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Conserved domains on  [gi|19114529|ref|NP_593617|]
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protein Fft3 [Schizosaccharomyces pombe]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
275-904 1.91e-129

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 405.38  E-value: 1.91e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 275 DLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGET 354
Cdd:COG0553 132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 355 SLVNFDQMKSFGTPANSSFITTPPASFspDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNI 434
Cdd:COG0553 212 ELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 435 NGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQvEREEIRERInsnkDSYNVMLTTYrlaATSKADRLFLRNQKFNV 514
Cdd:COG0553 290 ARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR-ERAKGANPF----EDADLVITSY---GLLRRDIELLAAVDWDL 361
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 515 CVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFdYGLKSldviFTmkkspeSDFERAL 594
Cdd:COG0553 362 VILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-GSLKA----FR------ERFARPI 430
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 595 L--SEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDdfaskqSVNSLLDENVmktnldTNANLA 672
Cdd:COG0553 431 EkgDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE------AVLEYLRREL------EGAEGI 498
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 673 KKKSTAGFVLVQLRKLADHPMLFrihykddilrqmakaimnepqykkanelyifedmqymsdielhnlcckfpsinsfqL 752
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL--------------------------------------------------------L 522
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 753 KDEPWMDAT--KVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESIN 830
Cdd:COG0553 523 EEGAELSGRsaKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP 602
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114529 831 VFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIAL 904
Cdd:COG0553 603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
275-904 1.91e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 405.38  E-value: 1.91e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 275 DLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGET 354
Cdd:COG0553 132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 355 SLVNFDQMKSFGTPANSSFITTPPASFspDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNI 434
Cdd:COG0553 212 ELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 435 NGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQvEREEIRERInsnkDSYNVMLTTYrlaATSKADRLFLRNQKFNV 514
Cdd:COG0553 290 ARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR-ERAKGANPF----EDADLVITSY---GLLRRDIELLAAVDWDL 361
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 515 CVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFdYGLKSldviFTmkkspeSDFERAL 594
Cdd:COG0553 362 VILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-GSLKA----FR------ERFARPI 430
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 595 L--SEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDdfaskqSVNSLLDENVmktnldTNANLA 672
Cdd:COG0553 431 EkgDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE------AVLEYLRREL------EGAEGI 498
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 673 KKKSTAGFVLVQLRKLADHPMLFrihykddilrqmakaimnepqykkanelyifedmqymsdielhnlcckfpsinsfqL 752
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL--------------------------------------------------------L 522
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 753 KDEPWMDAT--KVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESIN 830
Cdd:COG0553 523 EEGAELSGRsaKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP 602
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114529 831 VFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIAL 904
Cdd:COG0553 603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
387-569 1.52e-106

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: 327.42  E-value: 1.52e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELY 466
Cdd:cd17998   1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERINSNKDSYNVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLT 546
Cdd:cd17998  81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                       170       180
                ....*....|....*....|...
gi 19114529 547 GTPLQNNLKELISLLAFILPHVF 569
Cdd:cd17998 161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
386-906 8.37e-92

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 313.66  E-value: 8.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   465 LYYGSQVEREEIRERInSNKDSYNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVL 544
Cdd:PLN03142  249 KFHGNPEERAHQREEL-LVAGKFDVCVTSFEMAIKEKTA---LKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   545 LTGTPLQNNLKELISLLAFILPHVFDYGlKSLDVIFTMkkSPESDferallSEQRVSRAKMMMAPFVLRRKKSQVLDALP 624
Cdd:PLN03142  325 ITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQI--SGEND------QQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   625 KKTRIIEFCEFSEEERRRYDDFASKqsvnsllDENVMKTNLDTNANLAkkkstagfVLVQLRKLADHPMLFrihykddil 704
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKALLQK-------DLDVVNAGGERKRLLN--------IAMQLRKCCNHPYLF--------- 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   705 rQMAKAimnEPQYKKANELyifedmqymsdIElhnlcckfpsinsfqlkdepwmDATKVRKLKKLLTNAVENGDRVVLFS 784
Cdd:PLN03142  452 -QGAEP---GPPYTTGEHL-----------VE----------------------NSGKMVLLDKLLPKLKERDSRVLIFS 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   785 QFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESIN-VFLLSTKAGGFGINLACANMVILYDVSFNPFDD 863
Cdd:PLN03142  495 QMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVD 574
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 19114529   864 LQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIALDA 906
Cdd:PLN03142  575 LQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDA 617
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
390-695 6.80e-61

