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Conserved domains on  [gi|66811190|ref|XP_639303|]
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SNF2-related domain-containing protein [Dictyostelium discoideum AX4]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12784896)

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

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0004386|GO:0016887|GO:0005524|GO:0003676
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 283-521 1.45e-128

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: 387.03  E-value: 1.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFRGGFkGNGCILADDMGLGKSIQAITILWTLLKQGPKGESTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18004   1 LRPHQREGVQFLYDCLTGRRGYG-GGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDG-VNTVAIGESTKTGRAKLTELEFGKA-DVLIISYDQLRIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSM 440
Cdd:cd18004  80 KWLGLRrIKVVTADGNAKDVKASLDFFSSASTyPVLIISYETLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 441 IPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTSQFILR 520
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239


                .
gi 66811190 521 R 521
Cdd:cd18004 240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 279-767 4.19e-119

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 378.41  E-value: 4.19e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 279 LSQKLRPHQREGVQFM-FDCLLGFRGgfkgngcILADDMGLGKSIQAITILWTLLKQGPkgestAKKAVIVAPCTLVGNW 357
Cdd:COG0553 238 LKATLRPYQLEGAAWLlFLRRLGLGG-------LLADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNW 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKWlGDGVNTVAIGESTKtgRAKLTElEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKA 437
Cdd:COG0553 306 QRELAKF-APGLRVLVLDGTRE--RAKGAN-PFEDADLVITSYGLLRRDIELLAAV-DWDLVILDEAQHIKNPATKRAKA 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 438 VSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVaSRNPDASDEekeigrqrsleLSRLTSQF 517
Cdd:COG0553 381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE-KGDEEALER-----------LRRLLRPF 448

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 518 ILRRT-AFVNTQyLPPKVEYVIFCKLTPLQLSIYKHLIKEA-----KDSAFASTTGALPLITTLKKLSNCAELVYTPDKE 591
Cdd:COG0553 449 LLRRTkEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYLrreleGAEGIRRRGLILAALTRLRQICSHPALLLEEGAE 527

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 592 TDVGtsilklfpkewnpkvfqpqySSKLLFVDRLLANIRnsKSGDKTVIISNYTQTLEVLATMCKTRGYAYFQLDGSTAN 671
Cdd:COG0553 528 LSGR--------------------SAKLEALLELLEELL--AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 672 AKRQQLVNLYNDPARPEfVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARVWREGQKKIVSIYRTFTTGTIEE 751
Cdd:COG0553 586 EERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664

                       490
                ....*....|....*.
gi 66811190 752 KIFQRQLTKQALSTSI 767
Cdd:COG0553 665 KILELLEEKRALAESV 680
 
Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 283-521 1.45e-128

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: 387.03  E-value: 1.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFRGGFkGNGCILADDMGLGKSIQAITILWTLLKQGPKGESTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18004   1 LRPHQREGVQFLYDCLTGRRGYG-GGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDG-VNTVAIGESTKTGRAKLTELEFGKA-DVLIISYDQLRIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSM 440
Cdd:cd18004  80 KWLGLRrIKVVTADGNAKDVKASLDFFSSASTyPVLIISYETLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 441 IPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTSQFILR 520
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239


                .
gi 66811190 521 R 521
Cdd:cd18004 240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 279-767 4.19e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 378.41  E-value: 4.19e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 279 LSQKLRPHQREGVQFM-FDCLLGFRGgfkgngcILADDMGLGKSIQAITILWTLLKQGPkgestAKKAVIVAPCTLVGNW 357
Cdd:COG0553 238 LKATLRPYQLEGAAWLlFLRRLGLGG-------LLADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNW 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKWlGDGVNTVAIGESTKtgRAKLTElEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKA 437
Cdd:COG0553 306 QRELAKF-APGLRVLVLDGTRE--RAKGAN-PFEDADLVITSYGLLRRDIELLAAV-DWDLVILDEAQHIKNPATKRAKA 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 438 VSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVaSRNPDASDEekeigrqrsleLSRLTSQF 517
Cdd:COG0553 381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE-KGDEEALER-----------LRRLLRPF 448

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 518 ILRRT-AFVNTQyLPPKVEYVIFCKLTPLQLSIYKHLIKEA-----KDSAFASTTGALPLITTLKKLSNCAELVYTPDKE 591
Cdd:COG0553 449 LLRRTkEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYLrreleGAEGIRRRGLILAALTRLRQICSHPALLLEEGAE 527

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 592 TDVGtsilklfpkewnpkvfqpqySSKLLFVDRLLANIRnsKSGDKTVIISNYTQTLEVLATMCKTRGYAYFQLDGSTAN 671
Cdd:COG0553 528 LSGR--------------------SAKLEALLELLEELL--AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 672 AKRQQLVNLYNDPARPEfVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARVWREGQKKIVSIYRTFTTGTIEE 751
Cdd:COG0553 586 EERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664

                       490
                ....*....|....*.
gi 66811190 752 KIFQRQLTKQALSTSI 767
Cdd:COG0553 665 KILELLEEKRALAESV 680
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 286-580 1.92e-69

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: 232.57  E-value: 1.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   286 HQREGVQFMFDCLLGfrggfKGNGCILADDMGLGKSIQAITILWTLLKQGPKgesTAKKAVIVAPCTLVGNWGQELKKWL 365
Cdd:pfam00176   1 YQIEGVNWMLSLENN-----LGRGGILADEMGLGKTLQTISLLLYLKHVDKN---WGGPTLIVVPLSLLHNWMNEFERWV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   366 GDGVNTVAIGESTKTGRAKLTELE--FGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKAVSMIPT 443
Cdd:pfam00176  73 SPPALRVVVLHGNKRPQERWKNDPnfLADFDVVITTYETLRKHKELLKKV-HWHRIVLDEGHRLKNSKSKLSKALKSLKT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   444 ARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIvasRNPDASDeekeiGRQRsleLSRLTSQFILRRTA 523
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKK-----GVSR---LHKLLKPFLLRRTK 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66811190   524 FVNTQYLPPKVEYVIFCKLTPLQLSIYKHLIKEAKDSAFASTTGA-------LPLITTLKKLSN 580
Cdd:pfam00176 221 KDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGreikaslLNILMRLRKICN 284
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 274-763 2.29e-56

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 211.20  E-value: 2.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   274 VVDP-ILSQKLRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLK----QGPKgestakkaVIV 348
Cdd:PLN03142  160 LVQPsCIKGKMRDYQLAGLNWLIRL---YENGING---ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVV 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   349 APCTLVGNWGQELKKWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYdQLRIYCEDICKITSIGLVICDEGHRLK 428
Cdd:PLN03142  226 APKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSF-EMAIKEKTALKRFSWRYIIIDEAHRIK 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   429 NAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDApivasrnpDASDEEKEIGRQrsl 508
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI--------SGENDQQEVVQQ--- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   509 eLSRLTSQFILRRTAFVNTQYLPPKVEYVIFCKLTPLQLSIYKHLIKEAKDsafASTTGA-----LPLITTLKKLSNcae 583
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLD---VVNAGGerkrlLNIAMQLRKCCN--- 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   584 lvytpdketdvgtsilklfpkewNPKVFQ-----PQY---------SSKLLFVDRLLANIRNSKSgdKTVIISNYTQTLE 649
Cdd:PLN03142  447 -----------------------HPYLFQgaepgPPYttgehlvenSGKMVLLDKLLPKLKERDS--RVLIFSQMTRLLD 501

