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Conserved domains on  [gi|446429215|ref|WP_000507070|]
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MULTISPECIES: DEAD/DEAH box helicase [Bacillus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12052773)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
447-1044 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 618.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  447 EDAEYNFLYHIVPTLKGLVDIYATTAIKLRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYR 526
Cdd:COG0553    77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  527 LANGSLLSLESKEFNEINQFVKESGIRKEFLHGEEVNVPLIRSVKWMNGLHEGNVLSLDESVQDLVESIQNPKKLkFTVP 606
Cdd:COG0553   157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREAL-ESLP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  607 QTLRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFA 686
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELK--ERGLARPVLIVAPTSLVGNWQRELAKFA 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  687 PHIRAVIADGnQAERRKILKDVAEFDVVITSYPLLRRDIRSY-ARPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGL 765
Cdd:COG0553   314 PGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLaAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  766 TGTPVENSLEELWSIFHVVFPELLPGRKEFGDL-----------RREDIAKRVKPFVLRRLKEDVLKELPDKIEHLQSSE 834
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgdeeALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVE 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  835 LLPDQKRLYAAYLAKLREetlkHLDKDTLRKNKIRILAGLTRLRQICCHPALFVDD---YKGSSAKFEQLLDILEECRST 911
Cdd:COG0553   473 LTPEQRALYEAVLEYLRR----ELEGAEGIRRRGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAE 548
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  912 GKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEG-DLFLISLKAGGTGLNLTGADTVILYDL 990
Cdd:COG0553   549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDL 628
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446429215  991 WWNPAVEQQAADRAYRMGQKNTVQVIKLVAHGTIEEKMHELQESKKNLIAEVIE 1044
Cdd:COG0553   629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
235-606 2.61e-90

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


:

Pssm-ID: 462483  Cd Length: 370  Bit Score: 294.14  E-value: 2.61e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   235 IFIPPASWNDMLSALSRAEYVQLKQNEQLFHGLQISKGLLPLHFEFTKGNNGGFTLHIAGLnRVRVMEMYNNALYDGKLY 314
Cdd:pfam08455    1 LVLPPSLLDEFLELLKGRKFYLELDEGEELKEVKIVEENPPLSFSLKKEKDDGIILTLNKD-PILLGEDYLYFLYDGTIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   315 HLPMEDCMRLIELQKMMIRSNSNQFYIPENKMEHFVAKVVPGLMKLGTVRIDEGISDRVETPSLKAKLYLDRVKNRLLAG 394
Cdd:pfam08455   80 RLSKEQCKLLSPLLKLLNLLGTKEITISKEDLPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLDRDDDRITAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   395 LEFHYGNVVINPLEEdgqpSVFNRDEKKEKEILDIMSESAFAKTEGGYFMHNEDAEYNFLYHIVPTLKGLVDIYATTAIK 474
Cdd:pfam08455  160 VKFQYGDIEFNPLED----LILVRDVEKEAKILNLLEQYGFKVDDGKFYLDDEEKIYDFLTEGLPKLQELGEVYYSDAFK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   475 LRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYRLANGSLLSLESKEFNEINQFVKESGIRK 554
Cdd:pfam08455  236 NLKVKPSPSVSVGVSVDEEGNLLEISFDIDGIDEEELANILQALREKKKYYRLKDGSFLDLEEEELKELSELLDELGLSK 315
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446429215   555 EFLHGEEVNVPLIRSV---KWMNGLHEGNVLSLDESVQDLVESIQNPKKLKFTVP 606
Cdd:pfam08455  316 KDLENGTIKLPKYRALyldELLEENELIGSIKRDKEFKQLVEDLKNPEDSDFEVP 370
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
3-108 5.15e-18

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


:

Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 88.73  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    3 FTLNKSIIKEVCGETSYKRGEAYYKSNKVIvnHYDETKEICEATVKGNEDFHVTVEKAKKGDVVARCSCPslASFQTYCQ 82
Cdd:COG4715     4 LELTEDDIRRLAGPRIFERGREYAREGRVL--DLDVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCP--YGGGGFCK 79
                          90       100
                  ....*....|....*....|....*.
gi 446429215   83 HVAAVLIQInYNQQTGGMGSVSSRND 108
Cdd:COG4715    80 HVVAVLLAL-LDQPEEGAPRQSEREA 104
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
447-1044 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 618.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  447 EDAEYNFLYHIVPTLKGLVDIYATTAIKLRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYR 526
Cdd:COG0553    77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  527 LANGSLLSLESKEFNEINQFVKESGIRKEFLHGEEVNVPLIRSVKWMNGLHEGNVLSLDESVQDLVESIQNPKKLkFTVP 606
Cdd:COG0553   157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREAL-ESLP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  607 QTLRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFA 686
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELK--ERGLARPVLIVAPTSLVGNWQRELAKFA 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  687 PHIRAVIADGnQAERRKILKDVAEFDVVITSYPLLRRDIRSY-ARPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGL 765
Cdd:COG0553   314 PGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLaAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  766 TGTPVENSLEELWSIFHVVFPELLPGRKEFGDL-----------RREDIAKRVKPFVLRRLKEDVLKELPDKIEHLQSSE 834
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgdeeALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVE 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  835 LLPDQKRLYAAYLAKLREetlkHLDKDTLRKNKIRILAGLTRLRQICCHPALFVDD---YKGSSAKFEQLLDILEECRST 911
Cdd:COG0553   473 LTPEQRALYEAVLEYLRR----ELEGAEGIRRRGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAE 548
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  912 GKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEG-DLFLISLKAGGTGLNLTGADTVILYDL 990
Cdd:COG0553   549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDL 628
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446429215  991 WWNPAVEQQAADRAYRMGQKNTVQVIKLVAHGTIEEKMHELQESKKNLIAEVIE 1044
Cdd:COG0553   629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
609-816 6.22e-94

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: 297.94  E-value: 6.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  609 LRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKklPILVVSPSSLVYNWLSELKKFAPH 688
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKG--PSLVVAPTSLIYNWEEEAAKFAPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  689 IRAVIADGNQAERRKiLKDVAEFDVVITSYPLLRRDIRSYA-RPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTG 767
Cdd:cd18012    79 LKVLVIHGTKRKREK-LRALEDYDLVITSYGLLRRDIELLKeVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446429215  768 TPVENSLEELWSIFHVVFPELLPGRKEFGDL------------RREDIAKRVKPFVLRRLK 816
Cdd:cd18012   158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRfakpiekdgdeeALEELKKLISPFILRRLK 218
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
235-606 2.61e-90

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


Pssm-ID: 462483  Cd Length: 370  Bit Score: 294.14  E-value: 2.61e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   235 IFIPPASWNDMLSALSRAEYVQLKQNEQLFHGLQISKGLLPLHFEFTKGNNGGFTLHIAGLnRVRVMEMYNNALYDGKLY 314
Cdd:pfam08455    1 LVLPPSLLDEFLELLKGRKFYLELDEGEELKEVKIVEENPPLSFSLKKEKDDGIILTLNKD-PILLGEDYLYFLYDGTIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   315 HLPMEDCMRLIELQKMMIRSNSNQFYIPENKMEHFVAKVVPGLMKLGTVRIDEGISDRVETPSLKAKLYLDRVKNRLLAG 394
Cdd:pfam08455   80 RLSKEQCKLLSPLLKLLNLLGTKEITISKEDLPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLDRDDDRITAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   395 LEFHYGNVVINPLEEdgqpSVFNRDEKKEKEILDIMSESAFAKTEGGYFMHNEDAEYNFLYHIVPTLKGLVDIYATTAIK 474
Cdd:pfam08455  160 VKFQYGDIEFNPLED----LILVRDVEKEAKILNLLEQYGFKVDDGKFYLDDEEKIYDFLTEGLPKLQELGEVYYSDAFK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   475 LRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYRLANGSLLSLESKEFNEINQFVKESGIRK 554
Cdd:pfam08455  236 NLKVKPSPSVSVGVSVDEEGNLLEISFDIDGIDEEELANILQALREKKKYYRLKDGSFLDLEEEELKELSELLDELGLSK 315
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446429215   555 EFLHGEEVNVPLIRSV---KWMNGLHEGNVLSLDESVQDLVESIQNPKKLKFTVP 606
Cdd:pfam08455  316 KDLENGTIKLPKYRALyldELLEENELIGSIKRDKEFKQLVEDLKNPEDSDFEVP 370
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
603-1046 1.58e-79