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: 208.69  E-value: 6.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   390 YQIIGINWLYLLYE-LKLAGILADEMGLGKTCQTIAF--FSLLMDKNINGPHLVIAPASTMENWLREFAKFC--PKLKIE 464
Cdd:pfam00176   1 YQIEGVNWMLSLENnLGRGGILADEMGLGKTLQTISLllYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   465 LYYGSQVEREEIRERINSNKDsYNVMLTTYrlaatskaDRLFLRNQKFNVC-----VYDEGHYLKNRASERYRHLMSIPA 539
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLAD-FDVVITTY--------ETLRKHKELLKKVhwhriVLDEGHRLKNSKSKLSKALKSLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   540 DFRVLLTGTPLQNNLKELISLLAFILPHVFdyglkslDVIFTMKKSPESDFERAlLSEQRVSRAKMMMAPFVLRRKKSQV 619
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPF-------GSLSTFRNWFDRPIERG-GGKKGVSRLHKLLKPFLLRRTKKDV 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114529   620 LDALPKKTRIIEFCEFSEEERRRYDDFASKQSVNSLLDENVMKTNLDTNANLakkkstagfvLVQLRKLADHPMLF 695
Cdd:pfam00176 224 EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKASLLNI----------LMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
385-566 1.73e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.88  E-value: 1.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529    385 IKLQDYQIIGINWLYllyELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAP-ASTMENWLREFAKFCPKLKI 463
Cdd:smart00487   7 EPLRPYQKEAIEALL---SGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529    464 E--LYYGSQVEREEIRERINSNkdsYNVMLTTY-RLAATSKADRLFLRNqkFNVCVYDEGHYLKNRA-SERYRHLMS--I 537
Cdd:smart00487  84 KvvGLYGGDSKREQLRKLESGK---TDILVTTPgRLLDLLENDKLSLSN--VDLVILDEAHRLLDGGfGDQLEKLLKllP 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 19114529    538 PADFRVLLTGTP---LQNNLKELISLLAFILP 566
Cdd:smart00487 159 KNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
275-904 1.91e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 405.38  E-value: 1.91e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 275 DLESALVVKQPRPVIPKGRRGRREKTPLGPRLVGICMEIMRGYFVVDALIRQCEQLGGKIQRGIEAWGLSNTATSDEGET 354
Cdd:COG0553 132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 355 SLVNFDQMKSFGTPANSSFITTPPASFspDIKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNI 434
Cdd:COG0553 212 ELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 435 NGPHLVIAPASTMENWLREFAKFCPKLKIELYYGSQvEREEIRERInsnkDSYNVMLTTYrlaATSKADRLFLRNQKFNV 514
Cdd:COG0553 290 ARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR-ERAKGANPF----EDADLVITSY---GLLRRDIELLAAVDWDL 361
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 515 CVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFdYGLKSldviFTmkkspeSDFERAL 594
Cdd:COG0553 362 VILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL-GSLKA----FR------ERFARPI 430
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 595 L--SEQRVSRAKMMMAPFVLRRKKSQVLDALPKKTRIIEFCEFSEEERRRYDdfaskqSVNSLLDENVmktnldTNANLA 672
Cdd:COG0553 431 EkgDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE------AVLEYLRREL------EGAEGI 498
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 673 KKKSTAGFVLVQLRKLADHPMLFrihykddilrqmakaimnepqykkanelyifedmqymsdielhnlcckfpsinsfqL 752
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL--------------------------------------------------------L 522
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 753 KDEPWMDAT--KVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESIN 830
Cdd:COG0553 523 EEGAELSGRsaKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP 602
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114529 831 VFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIAL 904
Cdd:COG0553 603 VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
387-569 1.52e-106

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: 327.42  E-value: 1.52e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELY 466
Cdd:cd17998   1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERINSNKDSYNVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLT 546
Cdd:cd17998  81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                       170       180
                ....*....|....*....|...
gi 19114529 547 GTPLQNNLKELISLLAFILPHVF 569
Cdd:cd17998 161 GTPLQNNLLELMSLLNFIMPKPF 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
386-906 8.37e-92

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 313.66  E-value: 8.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   465 LYYGSQVEREEIRERInSNKDSYNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVL 544
Cdd:PLN03142  249 KFHGNPEERAHQREEL-LVAGKFDVCVTSFEMAIKEKTA---LKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   545 LTGTPLQNNLKELISLLAFILPHVFDYGlKSLDVIFTMkkSPESDferallSEQRVSRAKMMMAPFVLRRKKSQVLDALP 624
Cdd:PLN03142  325 ITGTPLQNNLHELWALLNFLLPEIFSSA-ETFDEWFQI--SGEND------QQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   625 KKTRIIEFCEFSEEERRRYDDFASKqsvnsllDENVMKTNLDTNANLAkkkstagfVLVQLRKLADHPMLFrihykddil 704
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKALLQK-------DLDVVNAGGERKRLLN--------IAMQLRKCCNHPYLF--------- 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   705 rQMAKAimnEPQYKKANELyifedmqymsdIElhnlcckfpsinsfqlkdepwmDATKVRKLKKLLTNAVENGDRVVLFS 784
Cdd:PLN03142  452 -QGAEP---GPPYTTGEHL-----------VE----------------------NSGKMVLLDKLLPKLKERDSRVLIFS 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   785 QFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESIN-VFLLSTKAGGFGINLACANMVILYDVSFNPFDD 863
Cdd:PLN03142  495 QMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVD 574
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 19114529   864 LQAEDRAHRVGQKKEVTVYKFVVKDTIEEHIQRLANAKIALDA 906
Cdd:PLN03142  575 LQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDA 617
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
387-569 5.06e-71

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: 232.46  E-value: 5.06e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLM-DKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQveREEIRERINSNKDSYNVMLTTYRLAatsKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLL 545
Cdd:cd17919  81 YHGSQ--RERAQIRAKEKLDKFDVVLTTYETL---RRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLL 155
                       170       180
                ....*....|....*....|....
gi 19114529 546 TGTPLQNNLKELISLLAFILPHVF 569
Cdd:cd17919 156 TGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
386-616 5.02e-67

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: 223.80  E-value: 5.02e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18009   3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDS---YNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFR 542
Cdd:cd18009  83 YHGTKEERERLRKKIMKREGTlqdFPVVVTSYEIAMR---DRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNR 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114529 543 VLLTGTPLQNNLKELISLLAFILPHVFDyGLKSLDVIFTMKKSPESDFERALLSEQR----VSRAKMMMAPFVLRRKK 616
Cdd:cd18009 160 LLLTGTPLQNNLSELWSLLNFLLPDVFD-DLSSFESWFDFSSLSDNAADISNLSEEReqniVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
387-614 2.09e-64

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: 216.06  E-value: 2.09e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFS-LLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERInSNKDSYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLL 545
Cdd:cd18003  81 YYGSAKERKLKRQGW-MKPNSFHVCITSYQLVVQ---DHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114529 546 TGTPLQNNLKELISLLAFILPHVFDyglkSLDVIFTMKKSPESDF--ERALLSEQRVSRAKMMMAPFVLRR 614
Cdd:cd18003 157 TGTPLQNSLMELWSLMHFLMPHIFQ----SHQEFKEWFSNPLTAMseGSQEENEELVRRLHKVLRPFLLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
390-695 6.80e-61

