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Conserved domains on  [gi|1832872348|ref|XP_033402759|]
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uncharacterized protein K452DRAFT_240179 [Aplosporella prunicola CBS 121167]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13756241)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to DNA repair and recombination protein RAD54 that plays a role in homologous recombination related repair of DNA double-strand breaks

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 ...
222-467 6.19e-146

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 cd18067:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 243  Bit Score: 428.81  E-value: 6.19e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPEaGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQ-CKPEIDKAIVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDaITPFAIDGKASKEELtQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18067    80 KWLGGR-LQPLAIDGGSKKEID-RKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLVN 461
Cdd:cd18067   158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd18067   238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
136-719 2.42e-127

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 2.42e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 136 RQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPVTPLEEGEKKTDEPEPPKLDAPLVHKSLADILGLKKKVDERPKVPvvid 215
Cdd:COG0553   160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 216 PRLAKVLRPHQVEGVRFLYRCTT-GLvdpkanGCIMADEMGLGKTLQCIALmwtlIKQSPEAGKstIQKCVIACPSSLVR 294
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRlGL------GGLLADDMGLGKTIQALAL----LLELKERGL--ARPVLIVAPTSLVG 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 295 NWANELVKWLgkDAITPFAIDGKASKEELTQQLRQwsiasgravvRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLK 374
Cdd:COG0553   304 NWQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIK 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 375 NDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDangtdkdrklgdERLS 454
Cdd:COG0553   372 NPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDE------------EALE 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 455 ELLTLVNKFIIRRT-NDILsKYLPVKYEHVVFCNLAPFQKDLYNLFIQSpEIRQLLRGKGSQP----LKAINILKKLCNH 529
Cdd:COG0553   440 RLRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSH 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 530 PDLLDlpsdlpgsescfpddfvpkdargRDRDVKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDVFDKLCRSRG 609
Cdd:COG0553   518 PALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERG 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 610 YGCLRLDGTMNVNKRQKLVDKFNDPEGGEfVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 689
Cdd:COG0553   574 IEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                         570       580       590
                  ....*....|....*....|....*....|
gi 1832872348 690 VYRFIATGTIEEKIFQRQSHKSALSSCVVD 719
Cdd:COG0553   653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
31-201 2.58e-93

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


:

Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 2.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  31 TPQSLDRLVKPFKCPGSATPTRASDKPARKRRKVDYSGADGDVVDG--DKPYTN-EDRLALATRDVNKFPVFKVKDKEST 107
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdsDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 108 FRQRFSVPLKNKDTGAYNAARPAPLLGMRQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPV---TPLEEGEKKTDEPEPP- 183
Cdd:pfam08658  81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKpeeEEEAEEEEEEEEPEEKa 160
                         170       180
                  ....*....|....*....|
gi 1832872348 184 --KLDAPLVHKSLADILGLK 201
Cdd:pfam08658 161 rkKLDNPLPHKSLAEILGIK 180
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
222-467 6.19e-146

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: 428.81  E-value: 6.19e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPEaGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQ-CKPEIDKAIVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDaITPFAIDGKASKEELtQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18067    80 KWLGGR-LQPLAIDGGSKKEID-RKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLVN 461
Cdd:cd18067   158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd18067   238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
136-719 2.42e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 2.42e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 136 RQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPVTPLEEGEKKTDEPEPPKLDAPLVHKSLADILGLKKKVDERPKVPvvid 215
Cdd:COG0553   160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 216 PRLAKVLRPHQVEGVRFLYRCTT-GLvdpkanGCIMADEMGLGKTLQCIALmwtlIKQSPEAGKstIQKCVIACPSSLVR 294
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRlGL------GGLLADDMGLGKTIQALAL----LLELKERGL--ARPVLIVAPTSLVG 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 295 NWANELVKWLgkDAITPFAIDGKASKEELTQQLRQwsiasgravvRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLK 374
Cdd:COG0553   304 NWQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIK 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 375 NDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDangtdkdrklgdERLS 454
Cdd:COG0553   372 NPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDE------------EALE 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 455 ELLTLVNKFIIRRT-NDILsKYLPVKYEHVVFCNLAPFQKDLYNLFIQSpEIRQLLRGKGSQP----LKAINILKKLCNH 529
Cdd:COG0553   440 RLRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSH 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 530 PDLLDlpsdlpgsescfpddfvpkdargRDRDVKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDVFDKLCRSRG 609
Cdd:COG0553   518 PALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERG 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 610 YGCLRLDGTMNVNKRQKLVDKFNDPEGGEfVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 689
Cdd:COG0553   574 IEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                         570       580       590
                  ....*....|....*....|....*....|
gi 1832872348 690 VYRFIATGTIEEKIFQRQSHKSALSSCVVD 719
Cdd:COG0553   653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
225-533 6.76e-97

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: 303.45  E-value: 6.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 225 HQVEGVRFLYRCTTGLVdpkaNGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTIqkcvIACPSSLVRNWANELVKWL 304
Cdd:pfam00176   1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTL----IVVPLSLLHNWMNEFERWV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 305 GKDAITPFAIDGKaskeelTQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTFTAL 384
Cdd:pfam00176  73 SPPALRVVVLHGN------KRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKAL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 385 NNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGrdangtdkdrkLGDERLSELLTLVNKFI 464
Cdd:pfam00176 147 KSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKPFL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832872348 465 IRRTNDILSKYLPVKYEHVVFCNLAPFQKDLYNLFIQSPEIRQLLRGKG-----SQPLKAINILKKLCNHPDLL 533
Cdd:pfam00176 216 LRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGgreikASLLNILMRLRKICNHPGLI 289
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
31-201 2.58e-93

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


Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 2.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  31 TPQSLDRLVKPFKCPGSATPTRASDKPARKRRKVDYSGADGDVVDG--DKPYTN-EDRLALATRDVNKFPVFKVKDKEST 107
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdsDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 108 FRQRFSVPLKNKDTGAYNAARPAPLLGMRQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPV---TPLEEGEKKTDEPEPP- 183
Cdd:pfam08658  81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKpeeEEEAEEEEEEEEPEEKa 160
                         170       180
                  ....*....|....*....|
gi 1832872348 184 --KLDAPLVHKSLADILGLK 201
Cdd:pfam08658 161 rkKLDNPLPHKSLAEILGIK 180
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
222-718 3.50e-64