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 281.69  E-value: 1.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  603 FTVPQTLRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSEL 682
Cdd:PLN03142  160 LVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLL-GYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  683 KKFAPHIRAVIADGNQAERRKI---LKDVAEFDVVITSYPLLRRDiRSYARPFH--TLFLDEAQAFKNPTTQTARAVKTI 757
Cdd:PLN03142  239 RRFCPVLRAVKFHGNPEERAHQreeLLVAGKFDVCVTSFEMAIKE-KTALKRFSwrYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  758 QAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF-------GDLRREDIA----KRVKPFVLRRLKEDVLKELPDK 826
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFdewfqisGENDQQEVVqqlhKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  827 IEHLQSSELLPDQKRLYAAYLAKlreeTLKHLDKDTLRKnkiRILAGLTRLRQICCHPALFVDDYKG-----------SS 895
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQK----DLDVVNAGGERK---RLLNIAMQLRKCCNHPYLFQGAEPGppyttgehlveNS 470
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  896 AKFEQLLDILEECRSTGKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNE--GEGDLFLISLKAG 973
Cdd:PLN03142  471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAG 550
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  974 GTGLNLTGADTVILYDLWWNPAVEQQAADRAYRMGQKNTVQVIKLVAHGTIEEKMHELQESKKNLIAEVIEPG 1046
Cdd:PLN03142  551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
616-887 1.13e-56

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: 197.91  E-value: 1.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   616 YQVYGFEWMKTLayYRF---GGILADDMGLGKTLQSIAYIDSVLPEIREKKLPILVVSPSSLVYNWLSELKKFA--PHIR 690
Cdd:pfam00176    1 YQIEGVNWMLSL--ENNlgrGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   691 AVIADGNQAERRKILKD---VAEFDVVITSYPLLRR--DIRSYARPFHtLFLDEAQAFKNPTTQTARAVKTIQAEYRFGL 765
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDpnfLADFDVVITTYETLRKhkELLKKVHWHR-IVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   766 TGTPVENSLEELWSIFHVVFPELLPGRKEF------------GDLRREDIAKRVKPFVLRRLKEDVLKELPDKIEHLQSS 833
Cdd:pfam00176  158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFrnwfdrpierggGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446429215   834 ELLPDQKRLYAAYLAKLREETLKHLDKDtlRKNKIRILAGLTRLRQICCHPALF 887
Cdd:pfam00176  238 RLSKLQRKLYQTFLLKKDLNAIKTGEGG--REIKASLLNILMRLRKICNHPGLI 289
HELICc smart00490
helicase superfamily c-terminal domain;
927-1008 8.44e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.35  E-value: 8.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    927 IIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEGDlFLISLKAGGTGLNLTGADTVILYDLWWNPAVEQQAADRAYR 1006
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK-VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 446429215   1007 MG 1008
Cdd:smart00490   81 AG 82
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
3-108 5.15e-18

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 88.73  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    3 FTLNKSIIKEVCGETSYKRGEAYYKSNKVIvnHYDETKEICEATVKGNEDFHVTVEKAKKGDVVARCSCPslASFQTYCQ 82
Cdd:COG4715     4 LELTEDDIRRLAGPRIFERGREYAREGRVL--DLDVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCP--YGGGGFCK 79
                          90       100
                  ....*....|....*....|....*.
gi 446429215   83 HVAAVLIQInYNQQTGGMGSVSSRND 108
Cdd:COG4715    80 HVVAVLLAL-LDQPEEGAPRQSEREA 104
SWIM pfam04434
SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is ...
53-92 2.47e-05

SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is predicted to be organized into two N-terminal beta-strands and a C-terminal alpha helix, thus possibly adopting a fold similar to that of the C2H2 zinc finger (pfam00096). SWIM is thought to be a versatile domain that can interact with DNA or proteins in different contexts.


Pssm-ID: 309540  Cd Length: 38  Bit Score: 42.41  E-value: 2.47e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 446429215    53 FHVTVEKAKKGDvvARCSCPSLASFQTYCQHVAAVLIQIN 92
Cdd:pfam04434    1 YRVQLDLDGLEK--ASCSCPDFQLNGIPCKHALAVLLALG 38
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
447-1044 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 618.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  447 EDAEYNFLYHIVPTLKGLVDIYATTAIKLRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYR 526
Cdd:COG0553    77 LSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  527 LANGSLLSLESKEFNEINQFVKESGIRKEFLHGEEVNVPLIRSVKWMNGLHEGNVLSLDESVQDLVESIQNPKKLkFTVP 606
Cdd:COG0553   157 LLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREAL-ESLP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  607 QTLRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFA 686
Cdd:COG0553   236 AGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELK--ERGLARPVLIVAPTSLVGNWQRELAKFA 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  687 PHIRAVIADGnQAERRKILKDVAEFDVVITSYPLLRRDIRSY-ARPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGL 765
Cdd:COG0553   314 PGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLaAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  766 TGTPVENSLEELWSIFHVVFPELLPGRKEFGDL-----------RREDIAKRVKPFVLRRLKEDVLKELPDKIEHLQSSE 834
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERfarpiekgdeeALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVE 472
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  835 LLPDQKRLYAAYLAKLREetlkHLDKDTLRKNKIRILAGLTRLRQICCHPALFVDD---YKGSSAKFEQLLDILEECRST 911
Cdd:COG0553   473 LTPEQRALYEAVLEYLRR----ELEGAEGIRRRGLILAALTRLRQICSHPALLLEEgaeLSGRSAKLEALLELLEELLAE 548
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  912 GKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEG-DLFLISLKAGGTGLNLTGADTVILYDL 990
Cdd:COG0553   549 GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEaPVFLISLKAGGEGLNLTAADHVIHYDL 628
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446429215  991 WWNPAVEQQAADRAYRMGQKNTVQVIKLVAHGTIEEKMHELQESKKNLIAEVIE 1044
Cdd:COG0553   629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
609-816 6.22e-94

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: 297.94  E-value: 6.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  609 LRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKklPILVVSPSSLVYNWLSELKKFAPH 688
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKG--PSLVVAPTSLIYNWEEEAAKFAPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  689 IRAVIADGNQAERRKiLKDVAEFDVVITSYPLLRRDIRSYA-RPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTG 767
Cdd:cd18012    79 LKVLVIHGTKRKREK-LRALEDYDLVITSYGLLRRDIELLKeVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446429215  768 TPVENSLEELWSIFHVVFPELLPGRKEFGDL------------RREDIAKRVKPFVLRRLK 816
Cdd:cd18012   158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRfakpiekdgdeeALEELKKLISPFILRRLK 218
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
235-606 2.61e-90

