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Conserved domains on  [gi|216548193|ref|NP_001136020|]
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DNA repair and recombination protein RAD54-like isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12785138)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as human DNA excision repair protein ERCC-6-like and DNA repair and recombination protein RAD54-like

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 ...
153-395 3.79e-176

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: 503.54  E-value: 3.79e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd18067   81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCL 392
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                 ...
gi 216548193 393 IRR 395
Cdd:cd18067  241 IRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
97-647 2.75e-120

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 376.10  E-value: 2.75e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  97 ALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDpilskvLRPHQREGVKFLWECvtsRRIPGs 176
Cdd:COG0553  192 LALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKAT------LRPYQLEGAAWLLFL---RRLGL- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 177 hGCIMADEMGLGKTLQCITLMWTLLRQSpeckpEIDKAVVVSPSSLVKNWYNEVGKWLGGrIQPLAIDGGSKDEidQKLE 256
Cdd:COG0553  262 -GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELAKFAPG-LRVLVLDGTRERA--KGAN 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 257 GFMNqrgarvsSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYF 336
Cdd:COG0553  333 PFED-------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELW 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 337 SLVHFVNSGILGTAHEFKKHFELPILKGRDAAAseadrqlgeERLRELtsiVNRCLIRRT-SDILsKYLPVKIEQVVCCR 415
Cdd:COG0553  406 SLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL---------ERLRRL---LRPFLLRRTkEDVL-KDLPEKTEETLYVE 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 416 LTPLQTELYKRFLRQAKpaEELLEGKMSVSSLSSITS---LKKLCNHPALIYdkcvEEEDGFVGAldlfppgysskalep 492
Cdd:COG0553  473 LTPEQRALYEAVLEYLR--RELEGAEGIRRRGLILAAltrLRQICSHPALLL----EEGAELSGR--------------- 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 493 qlSGKMLVLDYILAVTRSRsSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDfVFMLS 572
Cdd:COG0553  532 --SAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLIS 607
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548193 573 SKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVD 647
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
153-395 3.79e-176

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: 503.54  E-value: 3.79e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd18067   81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCL 392
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                 ...
gi 216548193 393 IRR 395
Cdd:cd18067  241 IRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
97-647 2.75e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 376.10  E-value: 2.75e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  97 ALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDpilskvLRPHQREGVKFLWECvtsRRIPGs 176
Cdd:COG0553  192 LALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKAT------LRPYQLEGAAWLLFL---RRLGL- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 177 hGCIMADEMGLGKTLQCITLMWTLLRQSpeckpEIDKAVVVSPSSLVKNWYNEVGKWLGGrIQPLAIDGGSKDEidQKLE 256
Cdd:COG0553  262 -GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELAKFAPG-LRVLVLDGTRERA--KGAN 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 257 GFMNqrgarvsSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYF 336
Cdd:COG0553  333 PFED-------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELW 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 337 SLVHFVNSGILGTAHEFKKHFELPILKGRDAAAseadrqlgeERLRELtsiVNRCLIRRT-SDILsKYLPVKIEQVVCCR 415
Cdd:COG0553  406 SLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL---------ERLRRL---LRPFLLRRTkEDVL-KDLPEKTEETLYVE 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 416 LTPLQTELYKRFLRQAKpaEELLEGKMSVSSLSSITS---LKKLCNHPALIYdkcvEEEDGFVGAldlfppgysskalep 492
Cdd:COG0553  473 LTPEQRALYEAVLEYLR--RELEGAEGIRRRGLILAAltrLRQICSHPALLL----EEGAELSGR--------------- 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 493 qlSGKMLVLDYILAVTRSRsSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDfVFMLS 572
Cdd:COG0553  532 --SAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLIS 607
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548193 573 SKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVD 647
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
156-463 4.61e-81

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: 260.31  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  156 HQREGVKFLWECVTSRripgSHGCIMADEMGLGKTLQCITLMWTLLRQSPecKPEiDKAVVVSPSSLVKNWYNEVGKWLG 235
Cdd:pfam00176   1 YQIEGVNWMLSLENNL----GRGGILADEMGLGKTLQTISLLLYLKHVDK--NWG-GPTLIVVPLSLLHNWMNEFERWVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  236 -GRIQPLAIDGGSKDeidqkLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDS 314
Cdd:pfam00176  74 pPALRVVVLHGNKRP-----QERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  315 LNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGrdaaaseadrqLGEERLRELTSIVNRCLIR 394
Cdd:pfam00176 149 LKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKPFLLR 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 216548193  395 RTSDILSKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLS---SITSLKKLCNHPALI 463
Cdd:pfam00176 218 RTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKASllnILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
180-648 2.41e-66

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 237.78  E-value: 2.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  180 IMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGKWLgGRIQPLAIDGGSKDEIDQKlEGFM 259
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGITGPHM----VVAPKSTLGNWMNEIRRFC-PVLRAVKFHGNPEERAHQR-EELL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  260 NQRGARVsspiLIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLV 339
Cdd:PLN03142  266 VAGKFDV----CVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALL 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  340 HFVNSGILGTAHEFKKHFELpilkgrdaaASEADRQlgeERLRELTSIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPL 419
Cdd:PLN03142  342 NFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQM 409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  420 QTELYKRFLRqaKPAEELLEGKMSVSSLSSITSLKKLCNHPALiydkcveeedgFVGAlDLFPPGYSSKALEPQlSGKML 499
Cdd:PLN03142  410 QKQYYKALLQ--KDLDVVNAGGERKRLLNIAMQLRKCCNHPYL-----------FQGA-EPGPPYTTGEHLVEN-SGKMV 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  500 VLDYILAVTRSRSSdKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDFVFMLSSKAGGCG 579
Cdd:PLN03142  475 LLDKLLPKLKERDS-RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 216548193  580 LNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDE 648
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
494-622 4.02e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 188.07  E-value: 4.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 494 LSGKMLVLDYILAVTRSrSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSpDFVFMLSS 573
Cdd:cd18793    9 VSGKLEALLELLEELRE-PGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 216548193 574 KAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLL 622
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
151-357 2.64e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   151 KVLRPHQREGVKFLWEcvtsrripGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECkpeidKAVVVSP-SSLVKNWYNE 229
Cdd:smart00487   7 EPLRPYQKEAIEALLS--------GLRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   230 VGKWLGG-RIQPLAIDGGskDEIDQKLEGFMNQRgarvsSPILIISYETFRLHV--GVLQKGSVGLVICDEGHRLKNSEN 306
Cdd:smart00487  74 LKKLGPSlGLKVVGLYGG--DSKREQLRKLESGK-----TDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGF 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 216548193   307 --QTYQALDSLNTSRRVLI-SGTP---IQNDLLEYFSLVHFVNSGIlgTAHEFKKHF 357
Cdd:smart00487 147 gdQLEKLLKLLPKNVQLLLlSATPpeeIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
496-611 2.13e-24

