKNWEKEFTKWLH-GRLLCLPMEGGTKENTIRALE 258
Cdd:cd18071  50 GGILADDMGLGKTLTTISLILA------------NFTLIVCPLSVLSNWETQFEEHVKpGQLKVYTYHGGERNRDPKLLS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 259 QFSmtsarlgtpVLLISYETFRIY-----AEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDL 333
Cdd:cd18071 118 KYD---------IVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSP 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17136368 334 TEYYSLVNFVNPEMLGTAAVFKRNFESAILRGqntDSTEQERQRAIEKT 382
Cdd:cd18071 189 KDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMG---DPTGLKRLQVLMKQ 234
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
156-367 1.44e-14

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: 74.05  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMyecVEGKRGNFNGCIMADEMGLGKTLQCVTLVW--------------TLLRQGPECK-----PTINkA 216
Cdd:cd18072   1 LLLHQKQALAWL---LWRERQKPRGGILADDMGLGKTLTMIALILaqkntqnrkeeekeKALTEWESKKdstlvPSAG-T 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 217 IVVSPSSLVKNWEKEFTKWLH-GRLLCLPMEGGTKENTIRALEQFSM--TSARLGTPVLLISYETFRIYAEILCKYEvgM 293
Cdd:cd18072  77 LVVCPASLVHQWKNEVESRVAsNKLRVCLYHGPNRERIGEVLRDYDIviTTYSLVAKEIPTYKEESRSSPLFRIAWA--R 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136368 294 VICDEGHRLKNSDNLTYQALMGLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEMLGTAAVFKRNFESAILRGQN 367
Cdd:cd18072 155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
156-347 3.49e-11

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 64.29  E-value: 3.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYEcvegkrgnfNGCIMADEMGLGKTLQCVTLV----------------WTLLRQGPECKPTINKA--- 216
Cdd:cd18070   1 LLPYQRRAVNWMLV---------PGGILADEMGLGKTVEVLALIllhprpdndldaadddSDEMVCCPDCLVAETPVssk 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 217 --IVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENtirALEqfSMTSARLGTP-VLLISYETFRiyAEILC------ 287
Cdd:cd18070  72 atLIVCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDG---ALA--SPAPEILAEYdIVVTTYDVLR--TELHYaeanrs 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136368 288 --------KYEVGM----------VICDEGHRLK-NSDNLTYQALMgLKTKRRVLLSGTPIQNDLTEYYSLVNFVNPEM 347
Cdd:cd18070 145 nrrrrrqkRYEAPPsplvlvewwrVCLDEAQMVEsSTSKAAEMARR-LPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
156-380 8.95e-11

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: 62.37  E-value: 8.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYEcvegkrgNFNGCIMADeMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPSSLVKN-WEKEFTK 234
Cdd:cd18013   1 PHPYQKVAINFIIE-------HPYCGLFLD-MGLGKTVTTLTALSDLQLDDF-----TRRVLVIAPLRVARStWPDEVEK 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLCLPMEGGTKENTIRALEqfsmTSARLgtpvLLISYETFriyaEILCKYEVG-----MVICDEGHRLKNSDNLT 309
Cdd:cd18013  68 WNHLRNLTVSVAVGTERQRSKAAN----TPADL----YVINRENL----KWLVNKSGDpwpfdMVVIDELSSFKSPRSKR 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 310 YQALMGL--KTKRRVLLSGTPIQNDLTEYYSLVNFVN-PEMLG-TAAVFK-RNFESAILRGQNT------DSTEQERQRA 378
Cdd:cd18013 136 FKALRKVrpVIKRLIGLTGTPSPNGLMDLWAQIALLDqGERLGrSITAYReRWFDPDKRNGQQVfkykpkPGAEEEIYRA 215