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   650 VLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDPARPEFVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARV 729
Cdd:PLN03142  502 ILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRA 581

                         490       500       510
                  ....*....|....*....|....*....|....
gi 66811190   730 WREGQKKIVSIYRTFTTGTIEEKIFQRQLTKQAL 763
Cdd:PLN03142  582 HRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 615-742 8.28e-48

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 166.50  E-value: 8.28e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 615 YSSKLLFVDRLLANIRnsKSGDKTVIISNYTQTLEVLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDPARPeFVFLLS 694
Cdd:cd18793   9 VSGKLEALLELLEELR--EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLS 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66811190 695 SKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARVWREGQKKIVSIYR 742
Cdd:cd18793  86 TKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYR 133
DEXDc smart00487
DEAD-like helicases superfamily;
282-475 1.29e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.04  E-value: 1.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    282 KLRPHQREGVQFMFDCLlgfrggfkgNGCILADDMGLGKSIQAITILWTLLKQGPKgestaKKAVIVAPC-TLVGNWGQE 360
Cdd:smart00487   8 PLRPYQKEAIEALLSGL---------RDVILAAPTGSGKTLAALLPALEALKRGKG-----GRVLVLVPTrELAEQWAEE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    361 LKKWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLRIYCE-DICKITSIGLVICDEGHRLKNA--EIKTTKA 437
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGgfGDQLEKL 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 66811190    438 VSMIPTARRVI-LSGTP---IQNDLTEFYAMVNFVNPGVLKN 475
Cdd:smart00487 154 LKLLPKNVQLLlLSATPpeeIENLLELFLNDPVFIDVGFTPL 195
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 624-733 8.32e-19

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 82.64  E-value: 8.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   624 RLLANIRNSKSGDKTVIISNYTQTLEvLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDParpEFVFLLSSKAGGVGLN 703
Cdd:pfam00271   4 EALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 66811190   704 LIGGNHLVLFDADWNPANDAQSMARVWREG 733
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
649-733 9.65e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 9.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    649 EVLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNdpaRPEFVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMAR 728
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 66811190    729 VWREG 733
Cdd:smart00490  78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
282-457 1.00e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.88  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVqfmfDCLLGFRGGFKGNGCILADdMGLGKSIQAITILWTLLkqgpkgesTAKKAVIVAP-CTLVGNWGQE 360
Cdd:COG1061  80 ELRPYQQEAL----EALLAALERGGGRGLVVAP-TGTGKTVLALALAAELL--------RGKRVLVLVPrRELLEQWAEE 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 361 LKKWLGDGVNTVAIGESTktgrakltelefgkADVLIISYDQL--RIYCEDICKitSIGLVICDEGHRLkNAEiKTTKAV 438
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSD--------------APITVATYQSLarRAHLDELGD--RFGLVIIDEAHHA-GAP-SYRRIL 208

                       170
                ....*....|....*....
gi 66811190 439 SMIPTARRVILSGTPIQND 457
Cdd:COG1061 209 EAFPAAYRLGLTATPFRSD 227
 
Name Accession Description Interval E-value
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 283-521 1.45e-128

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: 387.03  E-value: 1.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFRGGFkGNGCILADDMGLGKSIQAITILWTLLKQGPKGESTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18004   1 LRPHQREGVQFLYDCLTGRRGYG-GGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDG-VNTVAIGESTKTGRAKLTELEFGKA-DVLIISYDQLRIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSM 440
Cdd:cd18004  80 KWLGLRrIKVVTADGNAKDVKASLDFFSSASTyPVLIISYETLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 441 IPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTSQFILR 520
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239


                .
gi 66811190 521 R 521
Cdd:cd18004 240 R 240
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 279-767 4.19e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 378.41  E-value: 4.19e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 279 LSQKLRPHQREGVQFM-FDCLLGFRGgfkgngcILADDMGLGKSIQAITILWTLLKQGPkgestAKKAVIVAPCTLVGNW 357
Cdd:COG0553 238 LKATLRPYQLEGAAWLlFLRRLGLGG-------LLADDMGLGKTIQALALLLELKERGL-----ARPVLIVAPTSLVGNW 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKWlGDGVNTVAIGESTKtgRAKLTElEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKA 437
Cdd:COG0553 306 QRELAKF-APGLRVLVLDGTRE--RAKGAN-PFEDADLVITSYGLLRRDIELLAAV-DWDLVILDEAQHIKNPATKRAKA 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 438 VSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVaSRNPDASDEekeigrqrsleLSRLTSQF 517
Cdd:COG0553 381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE-KGDEEALER-----------LRRLLRPF 448

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 518 ILRRT-AFVNTQyLPPKVEYVIFCKLTPLQLSIYKHLIKEA-----KDSAFASTTGALPLITTLKKLSNCAELVYTPDKE 591
Cdd:COG0553 449 LLRRTkEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYLrreleGAEGIRRRGLILAALTRLRQICSHPALLLEEGAE 527

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 592 TDVGtsilklfpkewnpkvfqpqySSKLLFVDRLLANIRnsKSGDKTVIISNYTQTLEVLATMCKTRGYAYFQLDGSTAN 671
Cdd:COG0553 528 LSGR--------------------SAKLEALLELLEELL--AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 672 AKRQQLVNLYNDPARPEfVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARVWREGQKKIVSIYRTFTTGTIEE 751
Cdd:COG0553 586 EERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664

                       490
                ....*....|....*.
gi 66811190 752 KIFQRQLTKQALSTSI 767
Cdd:COG0553 665 KILELLEEKRALAESV 680
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 283-521 1.38e-87

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 279.74  E-value: 1.38e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFR-GGFkgNGCILADDMGLGKSIQAITILWTLLKQGPKGESTAKKAVIVAPCTLVGNWGQEL 361
Cdd:cd18067   1 LRPHQREGVKFLYRCVTGRRiRGS--HGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANEL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDGVNTVAI-GESTKTGRAKLTEleFGKAD-------VLIISYDQLRIYCEDICKiTSIGLVICDEGHRLKNAEIK 433
Cdd:cd18067  79 GKWLGGRLQPLAIdGGSKKEIDRKLVQ--WASQQgrrvstpVLIISYETFRLHVEVLQK-GEVGLVICDEGHRLKNSDNQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 434 TTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRL 513
Cdd:cd18067 156 TYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISI 235


                ....*...
gi 66811190 514 TSQFILRR 521
Cdd:cd18067 236 VNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 283-521 3.72e-82

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: 264.79  E-value: 3.72e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFR--GGFkgnGCILADDMGLGKSIQAITILWTLLKQGPKG-ESTAKKAVIVAPCTLVGNWGQ 359
Cdd:cd18066   1 LRPHQREGIEFLYECVMGMRvnERF---GAILADEMGLGKTLQCISLIWTLLRQGPYGgKPVIKRALIVTPGSLVKNWKK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 360 ELKKWLG-DGVNTVAIGESTKTGrakltelEFGKA---DVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTT 435
Cdd:cd18066  78 EFQKWLGsERIKVFTVDQDHKVE-------EFIASplySVLIISYEMLLRSLDQISKL-NFDLVICDEGHRLKNTSIKTT 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 436 KAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTS 515
Cdd:cd18066 150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTG 229


