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Conserved domains on  [gi|1063703870|ref|NP_001324537|]
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SNF2 domain-containing protein / helicase domain-containing protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13029103)

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_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 353-569 1.78e-89

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: 283.80  E-value: 1.78e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVA-----DDPGGCIMAHAPGSGKTFMIISFMQSFLAKYP-QAKPLVVLPKGILPTWKKEFVRWQ 426
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGtdvgsDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKKWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 427 VED-IPLLDFYSAKAENRAQQ-LSILKQWMEKKSILFLGYQQFSTIVCDDTTD----SLSCQEILLKVPSILILDEGHTP 500
Cdd:cd18007    81 PPDlRPLLVLVSLSASKRADArLRKINKWHKEGGVLLIGYELFRNLASNATTDprlkQEFIAALLDPGPDLLVLDEGHRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063703870 501 RNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK--LDTSKSAVKRILAYTPCDVRGR 569
Cdd:cd18007   161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGtlKEFKKKFVKPIEAGQCVDSTEE 231
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 351-833 1.45e-54

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 201.61  E-value: 1.45e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGFQFLCSNlvADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWqvedI 430
Cdd:COG0553   240 ATLRPYQLEGAAWLLFL--RRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKF----A 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLsilKQWMEKKSILFLGYQQFStivcddttdslSCQEILLKVP-SILILDEGHTPRNEDTNLLQ 509
Cdd:COG0553   314 PGLRVLVLDGTRERAKG---ANPFEDADLVITSYGLLR-----------RDIELLAAVDwDLVILDEAQHIKNPATKRAK 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 510 SLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLkldtsksavkrilaytpcdvrgrltGSnsdmASMFNETVEHTL 589
Cdd:COG0553   380 AVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-------------------------GS----LKAFRERFARPI 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 590 QKSEDftvkiKVIQDLREMTKKVLH-YYKGDFLDELPGLADFTVVLNLSPKQ-----------LNEVKKLRREKRKFKVS 657
Cdd:COG0553   431 EKGDE-----EALERLRRLLRPFLLrRTKEDVLKDLPEKTEETLYVELTPEQralyeavleylRRELEGAEGIRRRGLIL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 658 AvgSAIYL-----HPKLKVFSDKSDDVSDTTMDEMVEKLDlnEGVkakfflnlinlcdSAGEKLLVFSQYLiplKFLERL 732
Cdd:COG0553   506 A--ALTRLrqicsHPALLLEEGAELSGRSAKLEALLELLE--ELL-------------AEGEKVLVFSQFT---DTLDLL 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 733 AALAKgwKLGKEVFVLTGNTSSEQREWSMETFNSSPDAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAF 812
Cdd:COG0553   566 EERLE--ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAH 643

                         490       500
                  ....*....|....*....|.
gi 1063703870 813 RPGQKKMVHAYRLIAGSSPEE 833
Cdd:COG0553   644 RIGQTRDVQVYKLVAEGTIEE 664
 
Name Accession Description Interval E-value
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 353-569 1.78e-89

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: 283.80  E-value: 1.78e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVA-----DDPGGCIMAHAPGSGKTFMIISFMQSFLAKYP-QAKPLVVLPKGILPTWKKEFVRWQ 426
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGtdvgsDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKKWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 427 VED-IPLLDFYSAKAENRAQQ-LSILKQWMEKKSILFLGYQQFSTIVCDDTTD----SLSCQEILLKVPSILILDEGHTP 500
Cdd:cd18007    81 PPDlRPLLVLVSLSASKRADArLRKINKWHKEGGVLLIGYELFRNLASNATTDprlkQEFIAALLDPGPDLLVLDEGHRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063703870 501 RNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK--LDTSKSAVKRILAYTPCDVRGR 569
Cdd:cd18007   161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGtlKEFKKKFVKPIEAGQCVDSTEE 231
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 351-833 1.45e-54

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 201.61  E-value: 1.45e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGFQFLCSNlvADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWqvedI 430
Cdd:COG0553   240 ATLRPYQLEGAAWLLFL--RRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKF----A 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLsilKQWMEKKSILFLGYQQFStivcddttdslSCQEILLKVP-SILILDEGHTPRNEDTNLLQ 509
Cdd:COG0553   314 PGLRVLVLDGTRERAKG---ANPFEDADLVITSYGLLR-----------RDIELLAAVDwDLVILDEAQHIKNPATKRAK 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 510 SLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLkldtsksavkrilaytpcdvrgrltGSnsdmASMFNETVEHTL 589
Cdd:COG0553   380 AVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-------------------------GS----LKAFRERFARPI 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 590 QKSEDftvkiKVIQDLREMTKKVLH-YYKGDFLDELPGLADFTVVLNLSPKQ-----------LNEVKKLRREKRKFKVS 657
Cdd:COG0553   431 EKGDE-----EALERLRRLLRPFLLrRTKEDVLKDLPEKTEETLYVELTPEQralyeavleylRRELEGAEGIRRRGLIL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 658 AvgSAIYL-----HPKLKVFSDKSDDVSDTTMDEMVEKLDlnEGVkakfflnlinlcdSAGEKLLVFSQYLiplKFLERL 732
Cdd:COG0553   506 A--ALTRLrqicsHPALLLEEGAELSGRSAKLEALLELLE--ELL-------------AEGEKVLVFSQFT---DTLDLL 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 733 AALAKgwKLGKEVFVLTGNTSSEQREWSMETFNSSPDAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAF 812
Cdd:COG0553   566 EERLE--ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAH 643

                         490       500
                  ....*....|....*....|.
gi 1063703870 813 RPGQKKMVHAYRLIAGSSPEE 833
Cdd:COG0553   644 RIGQTRDVQVYKLVAEGTIEE 664
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 689-826 6.94e-39