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: 208.69  E-value: 6.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   390 YQIIGINWLYLLYE-LKLAGILADEMGLGKTCQTIAF--FSLLMDKNINGPHLVIAPASTMENWLREFAKFC--PKLKIE 464
Cdd:pfam00176   1 YQIEGVNWMLSLENnLGRGGILADEMGLGKTLQTISLllYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   465 LYYGSQVEREEIRERINSNKDsYNVMLTTYrlaatskaDRLFLRNQKFNVC-----VYDEGHYLKNRASERYRHLMSIPA 539
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLAD-FDVVITTY--------ETLRKHKELLKKVhwhriVLDEGHRLKNSKSKLSKALKSLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   540 DFRVLLTGTPLQNNLKELISLLAFILPHVFdyglkslDVIFTMKKSPESDFERAlLSEQRVSRAKMMMAPFVLRRKKSQV 619
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPF-------GSLSTFRNWFDRPIERG-GGKKGVSRLHKLLKPFLLRRTKKDV 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114529   620 LDALPKKTRIIEFCEFSEEERRRYDDFASKQSVNSLLDENVMKTNLDTNANLakkkstagfvLVQLRKLADHPMLF 695
Cdd:pfam00176 224 EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKASLLNI----------LMRLRKICNHPGLI 289
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
387-616 1.48e-60

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: 205.11  E-value: 1.48e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELY 466
Cdd:cd18012   5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERinsnkDSYNVMLTTYrlaATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLT 546
Cdd:cd18012  85 HGTKRKREKLRAL-----EDYDLVITSY---GLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALT 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114529 547 GTPLQNNLKELISLLAFILPHVfdygLKSLDViFTmkkspeSDFERALLSEQRVSRA---KMMMAPFVLRRKK 616
Cdd:cd18012 157 GTPIENHLGELWSIFDFLNPGL----LGSYKR-FK------KRFAKPIEKDGDEEALeelKKLISPFILRRLK 218
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
386-616 1.62e-59

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: 202.98  E-value: 1.62e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:cd17996   3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEkKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 465 LYYGSQVEREEIRERINSNKdsYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASE------RYRHlmsip 538
Cdd:cd17996  83 VYKGTPDVRKKLQSQIRAGK--FNVLLTTYEYIIK---DKPLLSKIKWKYMIIDEGHRMKNAQSKltqtlnTYYH----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 539 ADFRVLLTGTPLQNNLKELISLLAFILPHVFDyGLKSLDVIFTMKKSPESDFERALLSEQR----VSRAKMMMAPFVLRR 614
Cdd:cd17996 153 ARYRLLLTGTPLQNNLPELWALLNFLLPKIFK-SCKTFEQWFNTPFANTGEQVKIELNEEEtlliIRRLHKVLRPFLLRR 231

                ..
gi 19114529 615 KK 616
Cdd:cd17996 232 LK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
387-614 5.34e-57

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: 195.80  E-value: 5.34e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18002   1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEeHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSN----KDS-YNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPAD 540
Cdd:cd18002  81 YWGNPKDRKVLRKFWDRKnlytRDApFHVVITSYQLVVQ---DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114529 541 FRVLLTGTPLQNNLKELISLLAFILPHVFDyGLKSLDVIFTmkKSPESDFE-RALLSEQRVSRAKMMMAPFVLRR 614
Cdd:cd18002 158 NRLLLTGTPIQNSMAELWALLHFIMPTLFD-SHDEFNEWFS--KDIESHAEnKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
386-616 1.24e-56

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: 194.46  E-value: 1.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:cd17997   3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 465 LYYGSQVEREEIRERINSNKDsYNVMLTTYRLAATSKAdrlFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVL 544
Cdd:cd17997  83 VLIGDKEERADIIRDVLLPGK-FDVCITSYEMVIKEKT---VLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLL 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114529 545 LTGTPLQNNLKELISLLAFILPHVFDyglksldviftmkkSPEsDF-------ERALLSEQRVSRAKMMMAPFVLRRKK 616
Cdd:cd17997 159 LTGTPLQNNLHELWALLNFLLPDVFT--------------SSE-DFdewfnvnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
761-885 2.91e-54

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: 184.60  E-value: 2.91e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 761 TKVRKLKKLLTNAVENGDRVVLFSQFTQVLDILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESINVFLLSTKAGG 840
Cdd:cd18793  11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGG 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19114529 841 FGINLACANMVILYDVSFNPFDDLQAEDRAHRVGQKKEVTVYKFV 885
Cdd:cd18793  91 VGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
386-614 8.89e-54

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: 186.41  E-value: 8.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLM-DKNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:cd17993   1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 465 LYYGSQVEREEIRE----RINSNKDSYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPAD 540
Cdd:cd17993  81 VYLGDIKSRDTIREyefyFSQTKKLKFNVLLTTYEIILK---DKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTN 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114529 541 FRVLLTGTPLQNNLKELISLLAFILPHVFDYglksldviftmkkSPESDFERALLSEQRVSRAKMMMAPFVLRR 614
Cdd:cd17993 158 NRLLITGTPLQNSLKELWALLHFLMPGKFDI-------------WEEFEEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
387-614 4.66e-51

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: 178.79  E-value: 4.66e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDK-NINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDsYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLL 545
Cdd:cd18006  81 YMGDKEKRLDLQQDIKSTNR-FHVLLTTYEICLK---DASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114529 546 TGTPLQNNLKELISLLAFILPHVFdyGLKSLDVIftMKKSPESDFERALLSEqrvsrAKMMMAPFVLRR 614
Cdd:cd18006 157 TGTPIQNSLQELYALLSFIEPNVF--PKDKLDDF--IKAYSETDDESETVEE-----LHLLLQPFLLRR 216
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
387-614 2.02e-50