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: 98.44  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  496 GKMLVLDYILavtRSRSSDKVVLVSNYTQTLDLfEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPdfvFMLSSKA 575
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 216548193  576 GGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDG 611
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
527-611 3.44e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 3.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   527 DLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPsspDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMAR 606
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 216548193   607 VWRDG 611
Cdd:smart00490  78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
153-390 1.69e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 64.28  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRripGSHGCIMADeMGLGKTlqcITLMWTLLRQSpeckpEIDKAVVVSPS-SLVKNWYNEVG 231
Cdd:COG1061   81 LRPYQQEALEALLAALERG---GGRGLVVAP-TGTGKT---VLALALAAELL-----RGKRVLVLVPRrELLEQWAEELR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 232 KWLGgriqpLAIDGGSKDEIDqklegfmnqrgarvsSPILIISYETF--RLHVGVLQKgSVGLVICDEGHRLknSENQTY 309
Cdd:COG1061  149 RFLG-----DPLAGGGKKDSD---------------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 310 QALDSLNTSRRVLISGTPIQND----LLEYF-------SLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQL-- 376
Cdd:COG1061  206 RILEAFPAAYRLGLTATPFRSDgreiLLFLFdgivyeySLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERLREAla 285
                        250
                 ....*....|....*.
gi 216548193 377 -GEER-LRELTSIVNR 390
Cdd:COG1061  286 aDAERkDKILRELLRE 301
DpdE NF041062
protein DpdE;
182-343 2.82e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 47.66  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  182 ADEMGLGKTLQ-CITLMWTLLRqspecKPEiDKAVVVSPSSLVKNWynevgkwlggriqplaidggsKDEIDQK--LEGF 258
Cdd:NF041062  176 ADEVGLGKTIEaGLVIRQHLLD-----NPD-ARVLVLVPDALVRQW---------------------RRELRDKffLDDF 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  259 MNQRgarvsspILIISYETFRLhvgVLQKGSV-GLVICDEGHRL-------KNSENQTYQALDSL--NTSRRVLISGTPI 328
Cdd:NF041062  229 PGAR-------VRVLSHEEPER---WEPLLDApDLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLLLLSATPV 298
                         170
                  ....*....|....*
gi 216548193  329 QNDLLEYFSLVHFVN 343
Cdd:NF041062  299 LGNEETFLALLHLLD 313
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
153-395 3.79e-176

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: 503.54  E-value: 3.79e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd18067   81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCL 392
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                 ...
gi 216548193 393 IRR 395
Cdd:cd18067  241 IRR 243
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
153-395 5.47e-127

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: 377.78  E-value: 5.47e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLG-GRIQPLAIDGGSKDEIDQKLegfmnQRGARVSSPILIISYETFRLHVGVLQKG-SVGLVICDEGHRLKNSENQTYQ 310
Cdd:cd18004   81 WLGlRRIKVVTADGNAKDVKASLD-----FFSSASTYPVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKTTK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 311 ALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNR 390
Cdd:cd18004  156 ALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSR 235

                 ....*
gi 216548193 391 CLIRR 395
Cdd:cd18004  236 FILRR 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
97-647 2.75e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 376.10  E-value: 2.75e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  97 ALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDpilskvLRPHQREGVKFLWECvtsRRIPGs 176
Cdd:COG0553  192 LALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKAT------LRPYQLEGAAWLLFL---RRLGL- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 177 hGCIMADEMGLGKTLQCITLMWTLLRQSpeckpEIDKAVVVSPSSLVKNWYNEVGKWLGGrIQPLAIDGGSKDEidQKLE 256
Cdd:COG0553  262 -GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELAKFAPG-LRVLVLDGTRERA--KGAN 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 257 GFMNqrgarvsSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYF 336
Cdd:COG0553  333 PFED-------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELW 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 337 SLVHFVNSGILGTAHEFKKHFELPILKGRDAAAseadrqlgeERLRELtsiVNRCLIRRT-SDILsKYLPVKIEQVVCCR 415
Cdd:COG0553  406 SLLDFLNPGLLGSLKAFRERFARPIEKGDEEAL---------ERLRRL---LRPFLLRRTkEDVL-KDLPEKTEETLYVE 472
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 416 LTPLQTELYKRFLRQAKpaEELLEGKMSVSSLSSITS---LKKLCNHPALIYdkcvEEEDGFVGAldlfppgysskalep 492
Cdd:COG0553  473 LTPEQRALYEAVLEYLR--RELEGAEGIRRRGLILAAltrLRQICSHPALLL----EEGAELSGR--------------- 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 493 qlSGKMLVLDYILAVTRSRsSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDfVFMLS 572
Cdd:COG0553  532 --SAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLIS 607
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 216548193 573 SKAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVD 647
Cdd:COG0553  608 LKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
153-395 2.33e-81

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: 259.01  E-value: 2.33e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPE-CKPEIDKAVVVSPSSLVKNWYNEVG 231
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYgGKPVIKRALIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 232 KWLGG-RIQPLAIDGgskdeiDQKLEGFMNqrgARVSSpILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQ 310
Cdd:cd18066   81 KWLGSeRIKVFTVDQ------DHKVEEFIA---SPLYS-VLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 311 ALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNR 390
Cdd:cd18066  151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230

                 ....*
gi 216548193 391 CLIRR 395
Cdd:cd18066  231 FILRR 235
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
156-463 4.61e-81

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: 260.31  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  156 HQREGVKFLWECVTSRripgSHGCIMADEMGLGKTLQCITLMWTLLRQSPecKPEiDKAVVVSPSSLVKNWYNEVGKWLG 235
Cdd:pfam00176   1 YQIEGVNWMLSLENNL----GRGGILADEMGLGKTLQTISLLLYLKHVDK--NWG-GPTLIVVPLSLLHNWMNEFERWVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  236 -GRIQPLAIDGGSKDeidqkLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDS 314
Cdd:pfam00176  74 pPALRVVVLHGNKRP-----QERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  315 LNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGrdaaaseadrqLGEERLRELTSIVNRCLIR 394
Cdd:pfam00176 149 LKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKPFLLR 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 216548193  395 RTSDILSKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLS---SITSLKKLCNHPALI 463
Cdd:pfam00176 218 RTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKASllnILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
180-648 2.41e-66

