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Conserved domains on  [gi|564347124|ref|XP_006236662|]
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 isoform X2 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
484-995 4.18e-143

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 443.90  E-value: 4.18e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVN 563
Cdd:COG0553   233 SLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  564 LWCPTLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 643
Cdd:COG0553   311 KFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  644 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVKE 723
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTKE 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  724 EVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytaeklkemsQ 800
Cdd:COG0553   456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP----------------A 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  801 LMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRTLGCILSELKQKGDRVVLFSQFTMM 880
Cdd:COG0553   520 LLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDT 561
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  881 LDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDR 960
Cdd:COG0553   562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDR 641
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 564347124  961 CHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 995
Cdd:COG0553   642 AHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
484-995 4.18e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 443.90  E-value: 4.18e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVN 563
Cdd:COG0553   233 SLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  564 LWCPTLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 643
Cdd:COG0553   311 KFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  644 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVKE 723
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTKE 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  724 EVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytaeklkemsQ 800
Cdd:COG0553   456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP----------------A 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  801 LMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRTLGCILSELKQKGDRVVLFSQFTMM 880
Cdd:COG0553   520 LLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDT 561
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  881 LDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDR 960
Cdd:COG0553   562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDR 641
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 564347124  961 CHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 995
Cdd:COG0553   642 AHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
495-677 1.19e-124

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: 377.11  E-value: 1.19e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCY 574
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLT 654
Cdd:cd17998    81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                         170       180
                  ....*....|....*....|...
gi 564347124  655 GTPVQNNLLELMSLLNFVMPHMF 677
Cdd:cd17998   161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
474-996 1.15e-111

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 370.29  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  474 LTGNGGGWNIEQPSLLNQSLslKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPA 552
Cdd:PLN03142  151 LGGSGGTRLLVQPSCIKGKM--RDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  553 STIDNWLREVNLWCPTLNVLCYYGSQEERKQIRFNIHNKyEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLK 632
Cdd:PLN03142  229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVA-GKFDVCVTSFEMAIK---EKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  633 NMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKpADEQsiyekERIAHAKQI 712
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQISGE-NDQQ-----EVVQQLHKV 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  713 IKPFILRRVKEEVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQyyta 792
Cdd:PLN03142  378 LRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQG---- 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  793 eklkemsqlmlkepthCEANPdlifedmevmtdfelhvlckqyqhinSYQLDMDLILDSGKFRTLGCILSELKQKGDRVV 872
Cdd:PLN03142  454 ----------------AEPGP--------------------------PYTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  873 LFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTD-MDIFVFLLSTKAGGLGINLTSANVVILHDIDCNP 951
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 564347124  952 YNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLE 996
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALD 616
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
498-783 8.04e-78

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: 256.46  E-value: 8.04e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   498 YQKVGLNWL-ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK--GPHLIVVPASTIDNWLREVNLWC--PTLNVL 572
Cdd:pfam00176    1 YQIEGVNWMlSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   573 CYYGSQEERKQIrFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLL 652
Cdd:pfam00176   81 VLHGNKRPQERW-KNDPNFLADFDVVITTYETLRK---HKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   653 LTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSktkpaDEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPK 732
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSL-STFRNWFDR-----PIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564347124   733 KDQIELCAMSEKQEQLY-----SGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHP 783
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqtfllKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
DEXDc smart00487
DEAD-like helicases superfamily;
495-674 4.29e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 4.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124    495 LKPYQKVGLNWLalvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVP-ASTIDNWLREVNLWCP--TLNV 571
Cdd:smart00487    9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPslGLKV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124    572 LCYYGSQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRRlKLNYAIFDEGHMLKNMGsiRYQHLMTI-----N 646
Cdd:smart00487   86 VGLYGGDSKREQLRKLESGK---TDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGG--FGDQLEKLlkllpK 159
                           170       180       190
                    ....*....|....*....|....*....|.
gi 564347124    647 ARNRLLLTGTP---VQNNLLELMSLLNFVMP 674
Cdd:smart00487  160 NVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
484-995 4.18e-143

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 443.90  E-value: 4.18e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVN 563
Cdd:COG0553   233 SLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  564 LWCPTLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 643
Cdd:COG0553   311 KFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  644 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVKE 723
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTKE 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  724 EVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytaeklkemsQ 800
Cdd:COG0553   456 DVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP----------------A 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  801 LMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRTLGCILSELKQKGDRVVLFSQFTMM 880
Cdd:COG0553   520 LLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDT 561
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  881 LDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDR 960
Cdd:COG0553   562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDR 641
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 564347124  961 CHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 995
Cdd:COG0553   642 AHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
495-677 1.19e-124

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: 377.11  E-value: 1.19e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCY 574
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLT 654
Cdd:cd17998    81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                         170       180
                  ....*....|....*....|...
gi 564347124  655 GTPVQNNLLELMSLLNFVMPHMF 677
Cdd:cd17998   161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
474-996 1.15e-111