                ....*.
gi 66811190 516 QFILRR 521
Cdd:cd18066 230 LFILRR 235
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 286-580 1.92e-69

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: 232.57  E-value: 1.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   286 HQREGVQFMFDCLLGfrggfKGNGCILADDMGLGKSIQAITILWTLLKQGPKgesTAKKAVIVAPCTLVGNWGQELKKWL 365
Cdd:pfam00176   1 YQIEGVNWMLSLENN-----LGRGGILADEMGLGKTLQTISLLLYLKHVDKN---WGGPTLIVVPLSLLHNWMNEFERWV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   366 GDGVNTVAIGESTKTGRAKLTELE--FGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKAVSMIPT 443
Cdd:pfam00176  73 SPPALRVVVLHGNKRPQERWKNDPnfLADFDVVITTYETLRKHKELLKKV-HWHRIVLDEGHRLKNSKSKLSKALKSLKT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   444 ARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIvasRNPDASDeekeiGRQRsleLSRLTSQFILRRTA 523
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKK-----GVSR---LHKLLKPFLLRRTK 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66811190   524 FVNTQYLPPKVEYVIFCKLTPLQLSIYKHLIKEAKDSAFASTTGA-------LPLITTLKKLSN 580
Cdd:pfam00176 221 KDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGreikaslLNILMRLRKICN 284
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 283-506 1.60e-62

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: 211.38  E-value: 1.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLG-FRGGFKGNGCILADDMGLGKSIQAITILWTLLKQGPKGestaKKAVIVAPCTLVGNWGQEL 361
Cdd:cd18007   1 LKPHQVEGVRFLWSNLVGtDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRR----SRPLVLCPASTLYNWEDEF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDGVNTVAIGES---TKTGRAKLTELE--FGKADVLIISYDQLRI----------YCEDICKITSI---GLVICDE 423
Cdd:cd18007  77 KKWLPPDLRPLLVLVSlsaSKRADARLRKINkwHKEGGVLLIGYELFRNlasnattdprLKQEFIAALLDpgpDLLVLDE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 424 GHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIG 503
Cdd:cd18007 157 GHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLM 236


                ...
gi 66811190 504 RQR 506
Cdd:cd18007 237 LKR 239
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 283-473 1.78e-60

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: 203.57  E-value: 1.78e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLlgfrggFKGNGCILADDMGLGKSIQAITILWTLLKQGPKgestAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd17919   1 LRPYQLEGLNFLLELY------ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE----RGPVLVVCPLSVLENWEREFE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDgVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNAEIKTTKAVSMIP 442
Cdd:cd17919  71 KWTPD-LRVVVYHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKF-RWDLVVVDEAHRLKNPKSQLSKALKALR 148

                       170       180       190
                ....*....|....*....|....*....|.
gi 66811190 443 TARRVILSGTPIQNDLTEFYAMVNFVNPGVL 473
Cdd:cd17919 149 AKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 283-521 8.25e-57

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: 196.06  E-value: 8.25e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGfrggfkGNGCILADDMGLGKSIQAITILWTLL----------------KQGPKGESTAKKAV 346
Cdd:cd18005   1 LRDYQREGVEFMYDLYKN------GRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSAKKPVL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 347 IVAPCTLVGNWGQELKKWlgdGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHR 426
Cdd:cd18005  75 IVAPLSVLYNWKDELDTW---GHFEVGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSI-NWSAVIADEAHR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 427 LKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQR 506
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKR 230

                       250
                ....*....|....*
gi 66811190 507 SLELSRLTSQFILRR 521
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 274-763 2.29e-56

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 211.20  E-value: 2.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   274 VVDP-ILSQKLRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLK----QGPKgestakkaVIV 348
Cdd:PLN03142  160 LVQPsCIKGKMRDYQLAGLNWLIRL---YENGING---ILADEMGLGKTLQTISLLGYLHEyrgiTGPH--------MVV 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   349 APCTLVGNWGQELKKWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYdQLRIYCEDICKITSIGLVICDEGHRLK 428
Cdd:PLN03142  226 APKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSF-EMAIKEKTALKRFSWRYIIIDEAHRIK 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   429 NAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDApivasrnpDASDEEKEIGRQrsl 508
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI--------SGENDQQEVVQQ--- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   509 eLSRLTSQFILRRTAFVNTQYLPPKVEYVIFCKLTPLQLSIYKHLIKEAKDsafASTTGA-----LPLITTLKKLSNcae 583
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLD---VVNAGGerkrlLNIAMQLRKCCN--- 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   584 lvytpdketdvgtsilklfpkewNPKVFQ-----PQY---------SSKLLFVDRLLANIRNSKSgdKTVIISNYTQTLE 649
Cdd:PLN03142  447 -----------------------HPYLFQgaepgPPYttgehlvenSGKMVLLDKLLPKLKERDS--RVLIFSQMTRLLD 501

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   650 VLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDPARPEFVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARV 729
Cdd:PLN03142  502 ILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRA 581

                         490       500       510
                  ....*....|....*....|....*....|....
gi 66811190   730 WREGQKKIVSIYRTFTTGTIEEKIFQRQLTKQAL 763
Cdd:PLN03142  582 HRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 283-522 9.61e-53

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: 183.54  E-value: 9.61e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFM-FDCLLGFrggfkgnGCILADDMGLGKSIQAITILwtlLKQGPKGEstAKKAVIVAPCTLVGNWGQEL 361
Cdd:cd18012   5 LRPYQKEGFNWLsFLRHYGL-------GGILADDMGLGKTLQTLALL---LSRKEEGR--KGPSLVVAPTSLIYNWEEEA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWlGDGVNTVAIgesTKTGRAKLTELEFGKADVLIISYDQLRiycEDICKITSIG--LVICDEGHRLKNAEIKTTKAVS 439
Cdd:cd18012  73 AKF-APELKVLVI---HGTKRKREKLRALEDYDLVITSYGLLR---RDIELLKEVKfhYLVLDEAQNIKNPQTKTAKAVK 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 440 MIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIvasrnpdasdeEKEIGRQRSLELSRLTSQFIL 519
Cdd:cd18012 146 ALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPI-----------EKDGDEEALEELKKLISPFIL 214


                ...
gi 66811190 520 RRT 522
Cdd:cd18012 215 RRL 217
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 283-521 4.65e-49

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


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 173.69  E-value: 4.65e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdclLGFRGGFKGNGcILADDMGLGKSIQAITILWT---LLKQGPkgESTAKKAVIVAPCTLVGNWGQ 359
Cdd:cd17999   1 LRPYQQEGINW-----LAFLNKYNLHG-ILCDDMGLGKTLQTLCILASdhhKRANSF--NSENLPSLVVCPPTLVGHWVA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 360 ELKKWLGDGVNTVAIGESTKTGRAKLTElEFGKADVLIISYDQLRiycEDICKITSIGL--VICDEGHRLKNAEIKTTKA 437
Cdd:cd17999  73 EIKKYFPNAFLKPLAYVGPPQERRRLRE-QGEKHNVIVASYDVLR---NDIEVLTKIEWnyCVLDEGHIIKNSKTKLSKA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 438 VSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTSQF 517
Cdd:cd17999 149 VKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPF 228


                ....
gi 66811190 518 ILRR 521
Cdd:cd17999 229 LLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 615-742 8.28e-48