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 232.77  E-value: 3.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  222 LRPHQVEGVRFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLikqsPEAGKSTIQKCVIAcPSSLVRNWANELV 301
Cdd:PLN03142   170 MRDYQLAGLNWLIR----LYENGING-ILADEMGLGKTLQTISLLGYL----HEYRGITGPHMVVA-PKSTLGNWMNEIR 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  302 KWLgkDAITPFAIDGKAskEELTQQlRQWSIASGRAvvrPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:PLN03142   240 RFC--PVLRAVKFHGNP--EERAHQ-REELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdANGTDKDRKlgdERLSELLTLVN 461
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF---------QISGENDQQ---EVVQQLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  462 KFIIRRTNDILSKYLPVKYEHVVFCNLAPFQKDLYNLFIQSpEIRQLLRGKGSQPLkaINI---LKKLCNHPDLLDLPSd 538
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK-DLDVVNAGGERKRL--LNIamqLRKCCNHPYLFQGAE- 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  539 lPGSESCFPDDFVPKdargrdrdvkswySGKMMVLDRMLARIRQdtNDKIVLI-SNYTQTLDVFDKLCRSRGYGCLRLDG 617
Cdd:PLN03142   456 -PGPPYTTGEHLVEN-------------SGKMVLLDKLLPKLKE--RDSRVLIfSQMTRLLDILEDYLMYRGYQYCRIDG 519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  618 TMNVNKRQKLVDKFNDPEGGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATG 697
Cdd:PLN03142   520 NTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEY 599
                          490       500
                   ....*....|....*....|.
gi 1832872348  698 TIEEKIFQRQSHKSALSSCVV 718
Cdd:PLN03142   600 TIEEKVIERAYKKLALDALVI 620
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
566-694 1.62e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 1.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 566 YSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDVFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDPEGgEFVFLLSS 645
Cdd:cd18793     9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1832872348 646 KAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFI 694
Cdd:cd18793    87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
568-683 3.46e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 100.75  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 568 GKMMVLDRMLariRQDTNDKIVLISNYTQTLDvFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDpegGEFVFLLSSKA 647
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1832872348 648 GGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDG 683
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
214-413 4.85e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 100.64  E-value: 4.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  214 IDPRLAKVLRPHQVEGVRFLYRCTtglvdpkaNGCIMADEMGLGKTLQ-CIALMWTLIKQSPeagkstiQKCVIACP-SS 291
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL--------RDVILAAPTGSGKTLAaLLPALEALKRGKG-------GRVLVLVPtRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  292 LVRNWANELVKWLGKDAITPFAIDGKASKEELTQQLRqwsiaSGRAvvrPVLIVSYETLRLNVEE--LKNTPIGLLLCDE 369
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLE-----SGKT---DILVTTPGRLLDLLENdkLSLSNVDLVILDE 137
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1832872348  370 GHRLKND--ESQTFTALNNLNVQKRVI-LSGTP---IQNDLSEYFALLNF 413
Cdd:smart00487 138 AHRLLDGgfGDQLEKLLKLLPKNVQLLlLSATPpeeIENLLELFLNDPVF 187
HELICc smart00490
helicase superfamily c-terminal domain;
599-683 1.43e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.50  E-value: 1.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  599 DVFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDpegGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALAR 678
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 1832872348  679 VWRDG 683
Cdd:smart00490  78 AGRAG 82
DpdE NF041062
protein DpdE;
222-681 1.76e-10

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 64.99  E-value: 1.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  222 LRPHQVEGVRflyrctTGLVDPkangcIM----ADEMGLGKTLQCIALMWTLIKQSPEAgkstiqKCVIACPSSLVRNWA 297
Cdd:NF041062   154 LEPHQVAVVR------RVLQDP-----VQryllADEVGLGKTIEAGLVIRQHLLDNPDA------RVLVLVPDALVRQWR 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  298 NELvkwlgkdaITPFAIDgkaskEELTQQLRqwsiasgravvrpvlIVSYETLRLnVEELKNTPiGLLLCDEGHRL---- 373
Cdd:NF041062   217 REL--------RDKFFLD-----DFPGARVR---------------VLSHEEPER-WEPLLDAP-DLLVVDEAHQLarla 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  374 ---KNDESQTFTALNNL-NVQKRVI-LSGTPIQNDLSEYFALLNFANP-NY-LGTKNEFRKRFEL-----PILRGRDANG 441
Cdd:NF041062   267 wsgDPPERARYRELAALaHAAPRLLlLSATPVLGNEETFLALLHLLDPdLYpLDDLEAFRERLEEreelgRLVLGLDPDN 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  442 TD----------KDRKLGDERLSEL----LTLVNKFIIRRTNDI------LSKYLpvkyehvvfcnlapfqKDLYNLFiq 501
Cdd:NF041062   347 PNfllrqaldelRALFPEDEELQELaeelLPLLDEFDDEEPEERaravsaLRAHI----------------SETYRLH-- 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  502 speiRQLLRGKGSQPLKAI------NILKKLCNHPDLLDLPSDL------------PGSESCF----------------- 546
Cdd:NF041062   409 ----RRMIRNRRSSVLGADylvpgrAGPRVLVWESPAREAADEAledwreeaalldAESDPAAraayaralawlvarlgg 484
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  547 PDDFVPKdARGRDRDVK--SWYSGKMMVLDRMLARIRQDTND-------------------KIVLISNYTQTLD-VFDKL 604
Cdd:NF041062   485 PDDLAAL-LRWRLRGDAasADLAGERELLEALIAALEDEAKDadllaaladwllpllrgsgKAVVFCGDGSLADhLAAAL 563
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832872348  605 CRSRGYGCLRLDGTMNVNKRQKLVDKFNDPEGGeFVfLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWR 681
Cdd:NF041062   564 ARLGAGSVERHLSGQGADQAERAVRAFRQDPSA-RV-LVCDRSGEEGLNLQGADRLVHLDLPWSPNRLEQRIGRLDR 638
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
222-740 3.86e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 60.04  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGlvDPKANGCIMAdeMGLGKTLqcIALMwtLIKQSpeagkSTIQKCVIACPS-SLVRNWANEL 300
Cdd:COG1061    81 LRPYQQEALEALLAALER--GGGRGLVVAP--TGTGKTV--LALA--LAAEL-----LRGKRVLVLVPRrELLEQWAEEL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWLGKdaitPFAIDGKASKEeltqqlrqwsiasgravvRPVLIVSYETL--RLNVEELKNTpIGLLLCDEGHRLkndES 378
Cdd:COG1061   148 RRFLGD----PLAGGGKKDSD------------------APITVATYQSLarRAHLDELGDR-FGLVIIDEAHHA---GA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 379 QTFTA-LNNLNVQKRVILSGTPIQND-LSEYFALLnfanpnylgtkneFRKRFELPIlrgRDAngtdkdrklgderlsel 456
Cdd:COG1061   202 PSYRRiLEAFPAAYRLGLTATPFRSDgREILLFLF-------------DGIVYEYSL---KEA----------------- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 457 ltlvnkfiirrtndILSKYL-PVKYeHVVFCNLAPFQKDlYNLFIQspEIRQLLrgkgsqplkainilkklcnhpdlldl 535
Cdd:COG1061   249 --------------IEDGYLaPPEY-YGIRVDLTDERAE-YDALSE--RLREAL-------------------------- 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 536 psdlpgsescfpddfVPKDARgrdrdvkswysgKMMVLDRMLARIRQDtnDKIVLISNYTQTLDVFDKLCRSRGYGCLRL 615
Cdd:COG1061   285 ---------------AADAER------------KDKILRELLREHPDD--RKTLVFCSSVDHAEALAELLNEAGIRAAVV 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 616 DGTMNVNKRQKLVDKFNDpegGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQ-KKDCFVYRFI 694
Cdd:COG1061   336 TGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFV 412
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1832872348 695 ATGT-IEEKIFQRQSHKSALSSCVVDSAEDVERHFSIDSLRELFQYQ 740
Cdd:COG1061   413 GNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKG 459
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
222-467 6.19e-146