                ..
gi 17136368 379 IE 380
Cdd:cd18013 216 IS 217
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
156-415 8.14e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.96  E-value: 8.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYEcvEGKRGNFNGCIMADeMGLGKTlqcVTLVWTLLRQGpeckpTINKAIVVSPS-SLVKNWEKEFTK 234
Cdd:COG1061  81 LRPYQQEALEALLA--ALERGGGRGLVVAP-TGTGKT---VLALALAAELL-----RGKRVLVLVPRrELLEQWAEELRR 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 235 WLHGRLLclpmEGGTKENtiraleqfsmtsarlGTPVLLISYETFRIYAEI-LCKYEVGMVICDEGHRLKNSdnlTYQAL 313
Cdd:COG1061 150 FLGDPLA----GGGKKDS---------------DAPITVATYQSLARRAHLdELGDRFGLVIIDEAHHAGAP---SYRRI 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 314 MG-LKTKRRVLLSGTPIQNDLTEYYsLVNFVNPemlgtaaVFKRNFESAILRG--------QNTDSTEQERQRAIEKTQE 384
Cdd:COG1061 208 LEaFPAAYRLGLTATPFRSDGREIL-LFLFDGI-------VYEYSLKEAIEDGylappeyyGIRVDLTDERAEYDALSER 279
                       250       260       270
                ....*....|....*....|....*....|....
gi 17136368 385 LIGLVDQC---IIRRTNQILTKYLPVKFEMVICA 415
Cdd:COG1061 280 LREALAADaerKDKILRELLREHPDDRKTLVFCS 313
ResIII pfam04851
Type III restriction enzyme, res subunit;
156-329 1.85e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 57.30  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   156 LRPHQREGVRFMYECVegKRGNFNGCI-MAdeMGLGKTLQCVTLVWTLLRQGPeckptINKAIVVSPS-SLVKNWEKEFT 233
Cdd:pfam04851   4 LRPYQIEAIENLLESI--KNGQKRGLIvMA--TGSGKTLTAAKLIARLFKKGP-----IKKVLFLVPRkDLLEQALEEFK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   234 KWLHG-RLLCLPMEGGTKEntiraleqfsmtSARLGTPVLLISYETfrIYAEILCKYEV------GMVICDEGHRLkNSD 306
Cdd:pfam04851  75 KFLPNyVEIGEIISGDKKD------------ESVDDNKIVVTTIQS--LYKALELASLEllpdffDVIIIDEAHRS-GAS 139
                         170       180
                  ....*....|....*....|....
gi 17136368   307 NltYQALM-GLKTKRRVLLSGTPI 329
Cdd:pfam04851 140 S--YRNILeYFKPAFLLGLTATPE 161
DpdE NF041062
protein DpdE;
184-627 2.36e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 61.14  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   184 ADEMGLGKTLQCVTLVWTLLRQGPEckptiNKAIVVSPSSLVKNWEKEftkwLHGRLlclpmeggtkentirALEQFsmt 263
Cdd:NF041062  176 ADEVGLGKTIEAGLVIRQHLLDNPD-----ARVLVLVPDALVRQWRRE----LRDKF---------------FLDDF--- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   264 sarLGTPVLLISYETFRIYAEILCKYevGMVICDEGHRL-------KNSDNLTYQALMGL--KTKRRVLLSGTPIQNDLT 334
Cdd:NF041062  229 ---PGARVRVLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLLLLSATPVLGNEE 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   335 EYYSLVNFVNPEM--LGTAAVFKRN-----------------FESAILRGQ---------------------------NT 368
Cdd:NF041062  304 TFLALLHLLDPDLypLDDLEAFRERleereelgrlvlgldpdNPNFLLRQAldelralfpedeelqelaeellplldeFD 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   369 DSTEQERQRAIEKTQELIG---LVDQCIIR--RTNQILTKYLPVKFEMVICAKLTAIQLELYTNFLKSDQVRRSLADCN- 442
Cdd:NF041062  384 DEEPEERARAVSALRAHISetyRLHRRMIRnrRSSVLGADYLVPGRAGPRVLVWESPAREAADEALEDWREEAALLDAEs 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   443 EKASLTALA-DITTLKKICSHPDLIYEKLTAREKG-------------FENSQNVLPSNYKPKDLNPELSGkfMLLDFMl 508
Cdd:NF041062  464 DPAARAAYArALAWLVARLGGPDDLAALLRWRLRGdaasadlagerelLEALIAALEDEAKDADLLAALAD--WLLPLL- 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   509 aairaEGNDKVVLISNYTQTLD-LFEQLARKRKYGFVRLDGTMSIKKRSKVVDRFNDPESDSFLFMLSSkaGGCGLNLIG 587
Cdd:NF041062  541 -----RGSGKAVVFCGDGSLADhLAAALARLGAGSVERHLSGQGADQAERAVRAFRQDPSARVLVCDRS--GEEGLNLQG 613
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 17136368   588 ANRLFMFDPDWNPANDEQAMARV---WRDGQKKPCYIYRLVAS 627
Cdd:NF041062  614 ADRLVHLDLPWSPNRLEQRIGRLdryASLRGGRPVESYVLAPS 656
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
477-683 2.64e-08

