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Conserved domains on  [gi|528504085|ref|XP_688979|]
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DNA repair and recombination protein RAD54B [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13208550)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to Hamiltonella virus protein p41

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 308-542 2.03e-141

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


The actual alignment was detected with superfamily member cd18066:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 235  Bit Score: 419.64  E-value: 2.03e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:cd18066   81 KWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRLTGVFTLRR 542
Cdd:cd18066  161 IILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 308-799 1.65e-126

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 397.67  E-value: 1.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEcLMGMRLagrcGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpvMKRALVVCPGSLVKNWAAEFN 387
Cdd:COG0553  242 LRPYQLEGAAWLLF-LRRLGL----GGLLADDMGLGKTIQALALLLELKERGL------ARPVLIVAPTSLVGNWQRELA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTvDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:COG0553  311 KFAPGLRVLVLD-GTRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHR 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRqpscteeercigEERAAELFRLTGVFTLRRTQEII 547
Cdd:COG0553  390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDV 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 548 NQYLSERIEWTVFCKPTELQIRLYRVLLSTrpIRACLSGSHTYTHSPH-LVCINALKKLCNHPALLyntLQEKADemyeg 626
Cdd:COG0553  458 LKDLPEKTEETLYVELTPEQRALYEAVLEY--LRRELEGAEGIRRRGLiLAALTRLRQICSHPALL---LEEGAE----- 527

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 627 evkelfpeeystgafSTADSGKLLVLTDLLSAIqhVNRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQK 706
Cdd:COG0553  528 ---------------LSGRSAKLEALLELLEEL--LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 707 IVDSFN----------SPhsssfllllssKAGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFLTT 776
Cdd:COG0553  591 LVDRFQegpeapvfliSL-----------KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAE 659

                        490       500
                 ....*....|....*....|...
gi 528504085 777 GSIEEKIYQRQVSKQGLSGTVVD 799
Cdd:COG0553  660 GTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 308-542 2.03e-141

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: 419.64  E-value: 2.03e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:cd18066   81 KWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRLTGVFTLRR 542
Cdd:cd18066  161 IILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 308-799 1.65e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 397.67  E-value: 1.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEcLMGMRLagrcGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpvMKRALVVCPGSLVKNWAAEFN 387
Cdd:COG0553  242 LRPYQLEGAAWLLF-LRRLGL----GGLLADDMGLGKTIQALALLLELKERGL------ARPVLIVAPTSLVGNWQRELA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTvDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:COG0553  311 KFAPGLRVLVLD-GTRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHR 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRqpscteeercigEERAAELFRLTGVFTLRRTQEII 547
Cdd:COG0553  390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDV 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 548 NQYLSERIEWTVFCKPTELQIRLYRVLLSTrpIRACLSGSHTYTHSPH-LVCINALKKLCNHPALLyntLQEKADemyeg 626
Cdd:COG0553  458 LKDLPEKTEETLYVELTPEQRALYEAVLEY--LRRELEGAEGIRRRGLiLAALTRLRQICSHPALL---LEEGAE----- 527

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 627 evkelfpeeystgafSTADSGKLLVLTDLLSAIqhVNRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQK 706
Cdd:COG0553  528 ---------------LSGRSAKLEALLELLEEL--LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 707 IVDSFN----------SPhsssfllllssKAGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFLTT 776
Cdd:COG0553  591 LVDRFQegpeapvfliSL-----------KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAE 659

                        490       500
                 ....*....|....*....|...
gi 528504085 777 GSIEEKIYQRQVSKQGLSGTVVD 799
Cdd:COG0553  660 GTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 311-612 7.58e-70

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: 233.34  E-value: 7.58e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  311 HQKEGVVFLYECLMGMRlagrCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPvmkrALVVCPGSLVKNWAAEFNKWL 390
Cdd:pfam00176   1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGP----TLIVVPLSLLHNWMNEFERWV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  391 GRERISVY----TVDQDHRVEDFVSSPLC-SVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCT 465
Cdd:pfam00176  73 SPPALRVVvlhgNKRPQERWKNDPNFLADfDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  466 RRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPIlrsrqpscteeERCIGEERAAELFRLTGVFTLRRTQE 545
Cdd:pfam00176 153 NRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI-----------ERGGGKKGVSRLHKLLKPFLLRRTKK 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504085  546 IINQYLSERIEWTVFCKPTELQIRLYRVLLSTRPIRACLSG--SHTYTHSPhLVCINALKKLCNHPALL 612
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGegGREIKASL-LNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 335-820 2.00e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 247.02  E-value: 2.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  335 ILADEMGLGKTLQCVCVLWTLlrqgpYGGRPVMKRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRV---EDFVS 411
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYL-----HEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAhqrEELLV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  412 SPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:PLN03142  267 AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  492 GILGTSAAYRKIYeepilrsrQPSCTEEErcigEERAAELFRLTGVFTLRRTQEIINQYLSERIEWTVFCKPTELQIRLY 571
Cdd:PLN03142  347 EIFSSAETFDEWF--------QISGENDQ----QEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  572 RVLLStRPIRACLSGSHtytHSPHLVCINALKKLCNHPALlyntlqekademYEGevKELFPEeYSTGAFSTADSGKLLV 651
Cdd:PLN03142  415 KALLQ-KDLDVVNAGGE---RKRLLNIAMQLRKCCNHPYL------------FQG--AEPGPP-YTTGEHLVENSGKMVL 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  652 LTDLLSAIQHvnRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSSFLLLLSSKAGGVG 731
Cdd:PLN03142  476 LDKLLPKLKE--RDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  732 LNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFLTTGSIEEKIYQRQVSKQGLSGTVVDLTKKAEHISFSA 811
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633


                  ....*....
gi 528504085  812 EELRDLFRF 820
Cdd:PLN03142  634 DELLQMVRY 642
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 646-774 2.88e-48

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: 167.65  E-value: 2.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 646 SGKLLVLTDLLSAIQHvnRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPhSSSFLLLLSS 725
Cdd:cd18793   10 SGKLEALLELLEELRE--PGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLST 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528504085 726 KAGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFL 774
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
300-494 4.15e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 112.59  E-value: 4.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   300 IDPHLTNHLRPHQKEGVVFLYECLMGMrlagrcgaILADEMGLGKTLQCVCVLWTLLRQGPYggrpvmKRALVVCPG-SL 378
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV--------ILAAPTGSGKTLAALLPALEALKRGKG------GRVLVLVPTrEL 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   379 VKNWAAEFNKWLGR---ERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSV--DRLKELDFGVLICDEGHRLKNSN- 452
Cdd:smart00487  67 AEQWAEELKKLGPSlglKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGf 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 528504085   453 ---IKTAGALTAlSCTRRLILTGTP---VQNDLQEFYSIIEFVNPGIL 494
Cdd:smart00487 147 gdqLEKLLKLLP-KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFT 193
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 647-763 2.36e-18