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: 428.81  E-value: 6.19e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPEaGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQ-CKPEIDKAIVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDaITPFAIDGKASKEELtQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18067    80 KWLGGR-LQPLAIDGGSKKEID-RKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLVN 461
Cdd:cd18067   158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd18067   238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
136-719 2.42e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 2.42e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 136 RQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPVTPLEEGEKKTDEPEPPKLDAPLVHKSLADILGLKKKVDERPKVPvvid 215
Cdd:COG0553   160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 216 PRLAKVLRPHQVEGVRFLYRCTT-GLvdpkanGCIMADEMGLGKTLQCIALmwtlIKQSPEAGKstIQKCVIACPSSLVR 294
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRlGL------GGLLADDMGLGKTIQALAL----LLELKERGL--ARPVLIVAPTSLVG 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 295 NWANELVKWLgkDAITPFAIDGKASKEELTQQLRQwsiasgravvRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLK 374
Cdd:COG0553   304 NWQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIK 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 375 NDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDangtdkdrklgdERLS 454
Cdd:COG0553   372 NPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDE------------EALE 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 455 ELLTLVNKFIIRRT-NDILsKYLPVKYEHVVFCNLAPFQKDLYNLFIQSpEIRQLLRGKGSQP----LKAINILKKLCNH 529
Cdd:COG0553   440 RLRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSH 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 530 PDLLDlpsdlpgsescfpddfvpkdargRDRDVKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDVFDKLCRSRG 609
Cdd:COG0553   518 PALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERG 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 610 YGCLRLDGTMNVNKRQKLVDKFNDPEGGEfVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 689
Cdd:COG0553   574 IEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                         570       580       590
                  ....*....|....*....|....*....|
gi 1832872348 690 VYRFIATGTIEEKIFQRQSHKSALSSCVVD 719
Cdd:COG0553   653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
222-467 2.99e-113

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 344.27  E-value: 2.99e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPeAGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18004     1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGP-YGKPTAKKALIVCPSSLVGNWKAEFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKASKEELTQQlrqwsiASGRAVVRPVLIVSYETLRLNVEELKNT-PIGLLLCDEGHRLKNDESQT 380
Cdd:cd18004    80 KWLGLRRIKVVTADGNAKDVKASLD------FFSSASTYPVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 381 FTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLV 460
Cdd:cd18004   154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                  ....*..
gi 1832872348 461 NKFIIRR 467
Cdd:cd18004   234 SRFILRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
225-533 6.76e-97

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: 303.45  E-value: 6.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 225 HQVEGVRFLYRCTTGLVdpkaNGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTIqkcvIACPSSLVRNWANELVKWL 304
Cdd:pfam00176   1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTL----IVVPLSLLHNWMNEFERWV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 305 GKDAITPFAIDGKaskeelTQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTFTAL 384
Cdd:pfam00176  73 SPPALRVVVLHGN------KRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKAL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 385 NNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGrdangtdkdrkLGDERLSELLTLVNKFI 464
Cdd:pfam00176 147 KSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKPFL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832872348 465 IRRTNDILSKYLPVKYEHVVFCNLAPFQKDLYNLFIQSPEIRQLLRGKG-----SQPLKAINILKKLCNHPDLL 533
Cdd:pfam00176 216 LRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGgreikASLLNILMRLRKICNHPGLI 289
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
31-201 2.58e-93

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


Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 2.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  31 TPQSLDRLVKPFKCPGSATPTRASDKPARKRRKVDYSGADGDVVDG--DKPYTN-EDRLALATRDVNKFPVFKVKDKEST 107
Cdd:pfam08658   1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdsDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 108 FRQRFSVPLKNKDTGAYNAARPAPLLGMRQGAVFVAKPLHDPAGEFAIVLYDPTVDDKPV---TPLEEGEKKTDEPEPP- 183
Cdd:pfam08658  81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKpeeEEEAEEEEEEEEPEEKa 160
                         170       180
                  ....*....|....*....|
gi 1832872348 184 --KLDAPLVHKSLADILGLK 201
Cdd:pfam08658 161 rkKLDNPLPHKSLAEILGIK 180
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
222-467 3.43e-84

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: 268.25  E-value: 3.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKASKEELTQqlrqwsiasgrAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18066    81 KWLGSERIKVFTVDQDHKVEEFIA-----------SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLVN 461
Cdd:cd18066   150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTG 229

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd18066   230 LFILRR 235
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
222-452 9.42e-65

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: 216.39  E-value: 9.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYR--CTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPeagksTIQKCVIACPSSLVRNWANE 299
Cdd:cd18007     1 LKPHQVEGVRFLWSnlVGTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-----RRSRPLVLCPASTLYNWEDE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 300 LVKWLGKDAITPFAIDGKASKEELTQQLR---QWSIASGravvrpVLIVSYETLR---------------LNVEELKNTP 361
Cdd:cd18007    76 FKKWLPPDLRPLLVLVSLSASKRADARLRkinKWHKEGG------VLLIGYELFRnlasnattdprlkqeFIAALLDPGP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 362 iGLLLCDEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANG 441
Cdd:cd18007   150 -DLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDS 228
                         250
                  ....*....|.
gi 1832872348 442 TDKDRKLGDER 452
Cdd:cd18007   229 TEEDVRLMLKR 239
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
222-718 3.50e-64

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 232.77  E-value: 3.50e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  222 LRPHQVEGVRFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLikqsPEAGKSTIQKCVIAcPSSLVRNWANELV 301
Cdd:PLN03142   170 MRDYQLAGLNWLIR----LYENGING-ILADEMGLGKTLQTISLLGYL----HEYRGITGPHMVVA-PKSTLGNWMNEIR 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  302 KWLgkDAITPFAIDGKAskEELTQQlRQWSIASGRAvvrPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:PLN03142   240 RFC--PVLRAVKFHGNP--EERAHQ-REELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdANGTDKDRKlgdERLSELLTLVN 461
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF---------QISGENDQQ---EVVQQLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  462 KFIIRRTNDILSKYLPVKYEHVVFCNLAPFQKDLYNLFIQSpEIRQLLRGKGSQPLkaINI---LKKLCNHPDLLDLPSd 538
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK-DLDVVNAGGERKRL--LNIamqLRKCCNHPYLFQGAE- 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  539 lPGSESCFPDDFVPKdargrdrdvkswySGKMMVLDRMLARIRQdtNDKIVLI-SNYTQTLDVFDKLCRSRGYGCLRLDG 617
Cdd:PLN03142   456 -PGPPYTTGEHLVEN-------------SGKMVLLDKLLPKLKE--RDSRVLIfSQMTRLLDILEDYLMYRGYQYCRIDG 519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  618 TMNVNKRQKLVDKFNDPEGGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATG 697
Cdd:PLN03142   520 NTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEY 599
                          490       500
                   ....*....|....*....|.
gi 1832872348  698 TIEEKIFQRQSHKSALSSCVV 718
Cdd:PLN03142   600 TIEEKVIERAYKKLALDALVI 620
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
222-419 4.79e-59

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: 198.56  E-value: 4.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTtglvdPKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKstiqkCVIACPSSLVRNWANELV 301
Cdd:cd17919     1 LRPYQLEGLNFLLELY-----ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGP-----VLVVCPLSVLENWEREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKdaITPFAIDGkASKEELTQQLRQWSIASGravvrpVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd17919    71 KWTPD--LRVVVYHG-SQRERAQIRAKEKLDKFD------VVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLS 141
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYL 419
Cdd:cd17919   142 KALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
222-467 3.06e-58