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: 140.69  E-value: 6.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 689 EKLDLNEGVKAKFFLNLINLCDSAGEKLLVFSQYLIPLKFLERLAAlakgwKLGKEVFVLTGNTSSEQREWSMETFNSSP 768
Cdd:cd18793     3 PKIEEVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALR-----ERGIKYLRLDGSTSSKERQKLVDRFNEDP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063703870 769 DAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPGQKKMVHAYRLI 826
Cdd:cd18793    78 DIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 356-543 4.04e-22

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: 97.37  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 356 HQIEGFQFL---CSNLVAddpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQA--KPLVVLPKGILPTWKKEFVRWQVEdi 430
Cdd:pfam00176   1 YQIEGVNWMlslENNLGR----GGILADEMGLGKTLQTISLLLYLKHVDKNWggPTLIVVPLSLLHNWMNEFERWVSP-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLSILKQWM-EKKSILFLGYqqfstivcddttdslscqEILLKVPSIL--------ILDEGHTPR 501
Cdd:pfam00176  75 PALRVVVLHGNKRPQERWKNDPNFlADFDVVITTY------------------ETLRKHKELLkkvhwhriVLDEGHRLK 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1063703870 502 NEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:pfam00176 137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 698-815 4.41e-15

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: 71.86  E-value: 4.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 698 KAKFFLNLINLcdSAGEKLLVFSQY--LIPLKFLERlaalakgwKLGKEVFVLTGNTSSEQREWSMETFNSSpDAKIFFg 775
Cdd:pfam00271   2 KLEALLELLKK--ERGGKVLIFSQTkkTLEAELLLE--------KEGIKVARLHGDLSQEEREEILEDFRKG-KIDVLV- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063703870 776 SIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPG 815
Cdd:pfam00271  70 ATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 326-842 7.02e-15

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 79.46  E-value: 7.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  326 ESDNE-LKFSEEGLMIGG---LAAHPTH-AAEMKPHQIEGFQFLCsNLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAK 400
Cdd:PLN03142   138 EEDEEyLKEEEDGLGGSGgtrLLVQPSCiKGKMRDYQLAGLNWLI-RLYENGING-ILADEMGLGKTLQTISLL-GYLHE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  401 Y-----PQakpLVVLPKGILPTWKKEFVRWqvedIPLLDF--YSAKAENRAQQlsilkqwmeKKSILFLGyqQFSTIVcd 473
Cdd:PLN03142   215 YrgitgPH---MVVAPKSTLGNWMNEIRRF----CPVLRAvkFHGNPEERAHQ---------REELLVAG--KFDVCV-- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  474 dttdslSCQEILLKVPSIL--------ILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKF 545
Cdd:PLN03142   275 ------TSFEMAIKEKTALkrfswryiIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEI 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  546 LKldtskSAvkrilaytpcdvrgrltgsnsdmasmfnETVEHTLQKSEDfTVKIKVIQDLREMTKK-VLHYYKGDFLDEL 624
Cdd:PLN03142   349 FS-----SA----------------------------ETFDEWFQISGE-NDQQEVVQQLHKVLRPfLLRRLKSDVEKGL 394

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  625 PGLADFTVVLNLSPKQLNEVKKLRrEKRKFKVSAVGSAIYL------------HPKLkvFSDKSDDVSDTTMDEMVEkld 692
Cdd:PLN03142   395 PPKKETILKVGMSQMQKQYYKALL-QKDLDVVNAGGERKRLlniamqlrkccnHPYL--FQGAEPGPPYTTGEHLVE--- 468

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  693 lNEGvKAKFFLNLINLCDSAGEKLLVFSQYLIPLKFLERLAaLAKGWKLGKevfvLTGNTSSEQREWSMETFNSSPDAK- 771
Cdd:PLN03142   469 -NSG-KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL-MYRGYQYCR----IDGNTGGEDRDASIDAFNKPGSEKf 541

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063703870  772 IFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPGQKKMVHAYRLIAGSSPEEEDHNTCFKK 842
Cdd:PLN03142   542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
HELICc smart00490
helicase superfamily c-terminal domain;
740-815 5.38e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 5.38e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063703870  740 KLGKEVFVLTGNTSSEQREWSMETFNSSPdaKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPG 815
Cdd:smart00490   9 ELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
352-558 1.37e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 61.74  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  352 EMKPHQIEGFQFLCSNLvaddpGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLP-KGILPTWKKEFVRWqVEDI 430
Cdd:smart00487   8 PLRPYQKEAIEALLSGL-----RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKL-GPSL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  431 PLLDFYSAKAENRAQQLSILKqwMEKKSILFLGYQQFstivcddtTDSLSCQEILLKVPSILILDEGH--TPRNEDTNLL 508
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLE--SGKTDILVTTPGRL--------LDLLENDKLSLSNVDLVILDEAHrlLDGGFGDQLE 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063703870  509 QSLAQV-QTPRKVVLSGTLYQNHVKEVFNILNLVrpkfLKLDTSKSAVKRI 558
Cdd:smart00487 152 KLLKLLpKNVQLLLLSATPPEEIENLLELFLNDP----VFIDVGFTPLEPI 198
 
Name Accession Description Interval E-value
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 353-569 1.78e-89

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: 283.80  E-value: 1.78e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVA-----DDPGGCIMAHAPGSGKTFMIISFMQSFLAKYP-QAKPLVVLPKGILPTWKKEFVRWQ 426
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGtdvgsDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKKWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 427 VED-IPLLDFYSAKAENRAQQ-LSILKQWMEKKSILFLGYQQFSTIVCDDTTD----SLSCQEILLKVPSILILDEGHTP 500
Cdd:cd18007    81 PPDlRPLLVLVSLSASKRADArLRKINKWHKEGGVLLIGYELFRNLASNATTDprlkQEFIAALLDPGPDLLVLDEGHRL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063703870 501 RNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK--LDTSKSAVKRILAYTPCDVRGR 569
Cdd:cd18007   161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGtlKEFKKKFVKPIEAGQCVDSTEE 231
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 351-833 1.45e-54