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


Pssm-ID: 462483  Cd Length: 370  Bit Score: 294.14  E-value: 2.61e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   235 IFIPPASWNDMLSALSRAEYVQLKQNEQLFHGLQISKGLLPLHFEFTKGNNGGFTLHIAGLnRVRVMEMYNNALYDGKLY 314
Cdd:pfam08455    1 LVLPPSLLDEFLELLKGRKFYLELDEGEELKEVKIVEENPPLSFSLKKEKDDGIILTLNKD-PILLGEDYLYFLYDGTIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   315 HLPMEDCMRLIELQKMMIRSNSNQFYIPENKMEHFVAKVVPGLMKLGTVRIDEGISDRVETPSLKAKLYLDRVKNRLLAG 394
Cdd:pfam08455   80 RLSKEQCKLLSPLLKLLNLLGTKEITISKEDLPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLDRDDDRITAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   395 LEFHYGNVVINPLEEdgqpSVFNRDEKKEKEILDIMSESAFAKTEGGYFMHNEDAEYNFLYHIVPTLKGLVDIYATTAIK 474
Cdd:pfam08455  160 VKFQYGDIEFNPLED----LILVRDVEKEAKILNLLEQYGFKVDDGKFYLDDEEKIYDFLTEGLPKLQELGEVYYSDAFK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   475 LRIHKGDTAPLIRVRRKERIDWLSFRFDIKGIPEAEIKGVLVALEEKRKYYRLANGSLLSLESKEFNEINQFVKESGIRK 554
Cdd:pfam08455  236 NLKVKPSPSVSVGVSVDEEGNLLEISFDIDGIDEEELANILQALREKKKYYRLKDGSFLDLEEEELKELSELLDELGLSK 315
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446429215   555 EFLHGEEVNVPLIRSV---KWMNGLHEGNVLSLDESVQDLVESIQNPKKLKFTVP 606
Cdd:pfam08455  316 KDLENGTIKLPKYRALyldELLEENELIGSIKRDKEFKQLVEDLKNPEDSDFEVP 370
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
603-1046 1.58e-79

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 281.69  E-value: 1.58e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  603 FTVPQTLRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSEL 682
Cdd:PLN03142  160 LVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLL-GYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  683 KKFAPHIRAVIADGNQAERRKI---LKDVAEFDVVITSYPLLRRDiRSYARPFH--TLFLDEAQAFKNPTTQTARAVKTI 757
Cdd:PLN03142  239 RRFCPVLRAVKFHGNPEERAHQreeLLVAGKFDVCVTSFEMAIKE-KTALKRFSwrYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  758 QAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF-------GDLRREDIA----KRVKPFVLRRLKEDVLKELPDK 826
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFdewfqisGENDQQEVVqqlhKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  827 IEHLQSSELLPDQKRLYAAYLAKlreeTLKHLDKDTLRKnkiRILAGLTRLRQICCHPALFVDDYKG-----------SS 895
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQK----DLDVVNAGGERK---RLLNIAMQLRKCCNHPYLFQGAEPGppyttgehlveNS 470
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  896 AKFEQLLDILEECRSTGKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNE--GEGDLFLISLKAG 973
Cdd:PLN03142  471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAG 550
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  974 GTGLNLTGADTVILYDLWWNPAVEQQAADRAYRMGQKNTVQVIKLVAHGTIEEKMHELQESKKNLIAEVIEPG 1046
Cdd:PLN03142  551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
613-814 1.24e-64

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 216.28  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFL-AYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKIL--KDVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTP 769
Cdd:cd17919    80 VYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKASLRKfRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446429215  770 VENSLEELWSIFHVVFPellpgrkefgdlrrediakrvkPFVLRR 814
Cdd:cd17919   160 LQNNLEELWALLDFLDP----------------------PFLLRR 182
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
895-1019 1.60e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.23  E-value: 1.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  895 SAKFEQLLDILEECRSTGKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEGD-LFLISLKAG 973
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446429215  974 GTGLNLTGADTVILYDLWWNPAVEQQAADRAYRMGQKNTVQVIKLV 1019
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
616-887 1.13e-56

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: 197.91  E-value: 1.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   616 YQVYGFEWMKTLayYRF---GGILADDMGLGKTLQSIAYIDSVLPEIREKKLPILVVSPSSLVYNWLSELKKFA--PHIR 690
Cdd:pfam00176    1 YQIEGVNWMLSL--ENNlgrGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   691 AVIADGNQAERRKILKD---VAEFDVVITSYPLLRR--DIRSYARPFHtLFLDEAQAFKNPTTQTARAVKTIQAEYRFGL 765
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDpnfLADFDVVITTYETLRKhkELLKKVHWHR-IVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   766 TGTPVENSLEELWSIFHVVFPELLPGRKEF------------GDLRREDIAKRVKPFVLRRLKEDVLKELPDKIEHLQSS 833
Cdd:pfam00176  158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFrnwfdrpierggGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 446429215   834 ELLPDQKRLYAAYLAKLREETLKHLDKDtlRKNKIRILAGLTRLRQICCHPALF 887
Cdd:pfam00176  238 RLSKLQRKLYQTFLLKKDLNAIKTGEGG--REIKASLLNILMRLRKICNHPGLI 289
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
613-814 3.19e-49

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: 174.46  E-value: 3.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIA------YIDSVLPEIRekKLPILVVSPSSLVYNWLSELKKFA 686
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCilasdhHKRANSFNSE--NLPSLVVCPPTLVGHWVAEIKKYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  687 PH--IRAVIADGNQAERRKILKDVAEFDVVITSYPLLRRDIRSYA-RPFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRF 763
Cdd:cd17999    79 PNafLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTkIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446429215  764 GLTGTPVENSLEELWSIFHVVFPELLPGRKEF-----------------------GDLRREDIAKRVKPFVLRR 814
Cdd:cd17999   159 ILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFqrrflkpilasrdskasakeqeaGALALEALHKQVLPFLLRR 232
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
612-816 3.98e-45

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: 162.94  E-value: 3.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  612 VMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYidsvLPEIREKKL--PILVVSPSSLVYNWLSELKKFAPHI 689
Cdd:cd18009     3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIAL----LAHLRERGVwgPFLVIAPLSTLPNWVNEFARFTPSV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  690 RAVIADGNQAERRKILKDV-------AEFDVVITSYPLLRRDiRSYARPFHTLFL--DEAQAFKNPTTQTARAVKTIQAE 760
Cdd:cd18009    79 PVLLYHGTKEERERLRKKImkregtlQDFPVVVTSYEIAMRD-RKALQHYAWKYLivDEGHRLKNLNCRLIQELKTFNSD 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446429215  761 YRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF-------------------GDLRREDIAKR----VKPFVLRRLK 816
Cdd:cd18009   158 NRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFeswfdfsslsdnaadisnlSEEREQNIVHMlhaiLKPFLLRRLK 236
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
613-814 1.55e-44

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: 161.39  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVL-------------PEIREK------KLPILVVSPSS 673
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrPRFKKKppassaKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  674 LVYNWLSELKKFApHIR-AVIADGNQAERRKILKDVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTA 751
Cdd:cd18005    81 VLYNWKDELDTWG-HFEvGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSiNWSAVIADEAHRIKNPKSKLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  752 RAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF-----------------------GDLRREDIAKRVK 808
Cdd:cd18005   160 QAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFkkhfsepikrgqrhtatarelrlGRKRKQELAVKLS 239

                  ....*.
gi 446429215  809 PFVLRR 814
Cdd:cd18005   240 KFFLRR 245
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
613-814 1.67e-44