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: 177.06  E-value: 2.02e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFS-LLMDKNINGPHLVIAPASTMENWLREFAKFCPkLKIEL 465
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEhLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDSY----------NVMLTTYRLAAtskADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLM 535
Cdd:cd17995  80 YHGSGESRQIIQQYEMYFKDAQgrkkkgvykfDVLITTYEMVI---ADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 536 SIPADFRVLLTGTPLQNNLKELISLLAFILPHVFdyglksldviftmkkSPESDFERA---LLSEQRVSRAKMMMAPFVL 612
Cdd:cd17995 157 KLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKF---------------PSSEEFLEEfgdLKTAEQVEKLQALLKPYML 221

                ..
gi 19114529 613 RR 614
Cdd:cd17995 222 RR 223
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
387-614 1.96e-44

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: 160.23  E-value: 1.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIELY 466
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQV-EREEIRERINSNKdsyNVMLTTYRLaATSKADRL---FLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFR 542
Cdd:cd18001  81 HGTSKkERERNLERIQRGG---GVLLTTYGM-VLSNTEQLsadDHDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 543 VLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIF-------TMKKSpeSDFERALLSEqrVSRAKM-MMAPFVLRR 614
Cdd:cd18001 157 IILTGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFenpitrgRDKDA--TQGEKALGSE--VAENLRqIIKPYFLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
387-566 1.29e-43

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: 156.72  E-value: 1.29e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFF-SLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18000   1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLaALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGS---------QVEREEIRERINSNKDSYNVMLTTYRLAATSKAdrlFLRNQKFNVCVYDEGHYLKNRASERYRHLMS 536
Cdd:cd18000  81 LHSSgsgtgseekLGSIERKSQLIRKVVGDGGILITTYEGFRKHKD---LLLNHNWQYVILDEGHKIRNPDAEITLACKQ 157
                       170       180       190
                ....*....|....*....|....*....|
gi 19114529 537 IPADFRVLLTGTPLQNNLKELISLLAFILP 566
Cdd:cd18000 158 LRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
386-626 5.55e-43

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: 156.75  E-value: 5.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 386 KLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIE 464
Cdd:cd18064  15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 465 LYYGSQVEREE-IRERINSNKdsYNVMLTTYRLAATSKAdrLFlrnQKFN--VCVYDEGHYLKNRASERYRHLMSIPADF 541
Cdd:cd18064  95 CLIGDKDQRAAfVRDVLLPGE--WDVCVTSYEMLIKEKS--VF---KKFNwrYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 542 RVLLTGTPLQNNLKELISLLAFILPHVFDYGlKSLDVIFtmkkspesDFERALLSEQRVSRAKMMMAPFVLRRKKSQVLD 621
Cdd:cd18064 168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSA-EDFDSWF--------DTNNCLGDQKLVERLHMVLRPFLLRRIKADVEK 238

                ....*
gi 19114529 622 ALPKK 626
Cdd:cd18064 239 SLPPK 243
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
385-571 2.32e-42

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: 154.78  E-value: 2.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 385 IKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKN-INGPHLVIAPASTMENWLREFAKFCPKLKI 463
Cdd:cd18054  19 LELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHqLYGPFLLVVPLSTLTSWQREFEIWAPEINV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 464 ELYYGSQVEREEIRE----RINSNKDSYNVMLTTYRLAATSKAdrlFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPA 539
Cdd:cd18054  99 VVYIGDLMSRNTIREyewiHSQTKRLKFNALITTYEILLKDKT---VLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKS 175
                       170       180       190
                ....*....|....*....|....*....|..
gi 19114529 540 DFRVLLTGTPLQNNLKELISLLAFILPHVFDY 571
Cdd:cd18054 176 NHRLLITGTPLQNSLKELWSLLHFIMPEKFEF 207
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
387-614 1.10e-40

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: 150.13  E-value: 1.10e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLyllyeLKLAGILADEMGLGKTCQTIA----------FFSLLMDKNINGPH--------LVIAPASTME 448
Cdd:cd18008   1 LLPYQKQGLAWM-----LPRGGILADEMGLGKTIQALAlilatrpqdpKIPEELEENSSDPKklylskttLIVVPLSLLS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 449 NWLREFAKFC--PKLKIELYYGSqvereeirERINSNKD--SYNVMLTTY-RLAA------------TSKADRLFLRNQK 511
Cdd:cd18008  76 QWKDEIEKHTkpGSLKVYVYHGS--------KRIKSIEElsDYDIVITTYgTLASefpknkkgggrdSKEKEASPLHRIR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 512 FNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFI-LPHVFDYGLKSLDVIFTMKKSPESDF 590
Cdd:cd18008 148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrVEPFGDYPWFNSDISKPFSKNDRKAL 227
                       250       260
                ....*....|....*....|....
gi 19114529 591 ERallsEQRVSRakmmmaPFVLRR 614
Cdd:cd18008 228 ER----LQALLK------PILLRR 241
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
387-614 1.27e-40

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: 149.42  E-value: 1.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAffSLLMD--------KNINGPHLVIAPASTMENWLREFAKFC 458
Cdd:cd17999   1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLC--ILASDhhkransfNSENLPSLVVCPPTLVGHWVAEIKKYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 459 P--KLKIELYYGSQVEREEIRERINSNkdsyNVMLTTYrlaATSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMS 536
Cdd:cd17999  79 PnaFLKPLAYVGPPQERRRLREQGEKH----NVIVASY---DVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 537 IPADFRVLLTGTPLQNNLKELISLLAFILP------HVF--DYG---LKSLDviftmKKSPESDFERALLSEQRVSRAKM 605
Cdd:cd17999 152 LKANHRLILSGTPIQNNVLELWSLFDFLMPgylgteKQFqrRFLkpiLASRD-----SKASAKEQEAGALALEALHKQVL 226

                ....*....
gi 19114529 606 mmaPFVLRR 614
Cdd:cd17999 227 ---PFLLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
387-614 6.54e-40

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: 146.05  E-value: 6.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAF-FSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd17994   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFlYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSqvereeirerinsnkdsyNVMLTTYRLAATSKAdrlFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLL 545
Cdd:cd17994  81 YVGD------------------HVLLTSYELISIDQA---ILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114529 546 TGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKspesdferallsEQRVSRAKMMMAPFVLRR 614
Cdd:cd17994 140 TGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISK------------EDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
387-616 9.37e-40