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 201.61  E-value: 1.45e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGFQFLCSNlvADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWqvedI 430
Cdd:COG0553   240 ATLRPYQLEGAAWLLFL--RRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKF----A 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLsilKQWMEKKSILFLGYQQFStivcddttdslSCQEILLKVP-SILILDEGHTPRNEDTNLLQ 509
Cdd:COG0553   314 PGLRVLVLDGTRERAKG---ANPFEDADLVITSYGLLR-----------RDIELLAAVDwDLVILDEAQHIKNPATKRAK 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 510 SLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLkldtsksavkrilaytpcdvrgrltGSnsdmASMFNETVEHTL 589
Cdd:COG0553   380 AVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-------------------------GS----LKAFRERFARPI 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 590 QKSEDftvkiKVIQDLREMTKKVLH-YYKGDFLDELPGLADFTVVLNLSPKQ-----------LNEVKKLRREKRKFKVS 657
Cdd:COG0553   431 EKGDE-----EALERLRRLLRPFLLrRTKEDVLKDLPEKTEETLYVELTPEQralyeavleylRRELEGAEGIRRRGLIL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 658 AvgSAIYL-----HPKLKVFSDKSDDVSDTTMDEMVEKLDlnEGVkakfflnlinlcdSAGEKLLVFSQYLiplKFLERL 732
Cdd:COG0553   506 A--ALTRLrqicsHPALLLEEGAELSGRSAKLEALLELLE--ELL-------------AEGEKVLVFSQFT---DTLDLL 565

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 733 AALAKgwKLGKEVFVLTGNTSSEQREWSMETFNSSPDAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAF 812
Cdd:COG0553   566 EERLE--ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAH 643

                         490       500
                  ....*....|....*....|.
gi 1063703870 813 RPGQKKMVHAYRLIAGSSPEE 833
Cdd:COG0553   644 RIGQTRDVQVYKLVAEGTIEE 664
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 689-826 6.94e-39

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: 140.69  E-value: 6.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 689 EKLDLNEGVKAKFFLNLINLCDSAGEKLLVFSQYLIPLKFLERLAAlakgwKLGKEVFVLTGNTSSEQREWSMETFNSSP 768
Cdd:cd18793     3 PKIEEVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALR-----ERGIKYLRLDGSTSSKERQKLVDRFNEDP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063703870 769 DAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPGQKKMVHAYRLI 826
Cdd:cd18793    78 DIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 353-546 1.32e-29

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: 117.61  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLV-------ADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRW 425
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIeslerykGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 426 --QVEDIPLLDFYSAK-------AENRAQQLSILKQWMEKKSILFLGYQQFStivcddttdslscqeiLLKVPSILILDE 496
Cdd:cd18069    81 lpPPEALPNVRPRPFKvfilndeHKTTAARAKVIEDWVKDGGVLLMGYEMFR----------------LRPGPDVVICDE 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063703870 497 GHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18069   145 GHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFL 194
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 353-546 3.99e-29

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: 114.59  E-value: 3.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNlvADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqVEDIP 431
Cdd:cd17919     1 LRPYQLEGLNFLLEL--YENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPvLVVCPLSVLENWEREFEKW-TPDLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFYSAKAENRAQQlsilKQWMEKKS-ILFLGYQQFStivcddttdslSCQEILLKV-PSILILDEGHTPRNEDTNLLQ 509
Cdd:cd17919    78 VVVYHGSQRERAQIR----AKEKLDKFdVVLTTYETLR-----------RDKASLRKFrWDLVVVDEAHRLKNPKSQLSK 142

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063703870 510 SLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd17919   143 ALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 353-546 7.41e-28

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: 113.06  E-value: 7.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFL----CSNL--VADDPG-GCIMAHAPGSGKTFMIISFMQSFLAKYPQAK---PLVVLPKGILPTWKKEF 422
Cdd:cd18068     1 LKPHQVDGVQFMwdccCESLkkTKKSPGsGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsrVLVVCPLNTVLNWLNEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 423 VRWQV-----EDIPLLDFYSAK-AENRAQQLsilKQWMEKKSILFLGYQQFSTI-VCDDTTDSLSCQEILLKV-----PS 490
Cdd:cd18068    81 EKWQEglkdeEKIEVNELATYKrPQERSYKL---QRWQEEGGVMIIGYDMYRILaQERNVKSREKLKEIFNKAlvdpgPD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063703870 491 ILILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18068   158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLL 213
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 355-576 2.94e-25

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: 105.45  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 355 PHQIEGFQFL--CSNLVADDPG-GCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-----LVVLPKGILPTWKKEFVRW- 425
Cdd:cd18004     3 PHQREGVQFLydCLTGRRGYGGgGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkaLIVCPSSLVGNWKAEFDKWl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 426 QVEdipLLDFYSAKAENRAQQLSILKQWMEK-KSILFLGYQQFSTIVcddttDSLSCqeilLKVPSILILDEGHTPRNED 504
Cdd:cd18004    83 GLR---RIKVVTADGNAKDVKASLDFFSSAStYPVLIISYETLRRHA-----EKLSK----KISIDLLICDEGHRLKNSE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063703870 505 TNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLKldtSKSAVKRIlaYTPCDVRGRLTGSNSD 576
Cdd:cd18004   151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILG---SLASFRKV--FEEPILRSRDPDASEE 217
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 353-546 5.21e-25

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: 104.86  E-value: 5.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFL--C-SNLVADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-----LVVLPKGILPTWKKEFVR 424
Cdd:cd18067     1 LRPHQREGVKFLyrCvTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPeidkaIVVSPSSLVKNWANELGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 425 WQVEDI-PL-LDFYSAKAENRAqqlsiLKQWMEKKS------ILFLGYQQFSTIVcddttdslscqEILLKVP-SILILD 495
Cdd:cd18067    81 WLGGRLqPLaIDGGSKKEIDRK-----LVQWASQQGrrvstpVLIISYETFRLHV-----------EVLQKGEvGLVICD 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063703870 496 EGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18067   145 EGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGIL 195
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 356-543 4.04e-22