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 81.10  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  647 GKLLVLTDLLsaiqHVNRTDRVVLVSNHTQTLDLlQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSsfllllssK 726
Cdd:pfam00271   1 EKLEALLELL----KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDvlv---atD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528504085  727 AGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDG 763
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
679-763 3.19e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.47  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   679 DLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSSFLLLlssKAGGVGLNLIGASHLVLYDIDWNPANDIQAMAR 758
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVAT---DVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 528504085   759 VWRDG 763
Cdd:smart00490  78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
308-582 1.59e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 68.13  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVvflyECLMGMRLAGRCGAILADEMGLGKTLqcvcVLWTLLRQGPYGgrpvmKRALVVCPG-SLVKNWAAEF 386
Cdd:COG1061   81 LRPYQQEAL----EALLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRG-----KRVLVLVPRrELLEQWAEEL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKWLGRERISVYTVDQDHRVedfvssplcsvLVISYEMLLRSvDRLKEL--DFGVLICDEGHRL-KNSNIKTAGALTAls 463
Cdd:COG1061  148 RRFLGDPLAGGGKKDSDAPI-----------TVATYQSLARR-AHLDELgdRFGLVIIDEAHHAgAPSYRRILEAFPA-- 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 464 cTRRLILTGTPVQNDLQEFYsIIEFVNPgilgtsaAYRKIYEE---------PILRSRQPSCTEEERCIGEERAAELFRL 534
Cdd:COG1061  214 -AYRLGLTATPFRSDGREIL-LFLFDGI-------VYEYSLKEaiedgylapPEYYGIRVDLTDERAEYDALSERLREAL 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504085 535 TGvfTLRRTQEIINQYLSERIEWT---VFCKPTElQIRLYRVLLSTRPIRA 582
Cdd:COG1061  285 AA--DAERKDKILRELLREHPDDRktlVFCSSVD-HAEALAELLNEAGIRA 332
DpdE NF041062
protein DpdE;
336-482 9.29e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 56.13  E-value: 9.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  336 LADEMGLGKTLQ-CVCVLWTLLRQGpyggrpvMKRALVVCPGSLVKNWAAEFnkwlgRERIsvytvdqdhRVEDFvssPL 414
Cdd:NF041062  175 LADEVGLGKTIEaGLVIRQHLLDNP-------DARVLVLVPDALVRQWRREL-----RDKF---------FLDDF---PG 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504085  415 CSVLVISYEMLLRSVDRLKELDFgvLICDEGHRL----KNSNIKTAG---ALTAL--SCTRRLILTGTPVQNDLQEF 482
Cdd:NF041062  231 ARVRVLSHEEPERWEPLLDAPDL--LVVDEAHQLarlaWSGDPPERAryrELAALahAAPRLLLLSATPVLGNEETF 305
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
307-448 1.95e-04

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 45.21  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 307 HLRPHQkegvvfLY---EclMGMRLAGRcgAILADEMGLGKTLQCVCVLWTLLrqgpYGGRpvMKRALVVCPGSLVKNWA 383
Cdd:PRK04914 152 SLIPHQ------LYiahE--VGRRHAPR--VLLADEVGLGKTIEAGMIIHQQL----LTGR--AERVLILVPETLQHQWL 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504085 384 AE----FNkwLgreRISVYtvDQDhRVEDFVSSP----LCSVLVI-SYEMLLRSVDRLKEL---DFGVLICDEGHRL 448
Cdd:PRK04914 216 VEmlrrFN--L---RFSLF--DEE-RYAEAQHDAdnpfETEQLVIcSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHL 284
 
Name Accession Description Interval E-value
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 308-542 2.03e-141

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: 419.64  E-value: 2.03e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:cd18066   81 KWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRLTGVFTLRR 542
Cdd:cd18066  161 IILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 308-799 1.65e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 397.67  E-value: 1.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEcLMGMRLagrcGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpvMKRALVVCPGSLVKNWAAEFN 387
Cdd:COG0553  242 LRPYQLEGAAWLLF-LRRLGL----GGLLADDMGLGKTIQALALLLELKERGL------ARPVLIVAPTSLVGNWQRELA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTvDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:COG0553  311 KFAPGLRVLVLD-GTRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHR 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRqpscteeercigEERAAELFRLTGVFTLRRTQEII 547
Cdd:COG0553  390 LALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDV 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 548 NQYLSERIEWTVFCKPTELQIRLYRVLLSTrpIRACLSGSHTYTHSPH-LVCINALKKLCNHPALLyntLQEKADemyeg 626
Cdd:COG0553  458 LKDLPEKTEETLYVELTPEQRALYEAVLEY--LRRELEGAEGIRRRGLiLAALTRLRQICSHPALL---LEEGAE----- 527

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 627 evkelfpeeystgafSTADSGKLLVLTDLLSAIqhVNRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQK 706
Cdd:COG0553  528 ---------------LSGRSAKLEALLELLEEL--LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 707 IVDSFN----------SPhsssfllllssKAGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFLTT 776
Cdd:COG0553  591 LVDRFQegpeapvfliSL-----------KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAE 659

                        490       500
                 ....*....|....*....|...
gi 528504085 777 GSIEEKIYQRQVSKQGLSGTVVD 799
Cdd:COG0553  660 GTIEEKILELLEEKRALAESVLG 682
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 308-542 2.84e-122

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: 370.46  E-value: 2.84e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGgRPVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYG-KPTAKKALIVCPSSLVGNWKAEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFV-----SSPLCSVLVISYEMLLRSVDRLKEL-DFGVLICDEGHRLKNSNIKTAGALTA 461
Cdd:cd18004   80 KWLGLRRIKVVTADGNAKDVKASldffsSASTYPVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKTTKALNS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 462 LSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRLTGVFTLR 541
Cdd:cd18004  160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239


                 .
gi 528504085 542 R 542
Cdd:cd18004  240 R 240
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 308-542 3.85e-87

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: 278.20  E-value: 3.85e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGgRPVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQC-KPEIDKAIVVSPSSLVKNWANELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGReRISVYTVDQDHRVEDF-------------VSSPlcsVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIK 454
Cdd:cd18067   80 KWLGG-RLQPLAIDGGSKKEIDrklvqwasqqgrrVSTP---VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 455 TAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRL 534
Cdd:cd18067  156 TYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISI 235


