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Conserved domains on  [gi|1835284405|gb|KAF4330442|]
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DNA repair and recombination protein RAD54 [Plasmodium falciparum NF54]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13029066)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
133-371 2.50e-98

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: 313.07  E-value: 2.50e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQGFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18004      1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRC-NVTCVNDNAKEKIVSKLEgFKYDIQSTVLICSYECFRIN-NEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd18004     81 WLGLRRiKVVTADGNAKDVKASLDF-FSSASTYPVLIISYETLRRHaEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFILR 370
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239

                   .
gi 1835284405  371 R 371
Cdd:cd18004    240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
133-759 6.72e-94

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 316.78  E-value: 6.72e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFV-FECLMNIkddkisGCILADDMGLGKTLQSITVLYTLLKQGfhkkcAVRRCLILCPASLINNWNDEIS 211
Cdd:COG0553    242 LRPYQLEGAAWLlFLRRLGL------GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELA 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWIPNRcNVTCVNDNAKEKivSKLEGFKydiQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNL 291
Cdd:COG0553    311 KFAPGL-RVLVLDGTRERA--KGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  292 TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPIligrdkdatEKEQEIASERLTELsniTNKFILRR 371
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRL---LRPFLLRR 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  372 TNNLLSKVLPVKYLINIFIKLNPIQEALY--VLFLKDKKILKNDNTNNKVNVLINIKKLEKICNHPLLLnvndIKEIGQV 449
Cdd:COG0553    453 TKEDVLKDLPEKTEETLYVELTPEQRALYeaVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAEL 528
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  450 TLWkliedvifemqtnmkicnrgnkrdnkndskSGcvlKVDKsmssisnnnmkngndmnntnnntnnntnnntnnntnnn 529
Cdd:COG0553    529 SGR------------------------------SA---KLEA-------------------------------------- 537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  530 insninnninnninsninnninsnmnnntnlrcgsrgnqndasgyvgnkrkpieldynkpVKRIIEECKRDiyrsyynfs 609
Cdd:COG0553    538 ------------------------------------------------------------LLELLEELLAE--------- 548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  610 ckflllhfllknikqntNDKVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSADIFIFLLSSKSG 689
Cdd:COG0553    549 -----------------GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAG 611
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  690 GCGINLISSNRLILLDPDWNPANDKQALARVWREGQKKICYIYRLFCTGTIDEKVYQRQISKDGLSNMIV 759
Cdd:COG0553    612 GEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
 
Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
133-371 2.50e-98

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: 313.07  E-value: 2.50e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQGFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18004      1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRC-NVTCVNDNAKEKIVSKLEgFKYDIQSTVLICSYECFRIN-NEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd18004     81 WLGLRRiKVVTADGNAKDVKASLDF-FSSASTYPVLIISYETLRRHaEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFILR 370
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239

                   .
gi 1835284405  371 R 371
Cdd:cd18004    240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
133-759 6.72e-94

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 316.78  E-value: 6.72e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFV-FECLMNIkddkisGCILADDMGLGKTLQSITVLYTLLKQGfhkkcAVRRCLILCPASLINNWNDEIS 211
Cdd:COG0553    242 LRPYQLEGAAWLlFLRRLGL------GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELA 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWIPNRcNVTCVNDNAKEKivSKLEGFKydiQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNL 291
Cdd:COG0553    311 KFAPGL-RVLVLDGTRERA--KGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  292 TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPIligrdkdatEKEQEIASERLTELsniTNKFILRR 371
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRL---LRPFLLRR 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  372 TNNLLSKVLPVKYLINIFIKLNPIQEALY--VLFLKDKKILKNDNTNNKVNVLINIKKLEKICNHPLLLnvndIKEIGQV 449
Cdd:COG0553    453 TKEDVLKDLPEKTEETLYVELTPEQRALYeaVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAEL 528
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  450 TLWkliedvifemqtnmkicnrgnkrdnkndskSGcvlKVDKsmssisnnnmkngndmnntnnntnnntnnntnnntnnn 529
Cdd:COG0553    529 SGR------------------------------SA---KLEA-------------------------------------- 537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  530 insninnninnninsninnninsnmnnntnlrcgsrgnqndasgyvgnkrkpieldynkpVKRIIEECKRDiyrsyynfs 609
Cdd:COG0553    538 ------------------------------------------------------------LLELLEELLAE--------- 548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  610 ckflllhfllknikqntNDKVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSADIFIFLLSSKSG 689
Cdd:COG0553    549 -----------------GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAG 611
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  690 GCGINLISSNRLILLDPDWNPANDKQALARVWREGQKKICYIYRLFCTGTIDEKVYQRQISKDGLSNMIV 759
Cdd:COG0553    612 GEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
136-438 3.82e-65

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: 222.56  E-value: 3.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  136 HQREGVQFVFECLMNIKddkiSGCILADDMGLGKTLQSITVLYTLLKQgfhKKCAVRRCLILCPASLINNWNDEISKWI- 214
Cdd:pfam00176    1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHV---DKNWGGPTLIVVPLSLLHNWMNEFERWVs 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  215 PNRCNVTCVNDNAKEKIVSKLEG---FKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNL 291
Cdd:pfam00176   74 PPALRVVVLHGNKRPQERWKNDPnflADFD----VVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  292 TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDatekeqeiaseRLTELSNITNKFILRR 371
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKK-----------GVSRLHKLLKPFLLRR 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835284405  372 TNNLLSKVLPVKYLINIFIKLNPIQEALYVLFLKDKKILKNDNTN----NKVNVLINIKKLEKICNHPLLL 438
Cdd:pfam00176  219 TKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
627-735 2.55e-45

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: 159.56  E-value: 2.55e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  627 NDKVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSADIFIFLLSSKSGGCGINLISSNRLILLDP 706
Cdd:cd18793     27 GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDP 106
                           90       100
                   ....*....|....*....|....*....
gi 1835284405  707 DWNPANDKQALARVWREGQKKICYIYRLF 735
Cdd:cd18793    107 WWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
133-787 1.04e-33