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: 97.37  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 356 HQIEGFQFL---CSNLVAddpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQA--KPLVVLPKGILPTWKKEFVRWQVEdi 430
Cdd:pfam00176   1 YQIEGVNWMlslENNLGR----GGILADEMGLGKTLQTISLLLYLKHVDKNWggPTLIVVPLSLLHNWMNEFERWVSP-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLSILKQWM-EKKSILFLGYqqfstivcddttdslscqEILLKVPSIL--------ILDEGHTPR 501
Cdd:pfam00176  75 PALRVVVLHGNKRPQERWKNDPNFlADFDVVITTY------------------ETLRKHKELLkkvhwhriVLDEGHRLK 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1063703870 502 NEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:pfam00176 137 NSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 355-553 1.22e-20

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: 91.66  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 355 PHQIEGFQFLCSnlVADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQVeDIPLLD 434
Cdd:cd18001     3 PHQREGVAWLWS--LHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTP-GLRVKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 435 FYSA-KAENRAQQLSILKqwmeKKSILFLGYQqfstiVCDDTTDSLSCQEILLKVPSILILDEGHTPRNEDTNLLQSLAQ 513
Cdd:cd18001    80 FHGTsKKERERNLERIQR----GGGVLLTTYG-----MVLSNTEQLSADDHDEFKWDYVILDEGHKIKNSKTKSAKSLRE 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1063703870 514 VQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLkLDTSKS 553
Cdd:cd18001   151 IPAKNRIILTGTPIQNNLKELWALFDFACNGSL-LGTRKT 189
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 353-544 5.04e-19

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: 86.92  E-value: 5.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVADDpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQveDIP 431
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRR--NCILADEMGLGKTIQSIAFLEHLYQVEGIRGPfLVIAPLSTIPNWQREFETWT--DMN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFY-SAKAENRAQQLSILKQWMEKKS--------ILFLGYQqfsTIVCDDttdslscqEILLKVP-SILILDEGHTPR 501
Cdd:cd17995    77 VVVYHgSGESRQIIQQYEMYFKDAQGRKkkgvykfdVLITTYE---MVIADA--------EELRKIPwRVVVVDEAHRLK 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1063703870 502 NEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPK 544
Cdd:cd17995   146 NRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPE 188
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 353-543 1.26e-17

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: 83.20  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLvaDDPGGCIMAHAPGSGKTFMIISFMQSFLAK-------------------YPQAKP--LVVLP 411
Cdd:cd18005     1 LRDYQREGVEFMYDLY--KNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppASSAKKpvLIVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 412 KGILPTWKKEFVRW-----------QVEDIPLLDFYSAKAEnraqqlsilkqwmekksILFLGYQQFSTIVcddttDSLS 480
Cdd:cd18005    79 LSVLYNWKDELDTWghfevgvyhgsRKDDELEGRLKAGRLE-----------------VVVTTYDTLRRCI-----DSLN 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063703870 481 CQEIllkvpSILILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18005   137 SINW-----SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVP 194
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 353-543 1.26e-16

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: 79.69  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVadDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQveDIPL 432
Cdd:cd18059     1 LREYQLEGVNWLLFNWY--NTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT--ELNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 433 LDFYSAKAENRAQQLSILkQWMEKKSILFLGYQQFSTIVCDDTTDSLSCQEiLLKVP-SILILDEGHTPRNEDTNLLQSL 511
Cdd:cd18059    77 VVYHGSQASRRTIQLYEM-YFKDPQGRVIKGSYKFHAIITTFEMILTDCPE-LRNIPwRCVVIDEAHRLKNRNCKLLEGL 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063703870 512 AQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18059   155 KMMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 698-815 4.41e-15

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: 71.86  E-value: 4.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 698 KAKFFLNLINLcdSAGEKLLVFSQY--LIPLKFLERlaalakgwKLGKEVFVLTGNTSSEQREWSMETFNSSpDAKIFFg 775
Cdd:pfam00271   2 KLEALLELLKK--ERGGKVLIFSQTkkTLEAELLLE--------KEGIKVARLHGDLSQEEREEILEDFRKG-KIDVLV- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063703870 776 SIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPG 815
Cdd:pfam00271  70 ATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 353-543 5.99e-15

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: 75.09  E-value: 5.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVadDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQveDIPL 432
Cdd:cd18060     1 LREYQLEGVNWLLFNWY--NRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT--EMNT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 433 LDFYSAKAENRA-QQLSILKQwmEKKSILFLGYQQFSTIVCDDTTDSLSCQEILLKVPSILILDEGHTPRNEDTNLLQSL 511
Cdd:cd18060    77 IVYHGSLASRQMiQQYEMYCK--DSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSL 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063703870 512 AQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18060   155 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 326-842 7.02e-15

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 79.46  E-value: 7.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  326 ESDNE-LKFSEEGLMIGG---LAAHPTH-AAEMKPHQIEGFQFLCsNLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAK 400
Cdd:PLN03142   138 EEDEEyLKEEEDGLGGSGgtrLLVQPSCiKGKMRDYQLAGLNWLI-RLYENGING-ILADEMGLGKTLQTISLL-GYLHE 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  401 Y-----PQakpLVVLPKGILPTWKKEFVRWqvedIPLLDF--YSAKAENRAQQlsilkqwmeKKSILFLGyqQFSTIVcd 473
Cdd:PLN03142   215 YrgitgPH---MVVAPKSTLGNWMNEIRRF----CPVLRAvkFHGNPEERAHQ---------REELLVAG--KFDVCV-- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  474 dttdslSCQEILLKVPSIL--------ILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKF 545
Cdd:PLN03142   275 ------TSFEMAIKEKTALkrfswryiIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEI 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  546 LKldtskSAvkrilaytpcdvrgrltgsnsdmasmfnETVEHTLQKSEDfTVKIKVIQDLREMTKK-VLHYYKGDFLDEL 624
Cdd:PLN03142   349 FS-----SA----------------------------ETFDEWFQISGE-NDQQEVVQQLHKVLRPfLLRRLKSDVEKGL 394