                 ....*...
gi 528504085 535 TGVFTLRR 542
Cdd:cd18067  236 VNRCIIRR 243
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 311-612 7.58e-70

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: 233.34  E-value: 7.58e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  311 HQKEGVVFLYECLMGMRlagrCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPvmkrALVVCPGSLVKNWAAEFNKWL 390
Cdd:pfam00176   1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGP----TLIVVPLSLLHNWMNEFERWV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  391 GRERISVY----TVDQDHRVEDFVSSPLC-SVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCT 465
Cdd:pfam00176  73 SPPALRVVvlhgNKRPQERWKNDPNFLADfDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  466 RRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPIlrsrqpscteeERCIGEERAAELFRLTGVFTLRRTQE 545
Cdd:pfam00176 153 NRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI-----------ERGGGKKGVSRLHKLLKPFLLRRTKK 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504085  546 IINQYLSERIEWTVFCKPTELQIRLYRVLLSTRPIRACLSG--SHTYTHSPhLVCINALKKLCNHPALL 612
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGegGREIKASL-LNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 335-820 2.00e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 247.02  E-value: 2.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  335 ILADEMGLGKTLQCVCVLWTLlrqgpYGGRPVMKRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRV---EDFVS 411
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYL-----HEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAhqrEELLV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  412 SPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:PLN03142  267 AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  492 GILGTSAAYRKIYeepilrsrQPSCTEEErcigEERAAELFRLTGVFTLRRTQEIINQYLSERIEWTVFCKPTELQIRLY 571
Cdd:PLN03142  347 EIFSSAETFDEWF--------QISGENDQ----QEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  572 RVLLStRPIRACLSGSHtytHSPHLVCINALKKLCNHPALlyntlqekademYEGevKELFPEeYSTGAFSTADSGKLLV 651
Cdd:PLN03142  415 KALLQ-KDLDVVNAGGE---RKRLLNIAMQLRKCCNHPYL------------FQG--AEPGPP-YTTGEHLVENSGKMVL 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  652 LTDLLSAIQHvnRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSSFLLLLSSKAGGVG 731
Cdd:PLN03142  476 LDKLLPKLKE--RDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  732 LNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFLTTGSIEEKIYQRQVSKQGLSGTVVDLTKKAEHISFSA 811
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633


                  ....*....
gi 528504085  812 EELRDLFRF 820
Cdd:PLN03142  634 DELLQMVRY 642
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 308-491 1.20e-64

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: 215.12  E-value: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEclmgmRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd17919    1 LRPYQLEGLNFLLE-----LYENGPGGILADEMGLGKTLQAIAFLAYLLKEGK-----ERGPVLVVCPLSVLENWEREFE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPLCS--VLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCT 465
Cdd:cd17919   71 KWTPDLRVVVYHGSQRERAQIRAKEKLDKfdVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAK 150

                        170       180
                 ....*....|....*....|....*.
gi 528504085 466 RRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd17919  151 RRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 308-542 4.80e-55

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: 191.05  E-value: 4.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRlagrcGAILADEMGLGKTLQCVCVLWTLLRQgPYGGRPVM----------------KRAL 371
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGR-----GGILGDDMGLGKTVQVIAFLAAVLGK-TGTRRDREnnrprfkkkppassakKPVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 372 VVCPGSLVKNWAAEFNKWlGRERISVYTVDQDHRV-EDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKN 450
Cdd:cd18005   75 IVAPLSVLYNWKDELDTW-GHFEVGVYHGSRKDDElEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 451 SNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAE 530
Cdd:cd18005  154 PKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQE 233

                        250
                 ....*....|..
gi 528504085 531 LFRLTGVFTLRR 542
Cdd:cd18005  234 LAVKLSKFFLRR 245
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 308-521 1.57e-54

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: 189.04  E-value: 1.57e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRL---AGRcGAILADEMGLGKTLQCVCVLWTLLRQGPYGgrpvmKRALVVCPGSLVKNWAA 384
Cdd:cd18007    1 LKPHQVEGVRFLWSNLVGTDVgsdEGG-GCILAHTMGLGKTLQVITFLHTYLAAAPRR-----SRPLVLCPASTLYNWED 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 385 EFNKWLGRERISVY---------TVDQDHR-VEDFVSSPlcSVLVISYEMLLR------SVDRLKELDF--------GVL 440
Cdd:cd18007   75 EFKKWLPPDLRPLLvlvslsaskRADARLRkINKWHKEG--GVLLIGYELFRNlasnatTDPRLKQEFIaalldpgpDLL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 441 ICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEE 520
Cdd:cd18007  153 VLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEED 232


                 .
gi 528504085 521 R 521
Cdd:cd18007  233 V 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 308-542 5.86e-51

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: 179.10  E-value: 5.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmGMRLAGRcGAILADEMGLGKTLQCVCVLWTLLRQGpyggrpVMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18001    1 LYPHQREGVAWLW----SLHDGGK-GGILADDMGLGKTVQICAFLSGMFDSG------LIKSVLVVMPTSLIPHWVKEFA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVY--------TVDQDHRVEDFvssplcSVLVISYEMLLRSVDRLKELDFG-----VLICDEGHRLKNSNIK 454
Cdd:cd18001   70 KWTPGLRVKVFhgtskkerERNLERIQRGG------GVLLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNSKTK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 455 TAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPG-ILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFR 533
Cdd:cd18001  144 SAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQ 223


                 ....*....
gi 528504085 534 LTGVFTLRR 542
Cdd:cd18001  224 IIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 646-774 2.88e-48

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: 167.65  E-value: 2.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 646 SGKLLVLTDLLSAIQHvnRTDRVVLVSNHTQTLDLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPhSSSFLLLLSS 725
Cdd:cd18793   10 SGKLEALLELLEELRE--PGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLST 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528504085 726 KAGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDGQKKTVHIYRFL 774
Cdd:cd18793   87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 308-543 3.27e-48

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: 170.44  E-value: 3.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGvvflYECLMGMRLAGrCGAILADEMGLGKTLQCVCVLwtLLRQGPYGGRPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18012    5 LRPYQKEG----FNWLSFLRHYG-LGGILADDMGLGKTLQTLALL--LSRKEEGRKGPS----LVVAPTSLIYNWEEEAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPLcSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:cd18012   74 KFAPELKVLVIHGTKRKREKLRALEDY-DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQpscteeercigEERAAELFRLTGVFTLRRT 543
Cdd:cd18012  153 LALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEELKKLISPFILRRL 217
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 308-542 1.34e-47