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 370.29  E-value: 1.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  474 LTGNGGGWNIEQPSLLNQSLslKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPA 552
Cdd:PLN03142  151 LGGSGGTRLLVQPSCIKGKM--RDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  553 STIDNWLREVNLWCPTLNVLCYYGSQEERKQIRFNIHNKyEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLK 632
Cdd:PLN03142  229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVA-GKFDVCVTSFEMAIK---EKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  633 NMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKpADEQsiyekERIAHAKQI 712
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQISGE-NDQQ-----EVVQQLHKV 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  713 IKPFILRRVKEEVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQyyta 792
Cdd:PLN03142  378 LRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQG---- 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  793 eklkemsqlmlkepthCEANPdlifedmevmtdfelhvlckqyqhinSYQLDMDLILDSGKFRTLGCILSELKQKGDRVV 872
Cdd:PLN03142  454 ----------------AEPGP--------------------------PYTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  873 LFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTD-MDIFVFLLSTKAGGLGINLTSANVVILHDIDCNP 951
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 564347124  952 YNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLE 996
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALD 616
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
495-677 1.49e-81

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: 262.50  E-value: 1.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKErGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRfnIHNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd17919    81 YHGSQRERAQIR--AKEKLDKFDVVLTTYETL---RRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155
                         170       180
                  ....*....|....*....|....
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMF 677
Cdd:cd17919   156 TGTPLQNNLEELWALLDFLDPPFL 179
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
495-720 7.42e-79

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: 256.90  E-value: 7.42e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLaCEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd18003    81 YYGSAKERKLKRQGWMKPNS-FHVCITSYQLVVQ---DHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFSS-KTKPADEQSIYEKERIAHAKQIIKPFILRR 720
Cdd:cd18003   157 TGTPLQNSLMELWSLMHFLMPHIFQSHQ-EFKEWFSNpLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
498-783 8.04e-78

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: 256.46  E-value: 8.04e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   498 YQKVGLNWL-ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK--GPHLIVVPASTIDNWLREVNLWC--PTLNVL 572
Cdd:pfam00176    1 YQIEGVNWMlSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   573 CYYGSQEERKQIrFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLL 652
Cdd:pfam00176   81 VLHGNKRPQERW-KNDPNFLADFDVVITTYETLRK---HKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   653 LTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSktkpaDEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPK 732
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSL-STFRNWFDR-----PIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564347124   733 KDQIELCAMSEKQEQLY-----SGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHP 783
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqtfllKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
495-722 1.33e-74

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: 245.76  E-value: 1.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCY 574
Cdd:cd18009     4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLLY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRFNIHNK---YEDYNVIVTTYNCAIsssDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRL 651
Cdd:cd18009    84 HGTKEERERLRKKIMKRegtLQDFPVVVTSYEIAM---RDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564347124  652 LLTGTPVQNNLLELMSLLNFVMPHMFSS-STSEIRRMFSSKTKPADEQSIYEKERIAHA----KQIIKPFILRRVK 722
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPDVFDDlSSFESWFDFSSLSDNAADISNLSEEREQNIvhmlHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
495-722 5.17e-72

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: 237.99  E-value: 5.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd17997     4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNInGPHLIIVPKSTLDNWMREFKRWCPSLRVVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIHnKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd17997    84 LIGDKEERADIIRDVL-LPGKFDVCITSYEMVIK---EKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQsiyekERIAHAKQIIKPFILRRVK 722
Cdd:cd17997   160 TGTPLQNNLHELWALLNFLLPDVFTSS-EDFDEWFNVNNCDDDNQ-----EVVQRLHKVLRPFLLRRIK 222
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
495-722 1.16e-69

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: 231.30  E-value: 1.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCY 574
Cdd:cd18012     5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRfnihnKYEDYNVIVTTYNcaisssddrsLFRRL-------KLNYAIFDEGHMLKNMGSIRYQHLMTINA 647
Cdd:cd18012    85 HGTKRKREKLR-----ALEDYDLVITSYG----------LLRRDiellkevKFHYLVLDEAQNIKNPQTKTAKAVKALKA 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564347124  648 RNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSsktKPADEQSiyEKERIAHAKQIIKPFILRRVK 722
Cdd:cd18012   150 DHRLALTGTPIENHLGELWSIFDFLNPGLLGSY-KRFKKRFA---KPIEKDG--DEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
495-722 4.29e-65

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: 219.16  E-value: 4.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd17996     4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEkKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIhnKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMT-INARNRLL 652
Cdd:cd17996    84 YKGTPDVRKKLQSQI--RAGKFNVLLTTYEYIIK---DKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564347124  653 LTGTPVQNNLLELMSLLNFVMPHMFSSSTSeIRRMFS---SKTKPADEQSIYEKER---IAHAKQIIKPFILRRVK 722
Cdd:cd17996   159 LTGTPLQNNLPELWALLNFLLPKIFKSCKT-FEQWFNtpfANTGEQVKIELNEEETlliIRRLHKVLRPFLLRRLK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
495-720 2.82e-63