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 141.09  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLK----QGFHkkcavrrcLILCPASLINNWND 208
Cdd:PLN03142   170 MRDYQLAGLNW----LIRLYENGING-ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVVAPKSTLGNWMN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPnRCNVTCVNDNAKEKIVSK---LEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTY 285
Cdd:PLN03142   237 EIRRFCP-VLRAVKFHGNPEERAHQReelLVAGKFD----VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  286 TSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANpiligrdkDATEKEQEIASerltELSNITN 365
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI--------SGENDQQEVVQ----QLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  366 KFILRRTNNLLSKVLPVKYLINIFIKLNPIQEALYvlflkdKKILKND----NTNNKVNVLINIK-KLEKICNHPLLLNV 440
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY------KALLQKDldvvNAGGERKRLLNIAmQLRKCCNHPYLFQG 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  441 ndiKEIGQ--VTLWKLIEdvifemqtnmkicnrgnkrdnkndsksgcvlkvdksmssisnnnmkngndmnntnnntnnnt 518
Cdd:PLN03142   454 ---AEPGPpyTTGEHLVE-------------------------------------------------------------- 468
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  519 nnntnnntnnninsninnninnninsninnninsnmnnntnlrcgsrgnqndasgyvgNKRKPIELDynKPVKRIIEECK 598
Cdd:PLN03142   469 ----------------------------------------------------------NSGKMVLLD--KLLPKLKERDS 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  599 RdiyrsyynfsckflllhfllknikqntndkVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTH-SA 677
Cdd:PLN03142   489 R------------------------------VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpGS 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  678 DIFIFLLSSKSGGCGINLISSNRLILLDPDWNPANDKQALARVWREGQKKICYIYRlFCT-GTIDEKVYQRQISKDGLSN 756
Cdd:PLN03142   539 EKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFR-FCTeYTIEEKVIERAYKKLALDA 617
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1835284405  757 MIVT------TTNLSKD---QMSDENVKKLFNYKMNTVSE 787
Cdd:PLN03142   618 LVIQqgrlaeQKTVNKDellQMVRYGAEMVFSSKDSTITD 657
DEXDc smart00487
DEAD-like helicases superfamily;
133-321 1.45e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 108.35  E-value: 1.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   133 LREHQREGVQFVFECLMNikddkisgCILADDMGLGKTLQSITVLYTLLKQGFHKkcavrRCLILCP-ASLINNWNDEIS 211
Cdd:smart00487    9 LRPYQKEAIEALLSGLRD--------VILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELK 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   212 KWIPNRC--NVTCVNDNAKEKIVSKLEGFKYDIqstvLICSYECFR--INNEFLDKSSIDMIICDEAHRLKNDK-TKTYT 286
Cdd:smart00487   76 KLGPSLGlkVVGLYGGDSKREQLRKLESGKTDI----LVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGfGDQLE 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1835284405   287 SIYNLTAK--KRLLLSGTP---IQNDLGEFYALISLCNPD 321
Cdd:smart00487  152 KLLKLLPKnvQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
622-724 1.01e-19

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: 85.73  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  622 IKQNTNDKVVIVSNYTQTLDyMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSAdiFIFLLSSKSGGCGINLISSNRL 701
Cdd:pfam00271   10 LKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAERGLDLPDVDLV 86
                           90       100
                   ....*....|....*....|...
gi 1835284405  702 ILLDPDWNPANDKQALARVWREG 724
Cdd:pfam00271   87 INYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
641-724 4.17e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 68.78  E-value: 4.17e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   641 DYMEILCKENMYKFVRLDGGINIKKRHKVINDFThsADIFIFLLSSKSGGCGINLISSNRLILLDPDWNPANDKQALARV 720
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1835284405   721 WREG 724
Cdd:smart00490   79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
92-389 7.94e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.67  E-value: 7.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   92 RRSDETEEQEKIEEVIKKHEPLILYKDENDKIEVDPILAQY-------------LREHQREGVQFVFECLMNIKDDkisG 158
Cdd:COG1061     27 ELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEAleagdeasgtsfeLRPYQQEALEALLAALERGGGR---G 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  159 CILADdMGLGKTLQSITVLYTLLkqgfhkkcAVRRCLILCP-ASLINNWNDEISKWIPNRCNVtcvndnakekivskleG 237
Cdd:COG1061    104 LVVAP-TGTGKTVLALALAAELL--------RGKRVLVLVPrRELLEQWAEELRRFLGDPLAG----------------G 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  238 FKYDIQSTVLICSYECFRINNEFLD-KSSIDMIICDEAHRLkndKTKTYTSIYN-LTAKKRLLLSGTPIQNDLGEFYAli 315
Cdd:COG1061    159 GKKDSDAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHA---GAPSYRRILEaFPAAYRLGLTATPFRSDGREILL-- 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  316 slcnpDLFDDI-------NLFRKKF-ANPILIGRDKDATEKEQE--IASERLTELSNITNKFILRRTNNLLSKVLPVKYL 385
Cdd:COG1061    234 -----FLFDGIvyeyslkEAIEDGYlAPPEYYGIRVDLTDERAEydALSERLREALAADAERKDKILRELLREHPDDRKT 308

                   ....
gi 1835284405  386 InIF 389
Cdd:COG1061    309 L-VF 311
 
Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
133-371 2.50e-98

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: 313.07  E-value: 2.50e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQGFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18004      1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRC-NVTCVNDNAKEKIVSKLEgFKYDIQSTVLICSYECFRIN-NEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd18004     81 WLGLRRiKVVTADGNAKDVKASLDF-FSSASTYPVLIISYETLRRHaEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFILR 370
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239

                   .
gi 1835284405  371 R 371
Cdd:cd18004    240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
133-759 6.72e-94

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 316.78  E-value: 6.72e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFV-FECLMNIkddkisGCILADDMGLGKTLQSITVLYTLLKQGfhkkcAVRRCLILCPASLINNWNDEIS 211
Cdd:COG0553    242 LRPYQLEGAAWLlFLRRLGL------GGLLADDMGLGKTIQALALLLELKERG-----LARPVLIVAPTSLVGNWQRELA 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWIPNRcNVTCVNDNAKEKivSKLEGFKydiQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNL 291
Cdd:COG0553    311 KFAPGL-RVLVLDGTRERA--KGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRAL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  292 TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPIligrdkdatEKEQEIASERLTELsniTNKFILRR 371
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------EKGDEEALERLRRL---LRPFLLRR 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  372 TNNLLSKVLPVKYLINIFIKLNPIQEALY--VLFLKDKKILKNDNTNNKVNVLINIKKLEKICNHPLLLnvndIKEIGQV 449
Cdd:COG0553    453 TKEDVLKDLPEKTEETLYVELTPEQRALYeaVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAEL 528
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  450 TLWkliedvifemqtnmkicnrgnkrdnkndskSGcvlKVDKsmssisnnnmkngndmnntnnntnnntnnntnnntnnn 529
Cdd:COG0553    529 SGR------------------------------SA---KLEA-------------------------------------- 537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  530 insninnninnninsninnninsnmnnntnlrcgsrgnqndasgyvgnkrkpieldynkpVKRIIEECKRDiyrsyynfs 609
Cdd:COG0553    538 ------------------------------------------------------------LLELLEELLAE--------- 548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  610 ckflllhfllknikqntNDKVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSADIFIFLLSSKSG 689
Cdd:COG0553    549 -----------------GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAG 611
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  690 GCGINLISSNRLILLDPDWNPANDKQALARVWREGQKKICYIYRLFCTGTIDEKVYQRQISKDGLSNMIV 759
Cdd:COG0553    612 GEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
133-371 9.64e-81

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: 264.72  E-value: 9.64e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQGFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNAKEKIVSKLEGF----KYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSI 288
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWasqqGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  289 YNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFI 368
Cdd:cd18067    161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCI 240