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 237.78  E-value: 2.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  180 IMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGKWLgGRIQPLAIDGGSKDEIDQKlEGFM 259
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGITGPHM----VVAPKSTLGNWMNEIRRFC-PVLRAVKFHGNPEERAHQR-EELL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  260 NQRGARVsspiLIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLV 339
Cdd:PLN03142  266 VAGKFDV----CVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALL 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  340 HFVNSGILGTAHEFKKHFELpilkgrdaaASEADRQlgeERLRELTSIVNRCLIRRTSDILSKYLPVKIEQVVCCRLTPL 419
Cdd:PLN03142  342 NFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQM 409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  420 QTELYKRFLRqaKPAEELLEGKMSVSSLSSITSLKKLCNHPALiydkcveeedgFVGAlDLFPPGYSSKALEPQlSGKML 499
Cdd:PLN03142  410 QKQYYKALLQ--KDLDVVNAGGERKRLLNIAMQLRKCCNHPYL-----------FQGA-EPGPPYTTGEHLVEN-SGKMV 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  500 VLDYILAVTRSRSSdKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPDFVFMLSSKAGGCG 579
Cdd:PLN03142  475 LLDKLLPKLKERDS-RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 216548193  580 LNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDE 648
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
153-343 1.60e-62

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: 207.03  E-value: 1.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCIMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEVGK 232
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGP-----GGILADEMGLGKTLQAIAFLAYLLKEGKERGP----VLVVCPLSVLENWEREFEK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGrIQPLAIDGGSKDEIDQKlegfmnQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd17919   72 WTPD-LRVVVYHGSQRERAQIR------AKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKAL 144
                        170       180       190
                 ....*....|....*....|....*....|.
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVN 343
Cdd:cd17919  145 KALRAKRRLLLTGTPLQNNLEELWALLDFLD 175
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
153-380 4.76e-60

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: 202.52  E-value: 4.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECV--TSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKpeidKAVVVSPSSLVKNWYNEV 230
Cdd:cd18007    1 LKPHQVEGVRFLWSNLvgTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRS----RPLVLCPASTLYNWEDEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKWLGGRIQPLAI---DGGSKDEiDQKLEGFMN--QRGArvsspILIISYETFR--------------LHVGVLQKGSVG 291
Cdd:cd18007   77 KKWLPPDLRPLLVlvsLSASKRA-DARLRKINKwhKEGG-----VLLIGYELFRnlasnattdprlkqEFIAALLDPGPD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 292 LVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASE 371
Cdd:cd18007  151 LLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTE 230

                 ....*....
gi 216548193 372 ADRQLGEER 380
Cdd:cd18007  231 EDVRLMLKR 239
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
153-395 1.96e-56

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: 192.98  E-value: 1.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTsrripGSHGCIMADEMGLGKTLQCITLMWTLL------RQSPECKPEIDK----------AVV 216
Cdd:cd18005    1 LRDYQREGVEFMYDLYK-----NGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrRDRENNRPRFKKkppassakkpVLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 217 VSPSSLVKNWYNEVGKWlgGRIQPLAIDGGSKDEIdqkLEGFMNQRGARVsspiLIISYETFRLHVGVLQKGSVGLVICD 296
Cdd:cd18005   76 VAPLSVLYNWKDELDTW--GHFEVGVYHGSRKDDE---LEGRLKAGRLEV----VVTTYDTLRRCIDSLNSINWSAVIAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 297 EGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQL 376
Cdd:cd18005  147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRL 226
                        250
                 ....*....|....*....
gi 216548193 377 GEERLRELTSIVNRCLIRR 395
Cdd:cd18005  227 GRKRKQELAVKLSKFFLRR 245
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
494-622 4.02e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 188.07  E-value: 4.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 494 LSGKMLVLDYILAVTRSrSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSpDFVFMLSS 573
Cdd:cd18793    9 VSGKLEALLELLEELRE-PGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 216548193 574 KAGGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLL 622
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
153-395 7.09e-48

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: 169.09  E-value: 7.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRripgsHGCIMADEMGLGKTLQCITLMWTLLRQSpeckpEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGG-----KGGILADDMGLGKTVQICAFLSGMFDSG-----LIKSVLVVMPTSLIPHWVKEFAK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WlGGRIQPLAIDGGSKDEIDQKLEGFMNQRGarvsspILIISYETFRLHVGVLQKGSVG-----LVICDEGHRLKNSENQ 307
Cdd:cd18001   71 W-TPGLRVKVFHGTSKKERERNLERIQRGGG------VLLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNSKTK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 308 TYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFV-NSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTS 386
Cdd:cd18001  144 SAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQ 223

                 ....*....
gi 216548193 387 IVNRCLIRR 395
Cdd:cd18001  224 IIKPYFLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
153-380 1.11e-46

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: 166.22  E-value: 1.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECV-----TSRRIPGShGCIMADEMGLGKTLQCITLMWTLLRQspECKPEIDKAVVVSPSSLVKNWY 227
Cdd:cd18068    1 LKPHQVDGVQFMWDCCceslkKTKKSPGS-GCILAHCMGLGKTLQVVTFLHTVLLC--EKLENFSRVLVVCPLNTVLNWL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 228 NEVGKWLGGRIQPLAIDGGSKDEIDQKLE-GFMNQRGARVSSpILIISYETFR-LHVG---------------VLQKGSV 290
Cdd:cd18068   78 NEFEKWQEGLKDEEKIEVNELATYKRPQErSYKLQRWQEEGG-VMIIGYDMYRiLAQErnvksreklkeifnkALVDPGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 291 GLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAAS 370
Cdd:cd18068  157 DFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADST 236
                        250
                 ....*....|
gi 216548193 371 EADRQLGEER 380
Cdd:cd18068  237 LVDVRVMKKR 246
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
153-380 7.11e-46

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: 163.45  E-value: 7.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECV--TSRRIPGSHG--CIMADEMGLGKTLQCITLMWTLLRQSPeckpeIDKAVVVSPSSLVKNWYN 228
Cdd:cd18069    1 LKPHQIGGIRFLYDNIieSLERYKGSSGfgCILAHSMGLGKTLQVISFLDVLLRHTG-----AKTVLAIVPVNTLQNWLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 229 EVGKWL-----GGRIQPLAID----GGSKDEIDQKLEGFMNQRGarvSSPILIISYETFRLHVGVlqkgsvGLVICDEGH 299
Cdd:cd18069   76 EFNKWLpppeaLPNVRPRPFKvfilNDEHKTTAARAKVIEDWVK---DGGVLLMGYEMFRLRPGP------DVVICDEGH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 300 RLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEE 379
Cdd:cd18069  147 RIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRY 226

                 .
gi 216548193 380 R 380
Cdd:cd18069  227 R 227
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
153-395 7.49e-42