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 169.45  E-value: 1.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLyECLMGMRLAGrcgaILADEMGLGKTLQCVCVLWT--LLRQGPYGGRPVmkRALVVCPGSLVKNWAAE 385
Cdd:cd17999    1 LRPYQQEGINWL-AFLNKYNLHG----ILCDDMGLGKTLQTLCILASdhHKRANSFNSENL--PSLVVCPPTLVGHWVAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 386 FNKWLGRE--RISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALS 463
Cdd:cd17999   74 IKKYFPNAflKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504085 464 CTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTEEERCIGEERAAELFRLTGVFTLRR 542
Cdd:cd17999  154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 308-509 4.74e-41

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: 150.74  E-value: 4.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLY----ECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpvMKRALVVCPGSLVKNWA 383
Cdd:cd18069    1 LKPHQIGGIRFLYdniiESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTG------AKTVLAIVPVNTLQNWL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 384 AEFNKWLGRER---------ISVYTVDQDHRVEDFVSSPLCS------VLVISYEMLlrsvdRLKEldfG--VLICDEGH 446
Cdd:cd18069   75 SEFNKWLPPPEalpnvrprpFKVFILNDEHKTTAARAKVIEDwvkdggVLLMGYEMF-----RLRP---GpdVVICDEGH 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504085 447 RLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPIL 509
Cdd:cd18069  147 RIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 308-520 1.06e-40

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: 150.42  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEC----LMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGrpvMKRALVVCPGSLVKNWA 383
Cdd:cd18068    1 LKPHQVDGVQFMWDCccesLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLEN---FSRVLVVCPLNTVLNWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 384 AEFNKWL----GRERISVYTVDQDHRVEDFV-----SSPLCSVLVISYEML--------LRSVDRLKE------LDFG-- 438
Cdd:cd18068   78 NEFEKWQeglkDEEKIEVNELATYKRPQERSyklqrWQEEGGVMIIGYDMYrilaqernVKSREKLKEifnkalVDPGpd 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 439 VLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRQPSCTE 518
Cdd:cd18068  158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTL 237


                 ..
gi 528504085 519 EE 520
Cdd:cd18068  238 VD 239
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 308-542 1.03e-39

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: 146.43  E-value: 1.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRlagrcGAILADEMGLGKTLQCVCVLWTLlrqgpyGGRPVMKRA-LVVCPGSLVKNWAAEF 386
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQH-----GCILGDEMGLGKTCQTISLLWYL------AGRLKLLGPfLVLCPLSVLDNWKEEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKWLGRERISVYTVDQDHRVE---DFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALS 463
Cdd:cd18006   70 NRFAPDLSVITYMGDKEKRLDlqqDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 464 CTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSA------AYRKIYEEPilrsrqpscteeercigeERAAELFRLTGV 537
Cdd:cd18006  150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKlddfikAYSETDDES------------------ETVEELHLLLQP 211


                 ....*
gi 528504085 538 FTLRR 542
Cdd:cd18006  212 FLLRR 216
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 308-542 5.04e-37

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 139.44  E-value: 5.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVvflyECLMGMRLAGRCGaILADEMGLGKTLQCVCVLWTLLRQGPYGgrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18009    4 MRPYQLEGM----EWLRMLWENGING-ILADEMGLGKTIQTIALLAHLRERGVWG--PF----LVIAPLSTLPNWVNEFA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRvEDFV--------SSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGAL 459
Cdd:cd18009   73 RFTPSVPVLLYHGTKEER-ERLRkkimkregTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 460 TALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPILRSRqpscTEEERCIGEERAAELFR-LTGV- 537
Cdd:cd18009  152 KTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDN----AADISNLSEEREQNIVHmLHAIl 227


                 ....*..
gi 528504085 538 --FTLRR 542
Cdd:cd18009  228 kpFLLRR 234
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 308-491 5.14e-37

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: 137.84  E-value: 5.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYEclmgmrLAG-RCGAILADEMGLGKTLQCVCVLWTLlrqgpYGGRPVMKRALVVCPGSLVKNWAAEF 386
Cdd:cd18000    1 LFKYQQTGVQWLWE------LHCqRVGGILGDEMGLGKTIQIIAFLAAL-----HHSKLGLGPSLIVCPATVLKQWVKEF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKWLGRERISV------YTVDQDHRVEDFVSSPLCS-------VLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNI 453
Cdd:cd18000   70 HRWWPPFRVVVlhssgsGTGSEEKLGSIERKSQLIRkvvgdggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528504085 454 KTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd18000  150 EITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 308-500 1.37e-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: 137.76  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLmgmrLAGRcGAILADEMGLGKTLQCVCVLWTLLRQGPYGGrPvmkrALVVCPGSLVKNWAAEFN 387
Cdd:cd17995    1 LRDYQLEGVNWLLFNW----YNRR-NCILADEMGLGKTIQSIAFLEHLYQVEGIRG-P----FLVIAPLSTIPNWQREFE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWL------------GRERISVY-------TVDQDHRVEDFvssplcSVLVISYEMLLRSVDRLKELDFGVLICDEGHRL 448
Cdd:cd17995   71 TWTdmnvvvyhgsgeSRQIIQQYemyfkdaQGRKKKGVYKF------DVLITTYEMVIADAEELRKIPWRVVVVDEAHRL 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504085 449 KNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAY 500
Cdd:cd17995  145 KNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEF 196
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 308-504 8.37e-36

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: 135.03  E-value: 8.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFlyeclmGMRLAGRCgaILADEMGLGKTLQCVCVLWTLLRQGPyggrpvmkrALVVCPGSLVKNWAAEFN 387
Cdd:cd18010    1 LLPFQREGVCF------ALRRGGRV--LIADEMGLGKTVQAIAIAAYYREEWP---------LLIVCPSSLRLTWADEIE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLgreriSVYTVDQDHRVE---DFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTAL-- 462
Cdd:cd18010   64 RWL-----PSLPPDDIQVIVkskDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlk 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528504085 463 SCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIY 504
Cdd:cd18010  139 RAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRY 180
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 308-488 1.34e-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: 132.41  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFlyeclmgMRLagrCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGRPVMKRA------------LVVCP 375
Cdd:cd18008    1 LLPYQKQGLAW-------MLP---RGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSsdpkklylskttLIVVP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 376 GSLVKNWAAEFNKWLGRERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGV---------------- 439
Cdd:cd18008   71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPKNKKGGGRDskekeasplhrirwyr 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504085 440 LICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEF 488
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRF 199
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 335-542 4.43e-32