                   ...
gi 1835284405  369 LRR 371
Cdd:cd18067    241 IRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
133-371 1.54e-69

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: 232.81  E-value: 1.54e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQG-FHKKCAVRRCLILCPASLINNWNDEIS 211
Cdd:cd18066      1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGpYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWI-PNRCNVTCVNDNakekivSKLEGFKYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd18066     81 KWLgSERIKVFTVDQD------HKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFILR 370
Cdd:cd18066    155 LSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILR 234

                   .
gi 1835284405  371 R 371
Cdd:cd18066    235 R 235
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
136-438 3.82e-65

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: 222.56  E-value: 3.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  136 HQREGVQFVFECLMNIKddkiSGCILADDMGLGKTLQSITVLYTLLKQgfhKKCAVRRCLILCPASLINNWNDEISKWI- 214
Cdd:pfam00176    1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHV---DKNWGGPTLIVVPLSLLHNWMNEFERWVs 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  215 PNRCNVTCVNDNAKEKIVSKLEG---FKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNL 291
Cdd:pfam00176   74 PPALRVVVLHGNKRPQERWKNDPnflADFD----VVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  292 TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDatekeqeiaseRLTELSNITNKFILRR 371
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKK-----------GVSRLHKLLKPFLLRR 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835284405  372 TNNLLSKVLPVKYLINIFIKLNPIQEALYVLFLKDKKILKNDNTN----NKVNVLINIKKLEKICNHPLLL 438
Cdd:pfam00176  219 TKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreIKASLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
133-323 5.74e-59

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


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 200.48  E-value: 5.74e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKddkisGCILADDMGLGKTLQSITVLYTLLKQGFhkkcAVRRCLILCPASLINNWNDEISK 212
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGP-----GGILADEMGLGKTLQAIAFLAYLLKEGK----ERGPVLVVCPLSVLENWEREFEK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNrCNVTCVNDNAKEKivSKLEGFKYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLT 292
Cdd:cd17919     72 WTPD-LRVVVYHGSQRER--AQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1835284405  293 AKKRLLLSGTPIQNDLGEFYALISLCNPDLF 323
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
133-356 6.53e-57

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: 197.13  E-value: 6.53e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECL--MNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQgfHKKcaVRRCLILCPASLINNWNDEI 210
Cdd:cd18007      1 LKPHQVEGVRFLWSNLvgTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAA--APR--RSRPLVLCPASTLYNWEDEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  211 SKWIPNRCNV--TCVNDNAKEKIVSKLEGF-KYDIQSTVLICSYECFRI-----NNEFLDKSSI---------DMIICDE 273
Cdd:cd18007     77 KKWLPPDLRPllVLVSLSASKRADARLRKInKWHKEGGVLLIGYELFRNlasnaTTDPRLKQEFiaalldpgpDLLVLDE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  274 AHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIA 353
Cdd:cd18007    157 GHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLM 236

                   ...
gi 1835284405  354 SER 356
Cdd:cd18007    237 LKR 239
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
133-371 1.20e-53

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: 187.97  E-value: 1.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKddkisGCILADDMGLGKTLQSITVLYTLL----------------KQGFHKKCAVRRCLI 196
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGR-----GGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSAKKPVLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  197 LCPASLINNWNDEISKWipNRCNVTCVNDNAKEKIV-SKLEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAH 275
Cdd:cd18005     76 VAPLSVLYNWKDELDTW--GHFEVGVYHGSRKDDELeGRLKAGRLE----VVVTTYDTLRRCIDSLNSINWSAVIADEAH 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  276 RLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASE 355
Cdd:cd18005    150 RIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRK 229
                          250
                   ....*....|....*.
gi 1835284405  356 RLTELSNITNKFILRR 371
Cdd:cd18005    230 RKQELAVKLSKFFLRR 245
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
133-372 1.32e-50

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: 178.14  E-value: 1.32e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQ-FVFECLMNIkddkisGCILADDMGLGKTLQSITVLytllkQGFHKKCAVRRCLILCPASLINNWNDEIS 211
Cdd:cd18012      5 LRPYQKEGFNwLSFLRHYGL------GGILADDMGLGKTLQTLALL-----LSRKEEGRKGPSLVVAPTSLIYNWEEEAA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWIPNrcnVTCV---NDNAKEKIVSKLEgfKYDIqstvLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSI 288
Cdd:cd18012     74 KFAPE---LKVLvihGTKRKREKLRALE--DYDL----VITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  289 YNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEkeqeiaserltELSNITNKFI 368
Cdd:cd18012    145 KALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALE-----------ELKKLISPFI 213

                   ....
gi 1835284405  369 LRRT 372
Cdd:cd18012    214 LRRL 217
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
133-371 2.25e-50

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: 177.95  E-value: 2.25e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKddkisGCILADDMGLGKTLQSITVLytllkQGFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGK-----GGILADDMGLGKTVQICAFL-----SGMFDSGLIKSVLVVMPTSLIPHWVKEFAK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRcNVTC---VNDNAKEKIVSK-LEGFkydiqsTVLICSYECFRINNEFL-----DKSSIDMIICDEAHRLKNDKTK 283
Cdd:cd18001     71 WTPGL-RVKVfhgTSKKERERNLERiQRGG------GVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTK 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  284 TYTSIYNLTAKKRLLLSGTPIQNDLGEFYALIS-LCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSN 362
Cdd:cd18001    144 SAKSLREIPAKNRIILTGTPIQNNLKELWALFDfACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQ 223

                   ....*....
gi 1835284405  363 ITNKFILRR 371
Cdd:cd18001    224 IIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
627-735 2.55e-45

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: 159.56  E-value: 2.55e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  627 NDKVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSADIFIFLLSSKSGGCGINLISSNRLILLDP 706
Cdd:cd18793     27 GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDP 106
                           90       100
                   ....*....|....*....|....*....
gi 1835284405  707 DWNPANDKQALARVWREGQKKICYIYRLF 735
Cdd:cd18793    107 WWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
133-371 5.34e-45

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: 162.52  E-value: 5.34e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYtlLKQGFHK---KCAVRRCLILCPASLINNWNDE 209
Cdd:cd17999      1 LRPYQQEGINW----LAFLNKYNLHG-ILCDDMGLGKTLQTLCILA--SDHHKRAnsfNSENLPSLVVCPPTLVGHWVAE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  210 ISKWIPNRCNVTCVNDNAKEKIVSKLEGFKydiQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIY 289
Cdd:cd17999     74 IKKYFPNAFLKPLAYVGPPQERRRLREQGE---KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  290 NLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASERLTELSNITNKFIL 369
Cdd:cd17999    151 QLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLL 230

                   ..
gi 1835284405  370 RR 371
Cdd:cd17999    231 RR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
133-356 1.70e-40