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: 213.91  E-value: 2.82e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIwGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIHNK---YED--YNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINAR 648
Cdd:cd18002    81 YWGNPKDRKVLRKFWDRKnlyTRDapFHVVITSYQLVVQ---DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564347124  649 NRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKP-ADEQSIYEKERIAHAKQIIKPFILRR 720
Cdd:cd18002   158 NRLLLTGTPIQNSMAELWALLHFIMPTLFDSH-DEFNEWFSKDIEShAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
495-720 9.54e-63

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: 212.22  E-value: 9.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQyGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARN 649
Cdd:cd17993    82 YLGDIKSRDTIReyefYFSQTKKLKFNVLLTTYEIILK---DKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564347124  650 RLLLTGTPVQNNLLELMSLLNFVMPHMFssstsEIRRMFSsktkpaDEQSIYEKERIAHAKQIIKPFILRR 720
Cdd:cd17993   159 RLLITGTPLQNSLKELWALLHFLMPGKF-----DIWEEFE------EEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
495-720 4.81e-60

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: 204.79  E-value: 4.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCpTLNVLC 573
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGiRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIR 638
Cdd:cd17995    80 YHGSGESRQIIQ-----QYEMYfkdaqgrkkkgvykfDVLITTYEMVIA---DAEELRKIPWRVVVVDEAHRLKNRNSKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  639 YQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFsSKTKPADEqsiyekerIAHAKQIIKPFIL 718
Cdd:cd17995   152 LQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE-EFLEEF-GDLKTAEQ--------VEKLQALLKPYML 221

                  ..
gi 564347124  719 RR 720
Cdd:cd17995   222 RR 223
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
851-976 3.62e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.38  E-value: 3.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  851 SGKFRTLGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAG 930
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564347124  931 GLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLI 976
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
495-720 3.62e-54

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: 188.35  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCY 574
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YG-SQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRR--LKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRL 651
Cdd:cd18001    81 HGtSKKERERNLERIQRG---GGVLLTTYGMVLSNTEQLSADDHdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564347124  652 LLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERI------AHAKQIIKPFILRR 720
Cdd:cd18001   158 ILTGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgsevaENLRQIIKPYFLRR 232
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
495-720 1.45e-53

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: 186.10  E-value: 1.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIHNkYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd18006    81 YMGDKEKRLDLQQDIKS-TNRFHVLLTTYEICLK---DASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMFSSSTSEirRMFSSKTKPADEQSIYEKeriahAKQIIKPFILRR 720
Cdd:cd18006   157 TGTPIQNSLQELYALLSFIEPNVFPKDKLD--DFIKAYSETDDESETVEE-----LHLLLQPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
495-733 2.98e-51

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: 180.63  E-value: 2.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18064    16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNiPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd18064    96 LIGDKDQRAAFVRDVLLPGE-WDVCVTSYEMLIK---EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQSIyekERIahaKQIIKPFILRRVKEEVLKLLPPKK 733
Cdd:cd18064   172 TGTPLQNNLHELWALLNFLLPDVFNSA-EDFDSWFDTNNCLGDQKLV---ERL---HMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
484-720 2.15e-50

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: 177.89  E-value: 2.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLL-NQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLF-QEGNKGPHLIVVPASTIDNWLRE 561
Cdd:cd18054     9 KQPSYIgGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  562 VNLWCPTLNVLCYYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSI 637
Cdd:cd18054    89 FEIWAPEINVVVYIGDLMSRNTIReyewIHSQTKRLKFNALITTYEILLK---DKTVLGSINWAFLGVDEAHRLKNDDSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  638 RYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstSEIRRMFSSKTKPADEQSIYekeriahakQIIKPFI 717
Cdd:cd18054   166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEF--WEDFEEDHGKGRENGYQSLH---------KVLEPFL 234

                  ...
gi 564347124  718 LRR 720
Cdd:cd18054   235 LRR 237
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
484-722 1.04e-47

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: 170.20  E-value: 1.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLLNQSlSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREV 562
Cdd:cd18065     6 ESPSYVKGG-TLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNiPGPHMVLVPKSTLHNWMNEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  563 NLWCPTLNVLCYYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 642
Cdd:cd18065    85 KRWVPSLRAVCLIGDKDARAAFIRDVMMPGE-WDVCVTSYEMVIK---EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  643 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQSIyekERIaHAkqIIKPFILRRVK 722
Cdd:cd18065   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSA-DDFDSWFDTKNCLGDQKLV---ERL-HA--VLKPFLLRRIK 233
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
495-720 3.89e-47

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


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 168.30  E-value: 3.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLA---YLFQEGNKG---PHLIVVPASTIDNWLREVNLWCPT 568
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhHKRANSFNSenlPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  569 --LNVLCYYGSQEERKQIRFNIHNKyedyNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTIN 646
Cdd:cd17999    81 afLKPLAYVGPPQERRRLREQGEKH----NVIVASYDVLRNDIE---VLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  647 ARNRLLLTGTPVQNNLLELMSLLNFVMPHmFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQI------IKPFILRR 720
Cdd:cd17999   154 ANHRLILSGTPIQNNVLELWSLFDFLMPG-YLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALealhkqVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
495-674 7.22e-46