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: 152.12  E-value: 7.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECvtsRRIpGSHGcIMADEMGLGKTLQ--CITLMWTLLRQSpECKPEIDKAVVVSPSSLVKNWYNEV 230
Cdd:cd17999    1 LRPYQQEGINWLAFL---NKY-NLHG-ILCDDMGLGKTLQtlCILASDHHKRAN-SFNSENLPSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKWLG-GRIQPLAIDGGSKDeiDQKLEGFMNQrgarvsSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTY 309
Cdd:cd17999   75 KKYFPnAFLKPLAYVGPPQE--RRRLREQGEK------HNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 310 QALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVN 389
Cdd:cd17999  147 KAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVL 226

                 ....*.
gi 216548193 390 RCLIRR 395
Cdd:cd17999  227 PFLLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
153-396 1.12e-41

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: 151.18  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVK---FLWECvtsrripgSHGCIMADEMGLGKTLQCITLMwTLLRQSPECKPeidkAVVVSPSSLVKNWYNE 229
Cdd:cd18012    5 LRPYQKEGFNwlsFLRHY--------GLGGILADDMGLGKTLQTLALL-LSRKEEGRKGP----SLVVAPTSLIYNWEEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 230 VGKWlggriQP----LAIDG-GSKDEIDQKLEGFmnqrgarvssPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNS 304
Cdd:cd18012   72 AAKF-----APelkvLVIHGtKRKREKLRALEDY----------DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 305 ENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDaaaseadrqlgEERLREL 384
Cdd:cd18012  137 QTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEEL 205
                        250
                 ....*....|..
gi 216548193 385 TSIVNRCLIRRT 396
Cdd:cd18012  206 KKLISPFILRRL 217
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
152-395 2.25e-38

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: 142.53  E-value: 2.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 152 VLRPHQREGVKF---LWEcvtsrriPGSHGcIMADEMGLGKTLQCITLMwTLLRQSPECKPeidkAVVVSPSSLVKNWYN 228
Cdd:cd18009    3 VMRPYQLEGMEWlrmLWE-------NGING-ILADEMGLGKTIQTIALL-AHLRERGVWGP----FLVIAPLSTLPNWVN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 229 EVGKWLGGriQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQT 308
Cdd:cd18009   70 EFARFTPS--VPVLLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 309 YQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIV 388
Cdd:cd18009  148 IQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAIL 227

                 ....*..
gi 216548193 389 NRCLIRR 395
Cdd:cd18009  228 KPFLLRR 234
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
153-357 3.34e-36

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: 135.84  E-value: 3.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCIMADEMGLGKTLQCITLMwTLLRQSPECKPEIdkaVVVSPSSLVKNWYNEVGK 232
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRR-----NCILADEMGLGKTIQSIAFL-EHLYQVEGIRGPF---LVIAPLSTIPNWQREFET 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGRiqplAI---DGGSKDEIDQKLEGFMNQRGARVSSP-----ILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNS 304
Cdd:cd17995   72 WTDMN----VVvyhGSGESRQIIQQYEMYFKDAQGRKKKGvykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 216548193 305 ENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHF 357
Cdd:cd17995  148 NSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
153-395 1.63e-34

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: 131.64  E-value: 1.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrrIPgsHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAV-------------VVSP 219
Cdd:cd18008    1 LLPYQKQGLAWM--------LP--RGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSsdpkklylskttlIVVP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 220 SSLVKNWYNEVGK-WLGGRIQPLAIDGGSKDEIDQKLEGFMnqrgarvsspILIISYETFRLHVGVLQKGSVGL------ 292
Cdd:cd18008   71 LSLLSQWKDEIEKhTKPGSLKVYVYHGSKRIKSIEELSDYD----------IVITTYGTLASEFPKNKKGGGRDskekea 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 293 ----------VICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPIL 362
Cdd:cd18008  141 splhrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFS 220
                        250       260       270
                 ....*....|....*....|....*....|...
gi 216548193 363 KGRDAAaseadrqlgeerLRELTSIVNRCLIRR 395
Cdd:cd18008  221 KNDRKA------------LERLQALLKPILLRR 241
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
153-395 1.71e-31

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: 122.46  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWEcVTSRRIPGshgcIMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGK 232
Cdd:cd18003    1 LREYQHIGLDWLAT-LYEKNLNG----ILADEMGLGKTIQTIALLAHLACEKGNWGPHL----IVVPTSVMLNWEMEFKR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGriqpLAIDG--GSKDEIDQKLEGFMNQRgarvSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQ 310
Cdd:cd18003   72 WCPG----FKILTyyGSAKERKLKRQGWMKPN----SFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 311 ALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPIlkgrdAAASEADRQLGEERLRELTSIVNR 390
Cdd:cd18003  144 TLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL-----TAMSEGSQEENEELVRRLHKVLRP 218

                 ....*
gi 216548193 391 CLIRR 395
Cdd:cd18003  219 FLLRR 223
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
153-342 1.46e-30

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: 118.97  E-value: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWEcVTSRRIPGshgcIMADEMGLGKTLQCITLmwtlLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18000    1 LFKYQQTGVQWLWE-LHCQRVGG----ILGDEMGLGKTIQIIAF----LAALHHSKLGLGPSLIVCPATVLKQWVKEFHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGG-RIQPL---AIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQT 308
Cdd:cd18000   72 WWPPfRVVVLhssGSGTGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 216548193 309 YQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFV 342
Cdd:cd18000  152 TLACKQLRTPHRLILSGTPIQNNLKELWSLFDFV 185
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
153-395 4.12e-29

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: 115.38  E-value: 4.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFlwecVTSRRipgshG-CIMADEMGLGKTLQCITLM------WTLLrqspeckpeidkavVVSPSSLVKN 225
Cdd:cd18010    1 LLPFQREGVCF----ALRRG-----GrVLIADEMGLGKTVQAIAIAayyreeWPLL--------------IVCPSSLRLT 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 226 WYNEVGKWLggriqplaiDGGSKDEIdQKLEGfmNQRGARVSSP-ILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNS 304
Cdd:cd18010   58 WADEIERWL---------PSLPPDDI-QVIVK--SKDGLRDGDAkVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 305 ENQTYQALDSL--NTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFELPILKGRDAAASeadrqlGEERLR 382
Cdd:cd18010  126 KAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYS------GSSNLE 199
                        250
                 ....*....|....
gi 216548193 383 ELTSIV-NRCLIRR 395
Cdd:cd18010  200 ELHLLLlATIMIRR 213
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
153-395 3.24e-28

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: 112.92  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTsrripGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGK 232
Cdd:cd18006    1 LRPYQLEGVNWLLQCRA-----EQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFL----VLCPLSVLDNWKEELNR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WlGGRIQPLAIDGGSKDEIDQklegfmnQRGARVSSP--ILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQ 310
Cdd:cd18006   72 F-APDLSVITYMGDKEKRLDL-------QQDIKSTNRfhVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 311 ALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILG--TAHEFKKHFelpilkgrdaaaseADRQLGEERLRELTSIV 388
Cdd:cd18006  144 TLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAY--------------SETDDESETVEELHLLL 209