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 150.04  E-value: 1.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFEC----LMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQgfHKKCAVRRCLILCPASLINNWND 208
Cdd:cd18068      1 LKPHQVDGVQFMWDCccesLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLC--EKLENFSRVLVVCPLNTVLNWLN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIP--NRCNVTCVNDNA--KEKIVSKLEGFKYDIQSTVLICSYECFRI----------------NNEFLDKSSIDM 268
Cdd:cd18068     79 EFEKWQEglKDEEKIEVNELAtyKRPQERSYKLQRWQEEGGVMIIGYDMYRIlaqernvksreklkeiFNKALVDPGPDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  269 IICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEK 348
Cdd:cd18068    159 VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLV 238

                   ....*...
gi 1835284405  349 EQEIASER 356
Cdd:cd18068    239 DVRVMKKR 246
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
133-371 1.78e-39

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


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 146.04  E-value: 1.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKddkisGCILADDMGLGKTLQSITVLYTLLKqgfhKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQH-----GCILGDEMGLGKTCQTISLLWYLAG----RLKLLGPFLVLCPLSVLDNWKEELNR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDnaKEKIVSKLEGFKYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLT 292
Cdd:cd18006     72 FAPDLSVITYMGD--KEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  293 AKKRLLLSGTPIQNDLGEFYALISLCNPDLF--DDINLFRKKFANpiligrdkdaTEKEQEIASerltELSNITNKFILR 370
Cdd:cd18006    150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSE----------TDDESETVE----ELHLLLQPFLLR 215

                   .
gi 1835284405  371 R 371
Cdd:cd18006    216 R 216
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
133-371 8.57e-37

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: 139.34  E-value: 8.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfeclMNIKddkisGCILADDMGLGKTLQSITVLYTLLKQGF----------HKKCAVRRC---LILCP 199
Cdd:cd18008      1 LLPYQKQGLAW-----MLPR-----GGILADEMGLGKTIQALALILATRPQDPkipeeleensSDPKKLYLSkttLIVVP 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  200 ASLINNWNDEISKWIPNRCNVTCVNDNAKEKI-VSKLEgfKYDIqstVLIcSYEcfRINNEFLDKSSIDM---------- 268
Cdd:cd18008     71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKsIEELS--DYDI---VIT-TYG--TLASEFPKNKKGGGrdskekeasp 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  269 --------IICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIG 340
Cdd:cd18008    143 lhrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKN 222
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1835284405  341 RDKdatekeqeiASERlteLSNITNKFILRR 371
Cdd:cd18008    223 DRK---------ALER---LQALLKPILLRR 241
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
133-372 7.72e-36

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: 135.91  E-value: 7.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLyTLLKQ-----GFHkkcavrrcLILCPASLINNWN 207
Cdd:cd17997      4 MRDYQIRGLNW----LISLFENGING-ILADEMGLGKTLQTISLL-GYLKHykninGPH--------LIIVPKSTLDNWM 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  208 DEISKWIPNrCNVTCVNDNAKEK---IVSKLEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKT 284
Cdd:cd17997     70 REFKRWCPS-LRVVVLIGDKEERadiIRDVLLPGKFD----VCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  285 YTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKdatekeqeiasERLTELSNIT 364
Cdd:cd17997    145 SQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQ-----------EVVQRLHKVL 213

                   ....*...
gi 1835284405  365 NKFILRRT 372
Cdd:cd17997    214 RPFLLRRI 221
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
133-356 5.00e-35

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: 133.79  E-value: 5.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVF----ECLMNIKDDKISGCILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWND 208
Cdd:cd18069      1 LKPHQIGGIRFLYdniiESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTV-----LAIVPVNTLQNWLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPNRCNVTCV----------NDNAKEKIVSKLEGFKYDIQSTVLICSYECFRInnefldKSSIDMIICDEAHRLK 278
Cdd:cd18069     76 EFNKWLPPPEALPNVrprpfkvfilNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL------RPGPDVVICDEGHRIK 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835284405  279 NDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATEKEQEIASER 356
Cdd:cd18069    150 NCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
133-371 2.59e-34

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: 131.32  E-value: 2.59e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLKQ----GFHkkcavrrcLILCPASLINNWND 208
Cdd:cd18003      1 LREYQHIGLDW----LATLYEKNLNG-ILADEMGLGKTIQTIALLAHLACEkgnwGPH--------LIVVPTSVMLNWEM 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPNRCNVTCVNdNAKEKIVSKLEGFKYDiQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSI 288
Cdd:cd18003     68 EFKRWCPGFKILTYYG-SAKERKLKRQGWMKPN-SFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  289 YNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPIligrdKDATEKEQEIASERLTELSNITNKFI 368
Cdd:cd18003    146 LNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL-----TAMSEGSQEENEELVRRLHKVLRPFL 220

                   ...
gi 1835284405  369 LRR 371
Cdd:cd18003    221 LRR 223
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
133-787 1.04e-33

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 141.09  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLK----QGFHkkcavrrcLILCPASLINNWND 208
Cdd:PLN03142   170 MRDYQLAGLNW----LIRLYENGING-ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVVAPKSTLGNWMN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPnRCNVTCVNDNAKEKIVSK---LEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTY 285
Cdd:PLN03142   237 EIRRFCP-VLRAVKFHGNPEERAHQReelLVAGKFD----VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  286 TSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANpiligrdkDATEKEQEIASerltELSNITN 365
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI--------SGENDQQEVVQ----QLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  366 KFILRRTNNLLSKVLPVKYLINIFIKLNPIQEALYvlflkdKKILKND----NTNNKVNVLINIK-KLEKICNHPLLLNV 440
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY------KALLQKDldvvNAGGERKRLLNIAmQLRKCCNHPYLFQG 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  441 ndiKEIGQ--VTLWKLIEdvifemqtnmkicnrgnkrdnkndsksgcvlkvdksmssisnnnmkngndmnntnnntnnnt 518
Cdd:PLN03142   454 ---AEPGPpyTTGEHLVE-------------------------------------------------------------- 468
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  519 nnntnnntnnninsninnninnninsninnninsnmnnntnlrcgsrgnqndasgyvgNKRKPIELDynKPVKRIIEECK 598
Cdd:PLN03142   469 ----------------------------------------------------------NSGKMVLLD--KLLPKLKERDS 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  599 RdiyrsyynfsckflllhfllknikqntndkVVIVSNYTQTLDYMEILCKENMYKFVRLDGGINIKKRHKVINDFTH-SA 677
Cdd:PLN03142   489 R------------------------------VLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpGS 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  678 DIFIFLLSSKSGGCGINLISSNRLILLDPDWNPANDKQALARVWREGQKKICYIYRlFCT-GTIDEKVYQRQISKDGLSN 756
Cdd:PLN03142   539 EKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFR-FCTeYTIEEKVIERAYKKLALDA 617
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1835284405  757 MIVT------TTNLSKD---QMSDENVKKLFNYKMNTVSE 787
Cdd:PLN03142   618 LVIQqgrlaeQKTVNKDellQMVRYGAEMVFSSKDSTITD 657
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
133-335 1.25e-32

