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Conserved domains on  [gi|358438428|ref|NP_001240321|]
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 isoform 2 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

EC:  3.6.4.-
Gene Ontology:  GO:0004386

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, ...
295-807 1.65e-145

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 444.67  E-value: 1.65e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 295 REQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREV 374
Cdd:COG0553  232 ESLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:COG0553  310 AKFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAV 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVK 534
Cdd:COG0553  382 RALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTK 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 535 EEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytpeklkems 611
Cdd:COG0553  455 EDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP---------------- 518
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 612 QLMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRALGCILSELKQKGDRVVLFSQFTM 691
Cdd:COG0553  519 ALLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 692 MLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAED 771
Cdd:COG0553  561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 358438428 772 RCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 807
Cdd:COG0553  641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
295-807 1.65e-145

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 444.67  E-value: 1.65e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 295 REQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREV 374
Cdd:COG0553  232 ESLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:COG0553  310 AKFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAV 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVK 534
Cdd:COG0553  382 RALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTK 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 535 EEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytpeklkems 611
Cdd:COG0553  455 EDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP---------------- 518
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 612 QLMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRALGCILSELKQKGDRVVLFSQFTM 691
Cdd:COG0553  519 ALLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 692 MLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAED 771
Cdd:COG0553  561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 358438428 772 RCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 807
Cdd:COG0553  641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
307-489 3.48e-125

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: 373.64  E-value: 3.48e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCY 386
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLT 466
Cdd:cd17998   81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                        170       180
                 ....*....|....*....|...
gi 358438428 467 GTPVQNNLLELMSLLNFVMPHMF 489
Cdd:cd17998  161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
286-808 3.09e-114

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 372.21  E-value: 3.09e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  286 LTGNGGGWNREQPSLLNQSLslKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPA 364
Cdd:PLN03142  151 LGGSGGTRLLVQPSCIKGKM--RDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  365 STIDNWLREVNLWCPSLNVLCYYGSQEERKQIRFNIHNKyEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLK 444
Cdd:PLN03142  229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVA-GKFDVCVTSFEMAIK---EKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  445 NMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKpADEQsiyekERIAHAKQI 524
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQISGE-NDQQ-----EVVQQLHKV 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  525 IKPFILRRVKEEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQyytp 604
Cdd:PLN03142  378 LRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQG---- 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  605 eklkemsqlmlkepthCEANPdlifedmevmtdfelhvlckqyqhinSYQLDMDLILDSGKFRALGCILSELKQKGDRVV 684
Cdd:PLN03142  454 ----------------AEPGP--------------------------PYTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  685 LFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTD-MDIFVFLLSTKAGGLGINLTSANVVILHDIDCNP 763
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 358438428  764 YNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLE 808
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALD 616
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
310-595 1.80e-77

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: 252.60  E-value: 1.80e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  310 YQKVGLNWL-ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK--GPHLIVVPASTIDNWLREVNLWC--PSLNVL 384
Cdd:pfam00176   1 YQIEGVNWMlSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  385 CYYGSQEERKQIrFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLL 464
Cdd:pfam00176  81 VLHGNKRPQERW-KNDPNFLADFDVVITTYETLRK---HKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  465 LTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSktkpaDEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPK 544
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPGPFGSL-STFRNWFDR-----PIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 358438428  545 KDRIELCAMSEKQEQLY-----SGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHP 595
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqtfllKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
DEXDc smart00487
DEAD-like helicases superfamily;
307-486 6.12e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 123.37  E-value: 6.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428   307 LKPYQKVGLNWLalvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVP-ASTIDNWLREVNLWCPSLN--V 383
Cdd:smart00487   9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGlkV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428   384 LCYYGSQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRRlKLNYAIFDEGHMLKNMGsiRYQHLMTI-----N 458
Cdd:smart00487  86 VGLYGGDSKREQLRKLESGK---TDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGG--FGDQLEKLlkllpK 159
                          170       180       190
                   ....*....|....*....|....*....|.
gi 358438428   459 ARNRLLLTGTP---VQNNLLELMSLLNFVMP 486
Cdd:smart00487 160 NVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
295-807 1.65e-145

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 444.67  E-value: 1.65e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 295 REQPSLLNqsLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREV 374
Cdd:COG0553  232 ESLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQREL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQIrfnihNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:COG0553  310 AKFAPGLRVLVLDGTRERAKGA-----NPFEDADLVITSYGLL---RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAV 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEqsiyekERIAHAKQIIKPFILRRVK 534
Cdd:COG0553  382 RALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL-KAFRERFARPIEKGDE------EALERLRRLLRPFLLRRTK 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 535 EEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNV---MMQLRKMANHPllhrqyytpeklkems 611
Cdd:COG0553  455 EDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLIlaaLTRLRQICSHP---------------- 518
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 612 QLMLKEPThceanpdlifedmevmtdfelhvlckqyqhinsyqldmDLILDSGKFRALGCILSELKQKGDRVVLFSQFTM 691
Cdd:COG0553  519 ALLLEEGA--------------------------------------ELSGRSAKLEALLELLEELLAEGEKVLVFSQFTD 560
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 692 MLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAED 771
Cdd:COG0553  561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAID 640
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 358438428 772 RCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKL 807
Cdd:COG0553  641 RAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
307-489 3.48e-125