                 ....*..
gi 216548193 389 NRCLIRR 395
Cdd:cd18006  210 QPFLLRR 216
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
153-342 1.44e-26

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: 108.21  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFL---WECVTSrripgshgCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNE 229
Cdd:cd17993    2 LRDYQLTGLNWLahsWCKGNN--------GILADEMGLGKTVQTISFLSYLFHSQQQYGPFL----VVVPLSTMPAWQRE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 230 VGKW---------LGgriqplaiDGGSKDEIdQKLEgFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHR 300
Cdd:cd17993   70 FAKWapdmnvivyLG--------DIKSRDTI-REYE-FYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHR 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 216548193 301 LKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFV 342
Cdd:cd17993  140 LKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFL 181
DEXDc smart00487
DEAD-like helicases superfamily;
151-357 2.64e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   151 KVLRPHQREGVKFLWEcvtsrripGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECkpeidKAVVVSP-SSLVKNWYNE 229
Cdd:smart00487   7 EPLRPYQKEAIEALLS--------GLRDVILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   230 VGKWLGG-RIQPLAIDGGskDEIDQKLEGFMNQRgarvsSPILIISYETFRLHV--GVLQKGSVGLVICDEGHRLKNSEN 306
Cdd:smart00487  74 LKKLGPSlGLKVVGLYGG--DSKREQLRKLESGK-----TDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGF 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 216548193   307 --QTYQALDSLNTSRRVLI-SGTP---IQNDLLEYFSLVHFVNSGIlgTAHEFKKHF 357
Cdd:smart00487 147 gdQLEKLLKLLPKNVQLLLlSATPpeeIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
180-396 3.78e-25

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: 104.33  E-value: 3.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 180 IMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGKWLGG-RIQPLAidgGSKDEIDQklegF 258
Cdd:cd17997   26 ILADEMGLGKTLQTISLLGYLKHYKNINGPHL----IIVPKSTLDNWMREFKRWCPSlRVVVLI---GDKEERAD----I 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 259 MNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSL 338
Cdd:cd17997   95 IRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWAL 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548193 339 VHFVNSGILGTAHEFKKHFELpilkgrdaaasEADRQLGEERLRELTSIVNRCLIRRT 396
Cdd:cd17997  175 LNFLLPDVFTSSEDFDEWFNV-----------NNCDDDNQEVVQRLHKVLRPFLLRRI 221
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
153-342 4.43e-25

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 102.85  E-value: 4.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwECVTSRRIpgshGCIMADEMGLGKTLQCITLMwTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGK 232
Cdd:cd17998    1 LKDYQLIGLNWL-NLLYQKKL----SGILADEMGLGKTIQVIAFL-AYLKEIGIPGPHL----VVVPSSTLDNWLREFKR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGG-RIQPLAidgGSKDE-------IDQKLEGFmnqrgarvssPILIISYE---TFRLHVGVLQKGSVGLVICDEGHRL 301
Cdd:cd17998   71 WCPSlKVEPYY---GSQEErkhlrydILKGLEDF----------DVIVTTYNlatSNPDDRSFFKRLKLNYVVYDEGHML 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 216548193 302 KNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFV 342
Cdd:cd17998  138 KNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
496-611 2.13e-24

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: 98.44  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  496 GKMLVLDYILavtRSRSSDKVVLVSNYTQTLDLfEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPSSPdfvFMLSSKA 575
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 216548193  576 GGCGLNLIGANRLVMFDPDWNPANDEQAMARVWRDG 611
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
180-395 2.89e-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: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 180 IMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEVGKWLGgRIQPLAIDGGSKD-EIDQKLEGF 258
Cdd:cd18002   23 ILADEMGLGKTVQSIAVLAHLAEEHNIWGP----FLVIAPASTLHNWQQEISRFVP-QFKVLPYWGNPKDrKVLRKFWDR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 259 MNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSL 338
Cdd:cd18002   98 KNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWAL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 216548193 339 VHFVNSGILGTAHEFKKHFELPIlkgrdAAASEADRQLGEERLRELTSIVNRCLIRR 395
Cdd:cd18002  178 LHFIMPTLFDSHDEFNEWFSKDI-----ESHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
153-366 1.51e-23

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: 100.08  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFL---WeCvtsrripGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNE 229
Cdd:cd18054   21 LRDYQLEGLNWLahsW-C-------KNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGP----FLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 230 VGKWLGGRIQPLAI-DGGSKDEIDQKleGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQT 308
Cdd:cd18054   89 FEIWAPEINVVVYIgDLMSRNTIREY--EWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548193 309 YQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFvnsgILGTAHEFKKHFELPILKGRD 366
Cdd:cd18054  167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHF----IMPEKFEFWEDFEEDHGKGRE 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
153-395 8.19e-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: 97.43  E-value: 8.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCIMADEMGLGKTLQCITL---MWTLLRQSPeckpeidkAVVVSPSSLVKNWYNE 229
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQ-----NCILADEMGLGKTIQSIAFlqeVYNVGIHGP--------FLVIAPLSTITNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 230 VGKWLggRIQPLAIDGG-SKDEIDQKLEGFMNQRGARV-----SSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKN 303
Cdd:cd18060   68 FNTWT--EMNTIVYHGSlASRQMIQQYEMYCKDSRGRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 304 SENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaaseADRQLgEERLRE 383
Cdd:cd18060  146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF--------------GDLKT-EEQVQK 210
                        250
                 ....*....|..
gi 216548193 384 LTSIVNRCLIRR 395
Cdd:cd18060  211 LQAILKPMMLRR 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
180-395 5.62e-22

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: 95.51  E-value: 5.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 180 IMADEMGLGKTLQCITLMWTLLrqspECKPEIDKAVVVSPSSLVKNWYNEVGKWLggriqPLAIDGGSKDEIDQKLEGFM 259
Cdd:cd17996   26 ILADEMGLGKTIQTISLITYLM----EKKKNNGPYLVIVPLSTLSNWVSEFEKWA-----PSVSKIVYKGTPDVRKKLQS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 260 NQRGARVSspILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDS-LNTSRRVLISGTPIQNDLLEYFSL 338
Cdd:cd17996   97 QIRAGKFN--VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWAL 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 216548193 339 VHFVNSGILGTAHEFKKHFELPIlkgrdAAASEADR-QLGEER----LRELTSIVNRCLIRR 395
Cdd:cd17996  175 LNFLLPKIFKSCKTFEQWFNTPF-----ANTGEQVKiELNEEEtlliIRRLHKVLRPFLLRR 231
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
153-345 8.99e-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: 91.20  E-value: 8.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWEcvtsrriPGSHGCIMADEMGLGKTLQCITLMWTLLRQSpeckpEIDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18011    1 PLPHQIDAVLRALR-------KPPVRLLLADEVGLGKTIEAGLIIKELLLRG-----DAKRVLILCPASLVEQWQDELQD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGgrIQPLAIDGGSKDEIdQKLEGFMNQRGarvssPILIISYETFR---LHVGVLQKGSVGLVICDEGHRLKNSENQTY 309
Cdd:cd18011   69 KFG--LPFLILDRETAAQL-RRLIGNPFEEF-----PIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGGGKE 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 216548193 310 QALDSL------NTSRRVLISGTPIQNDLLEYFSLVHFVNSG 345
Cdd:cd18011  141 TKRYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPG 182
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
153-395 2.03e-20