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 166.50  E-value: 8.28e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 615 YSSKLLFVDRLLANIRnsKSGDKTVIISNYTQTLEVLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDPARPeFVFLLS 694
Cdd:cd18793   9 VSGKLEALLELLEELR--EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLS 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66811190 695 SKAGGVGLNLIGGNHLVLFDADWNPANDAQSMARVWREGQKKIVSIYR 742
Cdd:cd18793  86 TKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYR 133
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 283-521 2.50e-47

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: 168.70  E-value: 2.50e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFRGGfkgngcILADDMGLGKSIQAITILWTLLKQGpkgesTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGGKGG------ILADDMGLGKTVQICAFLSGMFDSG-----LIKSVLVVMPTSLIPHWVKEFA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWlGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLRIYCEDICKITSIGL----VICDEGHRLKNAEIKTTKAV 438
Cdd:cd18001  70 KW-TPGLRVKVFHGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEFkwdyVILDEGHKIKNSKTKSAKSL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 439 SMIPTARRVILSGTPIQNDLTEFYAMVNFVNPG-VLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLTSQF 517
Cdd:cd18001 149 REIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPY 228


                ....
gi 66811190 518 ILRR 521
Cdd:cd18001 229 FLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 283-506 1.93e-44

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: 160.37  E-value: 1.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGFRGGFKGN---GCILADDMGLGKSIQAITILWTLLKQGPkgestAKKAVIVAPCTLVGNWGQ 359
Cdd:cd18069   1 LKPHQIGGIRFLYDNIIESLERYKGSsgfGCILAHSMGLGKTLQVISFLDVLLRHTG-----AKTVLAIVPVNTLQNWLS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 360 ELKKWLGDGVNTVAI------------GESTKTGRAKLTELEFGKADVLIISYDQLRIYcedickiTSIGLVICDEGHRL 427
Cdd:cd18069  76 EFNKWLPPPEALPNVrprpfkvfilndEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLR-------PGPDVVICDEGHRI 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66811190 428 KNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQR 506
Cdd:cd18069 149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 283-506 9.78e-44

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: 158.90  E-value: 9.78e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCL---LGFRGGFKGNGCILADDMGLGKSIQAITILWTLLKQGPKgeSTAKKAVIVAPCTLVGNWGQ 359
Cdd:cd18068   1 LKPHQVDGVQFMWDCCcesLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKL--ENFSRVLVVCPLNTVLNWLN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 360 ELKKWLGDG-------VNTVAIGESTKTGRAKLTElEFGKADVLIISYDQLRIYC------------EDICK-ITSIG-- 417
Cdd:cd18068  79 EFEKWQEGLkdeekieVNELATYKRPQERSYKLQR-WQEEGGVMIIGYDMYRILAqernvksreklkEIFNKaLVDPGpd 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 418 LVICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASD 497
Cdd:cd18068 158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTL 237


                ....*....
gi 66811190 498 EEKEIGRQR 506
Cdd:cd18068 238 VDVRVMKKR 246
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 283-470 3.82e-35

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 132.45  E-value: 3.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDcLLGFR-GGfkgngcILADDMGLGKSIQAITILWTL----LKQGPkgestakkAVIVAPCTLVGNW 357
Cdd:cd18000   1 LFKYQQTGVQWLWE-LHCQRvGG------ILGDEMGLGKTIQIIAFLAALhhskLGLGP--------SLIVCPATVLKQW 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKW--------LGDGVNTVAIGE--STKTGRAKLTELEFGKADVLIISYDQLRIYCEDICKItSIGLVICDEGHRL 427
Cdd:cd18000  66 VKEFHRWwppfrvvvLHSSGSGTGSEEklGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNH-NWQYVILDEGHKI 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 66811190 428 KNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNP 470
Cdd:cd18000 145 RNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 283-521 1.73e-34

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 132.03  E-value: 1.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFdcllgFRGGfkgngcILADDMGLGKSIQAI-TILWTLLK------------QGPKGESTAKKAVIVA 349
Cdd:cd18008   1 LLPYQKQGLAWML-----PRGG------ILADEMGLGKTIQALaLILATRPQdpkipeeleensSDPKKLYLSKTTLIVV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 350 PCTLVGNWGQELKKWLGDGVNTVAIgeSTKTGRAKLTElEFGKADVLIISYDQLRIYC-------EDICKITSIGL---- 418
Cdd:cd18008  70 PLSLLSQWKDEIEKHTKPGSLKVYV--YHGSKRIKSIE-ELSDYDIVITTYGTLASEFpknkkggGRDSKEKEASPlhri 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 419 ----VICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVasrnpd 494
Cdd:cd18008 147 rwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFS------ 220

                       250       260
                ....*....|....*....|....*..
gi 66811190 495 asdEEKEIGRQRsleLSRLTSQFILRR 521
Cdd:cd18008 221 ---KNDRKALER---LQALLKPILLRR 241
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 283-483 1.95e-34

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: 131.22  E-value: 1.95e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLlgfrggFKGNGCILADDMGLGKSIQAITILWTLL----KQGPkgestakkAVIVAPCTLVGNWG 358
Cdd:cd17995   1 LRDYQLEGVNWLLFNW------YNRRNCILADEMGLGKTIQSIAFLEHLYqvegIRGP--------FLVIAPLSTIPNWQ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 359 QELKKWLGDGVnTVAIGESTKTGRAKLTELEF-----------GKADVLIISYDQLRIYCEDICKITSIGLVIcDEGHRL 427
Cdd:cd17995  67 REFETWTDMNV-VVYHGSGESRQIIQQYEMYFkdaqgrkkkgvYKFDVLITTYEMVIADAEELRKIPWRVVVV-DEAHRL 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66811190 428 KNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVY 483
Cdd:cd17995 145 KNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 282-521 7.71e-33

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: 127.12  E-value: 7.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFMfdcLLGFRGGFKGngcILADDMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGNWGQEL 361
Cdd:cd18009   3 VMRPYQLEGMEWL---RMLWENGING---ILADEMGLGKTIQTIALLAHLRERGVWG-----PFLVIAPLSTLPNWVNEF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDgVNTV---AIGESTKTGRAKLTELEFGKAD--VLIISYDqlrIYCEDICKITSIG--LVICDEGHRLKNAEIKT 434
Cdd:cd18009  72 ARFTPS-VPVLlyhGTKEERERLRKKIMKREGTLQDfpVVVTSYE---IAMRDRKALQHYAwkYLIVDEGHRLKNLNCRL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 435 TKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLELSRLT 514
Cdd:cd18009 148 IQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAIL 227


                ....*..
gi 66811190 515 SQFILRR 521
Cdd:cd18009 228 KPFLLRR 234
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 282-521 1.47e-31

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: 123.63  E-value: 1.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFM---FDCLLgfrggfkgNGcILADDMGLGKSIQAITILWTLLK----QGPkgestakkAVIVAPCTLV 354
Cdd:cd17996   3 TLKEYQLKGLQWMvslYNNNL--------NG-ILADEMGLGKTIQTISLITYLMEkkknNGP--------YLVIVPLSTL 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 355 GNWGQELKKWLgDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLrIYceDICKITSI--GLVICDEGHRLKNAEI 432
Cdd:cd17996  66 SNWVSEFEKWA-PSVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYI-IK--DKPLLSKIkwKYMIIDEGHRMKNAQS 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 433 KTTKAVS-MIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIV---ASRNPDASDEEKEIGRQRsl 508
Cdd:cd17996 142 KLTQTLNtYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFAntgEQVKIELNEEETLLIIRR-- 219