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: 163.26  E-value: 7.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVL- 572
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  573 ----CYYGSQEERKQIRFN----IHNKYEDYNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMG---SIRYQH 641
Cdd:cd18000    81 lhssGSGTGSEEKLGSIERksqlIRKVVGDGGILITTYEGFRKHKD---LLLNHNWQYVILDEGHKIRNPDaeiTLACKQ 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 564347124  642 LMTInarNRLLLTGTPVQNNLLELMSLLNFVMP 674
Cdd:cd18000   158 LRTP---HRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
484-720 7.42e-44

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: 159.06  E-value: 7.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  484 EQPSLL--NQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLR 560
Cdd:cd18053     8 KQPSYIggHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQlYGPFLLVVPLSTLTSWQR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  561 EVNLWCPTLNVLCYYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGS 636
Cdd:cd18053    88 EIQTWAPQMNAVVYLGDINSRNMIRthewMHPQTKRLKFNILLTTYEILLK---DKSFLGGLNWAFIGVDEAHRLKNDDS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  637 IRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstSEIRRMFSSKTKPADEQSIYEKeriahakqiIKPF 716
Cdd:cd18053   165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSS--WEDFEEEHGKGREYGYASLHKE---------LEPF 233

                  ....
gi 564347124  717 ILRR 720
Cdd:cd18053   234 LLRR 237
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
483-722 7.64e-43

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: 156.74  E-value: 7.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  483 IEQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLRE 561
Cdd:cd18062    12 VEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRiNGPFLIIVPLSTLSNWVYE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  562 VNLWCPTLNVLCYYGSQEERKQirFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQH 641
Cdd:cd18062    92 FDKWAPSVVKVSYKGSPAARRA--FVPQLRSGKFNVLLTTYEYIIK---DKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  642 LMT-INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKER----IAHAKQIIKPF 716
Cdd:cd18062   167 LNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIF-KSCSTFEQWFNAPFAMTGEKVDLNEEEtiliIRRLHKVLRPF 245

                  ....*.
gi 564347124  717 ILRRVK 722
Cdd:cd18062   246 LLRRLK 251
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
495-720 7.82e-43

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: 154.90  E-value: 7.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHsKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSqeerkqirfnihnkyedyNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 653
Cdd:cd17994    81 YVGD------------------HVLLTSYELI---SIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLL 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564347124  654 TGTPVQNNLLELMSLLNFVMPHMFSSSTSeirrmFSsktkpADEQSIYEKERIAHAKQIIKPFILRR 720
Cdd:cd17994   140 TGTPLQNNLEELFHLLNFLTPERFNNLQG-----FL-----EEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
483-722 8.22e-43

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: 156.76  E-value: 8.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  483 IEQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLRE 561
Cdd:cd18063    12 VEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  562 VNLWCPTLNVLCYYGSQEERKQIRFNIHNKyeDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQH 641
Cdd:cd18063    92 FDKWAPSVVKISYKGTPAMRRSLVPQLRSG--KFNVLLTTYEYIIK---DKHILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  642 LMT-INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKER----IAHAKQIIKPF 716
Cdd:cd18063   167 LNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIF-KSCSTFEQWFNAPFAMTGERVDLNEEEtiliIRRLHKVLRPF 245

                  ....*.
gi 564347124  717 ILRRVK 722
Cdd:cd18063   246 LLRRLK 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
495-720 5.19e-42

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: 153.98  E-value: 5.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLaLVHkhGlnGILADEMGLGKTIQAIA----------FLAYLFQEGNKGPH--------LIVVPASTID 556
Cdd:cd18008     1 LLPYQKQGLAWM-LPR--G--GILADEMGLGKTIQALAlilatrpqdpKIPEELEENSSDPKklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  557 NWLREVN--LWCPTLNVLCYYGSQeerkqirfNIHNKYE--DYNVIVTTYN-CAISSSDDRSLFRRLKLNYA-------- 623
Cdd:cd18008    76 QWKDEIEkhTKPGSLKVYVYHGSK--------RIKSIEElsDYDIVITTYGtLASEFPKNKKGGGRDSKEKEasplhrir 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  624 ----IFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNF--VMP-HMFSSSTSEIRRMFSSktkpad 696
Cdd:cd18008   148 wyrvILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFlrVEPfGDYPWFNSDISKPFSK------ 221
                         250       260
                  ....*....|....*....|....
gi 564347124  697 eqsiYEKERIAHAKQIIKPFILRR 720
Cdd:cd18008   222 ----NDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
495-720 6.23e-40