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: 160.60  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALL-AHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILKDVAE---FDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGT 768
Cdd:cd18003    80 TYYGSAKERKLKRQGWMKpnsFHVCITSYQLVVQDHQVFKRkKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446429215  769 PVENSLEELWSIFHVVFPELLPGRKEFGD-----LR-----REDIAKRV--------KPFVLRR 814
Cdd:cd18003   160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEwfsnpLTamsegSQEENEELvrrlhkvlRPFLLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
613-816 3.73e-44

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: 159.41  E-value: 3.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17997     4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLL-GYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILKDV---AEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGT 768
Cdd:cd17997    83 VLIGDKEERADIIRDVllpGKFDVCITSYEMVIKEKTVLKKfNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGT 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  769 PVENSLEELWSIFHVVFPELLPGRKEF--------GDLRREDIAKRVK----PFVLRRLK 816
Cdd:cd17997   163 PLQNNLHELWALLNFLLPDVFTSSEDFdewfnvnnCDDDNQEVVQRLHkvlrPFLLRRIK 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
614-814 1.29e-41

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: 152.83  E-value: 1.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  614 REYQVYGFEWMKTlayyrFGGILADDMGLGKTLQSIAYI------DSVLPEIREKKLPI----------LVVSPSSLVYN 677
Cdd:cd18008     2 LPYQKQGLAWMLP-----RGGILADEMGLGKTIQALALIlatrpqDPKIPEELEENSSDpkklylskttLIVVPLSLLSQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  678 WLSELKKF--APHIRAVIADGnqAERRKILKDVAEFDVVITSYPLLRRDIRS-----------------YARPFHTLFLD 738
Cdd:cd18008    77 WKDEIEKHtkPGSLKVYVYHG--SKRIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskekeasplHRIRWYRVILD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  739 EAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLP--------GRKEFGDLRREDIAK---RV 807
Cdd:cd18008   155 EAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGdypwfnsdISKPFSKNDRKALERlqaLL 234

                  ....*..
gi 446429215  808 KPFVLRR 814
Cdd:cd18008   235 KPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
615-814 1.85e-40

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: 149.44  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  615 EYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlpILVVSPSSLVYNWLSELKKFAPHIRAVIA 694
Cdd:cd18001     3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS--VLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  695 DG-NQAERRKILKDVA-EFDVVITSYPLLRRDIRSYARPFHTLF------LDEAQAFKNPTTQTARAVKTIQAEYRFGLT 766
Cdd:cd18001    81 HGtSKKERERNLERIQrGGGVLLTTYGMVLSNTEQLSADDHDEFkwdyviLDEGHKIKNSKTKSAKSLREIPAKNRIILT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446429215  767 GTPVENSLEELWSIFHVVFP-ELLPGRKEF-----------------------GDLRREDIAKRVKPFVLRR 814
Cdd:cd18001   161 GTPIQNNLKELWALFDFACNgSLLGTRKTFkmefenpitrgrdkdatqgekalGSEVAENLRQIIKPYFLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
613-816 1.19e-38

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: 144.05  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17996     4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLI-TYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILKDV--AEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKT-IQAEYRFGLTGT 768
Cdd:cd17996    83 VYKGTPDVRKKLQSQIraGKFNVLLTTYEYIIKDKPLLSKiKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGT 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446429215  769 PVENSLEELWSIFHVVFPELLPGRKEF----------------GDLRRED---IAKR----VKPFVLRRLK 816
Cdd:cd17996   163 PLQNNLPELWALLNFLLPKIFKSCKTFeqwfntpfantgeqvkIELNEEEtllIIRRlhkvLRPFLLRRLK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
613-826 2.52e-38

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: 143.65  E-value: 2.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18064    16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLL-GYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILKDV---AEFDVVITSYPLLRRDiRSYARPFH--TLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTG 767
Cdd:cd18064    95 CLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKE-KSVFKKFNwrYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  768 TPVENSLEELWSIFHVVFPELLPGRKEF----------GDLRR-EDIAKRVKPFVLRRLKEDVLKELPDK 826
Cdd:cd18064   174 TPLQNNLHELWALLNFLLPDVFNSAEDFdswfdtnnclGDQKLvERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
613-814 2.71e-38

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: 143.03  E-value: 2.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAyidsVLPEIREKKL---PILVVSPSSLVYNWLSELKKFAPHI 689
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIA----VLAHLAEEHNiwgPFLVIAPASTLHNWQQEISRFVPQF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  690 RAVIADGNQAERrKILKDV----------AEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQ 758
Cdd:cd18002    77 KVLPYWGNPKDR-KVLRKFwdrknlytrdAPFHVVITSYQLVVQDEKYFQRvKWQYMVLDEAQAIKSSSSSRWKTLLSFH 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446429215  759 AEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEFGDLRREDIA--------------KR----VKPFVLRR 814
Cdd:cd18002   156 CRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshaenktglnehqlKRlhmiLKPFMLRR 229
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
613-814 3.68e-37

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: 139.31  E-value: 3.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpEIREKKLPILVVSPSSLVYNWLSELKKFAPhIRAV 692
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLY-QVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKIL--------------KDVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTI 757
Cdd:cd17995    79 VYHGSGESRQIIQqyemyfkdaqgrkkKGVYKFDVLITTYEMVIADAEELRKiPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446429215  758 QAEYRFGLTGTPVENSLEELWSIFHVVFPELLPG----RKEFGDLRRED----IAKRVKPFVLRR 814
Cdd:cd17995   159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSseefLEEFGDLKTAEqvekLQALLKPYMLRR 223
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
613-814 5.49e-37

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: 139.73  E-value: 5.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWM-KTLA----YYRFGGILADDMGLGKTLQSIAYIDSVL-------PEIREkklpILVVSPSSLVYNWLS 680
Cdd:cd18004     1 LRPHQREGVQFLyDCLTgrrgYGGGGAILADEMGLGKTLQAIALVWTLLkqgpygkPTAKK----ALIVCPSSLVGNWKA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  681 ELKKFAPH--IRAVIADGNQAERRKILKDVAE---FDVVITSYPLLRRDIRSYARP--FHTLFLDEAQAFKNPTTQTARA 753
Cdd:cd18004    77 EFDKWLGLrrIKVVTADGNAKDVKASLDFFSSastYPVLIISYETLRRHAEKLSKKisIDLLICDEGHRLKNSESKTTKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  754 VKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF-----------------------GDLRREDIAKRVKPF 810
Cdd:cd18004   157 LNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseedkelGAERSQELSELTSRF 236

                  ....
gi 446429215  811 VLRR 814
Cdd:cd18004   237 ILRR 240
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
613-814 2.02e-36

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: 135.98  E-value: 2.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKlPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFL-AYLKEIGIPG-PHLVVVPSSTLDNWLREFKRWCPSLKVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRK----ILKDVAEFDVVITSYPLL--RRDIRSYAR--PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFG 764
Cdd:cd17998    79 PYYGSQEERKHlrydILKGLEDFDVIVTTYNLAtsNPDDRSFFKrlKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 446429215  765 LTGTPVENSLEELWSIFHVVFPellpgrkefgdlrrediakrvKPFVLRR 814
Cdd:cd17998   159 LTGTPLQNNLLELMSLLNFIMP---------------------KPFILRR 187
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
615-800 1.70e-35