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: 125.63  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDdkisgCILADDMGLGKTLQSITVLYTLLKQGfHKKCAVrrcLILCPASLINNWNDEISK 212
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTIQTIVFLYSLYKEG-HSKGPF---LVSAPLSTIINWEREFEM 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNakekivsklegfkydiqstVLICSYECFRINNEFLdkSSID--MIICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd17994     72 WAPDFYVVTYVGDH-------------------VLLTSYELISIDQAIL--GSIDwaVLVVDEAHRLKNNQSKFFRILNS 130
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd17994    131 YKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
133-371 3.24e-32

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: 125.96  E-value: 3.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVqfvfECLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLKQG----FhkkcavrrcLILCPASLINNWND 208
Cdd:cd18009      4 MRPYQLEGM----EWLRMLWENGING-ILADEMGLGKTIQTIALLAHLRERGvwgpF---------LVIAPLSTLPNWVN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPNrCNVTCVNDNAKEK--IVSKLEGFKYDIQST-VLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTY 285
Cdd:cd18009     70 EFARFTPS-VPVLLYHGTKEERerLRKKIMKREGTLQDFpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  286 TSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAnpilIGRDKDATEKEQEIASER----LTELS 361
Cdd:cd18009    149 QELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFD----FSSLSDNAADISNLSEEReqniVHMLH 224
                          250
                   ....*....|
gi 1835284405  362 NITNKFILRR 371
Cdd:cd18009    225 AILKPFLLRR 234
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
133-332 9.59e-32

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: 123.55  E-value: 9.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFeclmnikDDKISGCILADDMGLGKTLQSITVLYTLLKQGfhkkcAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18011      1 PLPHQIDAVLRAL-------RKPPVRLLLADEVGLGKTIEAGLIIKELLLRG-----DAKRVLILCPASLVEQWQDELQD 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 --WIPNRCnvtCVNDNAKEKIVSKLEGFKydiQSTVLICSYECFRINNE---FLDKSSIDMIICDEAHRLKNDKTKTYTS 287
Cdd:cd18011     69 kfGLPFLI---LDRETAAQLRRLIGNPFE---EFPIVIVSLDLLKRSEErrgLLLSEEWDLVVVDEAHKLRNSGGGKETK 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1835284405  288 IYNL------TAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKK 332
Cdd:cd18011    143 RYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
133-371 1.17e-30

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 120.77  E-value: 1.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFEclmnikddkISG-CILADDMGLGKTLQSITVLYTllkqgFHKKCAVrrcLILCPASLINNWNDEIS 211
Cdd:cd18010      1 LLPFQREGVCFALR---------RGGrVLIADEMGLGKTVQAIAIAAY-----YREEWPL---LIVCPSSLRLTWADEIE 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KWIPN--RCNVTCVNdNAKEKIvsklegfkYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIY 289
Cdd:cd18010     64 RWLPSlpPDDIQVIV-KSKDGL--------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAAL 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  290 NLT--AKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKDATekeqeiASERLTELSNI-TNK 366
Cdd:cd18010    135 PLLkrAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYS------GSSNLEELHLLlLAT 208

                   ....*
gi 1835284405  367 FILRR 371
Cdd:cd18010    209 IMIRR 213
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
133-333 1.32e-30

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: 120.82  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKddkisGCILADDMGLGKTLQSITVLYTLLKQGFHKKCAvrrcLILCPASLINNWNDEISK 212
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRR-----NCILADEMGLGKTIQSIAFLEHLYQVEGIRGPF----LVIAPLSTIPNWQREFET 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPnrCNVTCVNDNAKEK-IVSKLEGFKYD---------IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKT 282
Cdd:cd17995     72 WTD--MNVVVYHGSGESRqIIQQYEMYFKDaqgrkkkgvYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNS 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1835284405  283 KTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKF 333
Cdd:cd17995    150 KLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
133-315 3.23e-30

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 118.58  E-value: 3.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFEclmniKDDKISGCILADDMGLGKTLQSITVLYTLlkqgFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18000      1 LFKYQQTGVQWLWE-----LHCQRVGGILGDEMGLGKTIQIIAFLAAL----HHSKLGLGPSLIVCPATVLKQWVKEFHR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPN-RCNV---TCVNDNAKEKIVSKLEGFKYDIQST----VLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKT 284
Cdd:cd18000     72 WWPPfRVVVlhsSGSGTGSEEKLGSIERKSQLIRKVVgdggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1835284405  285 YTSIYNLTAKKRLLLSGTPIQNDLGEFYALI 315
Cdd:cd18000    152 TLACKQLRTPHRLILSGTPIQNNLKELWSLF 182
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
133-371 4.51e-30

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: 119.53  E-value: 4.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLKqgfhKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18002      1 LKEYQLKGLNW----LANLYEQGING-ILADEMGLGKTVQSIAVLAHLAE----EHNIWGPFLVIAPASTLHNWQQEISR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNAKEKIVSKLEGFKY----DIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSI 288
Cdd:cd18002     72 FVPQFKVLPYWGNPKDRKVLRKFWDRKNlytrDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  289 YNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPIligrdKDATEKEQEIASERLTELSNITNKFI 368
Cdd:cd18002    152 LSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDI-----ESHAENKTGLNEHQLKRLHMILKPFM 226

                   ...
gi 1835284405  369 LRR 371
Cdd:cd18002    227 LRR 229
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
133-371 5.94e-30

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: 119.40  E-value: 5.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLK----QGFHkkcavrrcLILCPASLINNWND 208
Cdd:cd17996      4 LKEYQLKGLQW----MVSLYNNNLNG-ILADEMGLGKTIQTISLITYLMEkkknNGPY--------LVIVPLSTLSNWVS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  209 EISKWIPN-RCNVTCVNDNAKEKIVSKLEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTK---T 284
Cdd:cd17996     71 EFEKWAPSvSKIVYKGTPDVRKKLQSQIRAGKFN----VLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKltqT 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  285 YTSIYNltAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILI--GRDKDA-TEKEQEIASERLTEls 361
Cdd:cd17996    147 LNTYYH--ARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtgEQVKIElNEEETLLIIRRLHK-- 222
                          250
                   ....*....|
gi 1835284405  362 nITNKFILRR 371
Cdd:cd17996    223 -VLRPFLLRR 231
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
159-323 2.90e-27

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: 109.78  E-value: 2.90e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  159 CILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWNDEISKWIPNrCNVTCVNDNAKEK------IV 232
Cdd:cd17998     22 GILADEMGLGKTIQVIAFLAYLKEIGIPGPH-----LVVVPSSTLDNWLREFKRWCPS-LKVEPYYGSQEERkhlrydIL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  233 SKLEGFKydiqstVLICSYECFRINNE---FLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLG 309
Cdd:cd17998     96 KGLEDFD------VIVTTYNLATSNPDdrsFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLL 169
                          170
                   ....*....|....
gi 1835284405  310 EFYALISLCNPDLF 323
Cdd:cd17998    170 ELMSLLNFIMPKPF 183
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
133-371 4.45e-27