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: 147.82  E-value: 6.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWL--ALVHKHGLNG---ILADEMGLGKTIQAIAFLAYLFQEG-NKGPH----LIVVPASTIDNWLREVNL 564
Cdd:cd18004     1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGpYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  565 WCP--TLNVLCYYGSQEERKQIRFNIhNKYEDYNVIVTTYNCAISSSddRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 642
Cdd:cd18004    81 WLGlrRIKVVTADGNAKDVKASLDFF-SSASTYPVLIISYETLRRHA--EKLSKKISIDLLICDEGHRLKNSESKTTKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  643 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMF------SSKTKPADEQSIYEKERIAHAKQIIKPF 716
Cdd:cd18004   158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSL-ASFRKVFeepilrSRDPDASEEDKELGAERSQELSELTSRF 236

                  ....
gi 564347124  717 ILRR 720
Cdd:cd18004   237 ILRR 240
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
495-720 8.77e-40

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: 147.11  E-value: 8.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpTLNVLCY 574
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQI-RFNIHNKYED---------YNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMT 644
Cdd:cd18058    80 HGSQISRQMIqQYEMYYRDEQgnplsgifkFQVVITTFEMILA---DCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564347124  645 INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILRR 720
Cdd:cd18058   157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
495-720 3.38e-37

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: 139.40  E-value: 3.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpTLNVLCY 574
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRFN-----------IHNKYEdYNVIVTTYNCAISSSDDrslFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 643
Cdd:cd18059    80 HGSQASRRTIQLYemyfkdpqgrvIKGSYK-FHAIITTFEMILTDCPE---LRNIPWRCVVIDEAHRLKNRNCKLLEGLK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564347124  644 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILRR 720
Cdd:cd18059   156 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKT----------EEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
495-720 5.59e-37

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: 139.03  E-value: 5.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpTLNVLCY 574
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRY 639
Cdd:cd18060    80 HGSLASRQMIQ-----QYEMYckdsrgrlipgaykfDALITTFEMILS---DCPELREIEWRCVIIDEAHRLKNRNCKLL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  640 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILR 719
Cdd:cd18060   152 DSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT----------EEQVQKLQAILKPMMLR 221

                  .
gi 564347124  720 R 720
Cdd:cd18060   222 R 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
495-720 9.71e-37

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: 138.66  E-value: 9.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEG-NKGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 634
Cdd:cd18057    81 YTGDKESRSVIREN-EFSFEDnairsgkkvfrmkkeaqikFHVLLTSYELI---TIDQAILGSIEWACLVVDEAHRLKNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  635 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 714
Cdd:cd18057   157 QSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-------AD---ISKEDQIKKLHDLLG 226

                  ....*.
gi 564347124  715 PFILRR 720
Cdd:cd18057   227 PHMLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
495-690 2.43e-36

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: 137.42  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLN--WLALVHKHGLNG-----ILADEMGLGKTIQAIAFLAYLFQEGNKGPH-LIVVPASTIDNWLREVNLWC 566
Cdd:cd18007     1 LKPHQVEGVRflWSNLVGTDVGSDegggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRpLVLCPASTLYNWEDEFKKWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  567 P----TLNVLCYYGSQEERKQIRFNIHNKYED-------YNVIVTTYNCAISSSDDRSLFRRLKL----NYAIFDEGHML 631
Cdd:cd18007    81 PpdlrPLLVLVSLSASKRADARLRKINKWHKEggvlligYELFRNLASNATTDPRLKQEFIAALLdpgpDLLVLDEGHRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564347124  632 KNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFSS 690
Cdd:cd18007   161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK-EFKKKFVK 218
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
495-720 1.50e-35

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: 135.14  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHtKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 634
Cdd:cd18055    81 YTGDKDSRAIIREN-EFSFDDnavkggkkafkmkreaqvkFHVLLTSYELV---TIDQAALGSIRWACLVVDEAHRLKNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  635 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 714
Cdd:cd18055   157 QSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-------AD---ISKEDQIKKLHDLLG 226

                  ....*.
gi 564347124  715 PFILRR 720
Cdd:cd18055   227 PHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
495-720 1.90e-35

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: 134.81  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEG-NKGPHLIVVPASTIDNWLREVNLWCPTLNVLC 573
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 634
Cdd:cd18056    81 YVGDKDSRAIIREN-EFSFEDnairggkkasrmkkeasvkFHVLLTSYELI---TIDMAILGSIDWACLIVDEAHRLKNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  635 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 714
Cdd:cd18056   157 QSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF-------AD---IAKEDQIKKLHDMLG 226

                  ....*.
gi 564347124  715 PFILRR 720
Cdd:cd18056   227 PHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
495-720 2.73e-35

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: 134.81  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ---------------------EGNKGPHLIVVPAS 553
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrennrprfkkkppaSSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  554 TIDNWLREVNLWcPTLNVLCYYGSQEERKQIRFNIHNKYEdynVIVTTYncaisssddrSLFRR-------LKLNYAIFD 626
Cdd:cd18005    81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGRLKAGRLE---VVVTTY----------DTLRRcidslnsINWSAVIAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  627 EGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFS-------SKTKPADEQS 699
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSR-SQFKKHFSepikrgqRHTATARELR 225
                         250       260
                  ....*....|....*....|.
gi 564347124  700 IYEKeRIAHAKQIIKPFILRR 720
Cdd:cd18005   226 LGRK-RKQELAVKLSKFFLRR 245
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
495-720 1.94e-33