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: 147.09  E-value: 9.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18065  16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREE-IRERINSNKdsYNVMLTTYRLAATSKAdrLFlrnQKFN--VCVYDEGHYLKNRASERYRHLMSIPADFR 542
Cdd:cd18065  96 LIGDKDARAAfIRDVMMPGE--WDVCVTSYEMVIKEKS--VF---KKFNwrYLVIDEAHRIKNEKSKLSEIVREFKTTNR 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114529 543 VLLTGTPLQNNLKELISLLAFILPHVFDYGlKSLDVIFtmkkspesDFERALLSEQRVSRAKMMMAPFVLRRKK 616
Cdd:cd18065 169 LLLTGTPLQNNLHELWALLNFLLPDVFNSA-DDFDSWF--------DTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
387-616 4.12e-39

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: 145.98  E-value: 4.12e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18063  24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKdsYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMS-IPADFRVL 544
Cdd:cd18063 104 YKGTPAMRRSLVPQLRSGK--FNVLLTTYEYIIK---DKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRIL 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114529 545 LTGTPLQNNLKELISLLAFILPHVFdyglKSLDVIFTMKKSPES-DFERALLSEQR----VSRAKMMMAPFVLRRKK 616
Cdd:cd18063 179 LTGTPLQNKLPELWALLNFLLPTIF----KSCSTFEQWFNAPFAmTGERVDLNEEEtiliIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
387-616 7.29e-39

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: 145.19  E-value: 7.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMD-KNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18062  24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKdsYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMS-IPADFRVL 544
Cdd:cd18062 104 YKGSPAARRAFVPQLRSGK--FNVLLTTYEYIIK---DKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLL 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114529 545 LTGTPLQNNLKELISLLAFILPHVFdyglKSLDVIFTMKKSPES-DFERALLSEQR----VSRAKMMMAPFVLRRKK 616
Cdd:cd18062 179 LTGTPLQNKLPELWALLNFLLPTIF----KSCSTFEQWFNAPFAmTGEKVDLNEEEtiliIRRLHKVLRPFLLRRLK 251
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
387-614 1.05e-36

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: 137.88  E-value: 1.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCpKLKIELY 466
Cdd:cd18060   1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERINSNKDS----------YNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLMS 536
Cdd:cd18060  80 HGSLASRQMIQQYEMYCKDSrgrlipgaykFDALITTFEMILSDCPE---LREIEWRCVIIDEAHRLKNRNCKLLDSLKH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 537 IPADFRVLLTGTPLQNNLKELISLLAFILPHVFdyglksldviftmkkSPESDFERA---LLSEQRVSRAKMMMAPFVLR 613
Cdd:cd18060 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQF---------------PSESEFLKDfgdLKTEEQVQKLQAILKPMMLR 221

                .
gi 19114529 614 R 614
Cdd:cd18060 222 R 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
387-614 3.18e-36

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: 136.71  E-value: 3.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCpKLKIELY 466
Cdd:cd18058   1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERINSNKDS----------YNVMLTTYRLAAtskADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMS 536
Cdd:cd18058  80 HGSQISRQMIQQYEMYYRDEqgnplsgifkFQVVITTFEMIL---ADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114529 537 IPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKkspesdferallSEQRVSRAKMMMAPFVLRR 614
Cdd:cd18058 157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLK------------TEEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
387-614 1.08e-35

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: 135.19  E-value: 1.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAF-FSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18057   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFlYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDS------------------YNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRA 527
Cdd:cd18057  81 YTGDKESRSVIRENEFSFEDNairsgkkvfrmkkeaqikFHVLLTSYELITI---DQAILGSIEWACLVVDEAHRLKNNQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 528 SERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKspesdferallsEQRVSRAKMMM 607
Cdd:cd18057 158 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISK------------EDQIKKLHDLL 225

                ....*..
gi 19114529 608 APFVLRR 614
Cdd:cd18057 226 GPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
387-614 1.16e-35

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: 134.77  E-value: 1.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCpKLKIELY 466
Cdd:cd18059   1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRE----------RINSNKDSYNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLMS 536
Cdd:cd18059  80 HGSQASRRTIQLyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPE---LRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 537 IPADFRVLLTGTPLQNNLKELISLLAFILPHVFdyglksldviftmkkSPESDFERA---LLSEQRVSRAKMMMAPFVLR 613
Cdd:cd18059 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRF---------------PSETTFMQEfgdLKTEEQVQKLQAILKPMMLR 221

                .
gi 19114529 614 R 614
Cdd:cd18059 222 R 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
385-569 3.21e-35

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: 134.02  E-value: 3.21e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 385 IKLQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLM-DKNINGPHLVIAPASTMENWLREFAKFCPKLKI 463
Cdd:cd18053  19 LELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 464 ELYYGSQVEREEIRER----INSNKDSYNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPA 539
Cdd:cd18053  99 VVYLGDINSRNMIRTHewmhPQTKRLKFNILLTTYEILLK---DKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKS 175
                       170       180       190
                ....*....|....*....|....*....|
gi 19114529 540 DFRVLLTGTPLQNNLKELISLLAFILPHVF 569
Cdd:cd18053 176 NHRLLITGTPLQNSLKELWSLLHFIMPEKF 205
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
387-570 3.50e-35

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


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 133.98  E-value: 3.50e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAF-FSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18055   1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFlYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDS------------------YNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRA 527
Cdd:cd18055  81 YTGDKDSRAIIRENEFSFDDNavkggkkafkmkreaqvkFHVLLTSYELVTI---DQAALGSIRWACLVVDEAHRLKNNQ 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19114529 528 SERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFD 570
Cdd:cd18055 158 SKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFN 200
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
387-614 4.86e-33