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 133.60  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  615 EYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAVI- 693
Cdd:cd18000     3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFL-AALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  694 ----ADGNQAE-------RRKILKDVA-EFDVVITSYPLLR---RDIRSYArpFHTLFLDEAQAFKNPTTQTARAVKTIQ 758
Cdd:cd18000    82 hssgSGTGSEEklgsierKSQLIRKVVgDGGILITTYEGFRkhkDLLLNHN--WQYVILDEGHKIRNPDAEITLACKQLR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446429215  759 AEYRFGLTGTPVENSLEELWSIFHVVFPELLpgrkefgdLRR 800
Cdd:cd18000   160 TPHRLILSGTPIQNNLKELWSLFDFVFPPYL--------LRR 193
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
613-816 5.03e-34

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: 130.91  E-value: 5.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALL-GYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILKDV---AEFDVVITSYPLLRRDiRSYARPFH--TLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTG 767
Cdd:cd18065    95 CLIGDKDARAAFIRDVmmpGEWDVCVTSYEMVIKE-KSVFKKFNwrYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  768 TPVENSLEELWSIFHVVFPELLPGRKEF----------GDLRR-EDIAKRVKPFVLRRLK 816
Cdd:cd18065   174 TPLQNNLHELWALLNFLLPDVFNSADDFdswfdtknclGDQKLvERLHAVLKPFLLRRIK 233
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
613-814 7.84e-33

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 126.78  E-value: 7.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLL-WYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAER---RKILKDVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGT 768
Cdd:cd18006    80 TYMGDKEKRldlQQDIKSTNRFHVLLTTYEICLKDASFLKSfPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446429215  769 PVENSLEELWSIFHVVFPELLPGR------KEFGDLRRE-----DIAKRVKPFVLRR 814
Cdd:cd18006   160 PIQNSLQELYALLSFIEPNVFPKDklddfiKAYSETDDEsetveELHLLLQPFLLRR 216
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
613-814 8.77e-33

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: 126.70  E-value: 8.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFL-SYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAER------------RKILKdvaeFDVVITSYPLLRRDiRSYARPFHTLFL--DEAQAFKNPTTQTARAVKTIQ 758
Cdd:cd17993    81 VYLGDIKSRdtireyefyfsqTKKLK----FNVLLTTYEIILKD-KAFLGSIKWQYLavDEAHRLKNDESLLYEALKEFK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  759 AEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEFGDLRRE-------DIAKRVKPFVLRR 814
Cdd:cd17993   156 TNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEeqekgiaDLHKELEPFILRR 218
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
633-781 3.52e-30

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: 119.88  E-value: 3.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  633 GGILADDMGLGKTLQSIAYIDSVlpeirekklPILVVSPSSLVYNWLselKKFAPHIRAVIAD---GNQAERRKILKDVA 709
Cdd:cd18071    50 GGILADDMGLGKTLTTISLILAN---------FTLIVCPLSVLSNWE---TQFEEHVKPGQLKvytYHGGERNRDPKLLS 117
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446429215  710 EFDVVITSYPLLRRDIRSYA-RPFHTL-----FLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIF 781
Cdd:cd18071   118 KYDIVLTTYNTLASDFGAKGdSPLHTInwlrvVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL 195
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
613-814 1.22e-29

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: 117.84  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFApHIRAV 692
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF--LMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILK--------------DVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTI 757
Cdd:cd18058    78 VYHGSQISRQMIQQyemyyrdeqgnplsGIFKFQVVITTFEMILADCPELKKiNWSCVIIDEAHRLKNRNCKLLEGLKLM 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446429215  758 QAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGR----KEFGDLRREDIAKR----VKPFVLRR 814
Cdd:cd18058   158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSEttflEEFGDLKTEEQVKKlqsiLKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
613-814 6.02e-29

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


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 116.26  E-value: 6.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFL-SYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILK--------DVAEFDVVITSYPLLRRDiRSYARPFHTLFL--DEAQAFKNPTTQTARAVKTIQAEYR 762
Cdd:cd18054   100 VYIGDLMSRNTIREyewihsqtKRLKFNALITTYEILLKD-KTVLGSINWAFLgvDEAHRLKNDDSLLYKTLIDFKSNHR 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446429215  763 FGLTGTPVENSLEELWSIFHVVFPELLPGRKEFGDLR---RED----IAKRVKPFVLRR 814
Cdd:cd18054   179 LLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHgkgRENgyqsLHKVLEPFLLRR 237
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
613-814 1.05e-28

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: 115.13  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYidsvLPEIREKKL--PILVVSPSSLVYNWLSELKKFApHIR 690
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITF----LYEIYLKGIhgPFLVIAPLSTIPNWEREFRTWT-ELN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  691 AVIADGNQAERR--------------KILKDVAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVK 755
Cdd:cd18059    76 VVVYHGSQASRRtiqlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNiPWRCVVIDEAHRLKNRNCKLLEGLK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446429215  756 TIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGR----KEFGDLRREDIAKR----VKPFVLRR 814
Cdd:cd18059   156 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSEttfmQEFGDLKTEEQVQKlqaiLKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
613-814 2.75e-28

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: 114.00  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPE-IREkklPILVVSPSSLVYNWLSELKKFApHIRA 691
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVgIHG---PFLVIAPLSTITNWEREFNTWT-EMNT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  692 VIADGNQAERRKI------LKD--------VAEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKT 756
Cdd:cd18060    77 IVYHGSLASRQMIqqyemyCKDsrgrlipgAYKFDALITTFEMILSDCPELREiEWRCVIIDEAHRLKNRNCKLLDSLKH 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446429215  757 IQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGR----KEFGDLRREDIAKR----VKPFVLRR 814
Cdd:cd18060   157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSEseflKDFGDLKTEEQVQKlqaiLKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
609-816 5.20e-28

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: 113.99  E-value: 5.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  609 LRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPH 688
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALI-TYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  689 IRAVIADGNQAERRKILKDV--AEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKT-IQAEYRFG 764
Cdd:cd18062    99 VVKVSYKGSPAARRAFVPQLrsGKFNVLLTTYEYIIKDKQILAKiRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLL 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  765 LTGTPVENSLEELWSIFHVVFPELLPGRKEFG--------------DLRRED-------IAKRVKPFVLRRLK 816
Cdd:cd18062   179 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekvDLNEEEtiliirrLHKVLRPFLLRRLK 251
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
896-1008 8.90e-28

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: 108.45  E-value: 8.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   896 AKFEQLLDILEEcrSTGKRILIFSQFTKMLSIigREL-NRQAIPYFYLDGNTPSQERVELCNRFNEGEGDlFLISLKAGG 974
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA--ELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKID-VLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 446429215   975 TGLNLTGADTVILYDLWWNPAVEQQAADRAYRMG 1008
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
609-816 2.46e-27

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: 112.08  E-value: 2.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  609 LRAVMREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIdSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPH 688
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALI-TYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  689 IRAVIADGNQAERRKILKDV--AEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKT-IQAEYRFG 764
Cdd:cd18063    99 VVKISYKGTPAMRRSLVPQLrsGKFNVLLTTYEYIIKDKHILAKiRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  765 LTGTPVENSLEELWSIFHVVFPELLPGRKEFG--------------DLRRED-------IAKRVKPFVLRRLK 816
Cdd:cd18063   179 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgervDLNEEEtiliirrLHKVLRPFLLRRLK 251
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
613-781 2.41e-26