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: 128.58  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpTLNVLCY 574
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 YGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISSSDDrslFRRLKLNYAIFDEGHMLKNMGSIRY 639
Cdd:cd18061    80 HGSLISRQMIQ-----QYEMYfrdsqgriirgayrfQAIITTFEMILGGCPE---LNAIDWRCVIIDEAHRLKNKNCKLL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  640 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILR 719
Cdd:cd18061   152 EGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT----------EEQVQKLQAILKPMMLR 221

                  .
gi 564347124  720 R 720
Cdd:cd18061   222 R 222
DEXDc smart00487
DEAD-like helicases superfamily;
495-674 4.29e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 4.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124    495 LKPYQKVGLNWLalvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVP-ASTIDNWLREVNLWCP--TLNV 571
Cdd:smart00487    9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPslGLKV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124    572 LCYYGSQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRRlKLNYAIFDEGHMLKNMGsiRYQHLMTI-----N 646
Cdd:smart00487   86 VGLYGGDSKREQLRKLESGK---TDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGG--FGDQLEKLlkllpK 159
                           170       180       190
                    ....*....|....*....|....*....|.
gi 564347124    647 ARNRLLLTGTP---VQNNLLELMSLLNFVMP 674
Cdd:smart00487  160 NVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
495-686 4.57e-30

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 118.46  E-value: 4.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWlALvhKHGLNGILADEMGLGKTIQAIAFLAYLFQEgnkGPHLIVVPASTIDNWLREVNLWCPTLNVlcy 574
Cdd:cd18010     1 LLPFQREGVCF-AL--RRGGRVLIADEMGLGKTVQAIAIAAYYREE---WPLLIVCPSSLRLTWADEIERWLPSLPP--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  575 ygsqeerkqirfnihnkyEDYNVIVTTyNCAISSSDDR------SLFRRL-------KLNYAIFDEGHMLKNMGSIRYQH 641
Cdd:cd18010    72 ------------------DDIQVIVKS-KDGLRDGDAKvvivsyDLLRRLekqllarKFKVVICDESHYLKNSKAKRTKA 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564347124  642 LMTI--NARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRR 686
Cdd:cd18010   133 ALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRR 179
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
495-720 9.05e-29

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: 115.71  E-value: 9.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWL-----ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPH------LIVVPASTIDNWLREVN 563
Cdd:cd18066     1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKpvikraLIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  564 LWCPTLNVLCYYGSQEerKQIRFNIHNKYedYNVIVTTYNCAISSSDDrslFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 643
Cdd:cd18066    81 KWLGSERIKVFTVDQD--HKVEEFIASPL--YSVLIISYEMLLRSLDQ---ISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  644 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKE------RIAHAKQIIKPFI 717
Cdd:cd18066   154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGIL-GSLSTYRKVYEEPIVRSREPTATPEEkklgeaRAAELTRLTGLFI 232

                  ...
gi 564347124  718 LRR 720
Cdd:cd18066   233 LRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
495-720 1.81e-26

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: 109.10  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWL----ALVHKHGLNG-ILADEMGLGKTIQAIAFLAYLFQEGNKGPHLI-----VVPASTIDNWLREVNL 564
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  565 WC-PTLNVLCYYGSQEE---RKQIRF-NIHNKYEDYNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMGSIRY 639
Cdd:cd18067    81 WLgGRLQPLAIDGGSKKeidRKLVQWaSQQGRRVSTPVLIISYETFRLHVE---VLQKGEVGLVICDEGHRLKNSDNQTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  640 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSS---KTKPAD--EQSIYE-KERIAHAKQII 713
Cdd:cd18067   158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTA-AEFKKNFELpilKGRDADasEKERQLgEEKLQELISIV 236

                  ....*..
gi 564347124  714 KPFILRR 720
Cdd:cd18067   237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
852-965 1.48e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 101.90  E-value: 1.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   852 GKFRTLGCILSelKQKGDRVVLFSQFTMMLDIlEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDmDIFVfLLSTKAGG 931
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 564347124   932 LGINLTSANVVILHDIDCNPYNDKQAEDRCHRVG 965
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
513-688 3.91e-25

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: 104.90  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  513 GLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCP-----------TLNVLCYYGSQEER 581
Cdd:cd18069    28 GFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPppealpnvrprPFKVFILNDEHKTT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  582 KQiRFNIHNKY-EDYNVIVTTYncaisssddrSLFR-RLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQ 659
Cdd:cd18069   108 AA-RAKVIEDWvKDGGVLLMGY----------EMFRlRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQ 176
                         170       180
                  ....*....|....*....|....*....
gi 564347124  660 NNLLELMSLLNFVMPHMFSSSTsEIRRMF 688
Cdd:cd18069   177 NNLIEYWCMVDFVRPDFLGTRQ-EFSNMF 204
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
495-719 2.03e-23