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  625 PGLADFTVVLNLSPKQLNEVKKLRrEKRKFKVSAVGSAIYL------------HPKLkvFSDKSDDVSDTTMDEMVEkld 692
Cdd:PLN03142   395 PPKKETILKVGMSQMQKQYYKALL-QKDLDVVNAGGERKRLlniamqlrkccnHPYL--FQGAEPGPPYTTGEHLVE--- 468

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  693 lNEGvKAKFFLNLINLCDSAGEKLLVFSQYLIPLKFLERLAaLAKGWKLGKevfvLTGNTSSEQREWSMETFNSSPDAK- 771
Cdd:PLN03142   469 -NSG-KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL-MYRGYQYCR----IDGNTGGEDRDASIDAFNKPGSEKf 541

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063703870  772 IFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPGQKKMVHAYRLIAGSSPEEEDHNTCFKK 842
Cdd:PLN03142   542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 353-543 1.72e-14

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: 73.96  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqVEDIP 431
Cdd:cd18009     4 MRPYQLEGMEWLRM-LWENGING-ILADEMGLGKTIQTIALL-AHLRERGVWGPfLVIAPLSTLPNWVNEFARF-TPSVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFYSAKAENR--AQQLSILKQWMEKKSILFLGYQqfstIVCDDTtDSLSCQEIllkvpSILILDEGHTPRNEDTNLLQ 509
Cdd:cd18009    80 VLLYHGTKEERErlRKKIMKREGTLQDFPVVVTSYE----IAMRDR-KALQHYAW-----KYLIVDEGHRLKNLNCRLIQ 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063703870 510 SLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18009   150 ELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLP 183
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 353-546 4.11e-14

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: 72.96  E-value: 4.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVA---DDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQ-AKP-----LVVLPKGILPTWKKEFV 423
Cdd:cd18066     1 LRPHQREGIEFLYECVMGmrvNERFGAILADEMGLGKTLQCISLIWTLLRQGPYgGKPvikraLIVTPGSLVKNWKKEFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 424 RW-QVEDIPLldfYSAKAENRAQQL--SILkqwmekKSILFLGYQQFstIVCDDTTDSLSCqeillkvpSILILDEGHTP 500
Cdd:cd18066    81 KWlGSERIKV---FTVDQDHKVEEFiaSPL------YSVLIISYEML--LRSLDQISKLNF--------DLVICDEGHRL 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063703870 501 RNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18066   142 KNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIL 187
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 355-546 4.79e-14

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: 71.59  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 355 PHQIEGFQFLcSNLVADDPGGcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqvedIPLL 433
Cdd:cd18000     3 KYQQTGVQWL-WELHCQRVGG-ILGDEMGLGKTIQIIAFLAALHHSKLGLGPsLIVCPATVLKQWVKEFHRW----WPPF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 434 D---FYSAKAENRAQqlsilkqwmEKKSILFLGYQQFSTIVCDD----TTDSL--SCQEILLKVP-SILILDEGHTPRNE 503
Cdd:cd18000    77 RvvvLHSSGSGTGSE---------EKLGSIERKSQLIRKVVGDGgiliTTYEGfrKHKDLLLNHNwQYVILDEGHKIRNP 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1063703870 504 DTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18000   148 DAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 353-557 6.76e-14

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: 71.70  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVADDpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVL-PKGILPTWKKEFVRWqvedip 431
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQH--GCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLcPLSVLDNWKEELNRF------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 lldfysakaenrAQQLSILKQWMEKKSILFLGYQQFSTivcDDTTDSLSCQEILLKVPS--------ILILDEGHTPRNE 503
Cdd:cd18006    73 ------------APDLSVITYMGDKEKRLDLQQDIKST---NRFHVLLTTYEICLKDASflksfpwaSLVVDEAHRLKNQ 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063703870 504 DTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLKLDTSKSAVKR 557
Cdd:cd18006   138 NSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKA 191
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 353-543 6.76e-14

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: 72.00  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVadDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQVEDIPL 432
Cdd:cd18058     1 LREYQLEGMNWLLFNWY--NRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 433 ldfYSAKAENRAQQLSILKQWMEKKSILFLGYQQFSTIVCDDTTDSLSCQEILLKVPSILILDEGHTPRNEDTNLLQSLA 512
Cdd:cd18058    79 ---YHGSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLK 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063703870 513 QVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18058   156 LMALEHKVLLTGTPLQNSVEELFSLLNFLEP 186
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 352-545 9.59e-14

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: 71.23  E-value: 9.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 352 EMKPHQIEGFQFLCSNLVADDPGgcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqvedI 430
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNG--ILADEMGLGKTVQTISFLSYLFHSQQQYGPfLVVVPLSTMPAWQREFAKW----A 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDF--YSAKAENRAqqlsILKQ--WM--EKKSIlflgyqQFSTIVcddTTdslscQEILLK----VPSI----LILDE 496
Cdd:cd17993    75 PDMNVivYLGDIKSRD----TIREyeFYfsQTKKL------KFNVLL---TT-----YEIILKdkafLGSIkwqyLAVDE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063703870 497 GHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP-KF 545
Cdd:cd17993   137 AHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPgKF 186
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 353-544 2.90e-13