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: 198.76  E-value: 3.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCttgLVDPKanGCIMADEMGLGKTLQCIALMWTLIKQS--------------PEAGKSTIQKCV-I 286
Cdd:cd18005     1 LRDYQREGVEFMYDL---YKNGR--GGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkKKPPASSAKKPVlI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 287 ACPSSLVRNWANELVKWlGKDAITPFAIDGKasKEELtqqlrQWSIASGRAvvrPVLIVSYETLRLNVEELKNTPIGLLL 366
Cdd:cd18005    76 VAPLSVLYNWKDELDTW-GHFEVGVYHGSRK--DDEL-----EGRLKAGRL---EVVVTTYDTLRRCIDSLNSINWSAVI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 367 CDEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDR 446
Cdd:cd18005   145 ADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATAREL 224
                         250       260
                  ....*....|....*....|.
gi 1832872348 447 KLGDERLSELLTLVNKFIIRR 467
Cdd:cd18005   225 RLGRKRKQELAVKLSKFFLRR 245
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
566-694 1.62e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 1.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 566 YSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDVFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDPEGgEFVFLLSS 645
Cdd:cd18793     9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLST 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1832872348 646 KAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFI 694
Cdd:cd18793    87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
222-468 5.91e-51

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: 177.76  E-value: 5.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYR-CTTGLvdpkanGCIMADEMGLGKTLQCIALMwTLIKQSPEAGKStiqkcVIACPSSLVRNWANEL 300
Cdd:cd18012     5 LRPYQKEGFNWLSFlRHYGL------GGILADDMGLGKTLQTLALL-LSRKEEGRKGPS-----LVVAPTSLIYNWEEEA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWlgkdaiTP----FAIDGKASKEELTQQLRQwsiasgravvRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKND 376
Cdd:cd18012    73 AKF------APelkvLVIHGTKRKREKLRALED----------YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNP 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 377 ESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDAngtdkdrklgdERLSEL 456
Cdd:cd18012   137 QTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDE-----------EALEEL 205
                         250
                  ....*....|..
gi 1832872348 457 LTLVNKFIIRRT 468
Cdd:cd18012   206 KKLISPFILRRL 217
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
222-467 3.05e-49

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: 173.33  E-value: 3.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYrcttGLVDPKANGcIMADEMGLGKTLQCIALMWTLikqspeAGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18001     1 LYPHQREGVAWLW----SLHDGGKGG-ILADDMGLGKTVQICAFLSGM------FDSGLIKSVLVVMPTSLIPHWVKEFA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWlgKDAITPFAIDGkASKEELTQQLRqwSIASGRAVvrpvLIVSYETLRLNVEELKNTPIG-----LLLCDEGHRLKND 376
Cdd:cd18001    70 KW--TPGLRVKVFHG-TSKKERERNLE--RIQRGGGV----LLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 377 ESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFA-NPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSE 455
Cdd:cd18001   141 KTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAEN 220
                         250
                  ....*....|..
gi 1832872348 456 LLTLVNKFIIRR 467
Cdd:cd18001   221 LRQIIKPYFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
222-467 7.07e-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: 166.76  E-value: 7.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd17999     1 LRPYQQEGINWL----AFLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPSLVVCPPTLVGHWVAEIK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKAskeeltQQLRQWSIASGRAvvrPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd17999    76 KYFPNAFLKPLAYVGPP------QERRRLREQGEKH---NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLTLVN 461
Cdd:cd17999   147 KAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVL 226

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd17999   227 PFLLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
222-452 1.69e-46

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 166.22  E-value: 1.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDPK----ANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTIqkcVIACPSSLVRNWA 297
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTkkspGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRV---LVVCPLNTVLNWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 298 NELVKWL----GKDAITPFAIDGKASKEELTQQLRQWSIASGravvrpVLIVSYETLRLNVEE----------------L 357
Cdd:cd18068    78 NEFEKWQeglkDEEKIEVNELATYKRPQERSYKLQRWQEEGG------VMIIGYDMYRILAQErnvksreklkeifnkaL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 358 KNTPIGLLLCDEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGR 437
Cdd:cd18068   152 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQ 231
                         250
                  ....*....|....*
gi 1832872348 438 DANGTDKDRKLGDER 452
Cdd:cd18068   232 CADSTLVDVRVMKKR 246
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
222-452 1.87e-45

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: 162.68  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLY----RCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLIKQSPeagkstIQKCVIACPSSLVRNWA 297
Cdd:cd18069     1 LKPHQIGGIRFLYdniiESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTG------AKTVLAIVPVNTLQNWL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 298 NELVKWL------GKDAITPFAI----DGKASKEELTQQLRQWSIASGravvrpVLIVSYETLRLnveelKNTPiGLLLC 367
Cdd:cd18069    75 SEFNKWLpppealPNVRPRPFKVfilnDEHKTTAARAKVIEDWVKDGG------VLLMGYEMFRL-----RPGP-DVVIC 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 368 DEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRK 447
Cdd:cd18069   143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222

                  ....*
gi 1832872348 448 LGDER 452
Cdd:cd18069   223 LMRYR 227
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
222-467 4.75e-36

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: 135.64  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGlvdpkANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAE-----QHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPF-----LVLCPLSVLDNWKEELN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDgKASKEELTQQLRQWSIASgravvrpVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18006    71 RFAPDLSVITYMGD-KEKRLDLQQDIKSTNRFH-------VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLG--TKNEFRKRFelpilrgrdangtdKDRKLGDERLSELLTL 459
Cdd:cd18006   143 KTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAY--------------SETDDESETVEELHLL 208

                  ....*...
gi 1832872348 460 VNKFIIRR 467
Cdd:cd18006   209 LQPFLLRR 216
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
221-467 1.94e-35

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: 134.44  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 221 VLRPHQVEGVRFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLIkqspEAGksTIQKCVIACPSSLVRNWANEL 300
Cdd:cd18009     3 VMRPYQLEGMEWLRM----LWENGING-ILADEMGLGKTIQTIALLAHLR----ERG--VWGPFLVIAPLSTLPNWVNEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWlgkdaiTPF--AIDGKASKEELTQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDES 378
Cdd:cd18009    72 ARF------TPSvpVLLYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 379 QTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGTDKDRKLGDERLSELLT 458
Cdd:cd18009   146 RLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHA 225

                  ....*....
gi 1832872348 459 LVNKFIIRR 467
Cdd:cd18009   226 ILKPFLLRR 234
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
222-429 5.39e-33

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: 126.98  E-value: 5.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKSTiqkcVIAcPSSLVRNWANELV 301
Cdd:cd17995     1 LRDYQLEGVNWLLFNWY-----NRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFL----VIA-PLSTIPNWQREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFaiDGKASKEELTQQLRQWSIASGRAVVRP----VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDE 377
Cdd:cd17995    71 TWTDMNVVVYH--GSGESRQIIQQYEMYFKDAQGRKKKGVykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRN 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1832872348 378 SQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 429
Cdd:cd17995   149 SKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
222-467 2.97e-32

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: 125.48  E-value: 2.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYrcttglvdpkANGCIMADEMGLGKTLQCIALM-----WTLIKQSPEAGKSTIQKCV-------IACP 289
Cdd:cd18008     1 LLPYQKQGLAWML----------PRGGILADEMGLGKTIQALALIlatrpQDPKIPEELEENSSDPKKLylskttlIVVP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 290 SSLVRNWANELVKWLGKDAITPFAIDGkASKEELTQQLRQWSIasgravvrpvLIVSYETLR--------LNVEELKNTP 361
Cdd:cd18008    71 LSLLSQWKDEIEKHTKPGSLKVYVYHG-SKRIKSIEELSDYDI----------VITTYGTLAsefpknkkGGGRDSKEKE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 362 IGLLLC--------DEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI 433
Cdd:cd18008   140 ASPLHRirwyrvilDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1832872348 434 LRGRDANGtdkdrklgdERLSELLtlvNKFIIRR 467
Cdd:cd18008   220 SKNDRKAL---------ERLQALL---KPILLRR 241
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
222-467 2.95e-31