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: 109.36  E-value: 2.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLayyrfGGILADDMGLGKTLQSIAYI-----------DSVLPEIREKKLPI-------------LV 668
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldAADDDSDEMVCCPDclvaetpvsskatLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  669 VSPSSLVYNWLSELKKFAP-HIRAVIADG---NQAERRKILKDVAEFDVVITSYPLLRRDIrSYARPFHT---------- 734
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPsSLKVLTYQGvkkDGALASPAPEILAEYDIVVTTYDVLRTEL-HYAEANRSnrrrrrqkry 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446429215  735 ------LF--------LDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIF 781
Cdd:cd18070   155 eappspLVlvewwrvcLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLL 215
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
613-814 6.64e-26

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: 107.01  E-value: 6.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFApHIRAV 692
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEIL--LTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERR--------------KILKDVAEFDVVITSYPLLRRDIRSY-ARPFHTLFLDEAQAFKNPTTQTARAVKTI 757
Cdd:cd18061    78 VYHGSLISRQmiqqyemyfrdsqgRIIRGAYRFQAIITTFEMILGGCPELnAIDWRCVIIDEAHRLKNKNCKLLEGLKLM 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446429215  758 QAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGR----KEFGDLRREDIAKR----VKPFVLRR 814
Cdd:cd18061   158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEstfmQEFGDLKTEEQVQKlqaiLKPMMLRR 222
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
633-814 1.75e-25

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: 106.41  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  633 GGILADDMGLGKTLQSIAYI---------------------DSVLPEIREKKLPILVVSPSSLVYNWLSELKKFAPH--I 689
Cdd:cd18072    22 GGILADDMGLGKTLTMIALIlaqkntqnrkeeekekaltewESKKDSTLVPSAGTLVVCPASLVHQWKNEVESRVASnkL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  690 RAVIADGNQaeRRKILKDVAEFDVVITSYPLLRRDIRSYAR--PFHTLF--------LDEAQAFKNPTTQTARAVKTIQA 759
Cdd:cd18072   102 RVCLYHGPN--RERIGEVLRDYDIVITTYSLVAKEIPTYKEesRSSPLFriawariiLDEAHNIKNPKVQASIAVCKLRA 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  760 EYRFGLTGTPVENSLEELWSIFHVV----FPELLPGRKEFgDLRREDIAKR----VKPFVLRR 814
Cdd:cd18072   180 HARWALTGTPIQNNLLDMYSLLKFLrcspFDDLKVWKKQV-DNKSRKGGERlnilTKSLLLRR 241
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
613-814 1.59e-24

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: 103.59  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEiREKKLPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHE-HQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAERRKILK--------DVAEFDVVITSYPLLRRDiRSYARPFHTLFL--DEAQAFKNPTTQTARAVKTIQAEYR 762
Cdd:cd18053   100 VYLGDINSRNMIRThewmhpqtKRLKFNILLTTYEILLKD-KSFLGGLNWAFIgvDEAHRLKNDDSLLYKTLIDFKSNHR 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446429215  763 FGLTGTPVENSLEELWSIFHVVFPELLPGRKEFG-------DLRREDIAKRVKPFVLRR 814
Cdd:cd18053   179 LLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEeehgkgrEYGYASLHKELEPFLLRR 237
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
631-814 1.65e-24

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: 103.39  E-value: 1.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  631 RFGGILADDMGLGKTLQSIAYIDSVLPEIREKKLPI----LVVSPSSLVYNWLSELKKF--APHIRAVIADGNQAERRKI 704
Cdd:cd18066    24 RFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVikraLIVTPGSLVKNWKKEFQKWlgSERIKVFTVDQDHKVEEFI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  705 LKDVaeFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIFHV 783
Cdd:cd18066   104 ASPL--YSVLIISYEMLLRSLDQISKlNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446429215  784 VFPELL-----------------------PGRKEFGDLRREDIAKRVKPFVLRR 814
Cdd:cd18066   182 VNPGILgslstyrkvyeepivrsreptatPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
616-810 5.81e-24

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: 101.13  E-value: 5.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  616 YQVYGFEWMktlayYRFGG--ILADDMGLGKTLQSIAyIDSVLPEirekKLPILVVSPSSLVYNWLSELKKFAPHIR--- 690
Cdd:cd18010     4 FQREGVCFA-----LRRGGrvLIADEMGLGKTVQAIA-IAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPSLPpdd 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  691 -AVIADGNQAERRKilkdvaEFDVVITSYPLLRR-DIRSYARPFHTLFLDEAQAFKNPTTQTARAVKTI--QAEYRFGLT 766
Cdd:cd18010    74 iQVIVKSKDGLRDG------DAKVVIVSYDLLRRlEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLS 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446429215  767 GTPVENSLEELWSIFHVVFPELLPGRKEFGdlRREDIAKRVKPF 810
Cdd:cd18010   148 GTPALSRPIELFTQLDALDPKLFGRFHDFG--RRYCAAKQGGFG 189
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
633-795 2.07e-23

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: 100.24  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  633 GGILADDMGLGKTLQSIAYIDSVLPEIREKKLPI---LVVSPSSLVYNWLSELKKF-APHIRAVIADGNQAERrKILKDV 708
Cdd:cd18067    26 GCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaIVVSPSSLVKNWANELGKWlGGRLQPLAIDGGSKKE-IDRKLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  709 AEFD---------VVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELW 778
Cdd:cd18067   105 QWASqqgrrvstpVLIISYETFRLHVEVLQKgEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYF 184
                         170
                  ....*....|....*..
gi 446429215  779 SIFHVVFPELLPGRKEF 795
Cdd:cd18067   185 SLVNFVNPGILGTAAEF 201
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
613-795 2.39e-23

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: 100.06  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWM-KTLAYYR------FGGILADDMGLGKTLQSIAYIDSVLPEIREKKLPiLVVSPSSLVYNWLSELKKF 685
Cdd:cd18007     1 LKPHQVEGVRFLwSNLVGTDvgsdegGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  686 AP--HIRAVIADGNQAERR--KILKDVAEF----DVVITSYPLLRRDIR---SYARPFHT------------LFLDEAQA 742
Cdd:cd18007    80 LPpdLRPLLVLVSLSASKRadARLRKINKWhkegGVLLIGYELFRNLASnatTDPRLKQEfiaalldpgpdlLVLDEGHR 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446429215  743 FKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF 795
Cdd:cd18007   160 LKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
613-814 4.92e-23

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: 97.90  E-value: 4.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKG-PFLVSAPLSTIINWEREFEMWAPDFYVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQaerrkilkdvaefdVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVE 771
Cdd:cd17994    80 TYVGDH--------------VLLTSYELISIDQAILGSiDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQ 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446429215  772 NSLEELWSIFHVVFPE----LLPGRKEFGDLRREDIAKRVK----PFVLRR 814
Cdd:cd17994   146 NNLEELFHLLNFLTPErfnnLQGFLEEFADISKEDQIKKLHdllgPHMLRR 196
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
613-814 1.72e-22

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


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 97.44  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlPILVVSPSSLVYNWLSELKKFAPHIRAV 692
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKG-PYLVSAPLSTIINWEREFEMWAPDFYVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  693 IADGNQAER------------------RKILKDVAE----FDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQ 749
Cdd:cd18057    80 TYTGDKESRsvirenefsfednairsgKKVFRMKKEaqikFHVLLTSYELITIDQAILGSiEWACLVVDEAHRLKNNQSK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446429215  750 TARAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPG----RKEFGDLRREDIAKRVK----PFVLRR 814
Cdd:cd18057   160 FFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNlegfLEEFADISKEDQIKKLHdllgPHMLRR 232
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
635-814 3.04e-22