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: 373.64  E-value: 3.48e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCY 386
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLT 466
Cdd:cd17998   81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                        170       180
                 ....*....|....*....|...
gi 358438428 467 GTPVQNNLLELMSLLNFVMPHMF 489
Cdd:cd17998  161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
286-808 3.09e-114

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 372.21  E-value: 3.09e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  286 LTGNGGGWNREQPSLLNQSLslKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPA 364
Cdd:PLN03142  151 LGGSGGTRLLVQPSCIKGKM--RDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  365 STIDNWLREVNLWCPSLNVLCYYGSQEERKQIRFNIHNKyEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLK 444
Cdd:PLN03142  229 STLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVA-GKFDVCVTSFEMAIK---EKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  445 NMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKpADEQsiyekERIAHAKQI 524
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQISGE-NDQQ-----EVVQQLHKV 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  525 IKPFILRRVKEEVLKLLPPKKDRIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQyytp 604
Cdd:PLN03142  378 LRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQG---- 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  605 eklkemsqlmlkepthCEANPdlifedmevmtdfelhvlckqyqhinSYQLDMDLILDSGKFRALGCILSELKQKGDRVV 684
Cdd:PLN03142  454 ----------------AEPGP--------------------------PYTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  685 LFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTD-MDIFVFLLSTKAGGLGINLTSANVVILHDIDCNP 763
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 358438428  764 YNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLE 808
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALD 616
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
307-489 1.67e-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: 259.42  E-value: 1.67e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKErGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRfnIHNKYEDYNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd17919   81 YHGSQRERAQIR--AKEKLDKFDVVLTTYETL---RRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155
                        170       180
                 ....*....|....*....|....
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMF 489
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 ...
307-532 5.94e-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: 254.20  E-value: 5.94e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLaCEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd18003   81 YYGSAKERKLKRQGWMKPNS-FHVCITSYQLVVQ---DHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFSS-KTKPADEQSIYEKERIAHAKQIIKPFILRR 532
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 ...
310-595 1.80e-77

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: 252.60  E-value: 1.80e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  310 YQKVGLNWL-ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK--GPHLIVVPASTIDNWLREVNLWC--PSLNVL 384
Cdd:pfam00176   1 YQIEGVNWMlSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  385 CYYGSQEERKQIrFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLL 464
Cdd:pfam00176  81 VLHGNKRPQERW-KNDPNFLADFDVVITTYETLRK---HKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  465 LTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSktkpaDEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPK 544
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPGPFGSL-STFRNWFDR-----PIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 358438428  545 KDRIELCAMSEKQEQLY-----SGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHP 595
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqtfllKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
307-534 3.69e-75

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: 244.60  E-value: 3.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCY 386
Cdd:cd18009    4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLLY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRFNIHNK---YEDYNVIVTTYNCAIsssDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRL 463
Cdd:cd18009   84 HGTKEERERLRKKIMKRegtLQDFPVVVTSYEIAM---RDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358438428 464 LLTGTPVQNNLLELMSLLNFVMPHMFSS-STSEIRRMFSSKTKPADEQSIYEKERIAHA----KQIIKPFILRRVK 534
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDlSSFESWFDFSSLSDNAADISNLSEEREQNIvhmlHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
307-534 2.17e-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: 236.45  E-value: 2.17e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd17997    4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNInGPHLIIVPKSTLDNWMREFKRWCPSLRVVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIHnKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd17997   84 LIGDKEERADIIRDVL-LPGKFDVCITSYEMVIK---EKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQsiyekERIAHAKQIIKPFILRRVK 534
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 ...
307-534 2.60e-70