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: 124.79  E-value: 4.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLWTLLR----QGPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVY--TVDQDHRVED 408
Cdd:cd17996   26 ILADEMGLGKTIQTISLITYLMEkkknNGPY---------LVIVPLSTLSNWVSEFEKWAPSVSKIVYkgTPDVRKKLQS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 409 FVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTR-RLILTGTPVQNDLQEFYSIIE 487
Cdd:cd17996   97 QIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARyRLLLTGTPLQNNLPELWALLN 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504085 488 FVNPGILGTSAAYRKIYEEPILR---SRQPSCTEEERCIGEERAAELFRltgVFTLRR 542
Cdd:cd17996  177 FLLPKIFKSCKTFEQWFNTPFANtgeQVKIELNEEETLLIIRRLHKVLR---PFLLRR 231
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 335-544 4.79e-32

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: 124.36  E-value: 4.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLwTLLRQ-----GPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRvEDF 409
Cdd:cd17997   26 ILADEMGLGKTLQTISLL-GYLKHykninGPH---------LIIVPKSTLDNWMREFKRWCPSLRVVVLIGDKEER-ADI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 410 VSSPLCS----VLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSI 485
Cdd:cd17997   95 IRDVLLPgkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWAL 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504085 486 IEFVNPGILGTSAAYRKIYeepilrsrqpsctEEERCIGE--ERAAELFRLTGVFTLRRTQ 544
Cdd:cd17997  175 LNFLLPDVFTSSEDFDEWF-------------NVNNCDDDnqEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 308-494 6.25e-31

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: 120.18  E-value: 6.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLyECLMGMRLAGrcgaILADEMGLGKTLQCVCVLWTLLRQGPYGGRpvmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd17998    1 LKDYQLIGLNWL-NLLYQKKLSG----ILADEMGLGKTIQVIAFLAYLKEIGIPGPH------LVVVPSSTLDNWLREFK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHR----------VEDFvssplcSVLVISYEMLL-RSVDR--LKELDFGVLICDEGHRLKNSNIK 454
Cdd:cd17998   70 RWCPSLKVEPYYGSQEERkhlrydilkgLEDF------DVIVTTYNLATsNPDDRsfFKRLKLNYVVYDEGHMLKNMTSE 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528504085 455 TAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFV--NPGIL 494
Cdd:cd17998  144 RYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFImpKPFIL 185
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 308-542 2.33e-29

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 116.68  E-value: 2.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGV---VFLYEclmgMRLAGrcgaILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVK 380
Cdd:cd18003    1 LREYQHIGLdwlATLYE----KNLNG----ILADEMGLGKTIQTIALLAHLACEkgnwGPH---------LIVVPTSVML 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 381 NWAAEFNKWLGRERISVYTVDQDHRVEDFV--SSPLC-SVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAG 457
Cdd:cd18003   64 NWEMEFKRWCPGFKILTYYGSAKERKLKRQgwMKPNSfHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 458 ALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRKIYEEPIlrsRQPSctEEERCIGEERAAELFRLTGV 537
Cdd:cd18003  144 TLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL---TAMS--EGSQEENEELVRRLHKVLRP 218


                 ....*
gi 528504085 538 FTLRR 542
Cdd:cd18003  219 FLLRR 223
DEXDc smart00487
DEAD-like helicases superfamily;
300-494 4.15e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 112.59  E-value: 4.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   300 IDPHLTNHLRPHQKEGVVFLYECLMGMrlagrcgaILADEMGLGKTLQCVCVLWTLLRQGPYggrpvmKRALVVCPG-SL 378
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV--------ILAAPTGSGKTLAALLPALEALKRGKG------GRVLVLVPTrEL 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   379 VKNWAAEFNKWLGR---ERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSV--DRLKELDFGVLICDEGHRLKNSN- 452
Cdd:smart00487  67 AEQWAEELKKLGPSlglKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGf 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 528504085   453 ---IKTAGALTAlSCTRRLILTGTP---VQNDLQEFYSIIEFVNPGIL 494
Cdd:smart00487 147 gdqLEKLLKLLP-KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFT 193
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 335-492 1.43e-27

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: 111.29  E-value: 1.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHR----- 405
Cdd:cd17993   24 ILADEMGLGKTVQTISFLSYLFHSqqqyGPF---------LVVVPLSTMPAWQREFAKWAPDMNVIVYLGDIKSRdtire 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 406 VEDFVSS--PL-CSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEF 482
Cdd:cd17993   95 YEFYFSQtkKLkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKEL 174

                        170
                 ....*....|
gi 528504085 483 YSIIEFVNPG 492
Cdd:cd17993  175 WALLHFLMPG 184
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 308-491 2.22e-27

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 110.22  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLmgmrlAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd17994    1 LHPYQLEGLNWLRFSW-----AQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKG-PF----LVSAPLSTIINWEREFE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLgrERISVYTVDQDHrvedfvssplcsVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRR 467
Cdd:cd17994   71 MWA--PDFYVVTYVGDH------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYK 136

                        170       180
                 ....*....|....*....|....
gi 528504085 468 LILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd17994  137 LLLTGTPLQNNLEELFHLLNFLTP 160
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 308-492 5.13e-27

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: 109.30  E-value: 5.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVvflyecLMGMRLaGRCGAILADEMGLGKTLQCVCVLWTLLRQGPyggrpvMKRALVVCPGSLVKNWAAEFN 387
Cdd:cd18011    1 PLPHQIDAV------LRALRK-PPVRLLLADEVGLGKTIEAGLIIKELLLRGD------AKRVLILCPASLVEQWQDELQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRVEDFVSSPL-CSVLVISYEMLLRSVDR---LKELDFGVLICDEGHRLKNSNIKTAGALTAL- 462
Cdd:cd18011   68 DKFGLPFLILDRETAAQLRRLIGNPFEeFPIVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLg 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 528504085 463 -----SCTRRLILTGTPVQNDLQEFYSIIEFVNPG 492
Cdd:cd18011  148 rllakRARHVLLLTATPHNGKEEDFRALLSLLDPG 182
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 334-554 1.48e-26

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: 109.37  E-value: 1.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 334 AILADEMGLGKTLQCVCVLWTLLRQgpyggRPVMKRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHR---VEDFV 410
Cdd:cd18064   37 GILADEMGLGKTLQTISLLGYMKHY-----RNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRaafVRDVL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 411 SSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVN 490
Cdd:cd18064  112 LPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLL 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504085 491 PGILGTSAAYRKIYeepilrsrqpsctEEERCIGEERAAE-LFRLTGVFTLRRTQEIINQYLSER 554
Cdd:cd18064  192 PDVFNSAEDFDSWF-------------DTNNCLGDQKLVErLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 308-502 1.58e-25