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: 95.82  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  635 ILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSPSSLVYNWLSELKKFApHIRAVIADGN--QAERRKILKDVAEFD 712
Cdd:cd18011    21 LLADEVGLGKTIEAGLIIKELL--LRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLILDREtaAQLRRLIGNPFEEFP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  713 VVITSYPLLRRDIRS----YARPFHTLFLDEAQAFKN----PTTQTARAVKTI--QAEYRFGLTGTPVENSLEELWSIFH 782
Cdd:cd18011    98 IVIVSLDLLKRSEERrgllLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRARHVLLLTATPHNGKEEDFRALLS 177
                         170       180       190
                  ....*....|....*....|....*....|..
gi 446429215  783 VVFPELLPGRKEFGDLRREDIakRVKPFVLRR 814
Cdd:cd18011   178 LLDPGRFAVLGRFLRLDGLRE--VLAKVLLRR 207
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
616-814 6.65e-22

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: 95.85  E-value: 6.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  616 YQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlPILVVSPSSLVYNWLSELKKFAPHIRAVIAD 695
Cdd:cd18055     4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKG-PFLVSAPLSTIINWEREFQMWAPDFYVVTYT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  696 GNQAER------------------RKILKDVAE----FDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTTQTAR 752
Cdd:cd18055    83 GDKDSRaiirenefsfddnavkggKKAFKMKREaqvkFHVLLTSYELVTIDQAALGSiRWACLVVDEAHRLKNNQSKFFR 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  753 AVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPG----RKEFGDLRREDIAKRVK----PFVLRR 814
Cdd:cd18055   163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNlegfLEEFADISKEDQIKKLHdllgPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
927-1008 8.44e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.35  E-value: 8.44e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    927 IIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEGDlFLISLKAGGTGLNLTGADTVILYDLWWNPAVEQQAADRAYR 1006
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK-VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 446429215   1007 MG 1008
Cdd:smart00490   81 AG 82
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
613-814 3.47e-21

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: 93.59  E-value: 3.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlPILVVSPSSLVYNWLSELKKFAPHI--- 689
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKG-PFLVSAPLSTIINWEREFEMWAPDMyvv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  690 --------RAVIAD------------GNQAERRKILKDVaEFDVVITSYPLLRRDIRSYAR-PFHTLFLDEAQAFKNPTT 748
Cdd:cd18056    80 tyvgdkdsRAIIREnefsfednairgGKKASRMKKEASV-KFHVLLTSYELITIDMAILGSiDWACLIVDEAHRLKNNQS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446429215  749 QTARAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPE----LLPGRKEFGDLRREDIAKRVK----PFVLRR 814
Cdd:cd18056   159 KFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPErfhnLEGFLEEFADIAKEDQIKKLHdmlgPHMLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
632-798 5.99e-21

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: 92.96  E-value: 5.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  632 FGGILADDMGLGKTLQSIAYIDSVLPEIREKKlpILVVSPSSLVYNWLSELKKFAP--------HIRA----VIADGNQ- 698
Cdd:cd18069    29 FGCILAHSMGLGKTLQVISFLDVLLRHTGAKT--VLAIVPVNTLQNWLSEFNKWLPppealpnvRPRPfkvfILNDEHKt 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  699 -AERRKILKD-VAEFDVVITSYPLLRrdirsyARPFHTLFL-DEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLE 775
Cdd:cd18069   107 tAARAKVIEDwVKDGGVLLMGYEMFR------LRPGPDVVIcDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                         170       180
                  ....*....|....*....|...
gi 446429215  776 ELWSIFHVVFPELLPGRKEFGDL 798
Cdd:cd18069   181 EYWCMVDFVRPDFLGTRQEFSNM 203
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
613-784 1.90e-18

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: 85.09  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWMKTlayYRFGGILADdMGLGKTLQSIAYIDSVLPEirEKKLPILVVSPSSLVYN-WLSELKKFA--PHI 689
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLD--DFTRRVLVIAPLRVARStWPDEVEKWNhlRNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  690 RAVIADGNQAERRKILKdvAEFDVVITSYPLLRRDIRSYAR--PFHTLFLDEAQAFKNPTTQTARAVKTI--QAEYRFGL 765
Cdd:cd18013    75 TVSVAVGTERQRSKAAN--TPADLYVINRENLKWLVNKSGDpwPFDMVVIDELSSFKSPRSKRFKALRKVrpVIKRLIGL 152
                         170
                  ....*....|....*....
gi 446429215  766 TGTPVENSLEELWSIFHVV 784
Cdd:cd18013   153 TGTPSPNGLMDLWAQIALL 171
DEXDc smart00487
DEAD-like helicases superfamily;
613-795 1.95e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.85  E-value: 1.95e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    613 MREYQVYGFEWMKTLayyRFGGILADDMGLGKTLQSIAYIDSVLpeIREKKLPILVVSP-SSLVYNWLSELKKFAPH--- 688
Cdd:smart00487    9 LRPYQKEAIEALLSG---LRDVILAAPTGSGKTLAALLPALEAL--KRGKGGRVLVLVPtRELAEQWAEELKKLGPSlgl 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    689 IRAVIADGN--QAERRKILKDVaeFDVVITSYPLLRRDIRSYA---RPFHTLFLDEAQAFKNP--TTQTARAVK-TIQAE 760
Cdd:smart00487   84 KVVGLYGGDskREQLRKLESGK--TDILVTTPGRLLDLLENDKlslSNVDLVILDEAHRLLDGgfGDQLEKLLKlLPKNV 161
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 446429215    761 YRFGLTGTP---VENSLEELWS--IFHVVFPELLPGRKEF 795
Cdd:smart00487  162 QLLLLSATPpeeIENLLELFLNdpVFIDVGFTPLEPIEQF 201
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
3-108 5.15e-18

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 88.73  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215    3 FTLNKSIIKEVCGETSYKRGEAYYKSNKVIvnHYDETKEICEATVKGNEDFHVTVEKAKKGDVVARCSCPslASFQTYCQ 82
Cdd:COG4715     4 LELTEDDIRRLAGPRIFERGREYAREGRVL--DLDVEDGRLEATVQGSEDYRVRVDLDDGGDLDSSCTCP--YGGGGFCK 79
                          90       100
                  ....*....|....*....|....*.
gi 446429215   83 HVAAVLIQInYNQQTGGMGSVSSRND 108
Cdd:COG4715    80 HVVAVLLAL-LDQPEEGAPRQSEREA 104
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
613-795 1.01e-15