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: 230.92  E-value: 2.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCY 386
Cdd:cd18012    5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRfnihnKYEDYNVIVTTYNcaisssddrsLFRRL-------KLNYAIFDEGHMLKNMGSIRYQHLMTINA 459
Cdd:cd18012   85 HGTKRKREKLR-----ALEDYDLVITSYG----------LLRRDiellkevKFHYLVLDEAQNIKNPQTKTAKAVKALKA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358438428 460 RNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSsktKPADEQSiyEKERIAHAKQIIKPFILRRVK 534
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 ...
307-534 1.55e-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: 218.39  E-value: 1.55e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ-EGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd17996    4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEkKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIhnKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMT-INARNRLL 464
Cdd:cd17996   84 YKGTPDVRKKLQSQI--RAGKFNVLLTTYEYIIK---DKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358438428 465 LTGTPVQNNLLELMSLLNFVMPHMFSSSTSeIRRMFS---SKTKPADEQSIYEKER---IAHAKQIIKPFILRRVK 534
Cdd:cd17996  159 LTGTPLQNNLPELWALLNFLLPKIFKSCKT-FEQWFNtpfANTGEQVKIELNEEETlliIRRLHKVLRPFLLRRLK 233
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
307-532 2.46e-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: 211.83  E-value: 2.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd17993    2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQyGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARN 461
Cdd:cd17993   82 YLGDIKSRDTIReyefYFSQTKKLKFNVLLTTYEIILK---DKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 358438428 462 RLLLTGTPVQNNLLELMSLLNFVMPHMFssstsEIRRMFSsktkpaDEQSIYEKERIAHAKQIIKPFILRR 532
Cdd:cd17993  159 RLLITGTPLQNSLKELWALLHFLMPGKF-----DIWEEFE------EEHDEEQEKGIADLHKELEPFILRR 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
307-532 2.49e-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: 212.36  E-value: 2.49e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNK-GPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIwGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIHNK---YED--YNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINAR 460
Cdd:cd18002   81 YWGNPKDRKVLRKFWDRKnlyTRDapFHVVITSYQLVVQ---DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 358438428 461 NRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKP-ADEQSIYEKERIAHAKQIIKPFILRR 532
Cdd:cd18002  158 NRLLLTGTPIQNSMAELWALLHFIMPTLFDSH-DEFNEWFSKDIEShAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
307-532 9.83e-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: 202.48  E-value: 9.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPsLNVLC 385
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGiRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIR 450
Cdd:cd17995   80 YHGSGESRQIIQ-----QYEMYfkdaqgrkkkgvykfDVLITTYEMVIA---DAEELRKIPWRVVVVDEAHRLKNRNSKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 451 YQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFSsktkpadeqSIYEKERIAHAKQIIKPFIL 530
Cdd:cd17995  152 LQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE-EFLEEFG---------DLKTAEQVEKLQALLKPYML 221

                 ..
gi 358438428 531 RR 532
Cdd:cd17995  222 RR 223
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
663-788 1.19e-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: 1.19e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 663 SGKFRALGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAG 742
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 358438428 743 GLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLI 788
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
307-532 4.60e-54

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: 186.49  E-value: 4.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIHNkYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd18006   81 YMGDKEKRLDLQQDIKS-TNRFHVLLTTYEICLK---DASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMFSSSTSEirRMFSSKTKPADEQSIYEKeriahAKQIIKPFILRR 532
Cdd:cd18006  157 TGTPIQNSLQELYALLSFIEPNVFPKDKLD--DFIKAYSETDDESETVEE-----LHLLLQPFLLRR 216
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
307-532 7.73e-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: 186.42  E-value: 7.73e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCY 386
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YG-SQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRR--LKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRL 463
Cdd:cd18001   81 HGtSKKERERNLERIQRG---GGVLLTTYGMVLSNTEQLSADDHdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 358438428 464 LLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERI------AHAKQIIKPFILRR 532
Cdd:cd18001  158 ILTGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgsevaENLRQIIKPYFLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
295-532 4.00e-51

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: 179.05  E-value: 4.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 295 REQPSLL-NQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLF-QEGNKGPHLIVVPASTIDNWLR 372
Cdd:cd18054    8 KKQPSYIgGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 373 EVNLWCPSLNVLCYYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGS 448
Cdd:cd18054   88 EFEIWAPEINVVVYIGDLMSRNTIReyewIHSQTKRLKFNALITTYEILLK---DKTVLGSINWAFLGVDEAHRLKNDDS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 449 IRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstSEIRRMFSSKTKPADEQSIYekeriahakQIIKPF 528
Cdd:cd18054  165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEF--WEDFEEDHGKGRENGYQSLH---------KVLEPF 233

                 ....
gi 358438428 529 ILRR 532
Cdd:cd18054  234 LLRR 237
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
307-545 4.41e-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: 179.09  E-value: 4.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18064   16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNiPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd18064   96 LIGDKDQRAAFVRDVLLPGE-WDVCVTSYEMLIK---EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQSIyekERIahaKQIIKPFILRRVKEEVLKLLPPKK 545
Cdd:cd18064  172 TGTPLQNNLHELWALLNFLLPDVFNSA-EDFDSWFDTNNCLGDQKLV---ERL---HMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
296-534 6.87e-48