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: 105.91  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmgMRLAGRCGAILADEMGLGKTLQCVCVLWTLLR---QGPYggrpvmkraLVVCPGSLVKNWAA 384
Cdd:cd18060    1 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSIAFLQEVYNvgiHGPF---------LVIAPLSTITNWER 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 385 EFNKWL------------GRERISVYTVD-QDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNS 451
Cdd:cd18060   67 EFNTWTemntivyhgslaSRQMIQQYEMYcKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504085 452 NIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAYRK 502
Cdd:cd18060  147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLK 197
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 334-544 1.66e-25

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


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 105.87  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 334 AILADEMGLGKTLQCVCVLWTLLRQgpyggRPVMKRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHR---VEDFV 410
Cdd:cd18065   37 GILADEMGLGKTLQTIALLGYLKHY-----RNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVCLIGDKDARaafIRDVM 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 411 SSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVN 490
Cdd:cd18065  112 MPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLL 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504085 491 PGILGTSAAYRKIYeepilrsrqpsctEEERCIGEERAAElfRLTGV---FTLRRTQ 544
Cdd:cd18065  192 PDVFNSADDFDSWF-------------DTKNCLGDQKLVE--RLHAVlkpFLLRRIK 233
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 308-500 4.26e-25

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: 104.35  E-value: 4.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmgMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGgrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18058    1 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRG--PF----LIIAPLSTITNWEREFR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KW------------LGRERISVYtvDQDHRveDFVSSPLCSV-----LVISYEMLLRSVDRLKELDFGVLICDEGHRLKN 450
Cdd:cd18058   70 TWtemnaivyhgsqISRQMIQQY--EMYYR--DEQGNPLSGIfkfqvVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504085 451 SNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPGILGTSAAY 500
Cdd:cd18058  146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTF 195
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 308-491 1.39e-24

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: 103.22  E-value: 1.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmgMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGGrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18056    1 LHPYQLEGLNWLR-----FSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKG-PF----LVSAPLSTIINWEREFE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLGRERISVYTVDQDHRV---------EDFV-------------SSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEG 445
Cdd:cd18056   71 MWAPDMYVVTYVGDKDSRAiirenefsfEDNAirggkkasrmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504085 446 HRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd18056  151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 308-491 7.75e-24

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: 101.24  E-value: 7.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYE--ClmgmrlagRCGA-ILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVK 380
Cdd:cd18054   21 LRDYQLEGLNWLAHswC--------KNNSvILADEMGLGKTIQTISFLSYLFHQhqlyGPF---------LLVVPLSTLT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 381 NWAAEFNKWLGRERISVYTVD----QDHRVEDFVSSPL----CSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSN 452
Cdd:cd18054   84 SWQREFEIWAPEINVVVYIGDlmsrNTIREYEWIHSQTkrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDD 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504085 453 IKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd18054  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP 202
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 335-491 1.72e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 100.09  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLWTLLRQGPYGGrPVmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRV-------- 406
Cdd:cd18055   23 ILADEMGLGKTIQTIVFLYSLYKEGHTKG-PF----LVSAPLSTIINWEREFQMWAPDFYVVTYTGDKDSRAiirenefs 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 407 -EDFV------------SSPL-CSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTG 472
Cdd:cd18055   98 fDDNAvkggkkafkmkrEAQVkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTG 177

                        170
                 ....*....|....*....
gi 528504085 473 TPVQNDLQEFYSIIEFVNP 491
Cdd:cd18055  178 TPLQNNLEELFHLLNFLTP 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 334-556 1.80e-23

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: 100.50  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 334 AILADEMGLGKTLQCVCVLWTLLR----QGPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRvEDF 409
Cdd:cd18062   45 GILADEMGLGKTIQTIALITYLMEhkriNGPF---------LIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAAR-RAF 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 410 V---SSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGAL-TALSCTRRLILTGTPVQNDLQEFYSI 485
Cdd:cd18062  115 VpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWAL 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504085 486 IEFVNPGILGTSAAYRKIYEEPIlrsrqpSCTEEERCIGEERAaelfrltgVFTLRRTQEIINQYLSERIE 556
Cdd:cd18062  195 LNFLLPTIFKSCSTFEQWFNAPF------AMTGEKVDLNEEET--------ILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 308-492 2.04e-23

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: 99.72  E-value: 2.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRlagrcGAILADEMGLGKTLQCVCVLWTLLRQGPYGgrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTR-----NCILADEMGLGKTIQSITFLYEIYLKGIHG--PF----LVIAPLSTIPNWEREFR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KWLgRERISVYTVDQDHR-----VEDFVSSPLCSVL---------VISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNI 453
Cdd:cd18059   70 TWT-ELNVVVYHGSQASRrtiqlYEMYFKDPQGRVIkgsykfhaiITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNC 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504085 454 KTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNPG 492
Cdd:cd18059  149 KLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS 187
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 308-491 2.38e-23

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: 99.31  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmgMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYGgrPVmkraLVVCPGSLVKNWAAEFN 387
Cdd:cd18061    1 LREYQLEGLNWLL-----FNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRG--PF----LIIAPLSTIANWEREFR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 388 KW------------LGRERISVYTV---DQDHRVedFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSN 452
Cdd:cd18061   70 TWtdlnvvvyhgslISRQMIQQYEMyfrDSQGRI--IRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKN 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504085 453 IKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd18061  148 CKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 334-556 2.41e-23

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


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 100.14  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 334 AILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVKNWAAEFNKWL-GRERISVYTVDQDHR--V 406
Cdd:cd18063   45 GILADEMGLGKTIQTIALITYLMEHkrlnGPY---------LIIVPLSTLSNWTYEFDKWApSVVKISYKGTPAMRRslV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 407 EDFVSSPLcSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGAL-TALSCTRRLILTGTPVQNDLQEFYSI 485
Cdd:cd18063  116 PQLRSGKF-NVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRILLTGTPLQNKLPELWAL 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504085 486 IEFVNPGILGTSAAYRKIYEEPIlrsrqpSCTEEERCIGEERAaelfrltgVFTLRRTQEIINQYLSERIE 556
Cdd:cd18063  195 LNFLLPTIFKSCSTFEQWFNAPF------AMTGERVDLNEEET--------ILIIRRLHKVLRPFLLRRLK 251
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 308-490 3.02e-23