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: 68.95  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLcsNLVADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWqVEDIPL 432
Cdd:cd17998     1 LKDYQLIGLNWL--NLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRW-CPSLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 433 LDFYSAKAENRAQQLSILKQwMEKKSILFLGYQqfstIVCDDTTDslscqEILLKVPSI--LILDEGHTPRNEDTNLLQS 510
Cdd:cd17998    78 EPYYGSQEERKHLRYDILKG-LEDFDVIVTTYN----LATSNPDD-----RSFFKRLKLnyVVYDEGHMLKNMTSERYRH 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063703870 511 LAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPK 544
Cdd:cd17998   148 LMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181
HELICc smart00490
helicase superfamily c-terminal domain;
740-815 5.38e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 5.38e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063703870  740 KLGKEVFVLTGNTSSEQREWSMETFNSSPdaKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPG 815
Cdd:smart00490   9 ELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 353-547 7.97e-13

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: 68.93  E-value: 7.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqVEDIP 431
Cdd:cd17996     4 LKEYQLKGLQWMVS-LYNNNLNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPyLVIVPLSTLSNWVSEFEKW-APSVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFYSAKAENRAQQLSILkqwmekksilflgYQQFSTIVcddTTdslscQEILLKVPSIL--------ILDEGHTPRNE 503
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIR-------------AGKFNVLL---TT-----YEYIIKDKPLLskikwkymIIDEGHRMKNA 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063703870 504 DTNLLQSLAQ-VQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK 547
Cdd:cd17996   140 QSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFK 184
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 352-544 9.59e-13

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: 68.88  E-value: 9.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 352 EMKPHQIEGFQFLCSNLVADDpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQVEDI 430
Cdd:cd18054    20 ELRDYQLEGLNWLAHSWCKNN--SVILADEMGLGKTIQTISFLSYLFHQHQLYGPfLLVVPLSTLTSWQREFEIWAPEIN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLsilkQWMEKKSILFlgyqQFSTIvcddttdsLSCQEILLKVPSILI--------LDEGHTPRN 502
Cdd:cd18054    98 VVVYIGDLMSRNTIREY----EWIHSQTKRL----KFNAL--------ITTYEILLKDKTVLGsinwaflgVDEAHRLKN 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1063703870 503 EDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPK 544
Cdd:cd18054   162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE 203
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 352-544 3.56e-12

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: 67.00  E-value: 3.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 352 EMKPHQIEGFQFLCSNLVADDpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQvedi 430
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGN--SCILADEMGLGKTIQTISFLNYLFHEHQLYGPfLLVVPLSTLTSWQREIQTWA---- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLSILKQWMEKKSILFlgyqQFSTIvcddttdsLSCQEILLKVPSILI--------LDEGHTPRN 502
Cdd:cd18053    94 PQMNAVVYLGDINSRNMIRTHEWMHPQTKRL----KFNIL--------LTTYEILLKDKSFLGglnwafigVDEAHRLKN 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1063703870 503 EDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPK 544
Cdd:cd18053   162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE 203
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 353-543 4.07e-12

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: 66.57  E-value: 4.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSNLVadDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQveDIPL 432
Cdd:cd18061     1 LREYQLEGLNWLLFNWY--NRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT--DLNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 433 LDFY-SAKAENRAQQLSILkqWMEKKSILFLGYQQFSTIVCDDTTDSLSCQEILLKVPSILILDEGHTPRNEDTNLLQSL 511
Cdd:cd18061    77 VVYHgSLISRQMIQQYEMY--FRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGL 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063703870 512 AQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18061   155 KLMNLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 351-546 4.37e-12

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: 66.44  E-value: 4.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGF---QFLCSN----LVADDpggciMahapGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFV 423
Cdd:cd18012     3 ATLRPYQKEGFnwlSFLRHYglggILADD-----M----GLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 424 RWQvEDIPLLDFYSAKAENRAQQLsilkqwMEKKSILFLGYQqfsTIVCDdttdslscQEILLKVP-SILILDEGHTPRN 502
Cdd:cd18012    74 KFA-PELKVLVIHGTKRKREKLRA------LEDYDLVITSYG---LLRRD--------IELLKEVKfHYLVLDEAQNIKN 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1063703870 503 EDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18012   136 PQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLL 179
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 352-545 2.45e-11

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: 64.27  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 352 EMKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAKYPQ-AKP-LVVLPKGILPTWKKEFVRWqVED 429
Cdd:cd17997     3 TMRDYQIRGLNWLIS-LFENGING-ILADEMGLGKTLQTISLL-GYLKHYKNiNGPhLIIVPKSTLDNWMREFKRW-CPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 430 IPLLDFYSAKAEnRAQqlsILKQWMEkksilflgYQQFStiVCddttdsLSCQEILLKVPSIL--------ILDEGHTPR 501
Cdd:cd17997    79 LRVVVLIGDKEE-RAD---IIRDVLL--------PGKFD--VC------ITSYEMVIKEKTVLkkfnwryiIIDEAHRIK 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1063703870 502 NEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKF 545
Cdd:cd17997   139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDV 182
DEXDc smart00487
DEAD-like helicases superfamily;
352-558 1.37e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 61.74  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  352 EMKPHQIEGFQFLCSNLvaddpGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLP-KGILPTWKKEFVRWqVEDI 430
Cdd:smart00487   8 PLRPYQKEAIEALLSGL-----RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKL-GPSL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870  431 PLLDFYSAKAENRAQQLSILKqwMEKKSILFLGYQQFstivcddtTDSLSCQEILLKVPSILILDEGH--TPRNEDTNLL 508
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLE--SGKTDILVTTPGRL--------LDLLENDKLSLSNVDLVILDEAHrlLDGGFGDQLE 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063703870  509 QSLAQV-QTPRKVVLSGTLYQNHVKEVFNILNLVrpkfLKLDTSKSAVKRI 558
Cdd:smart00487 152 KLLKLLpKNVQLLLLSATPPEEIENLLELFLNDP----VFIDVGFTPLEPI 198
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 351-547 8.82e-10