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: 169.81  E-value: 6.87e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 296 EQPSLLNQSlSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREV 374
Cdd:cd18065    6 ESPSYVKGG-TLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNiPGPHMVLVPKSTLHNWMNEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQIRFNIHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:cd18065   85 KRWVPSLRAVCLIGDKDARAAFIRDVMMPGE-WDVCVTSYEMVIK---EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSSKTKPADEQSIyekERIaHAkqIIKPFILRRVK 534
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 ...
307-532 3.90e-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: 167.53  E-value: 3.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLA---YLFQEGNKG---PHLIVVPASTIDNWLREVNLWCP- 379
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhHKRANSFNSenlPSLVVCPPTLVGHWVAEIKKYFPn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 380 -SLNVLCYYGSQEERKQIRFNIHNKyedyNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTIN 458
Cdd:cd17999   81 aFLKPLAYVGPPQERRRLREQGEKH----NVIVASYDVLRNDIE---VLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 459 ARNRLLLTGTPVQNNLLELMSLLNFVMPHmFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQI------IKPFILRR 532
Cdd:cd17999  154 ANHRLILSGTPIQNNVLELWSLFDFLMPG-YLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALealhkqVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
307-486 4.44e-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: 4.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYL-FQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVL- 384
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 385 ----CYYGSQEERKQIRFN----IHNKYEDYNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMG---SIRYQH 453
Cdd:cd18000   81 lhssGSGTGSEEKLGSIERksqlIRKVVGDGGILITTYEGFRKHKD---LLLNHNWQYVILDEGHKIRNPDaeiTLACKQ 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 358438428 454 LMTInarNRLLLTGTPVQNNLLELMSLLNFVMP 486
Cdd:cd18000  158 LRTP---HRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
295-532 5.07e-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: 5.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 295 REQPSLL--NQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWL 371
Cdd:cd18053    7 KKQPSYIggHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQlYGPFLLVVPLSTLTSWQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 372 REVNLWCPSLNVLCYYGSQEERKQIR----FNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMG 447
Cdd:cd18053   87 REIQTWAPQMNAVVYLGDINSRNMIRthewMHPQTKRLKFNILLTTYEILLK---DKSFLGGLNWAFIGVDEAHRLKNDD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 448 SIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstSEIRRMFSSKTKPADEQSIYEKeriahakqiIKP 527
Cdd:cd18053  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSS--WEDFEEEHGKGREYGYASLHKE---------LEP 232

                 ....*
gi 358438428 528 FILRR 532
Cdd:cd18053  233 FLLRR 237
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
307-532 6.79e-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: 154.52  E-value: 6.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHsKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSqeerkqirfnihnkyedyNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLL 465
Cdd:cd17994   81 YVGD------------------HVLLTSYELI---SIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLL 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358438428 466 TGTPVQNNLLELMSLLNFVMPHMFSSSTSeirrmFSsktkpADEQSIYEKERIAHAKQIIKPFILRR 532
Cdd:cd17994  140 TGTPLQNNLEELFHLLNFLTPERFNNLQG-----FL-----EEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
296-534 1.69e-42

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: 155.20  E-value: 1.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 296 EQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREV 374
Cdd:cd18062   13 EKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRiNGPFLIIVPLSTLSNWVYEF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQirFNIHNKYEDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:cd18062   93 DKWAPSVVKVSYKGSPAARRA--FVPQLRSGKFNVLLTTYEYIIK---DKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MT-INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKER----IAHAKQIIKPFI 529
Cdd:cd18062  168 NThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIF-KSCSTFEQWFNAPFAMTGEKVDLNEEEtiliIRRLHKVLRPFL 246

                 ....*
gi 358438428 530 LRRVK 534
Cdd:cd18062  247 LRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
296-534 1.89e-42

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: 155.22  E-value: 1.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 296 EQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREV 374
Cdd:cd18063   13 EKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYEF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLNVLCYYGSQEERKQIRFNIHNKyeDYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:cd18063   93 DKWAPSVVKISYKGTPAMRRSLVPQLRSG--KFNVLLTTYEYIIK---DKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MT-INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKER----IAHAKQIIKPFI 529
Cdd:cd18063  168 NThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIF-KSCSTFEQWFNAPFAMTGERVDLNEEEtiliIRRLHKVLRPFL 246

                 ....*
gi 358438428 530 LRRVK 534
Cdd:cd18063  247 LRRLK 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
307-532 4.06e-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: 4.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLaLVHkhGlnGILADEMGLGKTIQAIA----------FLAYLFQEGNKGPH--------LIVVPASTID 368
Cdd:cd18008    1 LLPYQKQGLAWM-LPR--G--GILADEMGLGKTIQALAlilatrpqdpKIPEELEENSSDPKklylskttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 369 NWLREVN--LWCPSLNVLCYYGSQeerkqirfNIHNKYE--DYNVIVTTYN-CAISSSDDRSLFRRLKLNYA-------- 435
Cdd:cd18008   76 QWKDEIEkhTKPGSLKVYVYHGSK--------RIKSIEElsDYDIVITTYGtLASEFPKNKKGGGRDSKEKEasplhrir 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 436 ----IFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNF--VMP-HMFSSSTSEIRRMFSSktkpad 508
Cdd:cd18008  148 wyrvILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFlrVEPfGDYPWFNSDISKPFSK------ 221
                        250       260
                 ....*....|....*....|....
gi 358438428 509 eqsiYEKERIAHAKQIIKPFILRR 532
Cdd:cd18008  222 ----NDRKALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
307-532 5.68e-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: 5.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWL--ALVHKHGLNG---ILADEMGLGKTIQAIAFLAYLFQEG-NKGPH----LIVVPASTIDNWLREVNL 376
Cdd:cd18004    1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGpYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 377 WCPS--LNVLCYYGSQEERKQIRFNIhNKYEDYNVIVTTYNCAISSSddRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHL 454
Cdd:cd18004   81 WLGLrrIKVVTADGNAKDVKASLDFF-SSASTYPVLIISYETLRRHA--EKLSKKISIDLLICDEGHRLKNSESKTTKAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 455 MTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMF------SSKTKPADEQSIYEKERIAHAKQIIKPF 528
Cdd:cd18004  158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSL-ASFRKVFeepilrSRDPDASEEDKELGAERSQELSELTSRF 236