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: 90.49  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCIMADEMGLGKTLQCITLMWTLLRQSPEckpeiDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRK-----NCILADEMGLGKTIQSITFLSEIFLMGIR-----GPFLIIAPLSTITNWEREFRT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLggRIQPLAIDGG--SKDEIDQKLEGFMNQRGARVSS----PILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSEN 306
Cdd:cd18058   71 WT--EMNAIVYHGSqiSRQMIQQYEMYYRDEQGNPLSGifkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 307 QTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaaseADRQLgEERLRELTS 386
Cdd:cd18058  149 KLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF--------------GDLKT-EEQVKKLQS 213

                 ....*....
gi 216548193 387 IVNRCLIRR 395
Cdd:cd18058  214 ILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
153-357 1.08e-19

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: 88.58  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrRIPGSHGC--IMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEV 230
Cdd:cd18057    1 LHPYQLEGLNWL-------RFSWAQGTdtILADEMGLGKTVQTIVFLYSLYKEGHSKGPYL----VSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKWLGG-RIQPLAIDGGSKDEIDQKLEGFMN------------QRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDE 297
Cdd:cd18057   70 EMWAPDfYVVTYTGDKESRSVIRENEFSFEDnairsgkkvfrmKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 298 GHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHF 357
Cdd:cd18057  150 AHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
153-395 1.91e-19

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: 87.75  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCIMADEMGLGKTLQCITLMWTLLRQSPEckpeiDKAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRR-----NCILADEMGLGKTIQSITFLYEILLTGIR-----GPFLIIAPLSTIANWEREFRT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLggRIQPLAIDGG--SKDEIDQKLEGFMNQRGARVSSPI----LIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSEN 306
Cdd:cd18061   71 WT--DLNVVVYHGSliSRQMIQQYEMYFRDSQGRIIRGAYrfqaIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 307 QTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaaseADRQLgEERLRELTS 386
Cdd:cd18061  149 KLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF--------------GDLKT-EEQVQKLQA 213

                 ....*....
gi 216548193 387 IVNRCLIRR 395
Cdd:cd18061  214 ILKPMMLRR 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
153-407 1.98e-19

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: 88.18  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSrripGSHGcIMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGK 232
Cdd:cd18064   16 LRDYQVRGLNWLISLYEN----GING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPHM----VLVPKSTLHNWMAEFKR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGgRIQPLAIDGGSKdeidqklegfmnQRGARVSSPIL-------IISYETFRLHVGVLQKGSVGLVICDEGHRLKNSE 305
Cdd:cd18064   87 WVP-TLRAVCLIGDKD------------QRAAFVRDVLLpgewdvcVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 306 NQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaasEADRQLGEERLRELT 385
Cdd:cd18064  154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-------------DTNNCLGDQKLVERL 220
                        250       260
                 ....*....|....*....|...
gi 216548193 386 SIVNR-CLIRRTSDILSKYLPVK 407
Cdd:cd18064  221 HMVLRpFLLRRIKADVEKSLPPK 243
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
153-358 3.19e-19

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: 86.34  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrRIPGSHG--CIMADEMGLGKTLQCITLMWTLLRQSpECKPEIdkaVVVSPSSLVKNWYNEV 230
Cdd:cd17994    1 LHPYQLEGLNWL-------RFSWAQGtdTILADEMGLGKTIQTIVFLYSLYKEG-HSKGPF---LVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKWlggriQPlaidggskdeiDQKLEGFmnqrgarVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQ 310
Cdd:cd17994   70 EMW-----AP-----------DFYVVTY-------VGDHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFR 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 216548193 311 ALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFE 358
Cdd:cd17994  127 ILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA 174
HELICc smart00490
helicase superfamily c-terminal domain;
527-611 3.44e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 3.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193   527 DLFEKLCRARRYLYVRLDGTMSIKKRAKVVERFNSPsspDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPANDEQAMAR 606
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 216548193   607 VWRDG 611
Cdd:smart00490  78 AGRAG 82
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
153-382 3.86e-19

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: 87.41  E-value: 3.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEVGK 232
Cdd:cd18053   21 LRDYQLNGLNWL-----AHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGP----FLLVVPLSTLTSWQREIQT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WlGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd18053   92 W-APQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFElpilKGRDAAASEADRQLGEERLR 382
Cdd:cd18053  171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHG----KGREYGYASLHKELEPFLLR 236
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
153-342 1.08e-18

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: 85.89  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrRIPGSHGC--IMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEV 230
Cdd:cd18056    1 LHPYQLEGLNWL-------RFSWAQGTdtILADEMGLGKTVQTAVFLYSLYKEGHSKGP----FLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKW---------LGGRIQPLAIDGGSKDEIDQKLEGFMN----QRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDE 297
Cdd:cd18056   70 EMWapdmyvvtyVGDKDSRAIIRENEFSFEDNAIRGGKKasrmKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDE 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 216548193 298 GHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFV 342
Cdd:cd18056  150 AHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFL 194
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
153-395 1.47e-18

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: 85.08  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFL---WEcvtsrripGSHGCIMADEMGLGKTLQCITLMWTLLRQSPEckpeiDKAVVVSPSSLVKNWYNE 229
Cdd:cd18059    1 LREYQLEGVNWLlfnWY--------NTRNCILADEMGLGKTIQSITFLYEIYLKGIH-----GPFLVIAPLSTIPNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 230 VGKWLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPI----LIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSE 305
Cdd:cd18059   68 FRTWTELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGSYkfhaIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 306 NQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaaseADRQLgEERLRELT 385
Cdd:cd18059  148 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF--------------GDLKT-EEQVQKLQ 212
                        250
                 ....*....|
gi 216548193 386 SIVNRCLIRR 395
Cdd:cd18059  213 AILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
153-357 1.82e-18