                       250
                ....*....|...
gi 66811190 509 eLSRLTSQFILRR 521
Cdd:cd17996 220 -LHKVLRPFLLRR 231
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 283-521 2.09e-31

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: 122.31  E-value: 2.09e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdcllgfrgGFKGNG-CILADDMGLGKSIQAITILWTLLKQGPkgestakkAVIVAPCTLVGNWGQEL 361
Cdd:cd18010   1 LLPFQREGVCF----------ALRRGGrVLIADEMGLGKTVQAIAIAAYYREEWP--------LLIVCPSSLRLTWADEI 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLG----DGVNTVAigestkTGRAKLTELEfgkADVLIISYDQLRIyCEDICKITSIGLVICDEGHRLKNAEIKTTKA 437
Cdd:cd18010  63 ERWLPslppDDIQVIV------KSKDGLRDGD---AKVVIVSYDLLRR-LEKQLLARKFKVVICDESHYLKNSKAKRTKA 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 438 V-SMIPTARRVI-LSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASdeekeiGRQRSLEL-SRLT 514
Cdd:cd18010 133 AlPLLKRAKRVIlLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYS------GSSNLEELhLLLL 206


                ....*..
gi 66811190 515 SQFILRR 521
Cdd:cd18010 207 ATIMIRR 213
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 283-521 3.17e-30

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: 119.08  E-value: 3.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLLGfrggfkGNGCILADDMGLGKSIQAITILWTL-LKQGPKGEStakkaVIVAPCTLVGNWGQEL 361
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAE------QHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPF-----LVLCPLSVLDNWKEEL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDGVNTVAIGEstKTGRAKL-----TELEFgkaDVLIISYDQLRIYCEDICKITSIGLVIcDEGHRLKNAEIKTTK 436
Cdd:cd18006  70 NRFAPDLSVITYMGD--KEKRLDLqqdikSTNRF---HVLLTTYEICLKDASFLKSFPWASLVV-DEAHRLKNQNSLLHK 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 437 AVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGV--LKNVATFKNVYdapivasrnpdaSDEEKEIGRQRslELSRLT 514
Cdd:cd18006 144 TLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVfpKDKLDDFIKAY------------SETDDESETVE--ELHLLL 209


                ....*..
gi 66811190 515 SQFILRR 521
Cdd:cd18006 210 QPFLLRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 282-522 2.98e-28

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: 113.57  E-value: 2.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILwTLLKQ-----GPKgestakkaVIVAPCTLVGN 356
Cdd:cd17997   3 TMRDYQIRGLNWLISL---FENGING---ILADEMGLGKTLQTISLL-GYLKHykninGPH--------LIIVPKSTLDN 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 357 WGQELKKWLgDGVNTVA-IGesTKTGRAKLTE--LEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNAEIK 433
Cdd:cd17997  68 WMREFKRWC-PSLRVVVlIG--DKEERADIIRdvLLPGKFDVCITSYEMV-IKEKTVLKKFNWRYIIIDEAHRIKNEKSK 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 434 TTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDapivasRNPDASDEEKEIGRqrsleLSRL 513
Cdd:cd17997 144 LSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN------VNNCDDDNQEVVQR-----LHKV 212


                ....*....
gi 66811190 514 TSQFILRRT 522
Cdd:cd17997 213 LRPFLLRRI 221
DEXDc smart00487
DEAD-like helicases superfamily;
282-475 1.29e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.04  E-value: 1.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    282 KLRPHQREGVQFMFDCLlgfrggfkgNGCILADDMGLGKSIQAITILWTLLKQGPKgestaKKAVIVAPC-TLVGNWGQE 360
Cdd:smart00487   8 PLRPYQKEAIEALLSGL---------RDVILAAPTGSGKTLAALLPALEALKRGKG-----GRVLVLVPTrELAEQWAEE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    361 LKKWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLRIYCE-DICKITSIGLVICDEGHRLKNA--EIKTTKA 437
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGgfGDQLEKL 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 66811190    438 VSMIPTARRVI-LSGTP---IQNDLTEFYAMVNFVNPGVLKN 475
Cdd:smart00487 154 LKLLPKNVQLLlLSATPpeeIENLLELFLNDPVFIDVGFTPL 195
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 278-521 4.54e-27

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


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 110.92  E-value: 4.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 278 ILSQKLRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLKQ----GPkgestakkAVIVAPCTL 353
Cdd:cd18063  19 LINGTLKHYQLQGLEWMVSL---YNNNLNG---ILADEMGLGKTIQTIALITYLMEHkrlnGP--------YLIIVPLST 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 354 VGNWGQELKKWlGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNAEIK 433
Cdd:cd18063  85 LSNWTYEFDKW-APSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYI-IKDKHILAKIRWKYMIVDEGHRMKNHHCK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 434 TTKAVSMIPTA-RRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLElsR 512
Cdd:cd18063 163 LTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLH--K 240


                ....*....
gi 66811190 513 LTSQFILRR 521
Cdd:cd18063 241 VLRPFLLRR 249
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 282-521 5.41e-27

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


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 109.75  E-value: 5.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFMFDCLlgfrggFKGNGCILADDMGLGKSIQAITILWTLLKQ----GPkgestakkAVIVAPCTLVGNW 357
Cdd:cd17993   1 ELRDYQLTGLNWLAHSW------CKGNNGILADEMGLGKTVQTISFLSYLFHSqqqyGP--------FLVVVPLSTMPAW 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKWLGDgVNTVA-IGesTKTGRAKLTELEFG-------KADVLIISYDQLRIYCEDICKITSIGLVIcDEGHRLKN 429
Cdd:cd17993  67 QREFAKWAPD-MNVIVyLG--DIKSRDTIREYEFYfsqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAV-DEAHRLKN 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 430 AEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKnvydapivasrnpDASDEEKEIGRQrslE 509
Cdd:cd17993 143 DESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKGIA---D 206

                       250
                ....*....|..
gi 66811190 510 LSRLTSQFILRR 521
Cdd:cd17993 207 LHKELEPFILRR 218
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 311-521 1.07e-26

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: 110.13  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 311 ILADDMGLGKSIQAITILWTLLK----QGPkgestakkAVIVAPCTLVGNWGQELKKWlGDGVNTVAIGESTKTGRAKLT 386
Cdd:cd18062  46 ILADEMGLGKTIQTIALITYLMEhkriNGP--------FLIIVPLSTLSNWVYEFDKW-APSVVKVSYKGSPAARRAFVP 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 387 ELEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSMIPTA-RRVILSGTPIQNDLTEFYAMV 465
Cdd:cd18062 117 QLRSGKFNVLLTTYEYI-IKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALL 195

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66811190 466 NFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRQRSLElsRLTSQFILRR 521
Cdd:cd18062 196 NFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLH--KVLRPFLLRR 249
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 283-471 4.01e-26