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


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 110.52  E-value: 4.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfeclMNIKDDKISGCILADDMGLGKTLQSITVLYTLlkqgFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd17993      2 LRDYQLTGLNW-----LAHSWCKGNNGILADEMGLGKTVQTISFLSYL----FHSQQQYGPFLVVVPLSTMPAWQREFAK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNAKEKIVSKLEGFKYD---IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIY 289
Cdd:cd17993     73 WAPDMNVIVYLGDIKSRDTIREYEFYFSQtkkLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  290 NLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDdinlFRKKFanpiligrdKDATEKEQEiasERLTELSNITNKFIL 369
Cdd:cd17993    153 EFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFD----IWEEF---------EEEHDEEQE---KGIADLHKELEPFIL 216

                   ..
gi 1835284405  370 RR 371
Cdd:cd17993    217 RR 218
DEXDc smart00487
DEAD-like helicases superfamily;
133-321 1.45e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 108.35  E-value: 1.45e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   133 LREHQREGVQFVFECLMNikddkisgCILADDMGLGKTLQSITVLYTLLKQGFHKkcavrRCLILCP-ASLINNWNDEIS 211
Cdd:smart00487    9 LRPYQKEAIEALLSGLRD--------VILAAPTGSGKTLAALLPALEALKRGKGG-----RVLVLVPtRELAEQWAEELK 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   212 KWIPNRC--NVTCVNDNAKEKIVSKLEGFKYDIqstvLICSYECFR--INNEFLDKSSIDMIICDEAHRLKNDK-TKTYT 286
Cdd:smart00487   76 KLGPSLGlkVVGLYGGDSKREQLRKLESGKTDI----LVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGfGDQLE 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 1835284405   287 SIYNLTAK--KRLLLSGTP---IQNDLGEFYALISLCNPD 321
Cdd:smart00487  152 KLLKLLPKnvQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
160-335 8.67e-26

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: 107.40  E-value: 8.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  160 ILADDMGLGKTLQSITVLYTLLKQGfHKKCAVrrcLILCPASLINNWNDEISKWIPNRCNVTCVNDNAKEKIVSKLEgFK 239
Cdd:cd18055     23 ILADEMGLGKTIQTIVFLYSLYKEG-HTKGPF---LVSAPLSTIINWEREFQMWAPDFYVVTYTGDKDSRAIIRENE-FS 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  240 YD------------------IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSG 301
Cdd:cd18055     98 FDdnavkggkkafkmkreaqVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTG 177
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1835284405  302 TPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd18055    178 TPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
160-335 9.19e-26

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


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 107.07  E-value: 9.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  160 ILADDMGLGKTLQSITVLYTLLKQGfHKKCAVrrcLILCPASLINNWNDEISKWIPNRCNVTCVNDNAKEKIVSKLEgFK 239
Cdd:cd18056     23 ILADEMGLGKTVQTAVFLYSLYKEG-HSKGPF---LVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENE-FS 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  240 YD------------------IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSG 301
Cdd:cd18056     98 FEdnairggkkasrmkkeasVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTG 177
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1835284405  302 TPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd18056    178 TPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD 211
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
133-324 1.39e-25

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: 106.63  E-value: 1.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFE--ClmnikddKISGCILADDMGLGKTLQSITVLYTLlkqgFHKKCAVRRCLILCPASLINNWNDEI 210
Cdd:cd18054     21 LRDYQLEGLNWLAHswC-------KNNSVILADEMGLGKTIQTISFLSYL----FHQHQLYGPFLLVVPLSTLTSWQREF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  211 SKWIPNRCNVTCVNDNAKEKIVSKLEGFKYD---IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTS 287
Cdd:cd18054     90 EIWAPEINVVVYIGDLMSRNTIREYEWIHSQtkrLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKT 169
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1835284405  288 IYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFD 324
Cdd:cd18054    170 LIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFE 206
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
133-383 1.59e-25

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: 106.67  E-value: 1.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLkqgfHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18064     16 LRDYQVRGLNW----LISLYENGING-ILADEMGLGKTLQTISLLGYMK----HYRNIPGPHMVLVPKSTLHNWMAEFKR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDnaKEKIVSKLEGFKYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLT 292
Cdd:cd18064     87 WVPTLRAVCLIGD--KDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  293 AKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGrDKDATEKeqeiaserlteLSNITNKFILRRT 372
Cdd:cd18064    165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG-DQKLVER-----------LHMVLRPFLLRRI 232
                          250
                   ....*....|.
gi 1835284405  373 NNLLSKVLPVK 383
Cdd:cd18064    233 KADVEKSLPPK 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
133-371 1.83e-25

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: 106.69  E-value: 1.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLKqgfHKKCAvRRCLILCPASLINNWNDEISK 212
Cdd:cd18063     24 LKHYQLQGLEW----MVSLYNNNLNG-ILADEMGLGKTIQTIALITYLME---HKRLN-GPYLIIVPLSTLSNWTYEFDK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNA-KEKIVSKLEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKtYTSIYN- 290
Cdd:cd18063     95 WAPSVVKISYKGTPAmRRSLVPQLRSGKFN----VLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK-LTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 -LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPI-LIGRDKDATEKEQEIASERLTElsnITNKFI 368
Cdd:cd18063    170 hYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLHK---VLRPFL 246

                   ...
gi 1835284405  369 LRR 371
Cdd:cd18063    247 LRR 249
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
160-335 2.85e-25

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: 105.92  E-value: 2.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  160 ILADDMGLGKTLQSITVLYTLLKQGfHKKCAVrrcLILCPASLINNWNDEISKWIPNRCNVTCVNDNAKEKIVSKLEgFK 239
Cdd:cd18057     23 ILADEMGLGKTVQTIVFLYSLYKEG-HSKGPY---LVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENE-FS 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  240 YD------------------IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSG 301
Cdd:cd18057     98 FEdnairsgkkvfrmkkeaqIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTG 177
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1835284405  302 TPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd18057    178 TPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
133-335 4.99e-25

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: 104.73  E-value: 4.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDdkisgCILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWNDEISK 212
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRN-----CILADEMGLGKTIQSITFLYEIYLKGIHGPF-----LVIAPLSTIPNWEREFRT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WipNRCNVTCVN-DNAKEKIVSKLEGFKYDIQSTVLICSYECFRINNEF---------LDKSSIDMIICDEAHRLKNDKT 282
Cdd:cd18059     71 W--TELNVVVYHgSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFemiltdcpeLRNIPWRCVVIDEAHRLKNRNC 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1835284405  283 KTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd18059    149 KLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
133-371 8.35e-25