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: 78.01  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYGFEWM---------KTLAYYRFGGILADDMGLGKTLQSIAYIDSVL-PEIREKKLPILVVSPSSLVYNWLSEL 682
Cdd:cd18068     1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLlCEKLENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  683 KKFAPHI-RAVIADGNQAERRKILKDVA--------EFDVVITSYPLLR-----RDIRSYARPFHTL------------F 736
Cdd:cd18068    81 EKWQEGLkDEEKIEVNELATYKRPQERSyklqrwqeEGGVMIIGYDMYRilaqeRNVKSREKLKEIFnkalvdpgpdfvV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446429215  737 LDEAQAFKNPTTQTARAVKTIQAEYRFGLTGTPVENSLEELWSIFHVVFPELLPGRKEF 795
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEF 219
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
613-1059 1.43e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 81.22  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVygfEWMKTLAYYRFG----GILADDMGLGKTLQSIAYIDSVLpeireKKLPILVVSPS-SLVYNWLSELKKFAP 687
Cdd:COG1061    81 LRPYQQ---EALEALLAALERgggrGLVVAPTGTGKTVLALALAAELL-----RGKRVLVLVPRrELLEQWAEELRRFLG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  688 HIRAViadGNQAERrkilkdvaEFDVVITSYPLLRRD--IRSYARPFHTLFLDEA-QAfknPTTQTARAVKTIQAEYRFG 764
Cdd:COG1061   153 DPLAG---GGKKDS--------DAPITVATYQSLARRahLDELGDRFGLVIIDEAhHA---GAPSYRRILEAFPAAYRLG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  765 LTGTPV-ENSLEELWSIF-HVVFpellpgRKEFGDLRREDIakrVKPFVLRRLKEDvlkelpdkiehlqsselLPDQKRL 842
Cdd:COG1061   219 LTATPFrSDGREILLFLFdGIVY------EYSLKEAIEDGY---LAPPEYYGIRVD-----------------LTDERAE 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  843 YAAYLAKLREEtlkhLDKDTLRKNKIrilagltrlrqicchpalfvddykgssakfeqLLDILEECRStGKRILIFSQFT 922
Cdd:COG1061   273 YDALSERLREA----LAADAERKDKI--------------------------------LRELLREHPD-DRKTLVFCSSV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  923 KMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEGDlFLISLKAGGTGLNLTGADTVILYDLWWNPAVEQQAAD 1002
Cdd:COG1061   316 DHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR-ILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLG 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446429215 1003 RAYRMGQ-KNTVQVIKLVAHGTieEKMHELQESKKNLIAEVIEPGEEKLSSITEEEIR 1059
Cdd:COG1061   395 RGLRPAPgKEDALVYDFVGNDV--PVLEELAKDLRDLAGYRVEFLDEEESEELALLIA 450
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
845-1061 2.55e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 64.75  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  845 AYLAKLREETlkhldkDTLRKNK-IRILAGLTRLRQicchpAL-FVDDYKGSSAKFEQLLDILEECRST--GKRILIFSQ 920
Cdd:COG1111   293 RYLERLEEEA------RSSGGSKaSKRLVSDPRFRK-----AMrLAEEADIEHPKLSKLREILKEQLGTnpDSRIIVFTQ 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  921 FTKMLSIIGRELNRQAIP--YFYLDGNTP-----SQ-ERVELCNRFNEGEGDLfLISLKAGGTGLNLTGADTVILYDLWW 992
Cdd:COG1111   362 YRDTAEMIVEFLSEPGIKagRFVGQASKEgdkglTQkEQIEILERFRAGEFNV-LVATSVAEEGLDIPEVDLVIFYEPVP 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  993 NPAVEQQaadRAYRMGQKNTVQVIKLVAHGTIEE-----------KMHELQESKKNLIAEVIEPGEEKLSSITEEEIRDI 1061
Cdd:COG1111   441 SEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEayywssrrkekKMKSILKKLKKLLDKQEKEKLKESAQATLDEFESI 517
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
613-769 8.26e-10

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 58.09  E-value: 8.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  613 MREYQVYG-FEWMKTLAYYRfgGILADDMGLGKTLQSIAyidsvLPEIReKKLPILVVSPS-SLVYNWLSELKKFAPHIR 690
Cdd:cd17926     1 LRPYQEEAlEAWLAHKNNRR--GILVLPTGSGKTLTALA-----LIAYL-KELRTLIVVPTdALLDQWKERFEDFLGDSS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  691 aviadgNQAERRKILKDVAEFDVVITSYPLLRRDIRSYARPFHT---LFLDEAQAFknPTTQTARAVKTIQAEYRFGLTG 767
Cdd:cd17926    73 ------IGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQfglLIVDEAHHL--PAKTFSEILKELNAKYRLGLTA 144

                  ..
gi 446429215  768 TP 769
Cdd:cd17926   145 TP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
632-743 3.73e-08

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: 53.56  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  632 FGGILADDMGLGKTLqsIAYIdSVLPEIREKKLPILVVSP-SSLVYNWLSELKK-FAPHIRAVIADG--NQAERRKILKD 707
Cdd:cd00046     2 ENVLITAPTGSGKTL--AALL-AALLLLLKKGKKVLVLVPtKALALQTAERLRElFGPGIRVAVLVGgsSAEEREKNKLG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446429215  708 VAefDVVITS----YPLLRRDIRSYARPFHTLFLDEAQAF 743
Cdd:cd00046    79 DA--DIIIATpdmlLNLLLREDRLFLKDLKLIIVDEAHAL 116
ResIII pfam04851
Type III restriction enzyme, res subunit;
612-769 7.42e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 47.28  E-value: 7.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   612 VMREYQVYGFE-WMKTLAYYRFGGILADDMGLGKTLQSIAYIDSVLPEIREKKlpILVVSPS-SLVYNWLSELKKFAPHI 689
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKK--VLFLVPRkDLLEQALEEFKKFLPNY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215   690 RAVIADGNQaerRKILKDVAEFDVVITSYPLLRRDIRSYARPF----HTLFL-DEAQAFknpTTQTARAVKT-IQAEYRF 763
Cdd:pfam04851   81 VEIGEIISG---DKKDESVDDNKIVVTTIQSLYKALELASLELlpdfFDVIIiDEAHRS---GASSYRNILEyFKPAFLL 154

                   ....*.
gi 446429215   764 GLTGTP 769
Cdd:pfam04851  155 GLTATP 160
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
891-986 1.61e-05

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) 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 DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 46.09  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  891 YKGSSAKFEQLLDILEECRSTGKrILIFSQFTKMLSIIGRELNRQAIpyfylDGNTPSQERVELCNRFNEGEGDLFLISl 970
Cdd:cd18789    29 AAMNPNKLRALEELLKRHEQGDK-IIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVS- 101
                          90
                  ....*....|....*.
gi 446429215  971 KAGGTGLNLTGADTVI 986
Cdd:cd18789   102 KVGDEGIDLPEANVAI 117
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
914-1019 2.06e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 43.46  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  914 RILIFSQFTKMLSIIGRELNrqaipyfyldgntpsqervelcnrfnegegdlFLISLKAGGTGLNLTGADTVILYDLWWN 993
Cdd:cd18785     5 KIIVFTNSIEHAEEIASSLE--------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSS 52
                          90       100
                  ....*....|....*....|....*.
gi 446429215  994 PAVEQQAADRAYRMGQKNtVQVIKLV 1019
Cdd:cd18785    53 AASYIQRVGRAGRGGKDE-GEVILFV 77
SWIM pfam04434
SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is ...
53-92 2.47e-05

SWIM zinc finger; This domain is found in bacterial, archaeal and eukaryotic proteins. It is predicted to be organized into two N-terminal beta-strands and a C-terminal alpha helix, thus possibly adopting a fold similar to that of the C2H2 zinc finger (pfam00096). SWIM is thought to be a versatile domain that can interact with DNA or proteins in different contexts.


Pssm-ID: 309540  Cd Length: 38  Bit Score: 42.41  E-value: 2.47e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 446429215    53 FHVTVEKAKKGDvvARCSCPSLASFQTYCQHVAAVLIQIN 92
Cdd:pfam04434    1 YRVQLDLDGLEK--ASCSCPDFQLNGIPCKHALAVLLALG 38
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
894-990 3.70e-03

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 38.64  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446429215  894 SSAKFEQLLDILEEcRSTGKRILIFSQFTKMLSIIGRELNRQAIPYFYLDGNTPSQERVELCNRFNEGEGDLfLISlkag 973
Cdd:cd18787    10 EEEKKLLLLLLLLE-KLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV-LVA---- 83
                          90       100
                  ....*....|....*....|..
gi 446429215  974 gT-----GLNLTGADTVILYDL 990
Cdd:cd18787    84 -TdvaarGLDIPGVDHVINYDL 104
 
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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