                 ....
gi 358438428 529 ILRR 532
Cdd:cd18004  237 ILRR 240
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
307-532 8.86e-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: 146.73  E-value: 8.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpSLNVLCY 386
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQI-RFNIHNKYED---------YNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMT 456
Cdd:cd18058   80 HGSQISRQMIqQYEMYYRDEQgnplsgifkFQVVITTFEMILA---DCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 358438428 457 INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILRR 532
Cdd:cd18058  157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
307-532 2.91e-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: 2.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpSLNVLCY 386
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRFN-----------IHNKYEdYNVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 455
Cdd:cd18059   80 HGSQASRRTIQLYemyfkdpqgrvIKGSYK-FHAIITTFEMILT---DCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358438428 456 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILRR 532
Cdd:cd18059  156 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKT----------EEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
307-532 3.12e-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: 139.42  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpSLNVLCY 386
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISssdDRSLFRRLKLNYAIFDEGHMLKNMGSIRY 451
Cdd:cd18060   80 HGSLASRQMIQ-----QYEMYckdsrgrlipgaykfDALITTFEMILS---DCPELREIEWRCVIIDEAHRLKNRNCKLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 452 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILR 531
Cdd:cd18060  152 DSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT----------EEQVQKLQAILKPMMLR 221

                 .
gi 358438428 532 R 532
Cdd:cd18060  222 R 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
307-532 4.17e-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: 139.43  E-value: 4.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEG-NKGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 446
Cdd:cd18057   81 YTGDKESRSVIREN-EFSFEDnairsgkkvfrmkkeaqikFHVLLTSYELI---TIDQAILGSIEWACLVVDEAHRLKNN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 447 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 526
Cdd:cd18057  157 QSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-------AD---ISKEDQIKKLHDLLG 226

                 ....*.
gi 358438428 527 PFILRR 532
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 ...
307-502 3.56e-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: 136.65  E-value: 3.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLN--WLALVHKHGLNG-----ILADEMGLGKTIQAIAFLAYLFQEGNKGPH-LIVVPASTIDNWLREVNLWC 378
Cdd:cd18007    1 LKPHQVEGVRflWSNLVGTDVGSDegggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRpLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 379 PS----LNVLCYYGSQEERKQIRFNIHNKYED-------YNVIVTTYNCAISSSDDRSLFRRLKL----NYAIFDEGHML 443
Cdd:cd18007   81 PPdlrpLLVLVSLSASKRADARLRKINKWHKEggvlligYELFRNLASNATTDPRLKQEFIAALLdpgpDLLVLDEGHRL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 358438428 444 KNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMFSS 502
Cdd:cd18007  161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK-EFKKKFVK 218
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
307-532 7.30e-36

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: 135.97  E-value: 7.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQ---------------------EGNKGPHLIVVPAS 365
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrennrprfkkkppaSSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 366 TIDNWLREVNLWcPSLNVLCYYGSQEERKQIRFNIHNKYEdynVIVTTYncaisssddrSLFRR-------LKLNYAIFD 438
Cdd:cd18005   81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGRLKAGRLE---VVVTTY----------DTLRRcidslnsINWSAVIAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 439 EGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFS-------SKTKPADEQS 511
Cdd:cd18005  147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSR-SQFKKHFSepikrgqRHTATARELR 225
                        250       260
                 ....*....|....*....|.
gi 358438428 512 IYEKeRIAHAKQIIKPFILRR 532
Cdd:cd18005  226 LGRK-RKQELAVKLSKFFLRR 245
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
307-532 9.51e-36

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: 135.52  E-value: 9.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGN-KGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHtKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 446
Cdd:cd18055   81 YTGDKDSRAIIREN-EFSFDDnavkggkkafkmkreaqvkFHVLLTSYELV---TIDQAALGSIRWACLVVDEAHRLKNN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 447 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 526
Cdd:cd18055  157 QSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-------AD---ISKEDQIKKLHDLLG 226

                 ....*.
gi 358438428 527 PFILRR 532
Cdd:cd18055  227 PHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
307-532 1.20e-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: 135.19  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEG-NKGPHLIVVPASTIDNWLREVNLWCPSLNVLC 385
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGSQEERKQIRFNiHNKYED-------------------YNVIVTTYNCAissSDDRSLFRRLKLNYAIFDEGHMLKNM 446
Cdd:cd18056   81 YVGDKDSRAIIREN-EFSFEDnairggkkasrmkkeasvkFHVLLTSYELI---TIDMAILGSIDWACLIVDEAHRLKNN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 447 GSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMfssktkpADeqsIYEKERIAHAKQIIK 526
Cdd:cd18056  157 QSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF-------AD---IAKEDQIKKLHDMLG 226