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: 105.13  E-value: 8.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLKqgfHKKCAvRRCLILCPASLINNWNDEISK 212
Cdd:cd18062     24 LKQYQIKGLEW----LVSLYNNNLNG-ILADEMGLGKTIQTIALITYLME---HKRIN-GPFLIIVPLSTLSNWVYEFDK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVND-NAKEKIVSKLEGFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKtYTSIYN- 290
Cdd:cd18062     95 WAPSVVKVSYKGSpAARRAFVPQLRSGKFN----VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCK-LTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 -LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPI-LIGRDKDATEKEQEIASERLTElsnITNKFI 368
Cdd:cd18062    170 hYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHK---VLRPFL 246

                   ...
gi 1835284405  369 LRR 371
Cdd:cd18062    247 LRR 249
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
133-371 1.15e-24

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: 103.58  E-value: 1.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDdkisgCILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWNDEISK 212
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSITFLSEIFLMGIRGPF-----LIIAPLSTITNWEREFRT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WipNRCNVTCVNDNA-KEKIVSKLEGFKYDIQST---------VLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKT 282
Cdd:cd18058     71 W--TEMNAIVYHGSQiSRQMIQQYEMYYRDEQGNplsgifkfqVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNC 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  283 KTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAnpiligrdkDATEKEQeiaserLTELSN 362
Cdd:cd18058    149 KLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG---------DLKTEEQ------VKKLQS 213

                   ....*....
gi 1835284405  363 ITNKFILRR 371
Cdd:cd18058    214 ILKPMMLRR 222
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
155-371 1.35e-24

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: 104.10  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  155 KISGCILADDMGLGKTLQSIT-VLYTLLKQ---GFHKK------------CAVRRC--LILCPASLINNWNDEI-SKWIP 215
Cdd:cd18072     19 KPRGGILADDMGLGKTLTMIAlILAQKNTQnrkEEEKEkalteweskkdsTLVPSAgtLVVCPASLVHQWKNEVeSRVAS 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  216 NRCNVTCVNDNAKEKIVSKLEgfKYDIQ-STVLICSYECFRINNEFLDKSSIDM----IICDEAHRLKNDKTKTYTSIYN 290
Cdd:cd18072     99 NKLRVCLYHGPNRERIGEVLR--DYDIViTTYSLVAKEIPTYKEESRSSPLFRIawarIILDEAHNIKNPKVQASIAVCK 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  291 LTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANpiligrdkdatekEQEIASERlteLSNITNKFILR 370
Cdd:cd18072    177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDN-------------KSRKGGER---LNILTKSLLLR 240

                   .
gi 1835284405  371 R 371
Cdd:cd18072    241 R 241
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
133-352 1.48e-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: 103.98  E-value: 1.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMnikddKISGCILADDMGLGKTLQSITVLYTLlkqgFHKKCAVRRCLILCPASLINNWNDEISK 212
Cdd:cd18053     21 LRDYQLNGLNWLAHSWC-----KGNSCILADEMGLGKTIQTISFLNYL----FHEHQLYGPFLLVVPLSTLTSWQREIQT 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WIPNRCNVTCVNDNAKEKIVSKLEGFKYD---IQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIY 289
Cdd:cd18053     92 WAPQMNAVVYLGDINSRNMIRTHEWMHPQtkrLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLI 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835284405  290 NLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANpiliGRDKDATEKEQEI 352
Cdd:cd18053    172 DFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GREYGYASLHKEL 230
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
122-343 3.05e-24

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: 102.79  E-value: 3.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  122 KIEVDP--ILAQYLREHQREGVQFvfecLMNIKDDKISGcILADDMGLGKTLQSITVLYTLLkqgfHKKCAVRRCLILCP 199
Cdd:cd18065      3 RFEESPsyVKGGTLRDYQVRGLNW----MISLYENGVNG-ILADEMGLGKTLQTIALLGYLK----HYRNIPGPHMVLVP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  200 ASLINNWNDEISKWIPNRCNVTCVNDnaKEKIVSKLEGFKYDIQSTVLICSYECFRINNEFLDKSSIDMIICDEAHRLKN 279
Cdd:cd18065     74 KSTLHNWMNEFKRWVPSLRAVCLIGD--KDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835284405  280 DKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDK 343
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK 215
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
154-371 7.65e-23

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: 98.70  E-value: 7.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  154 DKISGCILADDMGLGKTLQSITVLytllkqgfhkkcAVRRCLILCPASLINNWNDEISKWI-PNRCNVTCVNDNAKEKIV 232
Cdd:cd18071     46 ELVRGGILADDMGLGKTLTTISLI------------LANFTLIVCPLSVLSNWETQFEEHVkPGQLKVYTYHGGERNRDP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  233 SKLEgfKYDIqstvLICSYECfrINNEFLDKSSIDM-------IICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQ 305
Cdd:cd18071    114 KLLS--KYDI----VLTTYNT--LASDFGAKGDSPLhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQ 185
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835284405  306 NDLGEFYALISLCNPDLFDDINLFRKKFANPILIGRDKdatekeqeiASERLTEL-SNITnkfiLRR 371
Cdd:cd18071    186 NSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPT---------GLKRLQVLmKQIT----LRR 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
133-371 1.45e-22

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 97.43  E-value: 1.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDdkisgCILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWNDEISK 212
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQN-----CILADEMGLGKTIQSIAFLQEVYNVGIHGPF-----LVIAPLSTITNWEREFNT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WipNRCNVTCVNDN-AKEKIVSKLE-------------GFKYDiqstVLICSYECFRINNEFLDKSSIDMIICDEAHRLK 278
Cdd:cd18060     71 W--TEMNTIVYHGSlASRQMIQQYEmyckdsrgrlipgAYKFD----ALITTFEMILSDCPELREIEWRCVIIDEAHRLK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  279 NDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAnpiligrdkDATEKEQeiaserLT 358
Cdd:cd18060    145 NRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---------DLKTEEQ------VQ 209
                          250
                   ....*....|...
gi 1835284405  359 ELSNITNKFILRR 371
Cdd:cd18060    210 KLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
133-335 9.53e-22

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: 95.07  E-value: 9.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFVFECLMNIKDdkisgCILADDMGLGKTLQSITVLYTLLKQGFHKKCavrrcLILCPASLINNWNDEISK 212
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRN-----CILADEMGLGKTIQSITFLYEILLTGIRGPF-----LIIAPLSTIANWEREFRT 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  213 WipNRCNVTCVNDN-AKEKIVSKLEGFKYDIQSTVLICSYECFRINNEF---------LDKSSIDMIICDEAHRLKNDKT 282
Cdd:cd18061     71 W--TDLNVVVYHGSlISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFemilggcpeLNAIDWRCVIIDEAHRLKNKNC 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1835284405  283 KTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDDINLFRKKFAN 335
Cdd:cd18061    149 KLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
622-724 1.01e-19

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: 85.73  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  622 IKQNTNDKVVIVSNYTQTLDyMEILCKENMYKFVRLDGGINIKKRHKVINDFTHSAdiFIFLLSSKSGGCGINLISSNRL 701
Cdd:pfam00271   10 LKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAERGLDLPDVDLV 86
                           90       100
                   ....*....|....*....|...
gi 1835284405  702 ILLDPDWNPANDKQALARVWREG 724
Cdd:pfam00271   87 INYDLPWNPASYIQRIGRAGRAG 109
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
133-340 2.49e-14