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 121.69  E-value: 2.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd17993     2 LRDYQLTGLNWLAHSWC-----KGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPF-----LVVVPLSTMPAWQREFA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLgkDAITPFAIDGKASKEELTQQLrQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd17993    72 KWA--PDMNVIVYLGDIKSRDTIREY-EFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNylgtKNEFRKRFELPilrgrdangTDKDRKLGDERLSELLtlvN 461
Cdd:cd17993   149 EALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG----KFDIWEEFEEE---------HDEEQEKGIADLHKEL---E 212

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd17993   213 PFILRR 218
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
222-467 4.09e-31

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


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 121.69  E-value: 4.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18003     1 LREYQHIGLDWL----ATLYEKNLNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPH-----LIVVPTSVMLNWEMEFK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWL-GKDAITPFAidgkaSKEELTQQLRQWSiasgravvRP----VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKND 376
Cdd:cd18003    71 RWCpGFKILTYYG-----SAKERKLKRQGWM--------KPnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 377 ESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPiLRGRDANGTDKDRKLgderLSEL 456
Cdd:cd18003   138 KSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSEGSQEENEEL----VRRL 212
                         250
                  ....*....|.
gi 1832872348 457 LTLVNKFIIRR 467
Cdd:cd18003   213 HKVLRPFLLRR 223
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
222-419 1.38e-30

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 118.97  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLiKQSPEAGKSTIqkcvIACPSSLVRNWANELV 301
Cdd:cd18000     1 LFKYQQTGVQWLWE----LHCQRVGG-ILGDEMGLGKTIQIIAFLAAL-HHSKLGLGPSL----IVCPATVLKQWVKEFH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKASKEELTQQLRQWSIASGRAVVRP--VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQ 379
Cdd:cd18000    71 RWWPPFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVVGDggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1832872348 380 TFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYL 419
Cdd:cd18000   151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
222-467 8.26e-30

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: 117.69  E-value: 8.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFlyrcttGLvdpKANG-CIMADEMGLGKTLQCIALMWTLIKQSPeagkstiqkCVIACPSSLVRNWANEL 300
Cdd:cd18010     1 LLPFQREGVCF------AL---RRGGrVLIADEMGLGKTVQAIAIAAYYREEWP---------LLIVCPSSLRLTWADEI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWLGKDAITPFAIdgkaskeeltqqlrqwsIASGRAVVRP----VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKND 376
Cdd:cd18010    63 ERWLPSLPPDDIQV-----------------IVKSKDGLRDgdakVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNS 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 377 ESQTFTALNNLNVQ-KRVI-LSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPIL--RGRDANGTdkdrklgdER 452
Cdd:cd18010   126 KAKRTKAALPLLKRaKRVIlLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQggFGWDYSGS--------SN 197
                         250
                  ....*....|....*.
gi 1832872348 453 LSELLTLVNK-FIIRR 467
Cdd:cd18010   198 LEELHLLLLAtIMIRR 213
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
222-468 4.08e-29

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: 115.88  E-value: 4.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd17997     4 MRDYQIRGLNWL----ISLFENGING-ILADEMGLGKTLQTISLLGYLKHYKNINGPH-----LIIVPKSTLDNWMREFK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKdaitPFAIDGKASKEELTQQLRQwsiasgRAVVRP--VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQ 379
Cdd:cd17997    74 RWCPS----LRVVVLIGDKEERADIIRD------VLLPGKfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 380 TFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrdangTDKDRKLGDERLSELLTL 459
Cdd:cd17997   144 LSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-----------VNNCDDDNQEVVQRLHKV 212

                  ....*....
gi 1832872348 460 VNKFIIRRT 468
Cdd:cd17997   213 LRPFLLRRI 221
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
222-476 2.42e-28

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: 114.00  E-value: 2.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQspeagKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd17996     4 LKEYQLKGLQWM----VSLYNNNLNG-ILADEMGLGKTIQTISLITYLMEK-----KKNNGPYLVIVPLSTLSNWVSEFE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKdaITPFAIDG-KASKEELTQQLR--QWSiasgravvrpVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDES 378
Cdd:cd17996    74 KWAPS--VSKIVYKGtPDVRKKLQSQIRagKFN----------VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 379 QTFTALNN-LNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPIlrgrdANGTDKDrklgDERLSELL 457
Cdd:cd17996   142 KLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPF-----ANTGEQV----KIELNEEE 212
                         250
                  ....*....|....*....
gi 1832872348 458 TLVnkfIIRRTNDILSKYL 476
Cdd:cd17996   213 TLL---IIRRLHKVLRPFL 228
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
222-450 1.26e-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: 110.61  E-value: 1.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTIQTIVFLYSLYKEGHSKGPF-----LVSAPLSTIINWEREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGkaskeeltqqlrqwsiasgravvrpVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd17994    71 MWAPDFYVVTYVGDH-------------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFF 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrDANGTDKDRKLGD 450
Cdd:cd17994   126 RILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA-------DISKEDQIKKLHD 187
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
222-450 5.76e-27

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


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 110.15  E-value: 5.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTVQTIVFLYSLYKEGHSKGPY-----LVSAPLSTIINWEREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDgKASKEELTQQ---LRQWSIASGRAVVR---------PVLIVSYETLRLNVEELKNTPIGLLLCDE 369
Cdd:cd18057    71 MWAPDFYVVTYTGD-KESRSVIRENefsFEDNAIRSGKKVFRmkkeaqikfHVLLTSYELITIDQAILGSIEWACLVVDE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 370 GHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrDANGTDKDRKLG 449
Cdd:cd18057   150 AHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-------DISKEDQIKKLH 222

                  .
gi 1832872348 450 D 450
Cdd:cd18057   223 D 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
222-417 3.83e-26

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: 106.32  E-value: 3.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrcttGLVDPKANGCIMADEMGLGKTLQCIALMwTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd17998     1 LKDYQLIGLNWL-----NLLYQKKLSGILADEMGLGKTIQVIAFL-AYLKEIGIPGPH-----LVVVPSSTLDNWLREFK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFaidgKASKEElTQQLRQwsIASGRAVVRPVLIVSYETLRLNVEE---LKNTPIGLLLCDEGHRLKNDES 378
Cdd:cd17998    70 RWCPSLKVEPY----YGSQEE-RKHLRY--DILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTS 142
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1832872348 379 QTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPN 417
Cdd:cd17998   143 ERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
222-450 1.48e-25