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: 127.79  E-value: 4.86e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLY--LLYELKLAG---ILADEMGLGKTCQTIAFFSLLMDKNINGPH-----LVIAPASTMENWLREFAK 456
Cdd:cd18004   1 LRPHQREGVQFLYdcLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkaLIVCPSSLVGNWKAEFDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 457 FCP--KLKIELYYGSQVEREEIRERINSNKDsYNVMLTTYRLAATSkADRLfLRNQKFNVCVYDEGHYLKNRASERYRHL 534
Cdd:cd18004  81 WLGlrRIKVVTADGNAKDVKASLDFFSSAST-YPVLIISYETLRRH-AEKL-SKKISIDLLICDEGHRLKNSESKTTKAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 535 MSIPADFRVLLTGTPLQNNLKELISLLAFILPHVfdygLKSLDV---IFT----MKKSPESDFERALLSEQRVSRAKMMM 607
Cdd:cd18004 158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGI----LGSLASfrkVFEepilRSRDPDASEEDKELGAERSQELSELT 233

                ....*..
gi 19114529 608 APFVLRR 614
Cdd:cd18004 234 SRFILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
387-614 6.99e-32

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: 124.80  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDK---------------------NINGPHLVIAPAS 445
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 446 TMENWLREFAKFcPKLKIELYYGSQveREEIRE-RINSNKdsYNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLK 524
Cdd:cd18005  81 VLYNWKDELDTW-GHFEVGVYHGSR--KDDELEgRLKAGR--LEVVVTTYDTLRRCIDS---LNSINWSAVIADEAHRIK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 525 NRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVF----DYGLKSLDVIFTMKKSPESDFERAlLSEQRV 600
Cdd:cd18005 153 NPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALgsrsQFKKHFSEPIKRGQRHTATARELR-LGRKRK 231
                       250
                ....*....|....
gi 19114529 601 SRAKMMMAPFVLRR 614
Cdd:cd18005 232 QELAVKLSKFFLRR 245
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
409-604 9.61e-32

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: 124.33  E-value: 9.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 409 ILADEMGLGKTCQTIAFFSLLMDKNINGPH-LVIAPASTMENWLREFAKFCPKLKIE---LYYGSQVEREEIRER-INSN 483
Cdd:cd18007  30 ILAHTMGLGKTLQVITFLHTYLAAAPRRSRpLVLCPASTLYNWEDEFKKWLPPDLRPllvLVSLSASKRADARLRkINKW 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 484 KDSYNVMLTTY----RLAATSKAD-RLFLRNQKF------NVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQN 552
Cdd:cd18007 110 HKEGGVLLIGYelfrNLASNATTDpRLKQEFIAAlldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQN 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 19114529 553 NLKELISLLAFILPhvfDYgLKSLDVIFTMKKSP--ESDFERALLSEQRVSRAK 604
Cdd:cd18007 190 NLKEYWTMVDFARP---KY-LGTLKEFKKKFVKPieAGQCVDSTEEDVRLMLKR 239
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
387-614 1.07e-31

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: 124.02  E-value: 1.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAF-FSLLMDKNINGPHLVIAPASTMENWLREFAKFCPKLKIEL 465
Cdd:cd18056   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFlYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREEIRERINSNKDS------------------YNVMLTTYRLAATskaDRLFLRNQKFNVCVYDEGHYLKNRA 527
Cdd:cd18056  81 YVGDKDSRAIIRENEFSFEDNairggkkasrmkkeasvkFHVLLTSYELITI---DMAILGSIDWACLIVDEAHRLKNNQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 528 SERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLKSLDVIFTMKKspesdferallsEQRVSRAKMMM 607
Cdd:cd18056 158 SKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAK------------EDQIKKLHDML 225

                ....*..
gi 19114529 608 APFVLRR 614
Cdd:cd18056 226 GPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
387-614 3.42e-31

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: 122.04  E-value: 3.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKFCpKLKIELY 466
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 467 YGSQVEREEIRERINSNKDSYN-VMLTTYRLAATSKADRLF------LRNQKFNVCVYDEGHYLKNRASERYRHLMSIPA 539
Cdd:cd18061  80 HGSLISRQMIQQYEMYFRDSQGrIIRGAYRFQAIITTFEMIlggcpeLNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114529 540 DFRVLLTGTPLQNNLKELISLLAFILPHVFdyglksldviftmkkSPESDFERA---LLSEQRVSRAKMMMAPFVLRR 614
Cdd:cd18061 160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRF---------------PSESTFMQEfgdLKTEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
387-614 3.05e-28

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: 113.79  E-value: 3.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLY-----LLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPH------LVIAPASTMENWLREFA 455
Cdd:cd18066   1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKpvikraLIVTPGSLVKNWKKEFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 456 KFCPKLKIELYYGSQveREEIRERINSNkdSYNVMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLM 535
Cdd:cd18066  81 KWLGSERIKVFTVDQ--DHKVEEFIASP--LYSVLIISYEMLLRSLDQ---ISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 536 SIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDyGLKSLDVIF----TMKKSPESDFERALLSEQRVSRAKMMMAPFV 611
Cdd:cd18066 154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGILG-SLSTYRKVYeepiVRSREPTATPEEKKLGEARAAELTRLTGLFI 232

                ...
gi 19114529 612 LRR 614
Cdd:cd18066 233 LRR 235
DEXDc smart00487
DEAD-like helicases superfamily;
385-566 1.73e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.88  E-value: 1.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529    385 IKLQDYQIIGINWLYllyELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAP-ASTMENWLREFAKFCPKLKI 463
Cdd:smart00487   7 EPLRPYQKEAIEALL---SGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529    464 E--LYYGSQVEREEIRERINSNkdsYNVMLTTY-RLAATSKADRLFLRNqkFNVCVYDEGHYLKNRA-SERYRHLMS--I 537
Cdd:smart00487  84 KvvGLYGGDSKREQLRKLESGK---TDILVTTPgRLLDLLENDKLSLSN--VDLVILDEAHRLLDGGfGDQLEKLLKllP 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 19114529    538 PADFRVLLTGTP---LQNNLKELISLLAFILP 566
Cdd:smart00487 159 KNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
762-874 1.64e-23