                 ....*.
gi 358438428 527 PFILRR 532
Cdd:cd18056  227 PHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
307-532 3.01e-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: 127.81  E-value: 3.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCpSLNVLCY 386
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 YGSQEERKQIRfnihnKYEDY---------------NVIVTTYNCAISSSDDrslFRRLKLNYAIFDEGHMLKNMGSIRY 451
Cdd:cd18061   80 HGSLISRQMIQ-----QYEMYfrdsqgriirgayrfQAIITTFEMILGGCPE---LNAIDWRCVIIDEAHRLKNKNCKLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 452 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTkpadeqsiyeKERIAHAKQIIKPFILR 531
Cdd:cd18061  152 EGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT----------EEQVQKLQAILKPMMLR 221

                 .
gi 358438428 532 R 532
Cdd:cd18061  222 R 222
DEXDc smart00487
DEAD-like helicases superfamily;
307-486 6.12e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 123.37  E-value: 6.12e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428   307 LKPYQKVGLNWLalvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVP-ASTIDNWLREVNLWCPSLN--V 383
Cdd:smart00487   9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGlkV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428   384 LCYYGSQEERKQIRFNIHNKyedYNVIVTTYNCAISSSDDRSLFRRlKLNYAIFDEGHMLKNMGsiRYQHLMTI-----N 458
Cdd:smart00487  86 VGLYGGDSKREQLRKLESGK---TDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGG--FGDQLEKLlkllpK 159
                          170       180       190
                   ....*....|....*....|....*....|.
gi 358438428   459 ARNRLLLTGTP---VQNNLLELMSLLNFVMP 486
Cdd:smart00487 160 NVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
307-498 3.66e-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: 3.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWlALvhKHGLNGILADEMGLGKTIQAIAFLAYLFQEgnkGPHLIVVPASTIDNWLREVNLWCPSLNVlcy 386
Cdd:cd18010    1 LLPFQREGVCF-AL--RRGGRVLIADEMGLGKTVQAIAIAAYYREE---WPLLIVCPSSLRLTWADEIERWLPSLPP--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 387 ygsqeerkqirfnihnkyEDYNVIVTTyNCAISSSDDR------SLFRRL-------KLNYAIFDEGHMLKNMGSIRYQH 453
Cdd:cd18010   72 ------------------DDIQVIVKS-KDGLRDGDAKvvivsyDLLRRLekqllarKFKVVICDESHYLKNSKAKRTKA 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 358438428 454 LMTI--NARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRR 498
Cdd:cd18010  133 ALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRR 179
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
307-532 5.72e-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: 5.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWL-----ALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPH------LIVVPASTIDNWLREVN 375
Cdd:cd18066    1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKpvikraLIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 376 LWCPSLNVLCYYGSQEerKQIRFNIHNKYedYNVIVTTYNCAISSSDDrslFRRLKLNYAIFDEGHMLKNMGSIRYQHLM 455
Cdd:cd18066   81 KWLGSERIKVFTVDQD--HKVEEFIASPL--YSVLIISYEMLLRSLDQ---ISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 456 TINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFsSSTSEIRRMFSSKTKPADEQSIYEKE------RIAHAKQIIKPFI 529
Cdd:cd18066  154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGIL-GSLSTYRKVYEEPIVRSREPTATPEEkklgeaRAAELTRLTGLFI 232

                 ...
gi 358438428 530 LRR 532
Cdd:cd18066  233 LRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
307-532 1.36e-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: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWL----ALVHKHGLNG-ILADEMGLGKTIQAIAFLAYLFQEGNKGPHLI-----VVPASTIDNWLREVNL 376
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 377 WC-PSLNVLCYYGSQEE---RKQIRF-NIHNKYEDYNVIVTTYNCAISSSDdrsLFRRLKLNYAIFDEGHMLKNMGSIRY 451
Cdd:cd18067   81 WLgGRLQPLAIDGGSKKeidRKLVQWaSQQGRRVSTPVLIISYETFRLHVE---VLQKGEVGLVICDEGHRLKNSDNQTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 452 QHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSStSEIRRMFSS---KTKPAD--EQSIYE-KERIAHAKQII 525
Cdd:cd18067  158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTA-AEFKKNFELpilKGRDADasEKERQLgEEKLQELISIV 236

                 ....*..
gi 358438428 526 KPFILRR 532
Cdd:cd18067  237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
664-777 1.84e-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: 101.52  E-value: 1.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  664 GKFRALGCILSelKQKGDRVVLFSQFTMMLDIlEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDmDIFVfLLSTKAGG 743
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 358438428  744 LGINLTSANVVILHDIDCNPYNDKQAEDRCHRVG 777
Cdd:pfam00271  76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
325-500 2.65e-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: 2.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 325 GLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPSLNVLCYY----------GSQEERK 394
Cdd:cd18069   28 GFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEALPNVrprpfkvfilNDEHKTT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 395 QIRFNIHNKY-EDYNVIVTTYncaisssddrSLFR-RLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQN 472
Cdd:cd18069  108 AARAKVIEDWvKDGGVLLMGY----------EMFRlRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQN 177
                        170       180
                 ....*....|....*....|....*...
gi 358438428 473 NLLELMSLLNFVMPHMFSSSTsEIRRMF 500
Cdd:cd18069  178 NLIEYWCMVDFVRPDFLGTRQ-EFSNMF 204
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
307-531 5.27e-24