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: 105.92  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTVQTAVFLYSLYKEGHSKGPF-----LVSAPLSTIINWEREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFA--IDGKASKEELTQQLRQWSIASGRAVVR---------PVLIVSYETLRLNVEELKNTPIGLLLCDEG 370
Cdd:cd18056    71 MWAPDMYVVTYVgdKDSRAIIRENEFSFEDNAIRGGKKASRmkkeasvkfHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 371 HRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrDANGTDKDRKLGD 450
Cdd:cd18056   151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA-------DIAKEDQIKKLHD 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
222-429 1.49e-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: 105.52  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFL----YrcttglvdpKANGCIMADEMGLGKTLQCIAL---MWTLIKQSPeagkstiqkCVIACPSSLVR 294
Cdd:cd18060     1 LREYQLEGVNWLlfnwY---------NRQNCILADEMGLGKTIQSIAFlqeVYNVGIHGP---------FLVIAPLSTIT 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 295 NWANELVKWLGKDAITpfaIDGKASKEELTQQLRQWSIAS-GR----AVVRPVLIVSYETLRLNVEELKNTPIGLLLCDE 369
Cdd:cd18060    63 NWEREFNTWTEMNTIV---YHGSLASRQMIQQYEMYCKDSrGRlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDE 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 370 GHRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 429
Cdd:cd18060   140 AHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
568-683 3.46e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 100.75  E-value: 3.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 568 GKMMVLDRMLariRQDTNDKIVLISNYTQTLDvFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDpegGEFVFLLSSKA 647
Cdd:pfam00271   1 EKLEALLELL---KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1832872348 648 GGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDG 683
Cdd:pfam00271  74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
222-467 4.75e-25

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: 104.51  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQspeagKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18002     1 LKEYQLKGLNWL----ANLYEQGING-ILADEMGLGKTVQSIAVLAHLAEE-----HNIWGPFLVIAPASTLHNWQQEIS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAidGKASKEELTQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18002    71 RFVPQFKVLPYW--GNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRW 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANGtdkdrKLGDERLSELLTLVN 461
Cdd:cd18002   149 KTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKT-----GLNEHQLKRLHMILK 223

                  ....*.
gi 1832872348 462 KFIIRR 467
Cdd:cd18002   224 PFMLRR 229
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
222-450 7.82e-25

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: 103.94  E-value: 7.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTIQTIVFLYSLYKEGHTKGPF-----LVSAPLSTIINWEREFQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFA--IDGKASKEELTQQLRQWSIASGRAVVR---------PVLIVSYETLRLNVEELKNTPIGLLLCDEG 370
Cdd:cd18055    71 MWAPDFYVVTYTgdKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 371 HRLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrDANGTDKDRKLGD 450
Cdd:cd18055   151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-------DISKEDQIKKLHD 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
222-426 1.07e-24

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: 102.75  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrcttglVDPKANGCIMADEMGLGKTLQciALMwtLIKQSpeAGKSTIQKCVIACPSSLVRNWANELv 301
Cdd:cd18011     1 PLPHQIDAVLRA-------LRKPPVRLLLADEVGLGKTIE--AGL--IIKEL--LLRGDAKRVLILCPASLVEQWQDEL- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 kwLGKDAITPFAIDGKASKEELTQQLRQWsiasgraVVRPVLIVSYETLRLNVEE---LKNTPIGLLLCDEGHRLKN--- 375
Cdd:cd18011    67 --QDKFGLPFLILDRETAAQLRRLIGNPF-------EEFPIVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNsgg 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1832872348 376 -DESQTFTALNNL--NVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFR 426
Cdd:cd18011   138 gKETKRYKLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXDc smart00487
DEAD-like helicases superfamily;
214-413 4.85e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 100.64  E-value: 4.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  214 IDPRLAKVLRPHQVEGVRFLYRCTtglvdpkaNGCIMADEMGLGKTLQ-CIALMWTLIKQSPeagkstiQKCVIACP-SS 291
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL--------RDVILAAPTGSGKTLAaLLPALEALKRGKG-------GRVLVLVPtRE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  292 LVRNWANELVKWLGKDAITPFAIDGKASKEELTQQLRqwsiaSGRAvvrPVLIVSYETLRLNVEE--LKNTPIGLLLCDE 369
Cdd:smart00487  66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLE-----SGKT---DILVTTPGRLLDLLENdkLSLSNVDLVILDE 137
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1832872348  370 GHRLKND--ESQTFTALNNLNVQKRVI-LSGTP---IQNDLSEYFALLNF 413
Cdd:smart00487 138 AHRLLDGgfGDQLEKLLKLLPKNVQLLlLSATPpeeIENLLELFLNDPVF 187
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
222-441 2.55e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 99.69  E-value: 2.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYR--CttglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANE 299
Cdd:cd18054    21 LRDYQLEGLNWLAHswC-------KNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPF-----LLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 300 LVKWLGKDAITPFAIDGKASKeelTQQLRQWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQ 379
Cdd:cd18054    89 FEIWAPEINVVVYIGDLMSRN---TIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832872348 380 TFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNylgtKNEFRKRFELPILRGRDaNG 441
Cdd:cd18054   166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE----KFEFWEDFEEDHGKGRE-NG 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
222-429 5.63e-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: 98.18  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLIKqspeagKSTIQKCVIACPSSLVRNWANELV 301
Cdd:cd18059     1 LREYQLEGVNWLLFNWY-----NTRNCILADEMGLGKTIQSITFLYEIYL------KGIHGPFLVIAPLSTIPNWEREFR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAidGKASKEELTQQLRQWSIASGRAVVRP----VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDE 377
Cdd:cd18059    70 TWTELNVVVYHG--SQASRRTIQLYEMYFKDPQGRVIKGSykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1832872348 378 SQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 429
Cdd:cd18059   148 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
222-467 8.96e-23

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: 97.78  E-value: 8.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18065    16 LRDYQVRGLNWM----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH-----MVLVPKSTLHNWMNEFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKASKEELTQQLR--QWSiasgravvrpVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQ 379
Cdd:cd18065    86 RWVPSLRAVCLIGDKDARAAFIRDVMMpgEWD----------VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 380 TFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdangtDKDRKLGDERLSELLTL 459
Cdd:cd18065   156 LSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVERLHA 222

                  ....*....
gi 1832872348 460 VNK-FIIRR 467
Cdd:cd18065   223 VLKpFLLRR 231
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
222-479 1.03e-22

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: 98.20  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18064    16 LRDYQVRGLNWL----ISLYENGING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPH-----MVLVPKSTLHNWMAEFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLgkDAITPFAIDGKaskeeltqqlRQWSIASGRAVVRP----VLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDE 377
Cdd:cd18064    86 RWV--PTLRAVCLIGD----------KDQRAAFVRDVLLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 378 SQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdangtDKDRKLGDERLSELL 457
Cdd:cd18064   154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-------------DTNNCLGDQKLVERL 220
                         250       260
                  ....*....|....*....|...
gi 1832872348 458 TLVNK-FIIRRTNDILSKYLPVK 479
Cdd:cd18064   221 HMVLRpFLLRRIKADVEKSLPPK 243
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
222-429 1.16e-22

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


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 97.42  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFL----YrcttglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAgkstiqKCVIACPSSLVRNWA 297
Cdd:cd18058     1 LREYQLEGMNWLlfnwY---------NRKNCILADEMGLGKTIQSITFLSEIFLMGIRG------PFLIIAPLSTITNWE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 298 NELVKWLGKDAITpfaIDGKASKEELTQQLR------QWSIASGRAVVRpVLIVSYETLRLNVEELKNTPIGLLLCDEGH 371
Cdd:cd18058    66 REFRTWTEMNAIV---YHGSQISRQMIQQYEmyyrdeQGNPLSGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAH 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832872348 372 RLKNDESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 429
Cdd:cd18058   142 RLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
222-467 1.29e-22

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: 97.83  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18063    24 LKHYQLQGLEWM----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNGPY-----LIIVPLSTLSNWTYEFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWlgKDAITPFAIDGK-ASKEELTQQLRqwsiaSGRAvvrPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQT 380
Cdd:cd18063    94 KW--APSVVKISYKGTpAMRRSLVPQLR-----SGKF---NVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 381 FTALNNLNVQ-KRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI-LRGRDANGTDKDRKLGDERLSELLt 458
Cdd:cd18063   164 TQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLHKVL- 242