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 106.99  E-value: 4.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdCLLGFRggfkgNGCILADDMGLGKSIQAITILWTLLKQGPkgestAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18011   1 PLPHQIDAVLR---ALRKPP-----VRLLLADEVGLGKTIEAGLIIKELLLRGD-----AKRVLILCPASLVEQWQDELQ 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDGVnTVAIGESTKTGRaKLTELEFGKADVLIISYDQLR--IYCEDICKITSIGLVICDEGHRLKNAE-IKTTK--- 436
Cdd:cd18011  68 DKFGLPF-LILDRETAAQLR-RLIGNPFEEFPIVIVSLDLLKrsEERRGLLLSEEWDLVVVDEAHKLRNSGgGKETKryk 145

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 66811190 437 -AVSMIPTARRVI-LSGTPIQNDLTEFYAMVNFVNPG 471
Cdd:cd18011 146 lGRLLAKRARHVLlLTATPHNGKEEDFRALLSLLDPG 182
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 283-479 3.38e-24

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


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 102.04  E-value: 3.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMfdcLLGFrggFKGNGCILADDMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGNWGQELK 362
Cdd:cd18058   1 LREYQLEGMNWL---LFNW---YNRKNCILADEMGLGKTIQSITFLSEIFLMGIRG-----PFLIIAPLSTITNWEREFR 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWlgDGVNTVaIGESTKTGRAKLTELEFGKAD-------------VLIISYDQLRIYCEDICKItSIGLVICDEGHRLKN 429
Cdd:cd18058  70 TW--TEMNAI-VYHGSQISRQMIQQYEMYYRDeqgnplsgifkfqVVITTFEMILADCPELKKI-NWSCVIIDEAHRLKN 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66811190 430 AEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18058 146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTF 195
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 282-533 6.90e-23

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 98.58  E-value: 6.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLKQgpkgESTAKKAVIVAPCTLVGNWGQEL 361
Cdd:cd18064  15 KLRDYQVRGLNWLISL---YENGING---ILADEMGLGKTLQTISLLGYMKHY----RNIPGPHMVLVPKSTLHNWMAEF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSMI 441
Cdd:cd18064  85 KRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEML-IKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 442 PTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDApivasrnpdasdeEKEIGRQRSLE-LSRLTSQFILR 520
Cdd:cd18064 164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT-------------NNCLGDQKLVErLHMVLRPFLLR 230

                       250
                ....*....|...
gi 66811190 521 RTAFVNTQYLPPK 533
Cdd:cd18064 231 RIKADVEKSLPPK 243
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 283-479 7.64e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 97.79  E-value: 7.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFdcllgfRGGFKGNGCILADDMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGNWGQELK 362
Cdd:cd18059   1 LREYQLEGVNWLL------FNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHG-----PFLVIAPLSTIPNWEREFR 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWlgDGVNTVAIGESTKTGRA-KLTELEFG-----------KADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKNA 430
Cdd:cd18059  70 TW--TELNVVVYHGSQASRRTiQLYEMYFKdpqgrvikgsyKFHAIITTFEMILTDCPELRNI-PWRCVVIDEAHRLKNR 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66811190 431 EIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18059 147 NCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTF 195
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 283-479 1.14e-22

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


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 97.43  E-value: 1.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMfdcLLGFrggFKGNGCILADDMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGNWGQELK 362
Cdd:cd18060   1 LREYQLEGVNWL---LFNW---YNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHG-----PFLVIAPLSTITNWEREFN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWlgDGVNTVAIGESTKTgRAKLTELEFG-------------KADVLIISYDQLRIYCEDICKItSIGLVICDEGHRLKN 429
Cdd:cd18060  70 TW--TEMNTIVYHGSLAS-RQMIQQYEMYckdsrgrlipgayKFDALITTFEMILSDCPELREI-EWRCVIIDEAHRLKN 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66811190 430 AEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18060 146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF 195
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 310-474 1.30e-22

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: 96.30  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 310 CILADDMGLGKSIQAITILWTLLKQGPKGEStakkaVIVAPCTLVGNWGQELKKWLGDGVntVAIGESTKTGRAKLTELE 389
Cdd:cd17998  22 GILADEMGLGKTIQVIAFLAYLKEIGIPGPH-----LVVVPSSTLDNWLREFKRWCPSLK--VEPYYGSQEERKHLRYDI 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 390 ---FGKADVLIISYDQLRIYCED--ICKITSIGLVICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAM 464
Cdd:cd17998  95 lkgLEDFDVIVTTYNLATSNPDDrsFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSL 174

                       170
                ....*....|..
gi 66811190 465 VNFV--NPGVLK 474
Cdd:cd17998 175 LNFImpKPFILR 186
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 283-479 1.35e-22

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: 96.35  E-value: 1.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdclLGFRGGfKGNGCILADDMGLGKSIQAITILWTLLKQGpkgeSTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd17994   1 LHPYQLEGLNW-----LRFSWA-QGTDTILADEMGLGKTIQTIVFLYSLYKEG----HSKGPFLVSAPLSTIINWEREFE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDGVNTVAIGEStktgrakltelefgkadVLIISYDQLRIyceDICKITSI--GLVICDEGHRLKNAEIKTTKAVSM 440
Cdd:cd17994  71 MWAPDFYVVTYVGDH-----------------VLLTSYELISI---DQAILGSIdwAVLVVDEAHRLKNNQSKFFRILNS 130

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 66811190 441 IPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd17994 131 YKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGF 169
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 283-521 1.83e-22

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: 97.04  E-value: 1.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLKQ----GPKgestakkaVIVAPCTLVGNWG 358
Cdd:cd18003   1 LREYQHIGLDWLATL---YEKNLNG---ILADEMGLGKTIQTIALLAHLACEkgnwGPH--------LIVVPTSVMLNWE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 359 QELKKWLgDGVNTVAIGESTKtgRAKLTELEFGKAD---VLIISYdQLRIYCEDICKITSIGLVICDEGHRLKNAEIKTT 435
Cdd:cd18003  67 MEFKRWC-PGFKILTYYGSAK--ERKLKRQGWMKPNsfhVCITSY-QLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRW 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 436 KAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVAsrnpdASDEEKEIGRQRSLELSRLTS 515
Cdd:cd18003 143 QTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTA-----MSEGSQEENEELVRRLHKVLR 217


                ....*.
gi 66811190 516 QFILRR 521
Cdd:cd18003 218 PFLLRR 223
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 283-479 2.69e-21

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


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 93.59  E-value: 2.69e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdclLGFRGGfKGNGCILADDMGLGKSIQAITILWTLLKQGpkgeSTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18056   1 LHPYQLEGLNW-----LRFSWA-QGTDTILADEMGLGKTVQTAVFLYSLYKEG----HSKGPFLVSAPLSTIINWEREFE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDGVNTVAIGEstKTGRAKLTELEFGKAD---------------------VLIISYDQLRIyceDICKITSI--GLV 419
Cdd:cd18056  71 MWAPDMYVVTYVGD--KDSRAIIRENEFSFEDnairggkkasrmkkeasvkfhVLLTSYELITI---DMAILGSIdwACL 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 420 ICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18056 146 IVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF 205
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 283-479 9.37e-21

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 91.99  E-value: 9.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFdcllgfRGGFKGNGCILADDMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGNWGQELK 362
Cdd:cd18061   1 LREYQLEGLNWLL------FNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRG-----PFLIIAPLSTIANWEREFR 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWlgDGVNtVAIGESTKTGRAKLTELEFGKAD-------------VLIISYDQLRIYCEDICKItSIGLVICDEGHRLKN 429
Cdd:cd18061  70 TW--TDLN-VVVYHGSLISRQMIQQYEMYFRDsqgriirgayrfqAIITTFEMILGGCPELNAI-DWRCVIIDEAHRLKN 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 66811190 430 AEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18061 146 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF 195
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 283-479 2.11e-20