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: 100.88  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLaLVHKhglnGILADEMGLGKTIQAIAFL------------AYLFQEGNK--------------GPHLI 548
Cdd:cd18070     1 LLPYQRRAVNWM-LVPG----GILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVccpdclvaetpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  549 VVPASTIDNWLREVNLWCPT-LNVLCYYGsQEERKQIRFNIHNKYEDYNVIVTTYN-------CAISSSDDRSLfRRLKL 620
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSsLKVLTYQG-VKKDGALASPAPEILAEYDIVVTTYDvlrtelhYAEANRSNRRR-RRQKR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  621 NYAI-------------FDEGHMLKnmGSIRYQHLMT--INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIR 685
Cdd:cd18070   154 YEAPpsplvlvewwrvcLDEAQMVE--SSTSKAAEMArrLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWAR 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 564347124  686 RMFssktkpadeQSIYEKERIAHAKQIIKPFILR 719
Cdd:cd18070   232 VLI---------RPQGRNKAREPLAALLKELLWR 256
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
513-672 9.85e-23

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 98.31  E-value: 9.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  513 GLNGILADEMGLGKTIQAIAFLayLFQegnkgPHLIVVPASTIDNWLREV--NLWCPTLNVLCYYGSQEERKQirfnihN 590
Cdd:cd18071    48 VRGGILADDMGLGKTLTTISLI--LAN-----FTLIVCPLSVLSNWETQFeeHVKPGQLKVYTYHGGERNRDP------K 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  591 KYEDYNVIVTTYNCAIS--SSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSL 668
Cdd:cd18071   115 LLSKYDIVLTTYNTLASdfGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194

                  ....
gi 564347124  669 LNFV 672
Cdd:cd18071   195 LSFL 198
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
495-670 6.39e-22

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 95.05  E-value: 6.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNwLALVHKHgLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREvnLW-CPTLNVLC 573
Cdd:cd18011     1 PLPHQIDAVL-RALRKPP-VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDE--LQdKFGLPFLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  574 YYGsqEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTI------NA 647
Cdd:cd18011    77 LDR--ETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRA 154
                         170       180
                  ....*....|....*....|....*.
gi 564347124  648 RNRLLLTGTPVQNN---LLELMSLLN 670
Cdd:cd18011   155 RHVLLLTATPHNGKeedFRALLSLLD 180
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
495-688 1.29e-21

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: 95.34  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWL---------ALVHKHGLNGILADEMGLGKTIQAIAFLAYLF---QEGNKGPHLIVVPASTIDNWLREV 562
Cdd:cd18068     1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLlceKLENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  563 NLWCPTLN--------VLCYYGSQEERkqiRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKL-------------N 621
Cdd:cd18068    81 EKWQEGLKdeekievnELATYKRPQER---SYKLQRWQEEGGVMIIGYDMYRILAQERNVKSREKLkeifnkalvdpgpD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564347124  622 YAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMF 688
Cdd:cd18068   158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIK-EFRNRF 223
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
495-720 4.76e-21

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: 93.31  E-value: 4.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLALVHKHGLNG-ILADEMGLGKTIQAIAFLayLFQEGNK-------------------------GPHLI 548
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALI--LAQKNTQnrkeeekekalteweskkdstlvpsAGTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  549 VVPASTIDNWLREVN--LWCPTLNVLCYYGSQEERKQIRFnihnkyEDYNVIVTTYNCAIS------SSDDRSLFRRLKL 620
Cdd:cd18072    79 VCPASLVHQWKNEVEsrVASNKLRVCLYHGPNRERIGEVL------RDYDIVITTYSLVAKeiptykEESRSSPLFRIAW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  621 NYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstseirrmFSSKTKPADEQSI 700
Cdd:cd18072   153 ARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDD--------LKVWKKQVDNKSR 224
                         250       260
                  ....*....|....*....|
gi 564347124  701 YEKERIAhakQIIKPFILRR 720
Cdd:cd18072   225 KGGERLN---ILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
882-965 8.84e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.57  E-value: 8.84e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124    882 DILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMdiFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRC 961
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 564347124    962 HRVG 965
Cdd:smart00490   79 GRAG 82
ResIII pfam04851
Type III restriction enzyme, res subunit;
493-657 9.03e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 61.53  E-value: 9.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   493 LSLKPYQKVGL-NWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDN-WLREVNLWCPTLN 570
Cdd:pfam04851    2 LELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEqALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   571 VLCYYGSQEERKQIrfnihnkYEDYNVIVTTYNCAISSSDDRSL-FRRLKLNYAIFDEGHMLknmGSIRYQHLMTINARN 649
Cdd:pfam04851   82 EIGEIISGDKKDES-------VDDNKIVVTTIQSLYKALELASLeLLPDFFDVIIIDEAHRS---GASSYRNILEYFKPA 151