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: 60.44  E-value: 8.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQVED 429
Cdd:cd18062    22 GVLKQYQIKGLEWLVS-LYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPfLIIVPLSTLSNWVYEFDKWAPSV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 430 IPLldFYSAKAENRAQQLSILKQwmEKKSILFLGYQQfstIVCDdttdslscQEILLKVP-SILILDEGHTPRNEDTNLL 508
Cdd:cd18062   100 VKV--SYKGSPAARRAFVPQLRS--GKFNVLLTTYEY---IIKD--------KQILAKIRwKYMIVDEGHRMKNHHCKLT 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1063703870 509 QSL-AQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK 547
Cdd:cd18062   165 QVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFK 204
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 353-547 1.08e-09

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: 60.08  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQvediP 431
Cdd:cd18063    24 LKHYQLQGLEWMVS-LYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNGPyLIIVPLSTLSNWTYEFDKWA----P 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFYSAKAeNRAQQLSILKQWMEKKSILFLGYQQFstIVCDdttdslscQEILLKVP-SILILDEGHTPRNEDTNLLQS 510
Cdd:cd18063    98 SVVKISYKG-TPAMRRSLVPQLRSGKFNVLLTTYEY--IIKD--------KHILAKIRwKYMIVDEGHRMKNHHCKLTQV 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063703870 511 L-AQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLK 547
Cdd:cd18063   167 LnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFK 204
ResIII pfam04851
Type III restriction enzyme, res subunit;
352-498 5.61e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 56.14  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 352 EMKPHQIEGFQFLCSNLVADDPGGCImAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLP-KGILPTWKKEFVRWQVEDI 430
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNGQKRGLI-VMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063703870 431 PLLDFYSAKAENRaqqlsilkqWMEKKSILFLGYQQFSTIVCDDTTDSLSCQEILlkvpsiLILDEGH 498
Cdd:pfam04851  82 EIGEIISGDKKDE---------SVDDNKIVVTTIQSLYKALELASLELLPDFFDV------IIIDEAH 134
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 377-543 7.08e-09

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: 56.98  E-value: 7.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 377 IMAHAPGSGKTFMIISFMqSFLAKYPQ--AKPLVVLPKGILPTWKKEFVRWqvedIP---LLDFYSAKAENRAQQlsilK 451
Cdd:cd18003    23 ILADEMGLGKTIQTIALL-AHLACEKGnwGPHLIVVPTSVMLNWEMEFKRW----CPgfkILTYYGSAKERKLKR----Q 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 452 QWMEKKS--ILFLGYQQFstivcddTTDSLSCQEillKVPSILILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQN 529
Cdd:cd18003    94 GWMKPNSfhVCITSYQLV-------VQDHQVFKR---KKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQN 163

                         170
                  ....*....|....
gi 1063703870 530 HVKEVFNILNLVRP 543
Cdd:cd18003   164 SLMELWSLMHFLMP 177
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 351-543 9.01e-09

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: 56.98  E-value: 9.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 351 AEMKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAKYPQ--AKPLVVLPKGILPTWKKEFVRWqve 428
Cdd:cd18064    14 GKLRDYQVRGLNWLIS-LYENGING-ILADEMGLGKTLQTISLL-GYMKHYRNipGPHMVLVPKSTLHNWMAEFKRW--- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 429 dIPLLDFYS--AKAENRAQQLsilkqwmekKSILFLGYQQfstiVCddttdsLSCQEILLKVPSI--------LILDEGH 498
Cdd:cd18064    88 -VPTLRAVCliGDKDQRAAFV---------RDVLLPGEWD----VC------VTSYEMLIKEKSVfkkfnwryLVIDEAH 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063703870 499 TPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18064   148 RIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLP 192
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 375-548 1.79e-08

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: 56.32  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 375 GCIMAHAPGSGKTFMIISFMQSflakypqAKPLVVLPKGILPTWKKEFVRWQVEDIplLDFYSAKAENRAQQLSILKqwm 454
Cdd:cd18071    50 GGILADDMGLGKTLTTISLILA-------NFTLIVCPLSVLSNWETQFEEHVKPGQ--LKVYTYHGGERNRDPKLLS--- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 455 eKKSILFLGYQqfsTIVCDDTT-DSLSCQEI-LLKVpsilILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVK 532
Cdd:cd18071   118 -KYDIVLTTYN---TLASDFGAkGDSPLHTInWLRV----VLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189

                         170
                  ....*....|....*.
gi 1063703870 533 EVFNILNlvrpkFLKL 548
Cdd:cd18071   190 DLGSLLS-----FLHL 200
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 355-549 6.53e-08

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: 54.60  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 355 PHQIEGFQFLCsnlvaddPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP------------------LVVLPKGILP 416
Cdd:cd18008     3 PYQKQGLAWML-------PRGGILADEMGLGKTIQALALILATRPQDPKIPEeleenssdpkklylskttLIVVPLSLLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 417 TWKKEFVR-WQVEDIPLLDFYSAKAenraqqlSILKQWMEKKSILFLGYQ----QFSTIVCDDTTDSLSCQEILLKvpSI 491
Cdd:cd18008    76 QWKDEIEKhTKPGSLKVYVYHGSKR-------IKSIEELSDYDIVITTYGtlasEFPKNKKGGGRDSKEKEASPLH--RI 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063703870 492 ----LILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILnlvrpKFLKLD 549
Cdd:cd18008   147 rwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLL-----RFLRVE 203
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 353-546 9.86e-08