                  ....*....
gi 1832872348 459 lvNKFIIRR 467
Cdd:cd18063   243 --RPFLLRR 249
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
221-467 2.67e-22

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 97.04  E-value: 2.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 221 VLRPHQVEGVRFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANEL 300
Cdd:cd18062    23 VLKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPF-----LIIVPLSTLSNWVYEF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWlgKDAITPFAIDGK-ASKEELTQQLRqwsiaSGRAvvrPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQ 379
Cdd:cd18062    93 DKW--APSVVKVSYKGSpAARRAFVPQLR-----SGKF---NVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 380 TFTALNNLNVQ-KRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI-LRGRDANGTDKDRKLGDERLSELL 457
Cdd:cd18062   163 LTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHKVL 242
                         250
                  ....*....|
gi 1832872348 458 tlvNKFIIRR 467
Cdd:cd18062   243 ---RPFLLRR 249
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
222-429 4.41e-21

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: 92.76  E-value: 4.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAgkstiqKCVIACPSSLVRNWANELV 301
Cdd:cd18061     1 LREYQLEGLNWLLFNWY-----NRRNCILADEMGLGKTIQSITFLYEILLTGIRG------PFLIIAPLSTIANWEREFR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITpfaIDGKASKEELTQQLRQWSIASGRAVVR-----PVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKND 376
Cdd:cd18061    70 TWTDLNVVV---YHGSLISRQMIQQYEMYFRDSQGRIIRgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1832872348 377 ESQTFTALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 429
Cdd:cd18061   147 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
244-415 1.04e-20

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 92.16  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 244 KANGCIMADEMGLGKTLQCIAL-----------------MWTLIKQSPEAGKSTIQKCVIACPSSLVRNWANELVKWLGK 306
Cdd:cd18072    19 KPRGGILADDMGLGKTLTMIALilaqkntqnrkeeekekALTEWESKKDSTLVPSAGTLVVCPASLVHQWKNEVESRVAS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 307 DAITPFAIDGkASKEELTQQLRQWSIasgraVVRPVLIVSYEtLRLNVEELKNTPIGL-----LLCDEGHRLKNDESQTF 381
Cdd:cd18072    99 NKLRVCLYHG-PNRERIGEVLRDYDI-----VITTYSLVAKE-IPTYKEESRSSPLFRiawarIILDEAHNIKNPKVQAS 171
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFAN 415
Cdd:cd18072   172 IAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
HELICc smart00490
helicase superfamily c-terminal domain;
599-683 1.43e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.50  E-value: 1.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  599 DVFDKLCRSRGYGCLRLDGTMNVNKRQKLVDKFNDpegGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALAR 678
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 1832872348  679 VWRDG 683
Cdd:smart00490  78 AGRAG 82
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
222-448 1.08e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 88.95  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLIKQSPEAGKStiqkcVIACPSSLVRNWANELV 301
Cdd:cd18053    21 LRDYQLNGLNWLAHSWC-----KGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPF-----LLVVPLSTLTSWQREIQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 302 KWLGKDAITPFAIDGKASKEELTQQlrqWSIASGRAVVRPVLIVSYETLRLNVEELKNTPIGLLLCDEGHRLKNDESQTF 381
Cdd:cd18053    91 TWAPQMNAVVYLGDINSRNMIRTHE---WMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLY 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832872348 382 TALNNLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilRGRDANGTDKDRKL 448
Cdd:cd18053   168 KTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHG----KGREYGYASLHKEL 230
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
247-467 4.96e-18

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: 84.06  E-value: 4.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 247 GCIMADEMGLGKTLQCIALMWTlikqspeagkstiQKCVIACPSSLVRNWANELVKWLGKDAITPFAIDGKASKEELTQQ 326
Cdd:cd18071    50 GGILADDMGLGKTLTTISLILA-------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 327 LRQwsiasgravvrPVLIVSYETLRLNVEELKNTPIGLL-----LCDEGHRLKNDESQTFTALNNLNVQKRVILSGTPIQ 401
Cdd:cd18071   117 SKY-----------DIVLTTYNTLASDFGAKGDSPLHTInwlrvVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQ 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832872348 402 NDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDANgtdkdrklgderLSELLTLVNKFIIRR 467
Cdd:cd18071   186 NSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTG------------LKRLQVLMKQITLRR 239
DpdE NF041062
protein DpdE;
222-681 1.76e-10

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 64.99  E-value: 1.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  222 LRPHQVEGVRflyrctTGLVDPkangcIM----ADEMGLGKTLQCIALMWTLIKQSPEAgkstiqKCVIACPSSLVRNWA 297
Cdd:NF041062   154 LEPHQVAVVR------RVLQDP-----VQryllADEVGLGKTIEAGLVIRQHLLDNPDA------RVLVLVPDALVRQWR 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  298 NELvkwlgkdaITPFAIDgkaskEELTQQLRqwsiasgravvrpvlIVSYETLRLnVEELKNTPiGLLLCDEGHRL---- 373
Cdd:NF041062   217 REL--------RDKFFLD-----DFPGARVR---------------VLSHEEPER-WEPLLDAP-DLLVVDEAHQLarla 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  374 ---KNDESQTFTALNNL-NVQKRVI-LSGTPIQNDLSEYFALLNFANP-NY-LGTKNEFRKRFEL-----PILRGRDANG 441
Cdd:NF041062   267 wsgDPPERARYRELAALaHAAPRLLlLSATPVLGNEETFLALLHLLDPdLYpLDDLEAFRERLEEreelgRLVLGLDPDN 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  442 TD----------KDRKLGDERLSEL----LTLVNKFIIRRTNDI------LSKYLpvkyehvvfcnlapfqKDLYNLFiq 501
Cdd:NF041062   347 PNfllrqaldelRALFPEDEELQELaeelLPLLDEFDDEEPEERaravsaLRAHI----------------SETYRLH-- 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  502 speiRQLLRGKGSQPLKAI------NILKKLCNHPDLLDLPSDL------------PGSESCF----------------- 546
Cdd:NF041062   409 ----RRMIRNRRSSVLGADylvpgrAGPRVLVWESPAREAADEAledwreeaalldAESDPAAraayaralawlvarlgg 484
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348  547 PDDFVPKdARGRDRDVK--SWYSGKMMVLDRMLARIRQDTND-------------------KIVLISNYTQTLD-VFDKL 604
Cdd:NF041062   485 PDDLAAL-LRWRLRGDAasADLAGERELLEALIAALEDEAKDadllaaladwllpllrgsgKAVVFCGDGSLADhLAAAL 563
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832872348  605 CRSRGYGCLRLDGTMNVNKRQKLVDKFNDPEGGeFVfLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWR 681
Cdd:NF041062   564 ARLGAGSVERHLSGQGADQAERAVRAFRQDPSA-RV-LVCDRSGEEGLNLQGADRLVHLDLPWSPNRLEQRIGRLDR 638
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
222-409 9.12e-10