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: 99.48  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEgvvflyeCLMGMRLAGR---CGAILADEMGLGKTLQCVCVL-----------------WTLLRQGPYGGRPVM 367
Cdd:cd18072    1 LLLHQKQ-------ALAWLLWRERqkpRGGILADDMGLGKTLTMIALIlaqkntqnrkeeekekaLTEWESKKDSTLVPS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 368 KRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRVEDFVSSPLCSVLVISYEMLLRSVDRLKELD-----FGV--- 439
Cdd:cd18072   74 AGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEESrssplFRIawa 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504085 440 -LICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVN 490
Cdd:cd18072  154 rIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 308-491 1.79e-22

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: 97.06  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYeclmgMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQG----PYggrpvmkraLVVCPGSLVKNWA 383
Cdd:cd18057    1 LHPYQLEGLNWLR-----FSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhskgPY---------LVSAPLSTIINWE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 384 AEFNKWLGRERISVYTVDQDHRVE------DFVSSPLCS----------------VLVISYEMLLRSVDRLKELDFGVLI 441
Cdd:cd18057   67 REFEMWAPDFYVVTYTGDKESRSVirenefSFEDNAIRSgkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLV 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504085 442 CDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEFVNP 491
Cdd:cd18057  147 VDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 335-542 3.63e-22

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: 96.03  E-value: 3.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHR--VED 408
Cdd:cd18002   23 ILADEMGLGKTVQSIAVLAHLAEEhniwGPF---------LVIAPASTLHNWQQEISRFVPQFKVLPYWGNPKDRkvLRK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 409 FVS--------SPLcSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQ 480
Cdd:cd18002   94 FWDrknlytrdAPF-HVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMA 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504085 481 EFYSIIEFVNPGILGTSAAYRKIYEEPIlrsrqPSCTEEERCIGEERAAELFRLTGVFTLRR 542
Cdd:cd18002  173 ELWALLHFIMPTLFDSHDEFNEWFSKDI-----ESHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 333-489 3.32e-19

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: 87.91  E-value: 3.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 333 GAILADEMGLGKTLQCVCVLwtllrqgpyggrpVMKRALVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHRVEDFVSS 412
Cdd:cd18071   50 GGILADDMGLGKTLTTISLI-------------LANFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 413 PLCSVLVISYEMLlrSVDRLKELDFGV-------LICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSI 485
Cdd:cd18071  117 SKYDIVLTTYNTL--ASDFGAKGDSPLhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194


                 ....
gi 528504085 486 IEFV 489
Cdd:cd18071  195 LSFL 198
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 335-491 1.73e-18

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: 85.87  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 335 ILADEMGLGKTLQCVCVLWTLLRQ----GPYggrpvmkraLVVCPGSLVKNWAAEFNKWLGRERISVYTVDQDHR----- 405
Cdd:cd18053   43 ILADEMGLGKTIQTISFLNYLFHEhqlyGPF---------LLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRnmirt 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 406 ---VEDFVSSPLCSVLVISYEMLLRSVDRLKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEF 482
Cdd:cd18053  114 hewMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKEL 193


                 ....*....
gi 528504085 483 YSIIEFVNP 491
Cdd:cd18053  194 WSLLHFIMP 202
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 647-763 2.36e-18

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 81.10  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  647 GKLLVLTDLLsaiqHVNRTDRVVLVSNHTQTLDLlQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSsfllllssK 726
Cdd:pfam00271   1 EKLEALLELL----KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDvlv---atD 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528504085  727 AGGVGLNLIGASHLVLYDIDWNPANDIQAMARVWRDG 763
Cdd:pfam00271  73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 308-513 2.84e-15

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: 75.85  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLmgmrlagRCGAILadEMGLGKTLQCVCVLWTLLRQGPYGgrpvmkRALVVCPGSLVKN-WAAEF 386
Cdd:cd18013    1 PHPYQKVAINFIIEHP-------YCGLFL--DMGLGKTVTTLTALSDLQLDDFTR------RVLVIAPLRVARStWPDEV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKW-------------LGRERISVYTVDQDhrvedfvssplcsVLVISYEMLLRSVDRLKEL-DFGVLICDEGHRLKNSN 452
Cdd:cd18013   66 EKWnhlrnltvsvavgTERQRSKAANTPAD-------------LYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPR 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504085 453 IKTAGALTALS-CTRRLI-LTGTPVQNDLQEFYSIIEFVNPG-ILGTS-AAYRKIYEEPILRSRQ 513
Cdd:cd18013  133 SKRFKALRKVRpVIKRLIgLTGTPSPNGLMDLWAQIALLDQGeRLGRSiTAYRERWFDPDKRNGQ 197
HELICc smart00490
helicase superfamily c-terminal domain;
679-763 3.19e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.47  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085   679 DLLQDVCDQIGYKWCRLDGQTPVGQRQKIVDSFNSPHSSSFLLLlssKAGGVGLNLIGASHLVLYDIDWNPANDIQAMAR 758
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVAT---DVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 528504085   759 VWRDG 763
Cdd:smart00490  78 AGRAG 82
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 308-488 2.73e-12

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: 67.75  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFlyeclmgMRLAGrcgAILADEMGLGKTLQCV-CVLWTLLRQGPY------------------GGRPVMK 368
Cdd:cd18070    1 LLPYQRRAVNW-------MLVPG---GILADEMGLGKTVEVLaLILLHPRPDNDLdaadddsdemvccpdclvAETPVSS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 369 RA-LVVCPGSLVKNWAAEFNKWLGRE-RISVYT------VDQDHRVEDFVSsplCSVLVISYEML--------------- 425
Cdd:cd18070   71 KAtLIVCPSAILAQWLDEINRHVPSSlKVLTYQgvkkdgALASPAPEILAE---YDIVVTTYDVLrtelhyaeanrsnrr 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 426 LRSVDR-------LKELDFGVLICDEGHRLKNSNIKTAGALTALSCTRRLILTGTPVQNDLQEFYSIIEF 488
Cdd:cd18070  148 RRRQKRyeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSF 217
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
308-582 1.59e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 68.13  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVvflyECLMGMRLAGRCGAILADEMGLGKTLqcvcVLWTLLRQGPYGgrpvmKRALVVCPG-SLVKNWAAEF 386
Cdd:COG1061   81 LRPYQQEAL----EALLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRG-----KRVLVLVPRrELLEQWAEEL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKWLGRERISVYTVDQDHRVedfvssplcsvLVISYEMLLRSvDRLKEL--DFGVLICDEGHRL-KNSNIKTAGALTAls 463
Cdd:COG1061  148 RRFLGDPLAGGGKKDSDAPI-----------TVATYQSLARR-AHLDELgdRFGLVIIDEAHHAgAPSYRRILEAFPA-- 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 464 cTRRLILTGTPVQNDLQEFYsIIEFVNPgilgtsaAYRKIYEE---------PILRSRQPSCTEEERCIGEERAAELFRL 534
Cdd:COG1061  214 -AYRLGLTATPFRSDGREIL-LFLFDGI-------VYEYSLKEaiedgylapPEYYGIRVDLTDERAEYDALSERLREAL 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504085 535 TGvfTLRRTQEIINQYLSERIEWT---VFCKPTElQIRLYRVLLSTRPIRA 582
Cdd:COG1061  285 AA--DAERKDKILRELLREHPDDRktlVFCSSVD-HAEALAELLNEAGIRA 332
ResIII pfam04851
Type III restriction enzyme, res subunit;
308-474 3.00e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 62.69  E-value: 3.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  308 LRPHQKEGVvflyECLMGMRLAGRCGAILADEMGLGKTLQCVCVLWTLLRQGPYggrpvmKRALVVCPG-SLVKNWAAEF 386
Cdd:pfam04851   4 LRPYQIEAI----ENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPI------KKVLFLVPRkDLLEQALEEF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  387 NKWLG--RERISVYTVDqdhrvEDFVSSPLCSVLVISYEMLLRSVDRLKELD----FGVLICDEGHRLKNSNIKtaGALT 460
Cdd:pfam04851  74 KKFLPnyVEIGEIISGD-----KKDESVDDNKIVVTTIQSLYKALELASLELlpdfFDVIIIDEAHRSGASSYR--NILE 146