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: 91.28  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFmfdclLGFRGGfKGNGCILADDMGLGKSIQAITILWTLLKQGpkgeSTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18057   1 LHPYQLEGLNW-----LRFSWA-QGTDTILADEMGLGKTVQTIVFLYSLYKEG----HSKGPYLVSAPLSTIINWEREFE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDGVNTVAIGEstKTGRAKLTELEFGKAD---------------------VLIISYDQLRIyceDICKITSI--GLV 419
Cdd:cd18057  71 MWAPDFYVVTYTGD--KESRSVIRENEFSFEDnairsgkkvfrmkkeaqikfhVLLTSYELITI---DQAILGSIewACL 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 420 ICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18057 146 VVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGF 205
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 283-521 4.02e-20

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: 90.46  E-value: 4.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLKQgpkgESTAKKAVIVAPCTLVGNWGQELK 362
Cdd:cd18065  16 LRDYQVRGLNWMISL---YENGVNG---ILADEMGLGKTLQTIALLGYLKHY----RNIPGPHMVLVPKSTLHNWMNEFK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 363 KWLGDGVNTVAIGESTKTGRAKLTELEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAVSMIP 442
Cdd:cd18065  86 RWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMV-IKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 443 TARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDApivasrnpdasdeEKEIGRQRSLE-LSRLTSQFILRR 521
Cdd:cd18065 165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT-------------KNCLGDQKLVErLHAVLKPFLLRR 231
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 306-479 4.83e-20

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


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 90.07  E-value: 4.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 306 KGNGCILADDMGLGKSIQAITILWTLLKQGpkgeSTAKKAVIVAPCTLVGNWGQELKKWLGDGVNTVAIGEstKTGRAKL 385
Cdd:cd18055  18 QGTDTILADEMGLGKTIQTIVFLYSLYKEG----HTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTGD--KDSRAII 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 386 TELEFGKAD---------------------VLIISYDQLRIyceDICKITSI--GLVICDEGHRLKNAEIKTTKAVSMIP 442
Cdd:cd18055  92 RENEFSFDDnavkggkkafkmkreaqvkfhVLLTSYELVTI---DQAALGSIrwACLVVDEAHRLKNNQSKFFRVLNGYK 168

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 66811190 443 TARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATF 479
Cdd:cd18055 169 IDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGF 205
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 280-468 1.09e-19

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 89.07  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 280 SQKLRPHQREGVQFMFDCLLGFRGG---FKGNGCILADDMGLGKSIQAITILwtllkqgpkgesTAKKAVIVAPCTLVGN 356
Cdd:cd18071  18 SQDLPPFWEEAVGLFLNTITNFSQKkrpELVRGGILADDMGLGKTLTTISLI------------LANFTLIVCPLSVLSN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 357 WgqelKKWLGDGVNTVAIGESTKTGRAK-LTELEFGKADVLIISYDQLriyCEDICKITSIGL-------VICDEGHRLK 428
Cdd:cd18071  86 W----ETQFEEHVKPGQLKVYTYHGGERnRDPKLLSKYDIVLTTYNTL---ASDFGAKGDSPLhtinwlrVVLDEGHQIR 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66811190 429 NAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFV 468
Cdd:cd18071 159 NPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFL 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 624-733 8.32e-19

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 82.64  E-value: 8.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   624 RLLANIRNSKSGDKTVIISNYTQTLEvLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNDParpEFVFLLSSKAGGVGLN 703
Cdd:pfam00271   4 EALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 66811190   704 LIGGNHLVLFDADWNPANDAQSMARVWREG 733
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 282-521 8.50e-19

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: 86.60  E-value: 8.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVQFMFDCLLgfrggfKGNGCILADDMGLGKSIQAITILWTLLKQ----GPkgestakkAVIVAPCTLVGNW 357
Cdd:cd18054  20 ELRDYQLEGLNWLAHSWC------KNNSVILADEMGLGKTIQTISFLSYLFHQhqlyGP--------FLLVVPLSTLTSW 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 358 GQELKKWLGDGVNTVAIGE--STKTGR------AKLTELEFgkaDVLIISYDqlrIYCEDICKITSIGLVI--CDEGHRL 427
Cdd:cd18054  86 QREFEIWAPEINVVVYIGDlmSRNTIReyewihSQTKRLKF---NALITTYE---ILLKDKTVLGSINWAFlgVDEAHRL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 428 KNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYdapivasrnpdasDEEKEIGRQrs 507
Cdd:cd18054 160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDH-------------GKGRENGYQ-- 224

                       250
                ....*....|....
gi 66811190 508 lELSRLTSQFILRR 521
Cdd:cd18054 225 -SLHKVLEPFLLRR 237
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 280-470 3.15e-16

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: 78.94  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 280 SQKLRPHQREGVQFMFDCLLgfrggfKGNGCILADDMGLGKSIQAITILWTLLKQ----GPkgestakkAVIVAPCTLVG 355
Cdd:cd18053  18 GLELRDYQLNGLNWLAHSWC------KGNSCILADEMGLGKTIQTISFLNYLFHEhqlyGP--------FLLVVPLSTLT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 356 NWGQELKKWLGDGVNTVAIGESTKTGRAKLTE-----LEFGKADVLIISYDQLrIYCEDICKITSIGLVICDEGHRLKNA 430
Cdd:cd18053  84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEwmhpqTKRLKFNILLTTYEIL-LKDKSFLGGLNWAFIGVDEAHRLKND 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 66811190 431 EIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNP 470
Cdd:cd18053 163 DSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMP 202
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 283-521 8.04e-16

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: 77.91  E-value: 8.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFdcllgFRGGFKGNGCILADDMGLGKSIQAIT-ILWTLLKQGPKGESTAKK----------------- 344
Cdd:cd18072   1 LLLHQKQALAWLL-----WRERQKPRGGILADDMGLGKTLTMIAlILAQKNTQNRKEEEKEKAlteweskkdstlvpsag 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 345 AVIVAPCTLVGNWGQELKKWLGDGVNTVAI--GESTKTGRAKLTELefgkaDVLIISYD----QLRIYCEDICKITSIGL 418
Cdd:cd18072  76 TLVVCPASLVHQWKNEVESRVASNKLRVCLyhGPNRERIGEVLRDY-----DIVITTYSlvakEIPTYKEESRSSPLFRI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 419 ----VICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDApivasrnpd 494
Cdd:cd18072 151 awarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDN--------- 221

                       250       260
                ....*....|....*....|....*..
gi 66811190 495 asdeEKEIGRQRsleLSRLTSQFILRR 521
Cdd:cd18072 222 ----KSRKGGER---LNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
649-733 9.65e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 9.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190    649 EVLATMCKTRGYAYFQLDGSTANAKRQQLVNLYNdpaRPEFVFLLSSKAGGVGLNLIGGNHLVLFDADWNPANDAQSMAR 728
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                   ....*
gi 66811190    729 VWREG 733
Cdd:smart00490  78 AGRAG 82
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 283-521 1.92e-14