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: 102.04  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLaLVHKhglnGILADEMGLGKTIQAIAFL------------AYLFQEGNK--------------GPHLI 360
Cdd:cd18070    1 LLPYQRRAVNWM-LVPG----GILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVccpdclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 361 VVPASTIDNWLREVNLWCP-SLNVLCYYGsQEERKQIRFNIHNKYEDYNVIVTTYN-------CAISSSDDRSLfRRLKL 432
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsSLKVLTYQG-VKKDGALASPAPEILAEYDIVVTTYDvlrtelhYAEANRSNRRR-RRQKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 433 NYAI-------------FDEGHMLKnmGSIRYQHLMT--INARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIR 497
Cdd:cd18070  154 YEAPpsplvlvewwrvcLDEAQMVE--SSTSKAAEMArrLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWAR 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 358438428 498 RMFssktkpadeQSIYEKERIAHAKQIIKPFILR 531
Cdd:cd18070  232 VLI---------RPQGRNKAREPLAALLKELLWR 256
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
325-484 1.75e-22

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: 97.15  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 325 GLNGILADEMGLGKTIQAIAFLayLFQegnkgPHLIVVPASTIDNWLREV--NLWCPSLNVLCYYGSQEERKQirfnihN 402
Cdd:cd18071   48 VRGGILADDMGLGKTLTTISLI--LAN-----FTLIVCPLSVLSNWETQFeeHVKPGQLKVYTYHGGERNRDP------K 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 403 KYEDYNVIVTTYNCAIS--SSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSL 480
Cdd:cd18071  115 LLSKYDIVLTTYNTLASdfGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194

                 ....
gi 358438428 481 LNFV 484
Cdd:cd18071  195 LSFL 198
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
307-482 4.31e-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: 4.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNwLALVHKHgLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREvnLW-CPSLNVLC 385
Cdd:cd18011    1 PLPHQIDAVL-RALRKPP-VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDE--LQdKFGLPFLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 386 YYGsqEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTI------NA 459
Cdd:cd18011   77 LDR--ETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRA 154
                        170       180
                 ....*....|....*....|....*.
gi 358438428 460 RNRLLLTGTPVQNN---LLELMSLLN 482
Cdd:cd18011  155 RHVLLLTATPHNGKeedFRALLSLLD 180
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
307-500 1.42e-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: 94.95  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWL---------ALVHKHGLNGILADEMGLGKTIQAIAFLAYLF---QEGNKGPHLIVVPASTIDNWLREV 374
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLlceKLENFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 375 NLWCPSLN--------VLCYYGSQEERkqiRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKL-------------N 433
Cdd:cd18068   81 EKWQEGLKdeekievnELATYKRPQER---SYKLQRWQEEGGVMIIGYDMYRILAQERNVKSREKLkeifnkalvdpgpD 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 358438428 434 YAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTsEIRRMF 500
Cdd:cd18068  158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIK-EFRNRF 223
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
307-532 2.54e-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: 94.08  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLALVHKHGLNG-ILADEMGLGKTIQAIAFLayLFQEGNK-------------------------GPHLI 360
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALI--LAQKNTQnrkeeekekalteweskkdstlvpsAGTLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 361 VVPASTIDNWLREVNLWCPS--LNVLCYYGSQEERKQIRFnihnkyEDYNVIVTTYNCAIS------SSDDRSLFRRLKL 432
Cdd:cd18072   79 VCPASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEVL------RDYDIVITTYSLVAKeiptykEESRSSPLFRIAW 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 433 NYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSstseirrmFSSKTKPADEQSI 512
Cdd:cd18072  153 ARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDD--------LKVWKKQVDNKSR 224
                        250       260
                 ....*....|....*....|
gi 358438428 513 YEKERIAhakQIIKPFILRR 532
Cdd:cd18072  225 KGGERLN---ILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
694-777 1.34e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.80  E-value: 1.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428   694 DILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMdiFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRC 773
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 358438428   774 HRVG 777
Cdd:smart00490  79 GRAG 82
ResIII pfam04851
Type III restriction enzyme, res subunit;
305-469 7.20e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 61.53  E-value: 7.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  305 LSLKPYQKVGL-NWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDN-WLREVNLWCPSLN 382
Cdd:pfam04851   2 LELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEqALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  383 VLCYYGSQEERKQIrfnihnkYEDYNVIVTTYNCAISSSDDRSL-FRRLKLNYAIFDEGHMLknmGSIRYQHLMTINARN 461
Cdd:pfam04851  82 EIGEIISGDKKDES-------VDDNKIVVTTIQSLYKALELASLeLLPDFFDVIIIDEAHRS---GASSYRNILEYFKPA 151