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: 73.54  E-value: 2.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfeclmnIKDDKISGCILadDMGLGKTLQSITVLYTLLKQGFHkkcavRRCLILCPASLI-NNWNDEIS 211
Cdd:cd18013      1 PHPYQKVAINF-------IIEHPYCGLFL--DMGLGKTVTTLTALSDLQLDDFT-----RRVLVIAPLRVArSTWPDEVE 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  212 KW-IPNRCNVTCVNDNAKEKIVSklegfkYDIQSTVLICSYECFR-INNEFLDKSSIDMIICDEAHRLKNDKTKTYTSIY 289
Cdd:cd18013     67 KWnHLRNLTVSVAVGTERQRSKA------ANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALR 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835284405  290 NL--TAKKRLLLSGTPIQNDLGEFYALISLCN--PDLFDDINLFRKKFANPILIG 340
Cdd:cd18013    141 KVrpVIKRLIGLTGTPSPNGLMDLWAQIALLDqgERLGRSITAYRERWFDPDKRN 195
HELICc smart00490
helicase superfamily c-terminal domain;
641-724 4.17e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 68.78  E-value: 4.17e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   641 DYMEILCKENMYKFVRLDGGINIKKRHKVINDFThsADIFIFLLSSKSGGCGINLISSNRLILLDPDWNPANDKQALARV 720
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1835284405   721 WREG 724
Cdd:smart00490   79 GRAG 82
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
133-325 2.61e-13

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: 71.22  E-value: 2.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQFvfeclMnikddKISGCILADDMGLGKTLQSITVLYT-------LLKQGFHKKCA-----------VRRC 194
Cdd:cd18070      1 LLPYQRRAVNW-----M-----LVPGGILADEMGLGKTVEVLALILLhprpdndLDAADDDSDEMvccpdclvaetPVSS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  195 ---LILCPASLINNWNDEISKWIPNRCNVTCVNDNAKEKIVSKLEGFK---YDIqstvLICSYECFRI---------NNE 259
Cdd:cd18070     71 katLIVCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEIlaeYDI----VVTTYDVLRTelhyaeanrSNR 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835284405  260 FLDKSSIDM-------------IICDEAHRLKNDKTKTYTSIYNLTAKKRLLLSGTPIQNDLGEFYALISLCNPDLFDD 325
Cdd:cd18070    147 RRRRQKRYEappsplvlvewwrVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD 225
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
92-389 7.94e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.67  E-value: 7.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405   92 RRSDETEEQEKIEEVIKKHEPLILYKDENDKIEVDPILAQY-------------LREHQREGVQFVFECLMNIKDDkisG 158
Cdd:COG1061     27 ELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEAleagdeasgtsfeLRPYQQEALEALLAALERGGGR---G 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  159 CILADdMGLGKTLQSITVLYTLLkqgfhkkcAVRRCLILCP-ASLINNWNDEISKWIPNRCNVtcvndnakekivskleG 237
Cdd:COG1061    104 LVVAP-TGTGKTVLALALAAELL--------RGKRVLVLVPrRELLEQWAEELRRFLGDPLAG----------------G 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  238 FKYDIQSTVLICSYECFRINNEFLD-KSSIDMIICDEAHRLkndKTKTYTSIYN-LTAKKRLLLSGTPIQNDLGEFYAli 315
Cdd:COG1061    159 GKKDSDAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHA---GAPSYRRILEaFPAAYRLGLTATPFRSDGREILL-- 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  316 slcnpDLFDDI-------NLFRKKF-ANPILIGRDKDATEKEQE--IASERLTELSNITNKFILRRTNNLLSKVLPVKYL 385
Cdd:COG1061    234 -----FLFDGIvyeyslkEAIEDGYlAPPEYYGIRVDLTDERAEydALSERLREALAADAERKDKILRELLREHPDDRKT 308

                   ....
gi 1835284405  386 InIF 389
Cdd:COG1061    309 L-VF 311
ResIII pfam04851
Type III restriction enzyme, res subunit;
133-304 1.44e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 52.29  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVQfvfECLMNIKDDKISGCIladDM--GLGKTLQSITVLYTLLKQGFhkkcaVRRCLILCP-ASLINNWNDE 209
Cdd:pfam04851    4 LRPYQIEAIE---NLLESIKNGQKRGLI---VMatGSGKTLTAAKLIARLFKKGP-----IKKVLFLVPrKDLLEQALEE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  210 ISKWIPNrcnvtcvndnaKEKIVSKLEGFKYDIQST---VLICSYE----CFRINNEFLDKSSIDMIICDEAHRLkndKT 282
Cdd:pfam04851   73 FKKFLPN-----------YVEIGEIISGDKKDESVDdnkIVVTTIQslykALELASLELLPDFFDVIIIDEAHRS---GA 138
                          170       180
                   ....*....|....*....|...
gi 1835284405  283 KTYTSIYN-LTAKKRLLLSGTPI 304
Cdd:pfam04851  139 SSYRNILEyFKPAFLLGLTATPE 161
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
157-302 2.09e-05

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 45.86  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  157 SGCILADDMGLGKTLQ-SITVLYTLLKQGFhkkcavrRCLILCP-ASLINNWNDEISKWIPNRCNVTCVNDNAKEKIVSK 234
Cdd:cd00046      2 ENVLITAPTGSGKTLAaLLAALLLLLKKGK-------KVLVLVPtKALALQTAERLRELFGPGIRVAVLVGGSSAEEREK 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835284405  235 LEGFKYDIqstvLICSYECFRINNEFLDKSS---IDMIICDEAHRLKNDKTKTYTSIYNLTAK-----KRLLLSGT 302
Cdd:cd00046     75 NKLGDADI----IIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALLIDSRGALILDLAVRKAglknaQVILLSAT 146
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
133-303 6.66e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 44.22  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  133 LREHQREGVqfvFECLMNIKDDKisGCIladDM--GLGKTLQSITVLytllkqgfhKKCAVRRCLILCP-ASLINNWNDE 209
Cdd:cd17926      1 LRPYQEEAL---EAWLAHKNNRR--GIL---VLptGSGKTLTALALI---------AYLKELRTLIVVPtDALLDQWKER 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835284405  210 ISKWIPNR--CNVTCVNDNAKEKIVSKLegfkYDIQSTVlICSYECFRINNEFldkssiDMIICDEAHRLkndKTKTYTS 287
Cdd:cd17926     64 FEDFLGDSsiGLIGGGKKKDFDDANVVV----ATYQSLS-NLAEEEKDLFDQF------GLLIVDEAHHL---PAKTFSE 129
                          170
                   ....*....|....*..
gi 1835284405  288 IY-NLTAKKRLLLSGTP 303
Cdd:cd17926    130 ILkELNAKYRLGLTATP 146
 
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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