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: 96.13  E-value: 1.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   762 KVRKLKKLLtnAVENGDRVVLFSQFTQVLDIlQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADESInvFLLSTKAGGF 841
Cdd:pfam00271   2 KLEALLELL--KKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID--VLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19114529   842 GINLACANMVILYDVSFNPFDDLQAEDRAHRVG 874
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
403-564 8.27e-23

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 98.31  E-value: 8.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 403 ELKLAGILADEMGLGKTCQTIAFfsLLMDKNingphLVIAPASTMENWLREFAKFCPK--LKIELYYGSQvereeiRERI 480
Cdd:cd18071  46 ELVRGGILADDMGLGKTLTTISL--ILANFT-----LIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGGE------RNRD 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 481 NSNKDSYNVMLTTYRLAAT--SKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELI 558
Cdd:cd18071 113 PKLLSKYDIVLTTYNTLASdfGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192

                ....*.
gi 19114529 559 SLLAFI 564
Cdd:cd18071 193 SLLSFL 198
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
409-571 9.88e-23

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: 97.28  E-value: 9.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 409 ILADEMGLGKTCQTIAFFSLLMDkniNGPHLVIAPASTMENWLREFAKFCPKLKIElyygsqvereEIReRINSNKDSYN 488
Cdd:cd18010  20 LIADEMGLGKTVQAIAIAAYYRE---EWPLLIVCPSSLRLTWADEIERWLPSLPPD----------DIQ-VIVKSKDGLR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 489 -----VMLTTYRLAATSKADrlfLRNQKFNVCVYDEGHYLKNRASERYRHLMSI--PADFRVLLTGTPLQNNLKELISLL 561
Cdd:cd18010  86 dgdakVVIVSYDLLRRLEKQ---LLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQL 162
                       170
                ....*....|
gi 19114529 562 AFILPHVFDY 571
Cdd:cd18010 163 DALDPKLFGR 172
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
387-566 1.50e-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: 1.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLY------LLYELKLAG---ILADEMGLGKTCQTIAFF-SLLMDKNINGPH--LVIAPASTMENWLREF 454
Cdd:cd18068   1 LKPHQVDGVQFMWdcccesLKKTKKSPGsgcILAHCMGLGKTLQVVTFLhTVLLCEKLENFSrvLVVCPLNTVLNWLNEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 455 AKFCPKLK----IELYYGSQVEREEIRE-RINSNKDSYNVMLTTY---RLAATSKADRL----------FLRNQKFNVCV 516
Cdd:cd18068  81 EKWQEGLKdeekIEVNELATYKRPQERSyKLQRWQEEGGVMIIGYdmyRILAQERNVKSreklkeifnkALVDPGPDFVV 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 19114529 517 YDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILP 566
Cdd:cd18068 161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKP 210
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
409-570 5.96e-20

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: 89.27  E-value: 5.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 409 ILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLRE-FAKFcpKLKIELYYGSQVEReeIRERINSNKDSY 487
Cdd:cd18011  21 LLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDElQDKF--GLPFLILDRETAAQ--LRRLIGNPFEEF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 488 NVMLTTYRLAATSKADRLFLRNQKFNVCVYDEGHYLKNRA----SERYRHLMSIPADFR--VLLTGTPLQNNLKELISLL 561
Cdd:cd18011  97 PIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALL 176

                ....*....
gi 19114529 562 AFILPHVFD 570
Cdd:cd18011 177 SLLDPGRFA 185
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
387-566 8.89e-20

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: 89.45  E-value: 8.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYLLYELKLAG-----ILADEMGLGKTCQTIAF-FSLLMDKNINGPHL----VIAPASTMENWLREFAK 456
Cdd:cd18067   1 LRPHQREGVKFLYRCVTGRRIRgshgcIMADEMGLGKTLQCITLmWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 457 FCPKLKIELYYGSQVEREEIRERINS-NKDSYN----VMLTTYRlaaTSKADRLFLRNQKFNVCVYDEGHYLKNRASERY 531
Cdd:cd18067  81 WLGGRLQPLAIDGGSKKEIDRKLVQWaSQQGRRvstpVLIISYE---TFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19114529 532 RHLMSIPADFRVLLTGTPLQNNLKELISLLAFILP 566
Cdd:cd18067 158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNP 192
HELICc smart00490
helicase superfamily c-terminal domain;
791-874 2.12e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.42  E-value: 2.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529    791 DILQLVMKSLNLKFLRFDGSTQVDFRQDLIDQFYADEsiNVFLLSTKAGGFGINLACANMVILYDVSFNPFDDLQAEDRA 870
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 19114529    871 HRVG 874
Cdd:smart00490  79 GRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
387-566 7.20e-19

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: 86.41  E-value: 7.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLY-----LLYELK----LAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMENWLREFAKF 457
Cdd:cd18069   1 LKPHQIGGIRFLYdniieSLERYKgssgFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 458 CPK-----------LKIELYYGSQVEREEIRERINSNKDSYNVMLTTYrlaatskadRLFLRNQKFNVCVYDEGHYLKNR 526
Cdd:cd18069  81 LPPpealpnvrprpFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGY---------EMFRLRPGPDVVICDEGHRIKNC 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19114529 527 ASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILP 566
Cdd:cd18069 152 HASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRP 191
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
408-570 2.20e-18

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: 85.61  E-value: 2.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 408 GILADEMGLGKTCQTIAffSLLMDKN-------------------------INGPHLVIAPASTMENWLREFAKFCP--K 460
Cdd:cd18072  23 GILADDMGLGKTLTMIA--LILAQKNtqnrkeeekekalteweskkdstlvPSAGTLVVCPASLVHQWKNEVESRVAsnK 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 461 LKIELYYGSQvereeiRERINSNKDSYNVMLTTYRLAA----TSKADRLF--LRNQKFNVCVYDEGHYLKNRASERYRHL 534
Cdd:cd18072 101 LRVCLYHGPN------RERIGEVLRDYDIVITTYSLVAkeipTYKEESRSspLFRIAWARIILDEAHNIKNPKVQASIAV 174
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19114529 535 MSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFD 570
Cdd:cd18072 175 CKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFD 210
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
387-572 8.54e-12