                  ....*....
gi 358438428  462 RLL-LTGTP 469
Cdd:pfam04851 152 FLLgLTATP 160
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
307-477 1.20e-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: 61.98  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGLNWLAlvhKHGLNGILADeMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTI-DNWLREVNLW--CPSLNV 383
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLTV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 384 LCYYGSQEERkqirfnihNKYEDYNVIVTTYN-----CAISSSDDRSLFRRLklnyaIFDEGHMLKNMGSIRYQHLMTIN 458
Cdd:cd18013   77 SVAVGTERQR--------SKAANTPADLYVINrenlkWLVNKSGDPWPFDMV-----VIDELSSFKSPRSKRFKALRKVR 143
                        170       180
                 ....*....|....*....|.
gi 358438428 459 AR-NRLL-LTGTPVQNNLLEL 477
Cdd:cd18013  144 PViKRLIgLTGTPSPNGLMDL 164
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
304-470 1.50e-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: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 304 SLSLKPYQKVGLN-WLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFqegNKGPHLIVVPASTI-DNWLREVnlwcpsl 381
Cdd:COG1061   78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELL---RGKRVLVLVPRRELlEQWAEEL------- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 382 nvlcyygsQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLnyAIFDEGHmlkNMGSIRYQHLMT-INAR 460
Cdd:COG1061  148 --------RRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGL--VIIDEAH---HAGAPSYRRILEaFPAA 214
                        170
                 ....*....|
gi 358438428 461 NRLLLTGTPV 470
Cdd:COG1061  215 YRLGLTATPF 224
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
307-469 2.05e-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: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 307 LKPYQKVGL-NWLAlvHKHGLNGILADEMGLGKTIQAIAFLAYLFQEgnkgPHLIVVP-ASTIDNWLREvnlwcpslnvL 384
Cdd:cd17926    1 LRPYQEEALeAWLA--HKNNRRGILVLPTGSGKTLTALALIAYLKEL----RTLIVVPtDALLDQWKER----------F 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 385 CYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLnYAIFDEGHmlkNMGSIRYQHLMTI-NARNRL 463
Cdd:cd17926   65 EDFLGDSSIGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDQFG-LLIVDEAH---HLPAKTFSEILKElNAKYRL 140

                 ....*.
gi 358438428 464 LLTGTP 469
Cdd:cd17926  141 GLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
327-468 6.61e-07

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: 49.71  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 327 NGILADEMGLGKTIQAIAFLAYLFqEGNKGPHLIVVPASTIDN----WLREvnLWCPSLNVLCYYG--SQEERKQIRFNi 400
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLL-LKKGKKVLVLVPTKALALqtaeRLRE--LFGPGIRVAVLVGgsSAEEREKNKLG- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358438428 401 hnkyeDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHML------KNMGSIRYQHLMTINARnRLLLTGT 468
Cdd:cd00046   79 -----DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlidsrgALILDLAVRKAGLKNAQ-VILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
335-472 2.78e-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: 45.31  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428  335 GLGKTiqAIAFLAYL--FQEGNKGPH-LIVVP--------ASTIDNWLREVNLwcpslNVLCYYGSQEERKQIRfnihnK 403
Cdd:pfam00270  24 GSGKT--LAFLLPALeaLDKLDNGPQaLVLAPtrelaeqiYEELKKLGKGLGL-----KVASLLGGDSRKEQLE-----K 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 358438428  404 YEDYNVIVTTYNCAISSSDDRSLFRRLKlnYAIFDEGHMLKNMGsiRYQHLMTI-----NARNRLLLTGTPVQN 472
Cdd:pfam00270  92 LKGPDILVGTPGRLLDLLQERKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEIlrrlpKKRQILLLSATLPRN 161
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
664-755 2.11e-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: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 664 GKFRALGCILSELKQkGDRVVLFSQFTMMLD-ILEVLLKhhqhrYLrLDGKTQISERIHLIDEF-----NTdmdIFVfll 737
Cdd:cd18789   34 NKLRALEELLKRHEQ-GDKIIVFTDNVEALYrYAKRLLK-----PF-ITGETPQSEREEILQNFregeyNT---LVV--- 100
                         90
                 ....*....|....*...
gi 358438428 738 sTKAGGLGINLTSANVVI 755
Cdd:cd18789  101 -SKVGDEGIDLPEANVAI 117
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
330-471 4.96e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 40.59  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 330 LADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWL----REVNLWcPSLnvlcyygSQEERkqirfNIHNKYE 405
Cdd:PRK04914 174 LADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLvemlRRFNLR-FSL-------FDEER-----YAEAQHD 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 358438428 406 DYNVIVTTyNCAISSSDdrsLFRRLKLNY----------AIFDEGHML---KNMGSIRYQHLMTINARNR--LLLTGTPV 470
Cdd:PRK04914 241 ADNPFETE-QLVICSLD---FLRRNKQRLeqalaaewdlLVVDEAHHLvwsEEAPSREYQVVEQLAEVIPgvLLLTATPE 316

                 .
gi 358438428 471 Q 471
Cdd:PRK04914 317 Q 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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