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: 73.69  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCllgFRGGFKGngcILADDMGLGKSIQAITILWTLLKQ----GPkgestakkAVIVAPCTLVGNWG 358
Cdd:cd18002   1 LKEYQLKGLNWLANL---YEQGING---ILADEMGLGKTVQSIAVLAHLAEEhniwGP--------FLVIAPASTLHNWQ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 359 QELKKWLGDgVNTVAIGESTKTGRA-------KLTELEFGKADVLIISYdQLRIYCEDICKITSIGLVICDEGHRLKNAE 431
Cdd:cd18002  67 QEISRFVPQ-FKVLPYWGNPKDRKVlrkfwdrKNLYTRDAPFHVVITSY-QLVVQDEKYFQRVKWQYMVLDEAQAIKSSS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 432 IKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNFVNPGVLKNVATFKNVYDAPIVASRNPDASDEEKEIGRqrsleLS 511
Cdd:cd18002 145 SSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKR-----LH 219

                       250
                ....*....|
gi 66811190 512 RLTSQFILRR 521
Cdd:cd18002 220 MILKPFMLRR 229
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 283-471 4.62e-14

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 72.38  E-value: 4.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFDCLlgfrggfkgNGCILADdMGLGKSIQAITILWTLLKQGPKGestakKAVIVAPCTLVGN-WGQEL 361
Cdd:cd18013   1 PHPYQKVAINFIIEHP---------YCGLFLD-MGLGKTVTTLTALSDLQLDDFTR-----RVLVIAPLRVARStWPDEV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 362 KKWLGDGVNTVAIGESTKTGRAKLTELEfgkADVLIISYDQLRIYCEDICKITSIGLVICDEGHRLKNAEIKTTKAV-SM 440
Cdd:cd18013  66 EKWNHLRNLTVSVAVGTERQRSKAANTP---ADLYVINRENLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALrKV 142

                       170       180       190
                ....*....|....*....|....*....|..
gi 66811190 441 IPTARRVI-LSGTPIQNDLTEFYAMVNFVNPG 471
Cdd:cd18013 143 RPVIKRLIgLTGTPSPNGLMDLWAQIALLDQG 174
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 283-475 7.89e-13

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 69.68  E-value: 7.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 283 LRPHQREGVQFMFdcllgFRGGfkgngcILADDMGLGKSIQAITILwtLLKQGPKGES---------------------- 340
Cdd:cd18070   1 LLPYQRRAVNWML-----VPGG------ILADEMGLGKTVEVLALI--LLHPRPDNDLdaadddsdemvccpdclvaetp 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 341 -TAKKAVIVAPCTLVGNWGQELKKWLGDGVNT-VAIGESTKTGRAKLTELEFGKADVLIISYDQLR--IYCEDICK-ITS 415
Cdd:cd18070  68 vSSKATLIVCPSAILAQWLDEINRHVPSSLKVlTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRteLHYAEANRsNRR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 416 IGL------------------VICDEGHRLKNAEIKTTKAVSMIPTARRVILSGTPIQNDLTEFYAMVNF--VNPGVLKN 475
Cdd:cd18070 148 RRRqkryeappsplvlvewwrVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFlgVEPFCDSD 227
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
282-457 1.00e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.88  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 282 KLRPHQREGVqfmfDCLLGFRGGFKGNGCILADdMGLGKSIQAITILWTLLkqgpkgesTAKKAVIVAP-CTLVGNWGQE 360
Cdd:COG1061  80 ELRPYQQEAL----EALLAALERGGGRGLVVAP-TGTGKTVLALALAAELL--------RGKRVLVLVPrRELLEQWAEE 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 361 LKKWLGDGVNTVAIGESTktgrakltelefgkADVLIISYDQL--RIYCEDICKitSIGLVICDEGHRLkNAEiKTTKAV 438
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSD--------------APITVATYQSLarRAHLDELGD--RFGLVIIDEAHHA-GAP-SYRRIL 208

                       170
                ....*....|....*....
gi 66811190 439 SMIPTARRVILSGTPIQND 457
Cdd:COG1061 209 EAFPAAYRLGLTATPFRSD 227
ResIII pfam04851
Type III restriction enzyme, res subunit;
282-454 1.74e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   282 KLRPHQREGVQfmfDCLLGFRGGFKGNGCILAddMGLGKSIQAITILWTLLKQGPKgestaKKAVIVAPCT-LVGNWGQE 360
Cdd:pfam04851   3 ELRPYQIEAIE---NLLESIKNGQKRGLIVMA--TGSGKTLTAAKLIARLFKKGPI-----KKVLFLVPRKdLLEQALEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   361 LKKWLGDGVNTVAIgestKTGRAKLTELefGKADVLIISYDQL---RIYCEDICKITSIGLVICDEGHRLkNAEiKTTKA 437
Cdd:pfam04851  73 FKKFLPNYVEIGEI----ISGDKKDESV--DDNKIVVTTIQSLykaLELASLELLPDFFDVIIIDEAHRS-GAS-SYRNI 144

                         170
                  ....*....|....*..
gi 66811190   438 VSMIPTARRVILSGTPI 454
Cdd:pfam04851 145 LEYFKPAFLLGLTATPE 161
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 317-456 2.87e-04

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 42.61  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190   317 GLGKSIQA-ITILWTLLKQGPKgestaKKAVIVAPcT--LVGNWGQELKKWLGDGVNTVAIGESTKTGRAKLTELEfgKA 393
Cdd:pfam00270  24 GSGKTLAFlLPALEALDKLDNG-----PQALVLAP-TreLAEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKLK--GP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66811190   394 DVLIISYDQLRIYCEDICKITSIGLVICDEGHRL--KNAEIKTTKAVSMIPTARRVI-LSGTPIQN 456
Cdd:pfam00270  96 DILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILlLSATLPRN 161
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 319-469 7.33e-03

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 38.40  E-value: 7.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 319 GKSIQA-ITILWTLLKQGpkgestaKKAVIVAPC-TLVGNWGQELKKWLGDGVNTVAIgestKTGRAKLTELEFGKADVL 396
Cdd:cd17921  29 GKTLIAeLAILRALATSG-------GKAVYIAPTrALVNQKEADLRERFGPLGKNVGL----LTGDPSVNKLLLAEADIL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 397 IISYDQLRIYCED--ICKITSIGLVICDEGHRLKNAE--------IKTTKAVSmiPTARRVILSGTpIQN--DLTEFYAM 464
Cdd:cd17921  98 VATPEKLDLLLRNggERLIQDVRLVVVDEAHLIGDGErgvvlellLSRLLRIN--KNARFVGLSAT-LPNaeDLAEWLGV 174


                ....*
gi 66811190 465 VNFVN 469
Cdd:cd17921 175 EDLIR 179
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
359-456 9.87e-03

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 39.49  E-value: 9.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66811190 359 QELKKWLGD-GVNtvaIGESTktGRAKLTELEFGKADVLIISY---DQLRIYCEDIckITSIGLVICDEGHRLKNA---- 430
Cdd:COG1204  84 REFKRDFEElGIK---VGVST--GDYDSDDEWLGRYDILVATPeklDSLLRNGPSW--LRDVDLVVVDEAHLIDDEsrgp 156

                        90       100
                ....*....|....*....|....*...
gi 66811190 431 --EIKTTKAVSMIPTARRVILSGTpIQN 456
Cdd:COG1204 157 tlEVLLARLRRLNPEAQIVALSAT-IGN 183
 
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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