                         170
                  ....*....|....
gi 528504085  461 ALSCTRRLILTGTP 474
Cdd:pfam04851 147 YFKPAFLLGLTATP 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 308-474 3.12e-09

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: 56.55  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 308 LRPHQKEGVVFLYECLMGMRlagrcgAILADEMGLGKTLQCVCVLWTLLRqgpyggrpvmKRALVVCPG-SLVKNWAAEF 386
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR------GILVLPTGSGKTLTALALIAYLKE----------LRTLIVVPTdALLDQWKERF 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 387 NKWLGRERISVYTVDQDHRVEDfvssplCSVLVISYEMLLRSVDRLKEL--DFGVLICDEGHRLKNSNIKtaGALTALSC 464
Cdd:cd17926   65 EDFLGDSSIGLIGGGKKKDFDD------ANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLPAKTFS--EILKELNA 136

                        170
                 ....*....|
gi 528504085 465 TRRLILTGTP 474
Cdd:cd17926  137 KYRLGLTATP 146
DpdE NF041062
protein DpdE;
336-482 9.29e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 56.13  E-value: 9.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085  336 LADEMGLGKTLQ-CVCVLWTLLRQGpyggrpvMKRALVVCPGSLVKNWAAEFnkwlgRERIsvytvdqdhRVEDFvssPL 414
Cdd:NF041062  175 LADEVGLGKTIEaGLVIRQHLLDNP-------DARVLVLVPDALVRQWRREL-----RDKF---------FLDDF---PG 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504085  415 CSVLVISYEMLLRSVDRLKELDFgvLICDEGHRL----KNSNIKTAG---ALTAL--SCTRRLILTGTPVQNDLQEF 482
Cdd:NF041062  231 ARVRVLSHEEPERWEPLLDAPDL--LVVDEAHQLarlaWSGDPPERAryrELAALahAAPRLLLLSATPVLGNEETF 305
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 333-475 2.02e-06

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: 48.17  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 333 GAILADEMGLGKTLQCVCV-LWTLLRQGpyggrpvmKRALVVCP-GSLVKNWAAEFNKWLGR-ERISVYTVDQDHRVEDF 409
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAaLLLLLKKG--------KKVLVLVPtKALALQTAERLRELFGPgIRVAVLVGGSSAEEREK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504085 410 VSSPLCSVLVISYEMLLRSV---DRLKELDFGVLICDEGHRLKnsnIKTAGALTALSCTRRLILTGTPV 475
Cdd:cd00046   75 NKLGDADIIIATPDMLLNLLlreDRLFLKDLKLIIVDEAHALL---IDSRGALILDLAVRKAGLKNAQV 140
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
 305-478 3.96e-05

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


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 44.98  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 305 TNHLRPHQKEgvvflyeCLMGMRLAGR---------CGAilademglGKTLQCVCVLWTllrqgpyggrpVMKRALVVCP 375
Cdd:cd18029    6 STQLRPYQEK-------ALSKMFGNGRarsgvivlpCGA--------GKTLVGITAACT-----------IKKSTLVLCT 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 376 GSL-VKNWAAEFNKW--LGRERISVYTVDQdhrvedFVSSPLCSVLVISYEMLLRSVDR----------LKELDFGVLIC 442
Cdd:cd18029   60 SAVsVEQWRRQFLDWttIDDEQIGRFTSDK------KEIFPEAGVTVSTYSMLANTRKRspesekfmefITEREWGLIIL 133

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504085 443 DEGHRLKNSNIKTagALTALSCTRRLILTGTPVQND 478
Cdd:cd18029  134 DEVHVVPAPMFRR--VLTLQKAHCKLGLTATLVRED 167
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
307-448 1.95e-04

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 45.21  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 307 HLRPHQkegvvfLY---EclMGMRLAGRcgAILADEMGLGKTLQCVCVLWTLLrqgpYGGRpvMKRALVVCPGSLVKNWA 383
Cdd:PRK04914 152 SLIPHQ------LYiahE--VGRRHAPR--VLLADEVGLGKTIEAGMIIHQQL----LTGR--AERVLILVPETLQHQWL 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504085 384 AE----FNkwLgreRISVYtvDQDhRVEDFVSSP----LCSVLVI-SYEMLLRSVDRLKEL---DFGVLICDEGHRL 448
Cdd:PRK04914 216 VEmlrrFN--L---RFSLF--DEE-RYAEAQHDAdnpfETEQLVIcSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHL 284
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 343-452 2.64e-03

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 39.94  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504085 343 GKTLqcV---CVLWTLLRQGpyggrpvmKRALVVCP-GSLVKNWAAEFNKWLGRERISVYTVDQDHrVEDFVSSPLCSVL 418
Cdd:cd17921   29 GKTL--IaelAILRALATSG--------GKAVYIAPtRALVNQKEADLRERFGPLGKNVGLLTGDP-SVNKLLLAEADIL 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528504085 419 VISYE----MLLRSVDRLkELDFGVLICDEGHRLKNSN 452
Cdd:cd17921   98 VATPEkldlLLRNGGERL-IQDVRLVVVDEAHLIGDGE 134
 
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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