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: 53.36  E-value: 9.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSN----LVADDPGgcimahapgSGKTFMIISFMqsflAKYPQAKP-LVVLPKGILPTWKKEFVRWqv 427
Cdd:cd18010     1 LLPFQREGVCFALRRggrvLIADEMG---------LGKTVQAIAIA----AYYREEWPlLIVCPSSLRLTWADEIERW-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 428 ediplLDFYSAKAENraqqlSILKQWMEKKSIlflgyqqfSTIVCDDTTDSLSC-QEILLKVP-SILILDEGHTPRNED- 504
Cdd:cd18010    66 -----LPSLPPDDIQ-----VIVKSKDGLRDG--------DAKVVIVSYDLLRRlEKQLLARKfKVVICDESHYLKNSKa 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1063703870 505 --TNLLQSLAQvQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd18010   128 krTKAALPLLK-RAKRVILLSGTPALSRPIELFTQLDALDPKLF 170
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 353-544 2.26e-07

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: 52.76  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLcsNLVADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQVedip 431
Cdd:cd18057     1 LHPYQLEGLNWL--RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPyLVSAPLSTIINWEREFEMWAP---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 llDFYSAKAENRAQQLSILKQ----------WMEKKSILFLGYQQFSTIVCDDTTDSLSCQEILLKVP--SILILDEGHT 499
Cdd:cd18057    75 --DFYVVTYTGDKESRSVIREnefsfednaiRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIewACLVVDEAHR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063703870 500 PRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPK 544
Cdd:cd18057   153 LKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPE 197
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 353-543 3.18e-07

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: 52.33  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLCSnLVADDPGGcIMAHAPGSGKTFMIISFMqSFLAKYPQ--AKPLVVLPKGILPTWKKEFVRWqvedI 430
Cdd:cd18065    16 LRDYQVRGLNWMIS-LYENGVNG-ILADEMGLGKTLQTIALL-GYLKHYRNipGPHMVLVPKSTLHNWMNEFKRW----V 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 431 PLLDFYSAKAENRAQQLSILKQWMEKKsilflgyqqfsTIVCddttdsLSCQEILLKVPSI--------LILDEGHTPRN 502
Cdd:cd18065    89 PSLRAVCLIGDKDARAAFIRDVMMPGE-----------WDVC------VTSYEMVIKEKSVfkkfnwryLVIDEAHRIKN 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063703870 503 EDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18065   152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLP 192
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 355-543 5.27e-07

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: 50.90  E-value: 5.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 355 PHQIEGFQFLCSNLVADDpgGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWQvediPll 433
Cdd:cd17994     3 PYQLEGLNWLRFSWAQGT--DTILADEMGLGKTIQTIVFLYSLYKEGHSKGPfLVSAPLSTIINWEREFEMWA----P-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 434 DFYSAKAENraqqlsilkqwmekKSILFLGYQQFSTivcddttDSLSCQEILLKVpsiLILDEGHTPRNEDTNLLQSLAQ 513
Cdd:cd17994    75 DFYVVTYVG--------------DHVLLTSYELISI-------DQAILGSIDWAV---LVVDEAHRLKNNQSKFFRILNS 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1063703870 514 VQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd17994   131 YKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 353-543 6.50e-07

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: 51.35  E-value: 6.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 353 MKPHQIEGFQFLcSNLVADDPGGcIMAHAPGSGKTFMIISFMQSFLAKYPQAKP-LVVLPKGILPTWKKEFVRWqVEDIP 431
Cdd:cd18002     1 LKEYQLKGLNWL-ANLYEQGING-ILADEMGLGKTVQSIAVLAHLAEEHNIWGPfLVIAPASTLHNWQQEISRF-VPQFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 432 LLDFYSAkaenrAQQLSILKQWMEKKS---------ILFLGYQQFstivcddTTDSLSCQEILLKVpsiLILDEGHTPRN 502
Cdd:cd18002    78 VLPYWGN-----PKDRKVLRKFWDRKNlytrdapfhVVITSYQLV-------VQDEKYFQRVKWQY---MVLDEAQAIKS 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063703870 503 EDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRP 543
Cdd:cd18002   143 SSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMP 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
713-891 4.21e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 47.33  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 713 GEKLLVFSQYLiplKFLERLAALAKgwKLGKEVFVLTGNTSSEQREWSMETFNSSPDAKIFfgSIKACGEGISLVGASRI 792
Cdd:COG1061   305 DRKTLVFCSSV---DHAEALAELLN--EAGIRAAVVTGDTPKKEREEILEAFRDGELRILV--TVDVLNEGVDVPRLDVA 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 793 LILDVPLNPSVTRQAIGRAFRPGQKK------------------MVHAYRLIAGSSPEEEDHNTCFKKEVISKMWFEWNE 854
Cdd:COG1061   378 ILLRPTGSPREFIQRLGRGLRPAPGKedalvydfvgndvpvleeLAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEV 457

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063703870 855 YCGYQNFEVETIDVDEAGDTFLESPALREDIRVLYKR 891
Cdd:COG1061   458 KGELEEELLEELELLEDALLLVLAELLLLELLALALE 494
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 492-546 4.61e-05

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: 45.80  E-value: 4.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063703870 492 LILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFL 546
Cdd:cd17999   130 CVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYL 184
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 373-555 8.32e-04

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: 42.08  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 373 PGGCIMAHAPGSGKTF-MIISFMQSFLAK----------------------YPQAKPLVVLPKGILPTWKKEfVRWQVED 429
Cdd:cd18072    20 PRGGILADDMGLGKTLtMIALILAQKNTQnrkeeekekalteweskkdstlVPSAGTLVVCPASLVHQWKNE-VESRVAS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063703870 430 iPLLDFYSAKAENRAQQLSILKQWmekkSILFLGYqqfSTIVCDDTTDSLSCQ-EILLKVP-SILILDEGHTPRNEDTNL 507
Cdd:cd18072    99 -NKLRVCLYHGPNRERIGEVLRDY----DIVITTY---SLVAKEIPTYKEESRsSPLFRIAwARIILDEAHNIKNPKVQA 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1063703870 508 LQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVR-PKFLKLDTSKSAV 555
Cdd:cd18072   171 SIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRcSPFDDLKVWKKQV 219
 
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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