                   ....*....
gi 564347124   650 RLL-LTGTP 657
Cdd:pfam04851  152 FLLgLTATP 160
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
495-665 3.83e-10

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 60.83  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGLNWLAlvhKHGLNGILADeMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTI-DNWLREVNLW--CPTLNV 571
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  572 LCYYGSQEERkqirfnihNKYEDYNVIVTTYN-----CAISSSDDRSLFRRLklnyaIFDEGHMLKNMGSIRYQHLMTIN 646
Cdd:cd18013    77 SVAVGTERQR--------SKAANTPADLYVINrenlkWLVNKSGDPWPFDMV-----VIDELSSFKSPRSKRFKALRKVR 143
                         170       180
                  ....*....|....*....|.
gi 564347124  647 AR-NRLL-LTGTPVQNNLLEL 665
Cdd:cd18013   144 PViKRLIgLTGTPSPNGLMDL 164
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
492-658 1.97e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.58  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  492 SLSLKPYQKVGLN-WLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFqegNKGPHLIVVPASTI-DNWLREVnlwcptl 569
Cdd:COG1061    78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELL---RGKRVLVLVPRRELlEQWAEEL------- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  570 nvlcyygsQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLnyAIFDEGHmlkNMGSIRYQHLMT-INAR 648
Cdd:COG1061   148 --------RRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGL--VIIDEAH---HAGAPSYRRILEaFPAA 214
                         170
                  ....*....|
gi 564347124  649 NRLLLTGTPV 658
Cdd:COG1061   215 YRLGLTATPF 224
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
495-657 2.56e-09

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 56.93  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  495 LKPYQKVGL-NWLAlvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEgnkgPHLIVVP-ASTIDNWLREvnlwcptlnvL 572
Cdd:cd17926     1 LRPYQEEALeAWLA--HKNNRRGILVLPTGSGKTLTALALIAYLKEL----RTLIVVPtDALLDQWKER----------F 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  573 CYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLnYAIFDEGHmlkNMGSIRYQHLMTI-NARNRL 651
Cdd:cd17926    65 EDFLGDSSIGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG-LLIVDEAH---HLPAKTFSEILKElNAKYRL 140

                  ....*.
gi 564347124  652 LLTGTP 657
Cdd:cd17926   141 GLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
515-656 2.61e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.17  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  515 NGILADEMGLGKTIQAIAFLAYLFqEGNKGPHLIVVPASTIDN----WLREvnLWCPTLNVLCYYG--SQEERKQIRFNi 588
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALqtaeRLRE--LFGPGIRVAVLVGgsSAEEREKNKLG- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564347124  589 hnkyeDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHML------KNMGSIRYQHLMTINARnRLLLTGT 656
Cdd:cd00046    79 -----DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlidsrgALILDLAVRKAGLKNAQ-VILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
523-660 2.83e-05

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: 45.70  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124   523 GLGKTiqAIAFLAYL--FQEGNKGPH-LIVVP--------ASTIDNWLREVNLwcptlNVLCYYGSQEERKQIRfnihnK 591
Cdd:pfam00270   24 GSGKT--LAFLLPALeaLDKLDNGPQaLVLAPtrelaeqiYEELKKLGKGLGL-----KVASLLGGDSRKEQLE-----K 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564347124   592 YEDYNVIVTTYNCAISSSDDRSLFRRLKlnYAIFDEGHMLKNMGsiRYQHLMTI-----NARNRLLLTGTPVQN 660
Cdd:pfam00270   92 LKGPDILVGTPGRLLDLLQERKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEIlrrlpKKRQILLLSATLPRN 161
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
852-943 2.56e-03

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 39.54  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  852 GKFRTLGCILSELKQkGDRVVLFSQFTMMLD-ILEVLLKhhqhrYLrLDGKTQISERIHLIDEF-----NTdmdIFVfll 925
Cdd:cd18789    34 NKLRALEELLKRHEQ-GDKIIVFTDNVEALYrYAKRLLK-----PF-ITGETPQSEREEILQNFregeyNT---LVV--- 100
                          90
                  ....*....|....*...
gi 564347124  926 sTKAGGLGINLTSANVVI 943
Cdd:cd18789   101 -SKVGDEGIDLPEANVAI 117
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
518-659 8.51e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 40.21  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  518 LADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVnlwcptlnvlcyygsqeERkqiRFNIH-------- 589
Cdd:PRK04914  174 LADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLVEM-----------------LR---RFNLRfslfdeer 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564347124  590 ---NKYEDYNVIVTTyNCAISSSDdrsLFRRLKLNY----------AIFDEGHML---KNMGSIRYQHLMTINARNR--L 651
Cdd:PRK04914  234 yaeAQHDADNPFETE-QLVICSLD---FLRRNKQRLeqalaaewdlLVVDEAHHLvwsEEAPSREYQVVEQLAEVIPgvL 309

                  ....*...
gi 564347124  652 LLTGTPVQ 659
Cdd:PRK04914  310 LLTATPEQ 317
 
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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