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 55.80  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   477 FENSQNV------LPSNYKPKDLN--------PELSGKFMLL-DFMLAAIRAEGND--KVVLISNYTQTLDLFEQLARKR 539
Cdd:pfam11496  54 LENLSLVathpylLVDHYMPKSLLlkdepeklAYTSGKFLVLnDLVNLLIERDRKEpiNVAIVARSGKTLDLVEALLLGK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   540 KYGFVRLDGTMSIKKRSKV-VDRFNDPESDSFLFM-----LSSKAGGcgLNLIGANRLFMFDPDWNPANDEQAMARVWRD 613
Cdd:pfam11496 134 GLSYKRYSGEMLYGENKKVsDSGNKKIHSTTCHLLsstgqLTNDDSL--LENYKFDLIIAFDSSVDTSSPSVEHLRTQNR 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   614 GQKKPCYIYRLVASGSIEEKILQRQTHKKSLSstIIDNNESAEKHFtRDDLKDLftfDANILSDTHDKLK 683
Cdd:pfam11496 212 RKGNLAPIIRLVVINSIEHVELCFPKPPDSPD--YLYKVIAAIVVL-RDVVGDL---PDDLLPIYEQKLK 275
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
156-328 1.65e-07

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 51.15  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 156 LRPHQREGVRFMYECVEGKRGNFNgciMAdeMGLGKTLQCVTLVWTLLrqgpeCKPTInkaIVVSPSSLVKNWEKEFTKW 235
Cdd:cd17926   1 LRPYQEEALEAWLAHKNNRRGILV---LP--TGSGKTLTALALIAYLK-----ELRTL---IVVPTDALLDQWKERFEDF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 236 LHGRLLCLpmEGGTKENTIraleqfsmtsarLGTPVLLISYETFRIYAEILCKY--EVGMVICDEGHRLkNSDNLTyQAL 313
Cdd:cd17926  68 LGDSSIGL--IGGGKKKDF------------DDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL-PAKTFS-EIL 131
                       170
                ....*....|....*
gi 17136368 314 MGLKTKRRVLLSGTP 328
Cdd:cd17926 132 KELNAKYRLGLTATP 146
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
76-126 8.70e-04

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 41.09  E-value: 8.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136368    76 IAKVLARKFKVPMDNYVP-DYGGKRV---LGVRRCIS--RRPLHDPMACNALVLFHP 126
Cdd:pfam08658  77 KETVFRKSFSVPLKNKKQgAYNPRRPpptLGTRRGAIfvPRPLHDPTGEFAIVLYDP 133
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
179-327 9.05e-04

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 40.46  E-value: 9.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 179 NGCIMADEMGLGKTLQC-VTLVWTLLRQGPeckptinKAIVVSP-SSLVKNWEKEFTKWLHGRLLCLPMEGGTKentirA 256
Cdd:cd00046   2 ENVLITAPTGSGKTLAAlLAALLLLLKKGK-------KVLVLVPtKALALQTAERLRELFGPGIRVAVLVGGSS-----A 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368 257 LEQFSMtsaRLGTPVLLI-SYETFRIY---AEILCKYEVGMVICDEGHRL------KNSDNLTYQALMgLKTKRRVLLSG 326
Cdd:cd00046  70 EEREKN---KLGDADIIIaTPDMLLNLllrEDRLFLKDLKLIIVDEAHALlidsrgALILDLAVRKAG-LKNAQVILLSA 145

                .
gi 17136368 327 T 327
Cdd:cd00046 146 T 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
188-331 1.97e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.53  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   188 GLGKTLqcVTLVWTLLRQGPECKPTinKAIVVSPS-SLVKNWEKEFTKWL--HGRLLCLPMEGGTKENTIRALEQFSMTs 264
Cdd:pfam00270  24 GSGKTL--AFLLPALEALDKLDNGP--QALVLAPTrELAEQIYEELKKLGkgLGLKVASLLGGDSRKEQLEKLKGPDIL- 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136368   265 arLGTPVLLISYETFRIYAEilckyEVGMVICDEGHRLKNS---DNLTYQALMGLKTKRRVLLSGTPIQN 331
Cdd:pfam00270  99 --VGTPGRLLDLLQERKLLK-----NLKLLVLDEAHRLLDMgfgPDLEEILRRLPKKRQILLLSATLPRN 161
 
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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