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: 85.06  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrRIPGSHGC--IMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEV 230
Cdd:cd18055    1 LHMYQLEGLNWL-------RFSWAQGTdtILADEMGLGKTIQTIVFLYSLYKEGHTKGP----FLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKW---------LGGR------------IQPLAIDGGSKdeidqkleGFMNQRGARVSSPILIISYETFRLHVGVLQKGS 289
Cdd:cd18055   70 QMWapdfyvvtyTGDKdsraiirenefsFDDNAVKGGKK--------AFKMKREAQVKFHVLLTSYELVTIDQAALGSIR 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 216548193 290 VGLVICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHF 357
Cdd:cd18055  142 WACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
153-395 1.37e-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: 82.90  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFL------------WE-----------CVTSRRIPGS-HGCIMADEMGLGKTLQCITLMWTllrqspeck 208
Cdd:cd18071    1 LLPHQKQALAWMvsrensqdlppfWEeavglflntitNFSQKKRPELvRGGILADDMGLGKTLTTISLILA--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 209 peiDKAVVVSPSSLVKNWYNEVGKwlggRIQPLAID-----GGSKDEIDQKLEGFmnqrgarvssPILIISYETFRLHVG 283
Cdd:cd18071   72 ---NFTLIVCPLSVLSNWETQFEE----HVKPGQLKvytyhGGERNRDPKLLSKY----------DIVLTTYNTLASDFG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 284 vlQKGSVGL-------VICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKH 356
Cdd:cd18071  135 --AKGDSPLhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRL 212
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 216548193 357 FELPILKGRDAAaseadrqlgeerLRELTSIVNRCLIRR 395
Cdd:cd18071  213 IQRPLTMGDPTG------------LKRLQVLMKQITLRR 239
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
180-395 1.55e-17

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: 82.80  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 180 IMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGKWLGG--RIQPLAIDGGSKDEIDQKLEG 257
Cdd:cd18063   46 ILADEMGLGKTIQTIALITYLMEHKRLNGPYL----IIVPLSTLSNWTYEFDKWAPSvvKISYKGTPAMRRSLVPQLRSG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 258 FMNqrgarvsspILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTS-RRVLISGTPIQNDLLEYF 336
Cdd:cd18063  122 KFN---------VLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELW 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 337 SLVHFVNSGILGTAHEFKKHFELPI-LKGRDAAASEADRQLgeeRLRELTSIVNRCLIRR 395
Cdd:cd18063  193 ALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETIL---IIRRLHKVLRPFLLRR 249
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
153-343 3.11e-17

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: 81.76  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVK-FLWEcvtSRRIPgsHGCIMADEMGLGKTLQCITLMW--------------TLLRQSPECKPEID----K 213
Cdd:cd18072    1 LLLHQKQALAwLLWR---ERQKP--RGGILADDMGLGKTLTMIALILaqkntqnrkeeekeKALTEWESKKDSTLvpsaG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 214 AVVVSPSSLVKNWYNEVGKWL-GGRIQPLAIDGGSKDEIDQKLEGFmnqrgarvssPILIISYETFRLHVGVLQKGSVGL 292
Cdd:cd18072   76 TLVVCPASLVHQWKNEVESRVaSNKLRVCLYHGPNRERIGEVLRDY----------DIVITTYSLVAKEIPTYKEESRSS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 293 ---------VICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVN 343
Cdd:cd18072  146 plfriawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
180-395 5.83e-17

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: 81.24  E-value: 5.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 180 IMADEMGLGKTLQCITLMWTLLRQSPECKPeidkAVVVSPSSLVKNWYNEVGKWlggriQPLAIDGGSKDEIDQKLEGFM 259
Cdd:cd18062   46 ILADEMGLGKTIQTIALITYLMEHKRINGP----FLIIVPLSTLSNWVYEFDKW-----APSVVKVSYKGSPAARRAFVP 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 260 NQRGARVSspILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTS-RRVLISGTPIQNDLLEYFSL 338
Cdd:cd18062  117 QLRSGKFN--VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWAL 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 216548193 339 VHFVNSGILGTAHEFKKHFELPI-LKGRDAAASEADRQLgeeRLRELTSIVNRCLIRR 395
Cdd:cd18062  195 LNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETIL---IIRRLHKVLRPFLLRR 249
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
153-395 5.86e-17

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


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 80.83  E-value: 5.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSrripGSHGcIMADEMGLGKTLQCITLMWTLLRQSPECKPEIdkavVVSPSSLVKNWYNEVGK 232
Cdd:cd18065   16 LRDYQVRGLNWMISLYEN----GVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPHM----VLVPKSTLHNWMNEFKR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 233 WLGGRIQPLAIdgGSKDeidqKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQAL 312
Cdd:cd18065   87 WVPSLRAVCLI--GDKD----ARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 313 DSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTAHEFKKHFelpilkgrdaaasEADRQLGEERLRE-LTSIVNRC 391
Cdd:cd18065  161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVErLHAVLKPF 227

                 ....
gi 216548193 392 LIRR 395
Cdd:cd18065  228 LLRR 231
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
153-341 9.53e-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: 62.75  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLwecvtsrRIPGShgcIMADEMGLGKTLQCITLM----------------WTLLRQSPECKPEIDKAV- 215
Cdd:cd18070    1 LLPYQRRAVNWM-------LVPGG---ILADEMGLGKTVEVLALIllhprpdndldaadddSDEMVCCPDCLVAETPVSs 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 216 ----VVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKlegfmnQRGARVSSP-ILIISYETFR--LHV------ 282
Cdd:cd18070   71 katlIVCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALAS------PAPEILAEYdIVVTTYDVLRteLHYaeanrs 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 216548193 283 ---GVLQKGSVGL-----------VICDEGHRLKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHF 341
Cdd:cd18070  145 nrrRRRQKRYEAPpsplvlvewwrVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSF 217
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
153-390 1.69e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 64.28  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRripGSHGCIMADeMGLGKTlqcITLMWTLLRQSpeckpEIDKAVVVSPS-SLVKNWYNEVG 231
Cdd:COG1061   81 LRPYQQEALEALLAALERG---GGRGLVVAP-TGTGKT---VLALALAAELL-----RGKRVLVLVPRrELLEQWAEELR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 232 KWLGgriqpLAIDGGSKDEIDqklegfmnqrgarvsSPILIISYETF--RLHVGVLQKgSVGLVICDEGHRLknSENQTY 309
Cdd:COG1061  149 RFLG-----DPLAGGGKKDSD---------------APITVATYQSLarRAHLDELGD-RFGLVIIDEAHHA--GAPSYR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 310 QALDSLNTSRRVLISGTPIQND----LLEYF-------SLVHFVNSGILGTAHEFKKHFELPILKGRDAAASEADRQL-- 376
Cdd:COG1061  206 RILEAFPAAYRLGLTATPFRSDgreiLLFLFdgivyeySLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERLREAla 285
                        250
                 ....*....|....*.
gi 216548193 377 -GEER-LRELTSIVNR 390
Cdd:COG1061  286 aDAERkDKILRELLRE 301
ResIII pfam04851
Type III restriction enzyme, res subunit;
151-328 1.02e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 58.07  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  151 KVLRPHQREGVKFLWECVTSRRipgSHGCI-MAdeMGLGKTLQCITLMWTLLRQSPeckpeIDKAVVVSPS-SLVKNWYN 228
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGQ---KRGLIvMA--TGSGKTLTAAKLIARLFKKGP-----IKKVLFLVPRkDLLEQALE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  229 EVGKWLGG-RIQPLAIDGGSKDEIdqklegfmnqrgaRVSSPILIISYETF--RLHVGVLQ--KGSVGLVICDEGHRLkN 303
Cdd:pfam04851  72 EFKKFLPNyVEIGEIISGDKKDES-------------VDDNKIVVTTIQSLykALELASLEllPDFFDVIIIDEAHRS-G 137
                         170       180
                  ....*....|....*....|....*
gi 216548193  304 SENQTyQALDSLNTSRRVLISGTPI 328
Cdd:pfam04851 138 ASSYR-NILEYFKPAFLLGLTATPE 161
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
153-345 2.72e-09