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: 65.45  E-value: 8.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLYllyELKLAGILADeMGLGKTCQTIAFFSLLMDKNINGPHLVIAPASTMEN-WLREFAKFcpKLKIEL 465
Cdd:cd18013   1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW--NHLRNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 466 YYGSQVEREeiRERINSNKDSYNVMLTTYRLaaTSKADRLFLRNQKFNVCVYDEGHYLKNRASERYRHLMSIPADFR--V 543
Cdd:cd18013  75 TVSVAVGTE--RQRSKAANTPADLYVINREN--LKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKrlI 150
                       170       180
                ....*....|....*....|....*....
gi 19114529 544 LLTGTPLQNNLKELISLLAFIlphvfDYG 572
Cdd:cd18013 151 GLTGTPSPNGLMDLWAQIALL-----DQG 174
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
387-597 1.96e-11

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: 65.44  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 387 LQDYQIIGINWLyllyeLKLAGILADEMGLGKTCQTIAFfsLLMDKNINGPH---------------------------- 438
Cdd:cd18070   1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLAL--ILLHPRPDNDLdaadddsdemvccpdclvaetpvsskat 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 439 LVIAPASTMENWLREFAKFCPK-LKIELYYG---SQVEREEIRERINsnkdSYNVMLTTYR-LA-----ATSKADRLFLR 508
Cdd:cd18070  74 LIVCPSAILAQWLDEINRHVPSsLKVLTYQGvkkDGALASPAPEILA----EYDIVVTTYDvLRtelhyAEANRSNRRRR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 509 NQK--------------FNVCVyDEGHYLKNRASERYRHLMSIPADFRVLLTGTPLQNNLKELISLLAFILPHVFDYGLK 574
Cdd:cd18070 150 RQKryeappsplvlvewWRVCL-DEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDW 228
                       250       260
                ....*....|....*....|....
gi 19114529 575 SLDVIFTMKKSPE-SDFERALLSE 597
Cdd:cd18070 229 WARVLIRPQGRNKaREPLAALLKE 252
ResIII pfam04851
Type III restriction enzyme, res subunit;
384-549 1.17e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.99  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   384 DIKLQDYQIIGI-NWLYLLYELKLAGILADEMGLGKTCQTIAFFSLLMDKNINGPHLVIAP-ASTMENWLREFAKF--CP 459
Cdd:pfam04851   1 KLELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFlpNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529   460 KLKIELYYGsqvereeirERINSNKDSYNVMLTTY-RLAATSKADRLFLRNQKFNVCVYDEGHYLknrASERYRHLM-SI 537
Cdd:pfam04851  81 VEIGEIISG---------DKKDESVDDNKIVVTTIqSLYKALELASLELLPDFFDVIIIDEAHRS---GASSYRNILeYF 148
                         170
                  ....*....|..
gi 19114529   538 PADFRVLLTGTP 549
Cdd:pfam04851 149 KPAFLLGLTATP 160
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
382-634 2.24e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 57.73  E-value: 2.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 382 SPDIKLQDYQIIGIN-WLYLLYELKLAGILADEMGLGKTcqtiAFFSLLMDKNINGPH-LVIAPAST-MENWLREFAKFc 458
Cdd:COG1061  76 GTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKT----VLALALAAELLRGKRvLVLVPRRElLEQWAEELRRF- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 459 pkLKIELYYGsqvereeireriNSNKDSYNVMLTTYRLAATSKADRLFLRNqkFNVCVYDEGHYLknrASERYRHLMS-I 537
Cdd:COG1061 151 --LGDPLAGG------------GKKDSDAPITVATYQSLARRAHLDELGDR--FGLVIIDEAHHA---GAPSYRRILEaF 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 538 PADFRVLLTGTPLQNNLKELisLLAFILPHVFDYGLKSL-------DVIFTMKKSPESDFERALLSEQRVSRAKMMMAPF 610
Cdd:COG1061 212 PAAYRLGLTATPFRSDGREI--LLFLFDGIVYEYSLKEAiedgylaPPEYYGIRVDLTDERAEYDALSERLREALAADAE 289
                       250       260
                ....*....|....*....|....
gi 19114529 611 VLRRKKSQVLDALPKKTRIIEFCE 634
Cdd:COG1061 290 RKDKILRELLREHPDDRKTLVFCS 313
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
762-882 2.40e-04

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 42.34  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 762 KVRKLKKLLTNAVENGD-----RVVLFSQFTQ-VLDILQLVMK-SLNLKFLRF---------DGSTQVDfRQDLIDQFyA 825
Cdd:cd18801  10 KLEKLEEIVKEHFKKKQegsdtRVIIFSEFRDsAEEIVNFLSKiRPGIRATRFigqasgkssKGMSQKE-QKEVIEQF-R 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19114529 826 DESINVfLLSTKAGGFGINLACANMVILYDVSFNPFDDLQaedRAHRVGQKKEVTVY 882
Cdd:cd18801  88 KGGYNV-LVATSIGEEGLDIGEVDLIICYDASPSPIRMIQ---RMGRTGRKRQGRVV 140
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
758-852 3.33e-04

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: 41.85  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114529 758 MDATKVRKLKKLLTNAvENGDRVVLFSQFtqvLDILQLVMKSLNLKFLrfDGSTQVDFRQDLIDQFyADESINVFLLStK 837
Cdd:cd18789  31 MNPNKLRALEELLKRH-EQGDKIIVFTDN---VEALYRYAKRLLKPFI--TGETPQSEREEILQNF-REGEYNTLVVS-K 102
                        90
                ....*....|....*
gi 19114529 838 AGGFGINLACANMVI 852
Cdd:cd18789 103 VGDEGIDLPEANVAI 117
 
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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