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: 59.29  E-value: 9.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrcttgLVDPKAngCIMADeMGLGKTLQCIALMWTLIKQSPeagkstIQKCVIACPSSLVRN-WANEL 300
Cdd:cd18013     1 PHPYQKVAINFI------IEHPYC--GLFLD-MGLGKTVTTLTALSDLQLDDF------TRRVLVIAPLRVARStWPDEV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWLGKDAITPFAIDGKASKeeltqqlRQWSIASGRAvvrpVLIVSYETLRLNVEELKNT-PIGLLLCDEGHRLKNDESQ 379
Cdd:cd18013    66 EKWNHLRNLTVSVAVGTERQ-------RSKAANTPAD----LYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSK 134
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1832872348 380 TFTALNNLNVQ-KRVI-LSGTPIQNDLSEYFA 409
Cdd:cd18013   135 RFKALRKVRPViKRLIgLTGTPSPNGLMDLWA 166
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
222-413 2.21e-09

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: 58.89  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLyrcttglvdpKANGCIMADEMGLGKTLQCIALMWT------------------------LIKQSPEAG 277
Cdd:cd18070     1 LLPYQRRAVNWM----------LVPGGILADEMGLGKTVEVLALILLhprpdndldaadddsdemvccpdcLVAETPVSS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 278 KSTIqkcvIACPSSLVRNWANEL-------VKWLGKDAITpfaiDGKASKEELTQQLRQWSIasgravvrpvLIVSYETL 350
Cdd:cd18070    71 KATL----IVCPSAILAQWLDEInrhvpssLKVLTYQGVK----KDGALASPAPEILAEYDI----------VVTTYDVL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 351 RLNVEELK-----------------NTPigLLLCdEGHRLKNDESQ-----TFTALN---NLNVQKRVILSGTPIQNDLS 405
Cdd:cd18070   133 RTELHYAEanrsnrrrrrqkryeapPSP--LVLV-EWWRVCLDEAQmvessTSKAAEmarRLPRVNRWCVSGTPIQRGLD 209

                  ....*...
gi 1832872348 406 EYFALLNF 413
Cdd:cd18070   210 DLFGLLSF 217
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
222-740 3.86e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 60.04  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 222 LRPHQVEGVRFLYRCTTGlvDPKANGCIMAdeMGLGKTLqcIALMwtLIKQSpeagkSTIQKCVIACPS-SLVRNWANEL 300
Cdd:COG1061    81 LRPYQQEALEALLAALER--GGGRGLVVAP--TGTGKTV--LALA--LAAEL-----LRGKRVLVLVPRrELLEQWAEEL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 301 VKWLGKdaitPFAIDGKASKEeltqqlrqwsiasgravvRPVLIVSYETL--RLNVEELKNTpIGLLLCDEGHRLkndES 378
Cdd:COG1061   148 RRFLGD----PLAGGGKKDSD------------------APITVATYQSLarRAHLDELGDR-FGLVIIDEAHHA---GA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 379 QTFTA-LNNLNVQKRVILSGTPIQND-LSEYFALLnfanpnylgtkneFRKRFELPIlrgRDAngtdkdrklgderlsel 456
Cdd:COG1061   202 PSYRRiLEAFPAAYRLGLTATPFRSDgREILLFLF-------------DGIVYEYSL---KEA----------------- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 457 ltlvnkfiirrtndILSKYL-PVKYeHVVFCNLAPFQKDlYNLFIQspEIRQLLrgkgsqplkainilkklcnhpdlldl 535
Cdd:COG1061   249 --------------IEDGYLaPPEY-YGIRVDLTDERAE-YDALSE--RLREAL-------------------------- 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 536 psdlpgsescfpddfVPKDARgrdrdvkswysgKMMVLDRMLARIRQDtnDKIVLISNYTQTLDVFDKLCRSRGYGCLRL 615
Cdd:COG1061   285 ---------------AADAER------------KDKILRELLREHPDD--RKTLVFCSSVDHAEALAELLNEAGIRAAVV 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 616 DGTMNVNKRQKLVDKFNDpegGEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQ-KKDCFVYRFI 694
Cdd:COG1061   336 TGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFV 412
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1832872348 695 ATGT-IEEKIFQRQSHKSALSSCVVDSAEDVERHFSIDSLRELFQYQ 740
Cdd:COG1061   413 GNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKG 459
ResIII pfam04851
Type III restriction enzyme, res subunit;
220-400 2.73e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 51.13  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 220 KVLRPHQVEGVRflyRCTTGLVDPKANGCI-MAdeMGLGKTLQCIALMWTLIKqspeagKSTIQKCVIACPS-SLVRNWA 297
Cdd:pfam04851   2 LELRPYQIEAIE---NLLESIKNGQKRGLIvMA--TGSGKTLTAAKLIARLFK------KGPIKKVLFLVPRkDLLEQAL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 298 NELVKWLGKDAITPFAIDGKASKEELTQqlrqwsiasgravvRPVLIVSYETL----RLNVEELKNTPIGLLLCDEGHRL 373
Cdd:pfam04851  71 EEFKKFLPNYVEIGEIISGDKKDESVDD--------------NKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRS 136
                         170       180
                  ....*....|....*....|....*..
gi 1832872348 374 kNDESQTfTALNNLNVQKRVILSGTPI 400
Cdd:pfam04851 137 -GASSYR-NILEYFKPAFLLGLTATPE 161
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
245-398 7.55e-05

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: 43.55  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 245 ANGCIMADEMGLGKTLqcIALMWTLikqspEAGKSTIQKCVIACP-SSLVRNWANELVKWLGKDaITPFAIDGKASKEEL 323
Cdd:cd00046     1 GENVLITAPTGSGKTL--AALLAAL-----LLLLKKGKKVLVLVPtKALALQTAERLRELFGPG-IRVAVLVGGSSAEER 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 324 TqqlrqwSIASGRAvvrPVLIVSYETLRLNVEELKN---TPIGLLLCDEGHRLKNDE------SQTFTALNNLNVQkRVI 394
Cdd:cd00046    73 E------KNKLGDA---DIIIATPDMLLNLLLREDRlflKDLKLIIVDEAHALLIDSrgalilDLAVRKAGLKNAQ-VIL 142

                  ....
gi 1832872348 395 LSGT 398
Cdd:cd00046   143 LSAT 146
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
214-373 6.20e-04

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: 41.52  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 214 IDPRLAKVLRPHQVEGVRFLY---RCTTGL-VDPkangCimademGLGKTLQCIALMwtlikqspeagkSTIQK-CVIAC 288
Cdd:cd18029     1 IDLKPSTQLRPYQEKALSKMFgngRARSGViVLP----C------GAGKTLVGITAA------------CTIKKsTLVLC 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 289 PSSL-VRNWANELVKW--LGKDAITPFAIDGKAskeeltqqlrqwsiasgRAVVRPVLIVSYETLR----------LNVE 355
Cdd:cd18029    59 TSAVsVEQWRRQFLDWttIDDEQIGRFTSDKKE-----------------IFPEAGVTVSTYSMLAntrkrspeseKFME 121
                         170
                  ....*....|....*...
gi 1832872348 356 ELKNTPIGLLLCDEGHRL 373
Cdd:cd18029   122 FITEREWGLIILDEVHVV 139
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
569-710 1.18e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.41  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832872348 569 KMMVLDRMLARIRQ-DTNDKIVLISNYTQTLDVFDKLCRSRGYGCLRL--------DGTMNVNKRQKLVDKFNDpegGEF 639
Cdd:COG1111   336 KLSKLREILKEQLGtNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRA---GEF 412
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832872348 640 VFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKdcfVYRFIATGTIEEKIFQRQSHK 710
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR---VVVLIAKGTRDEAYYWSSRRK 480
 
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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