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: 57.74  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWEcvtSRRipgshGCIMADeMGLGKTLQCITLMWTLLRQSPeckpeIDKAVVVSPSSLVKN-WYNEVG 231
Cdd:cd18013    1 PHPYQKVAINFIIE---HPY-----CGLFLD-MGLGKTVTTLTALSDLQLDDF-----TRRVLVIAPLRVARStWPDEVE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 232 KWLGGRIQPLAIDGGSKdeidqklegfmNQRGARVSSP--ILIISYEtfRLHVGVLQKG---SVGLVICDEGHRLKNSEN 306
Cdd:cd18013   67 KWNHLRNLTVSVAVGTE-----------RQRSKAANTPadLYVINRE--NLKWLVNKSGdpwPFDMVVIDELSSFKSPRS 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 216548193 307 QTYQALDSLN--TSRRVLISGTPIQNDLLEYFSLVHFVNSG 345
Cdd:cd18013  134 KRFKALRKVRpvIKRLIGLTGTPSPNGLMDLWAQIALLDQG 174
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
153-327 1.61e-05

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: 45.37  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 153 LRPHQREGVKFLWECVTSRRipgshGCI-MAdeMGLGKTLQCITLMWTLLRqspeckpeiDKAVVVSPS-SLVKNWYNEV 230
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR-----GILvLP--TGSGKTLTALALIAYLKE---------LRTLIVVPTdALLDQWKERF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 231 GKWLGGRIQPLaIDGGSKDEIDqklegfmnqrgarvSSPILIISYET--FRLHVGVLQKGSVGLVICDEGHRLkNSEnqT 308
Cdd:cd17926   65 EDFLGDSSIGL-IGGGKKKDFD--------------DANVVVATYQSlsNLAEEEKDLFDQFGLLIVDEAHHL-PAK--T 126
                        170       180
                 ....*....|....*....|
gi 216548193 309 Y-QALDSLNTSRRVLISGTP 327
Cdd:cd17926  127 FsEILKELNAKYRLGLTATP 146
DpdE NF041062
protein DpdE;
182-343 2.82e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 47.66  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  182 ADEMGLGKTLQ-CITLMWTLLRqspecKPEiDKAVVVSPSSLVKNWynevgkwlggriqplaidggsKDEIDQK--LEGF 258
Cdd:NF041062  176 ADEVGLGKTIEaGLVIRQHLLD-----NPD-ARVLVLVPDALVRQW---------------------RRELRDKffLDDF 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  259 MNQRgarvsspILIISYETFRLhvgVLQKGSV-GLVICDEGHRL-------KNSENQTYQALDSL--NTSRRVLISGTPI 328
Cdd:NF041062  229 PGAR-------VRVLSHEEPER---WEPLLDApDLLVVDEAHQLarlawsgDPPERARYRELAALahAAPRLLLLSATPV 298
                         170
                  ....*....|....*
gi 216548193  329 QNDLLEYFSLVHFVN 343
Cdd:NF041062  299 LGNEETFLALLHLLD 313
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
186-330 3.19e-05

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.93  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  186 GLGKTLqciTLMWTLLRQSPECKPEIdKAVVVSPS-SLVKNWYNEV---GKWLGGRIQpLAIDGGSKDEIDQKLEGfmnq 261
Cdd:pfam00270  24 GSGKTL---AFLLPALEALDKLDNGP-QALVLAPTrELAEQIYEELkklGKGLGLKVA-SLLGGDSRKEQLEKLKG---- 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 216548193  262 rgarvsSPILIISYETFRLHVGVLQK-GSVGLVICDEGHRL--KNSENQTYQALDSLNTSRR-VLISGTPIQN 330
Cdd:pfam00270  95 ------PDILVGTPGRLLDLLQERKLlKNLKLLVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATLPRN 161
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
495-628 1.25e-04

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: 44.63  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193  495 SGKMLVLDYILAVTRSRSSDK---VVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIKKRAKV-VERFNSPSSPDFVFM 570
Cdd:pfam11496  89 SGKFLVLNDLVNLLIERDRKEpinVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVsDSGNKKIHSTTCHLL 168
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 216548193  571 -----LSSKAGGcgLNLIGANRLVMFDPDWNPANDEQAMARVWRDGQKKTCYIYRLLSAGTIE 628
Cdd:pfam11496 169 sstgqLTNDDSL--LENYKFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
177-326 3.37e-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: 41.62  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 177 HGCIMADEMGLGKTLqcITLMWTLLRqspeCKPEIDKAVVVSP-SSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKL 255
Cdd:cd00046    2 ENVLITAPTGSGKTL--AALLAALLL----LLKKGKKVLVLVPtKALALQTAERLRELFGPGIRVAVLVGGSSAEEREKN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548193 256 egfmnqrgARVSSPILIISYETFR---LHVGVLQKGSVGLVICDEGHRL------KNSENQTYQALDSLNtSRRVLISGT 326
Cdd:cd00046   76 --------KLGDADIIIATPDMLLnllLREDRLFLKDLKLIIVDEAHALlidsrgALILDLAVRKAGLKN-AQVILLSAT 146
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
76-123 1.70e-03

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


Pssm-ID: 430137  Cd Length: 180  Bit Score: 39.94  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 216548193   76 SILSKPFKVPIPNY-QGPLGSR----ALGLKR--AGVRRALHDPLEKDALVLYEP 123
Cdd:pfam08658  79 TVFRKSFSVPLKNKkQGAYNPRrpppTLGTRRgaIFVPRPLHDPTGEFAIVLYDP 133
 
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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