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Conserved domains on  [gi|30687235|ref|NP_197432|]
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homeotic protein regulator [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13327550)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
373-893 6.64e-177

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 544.78  E-value: 6.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   373 KVTKQPSLLQGgELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWEN 452
Cdd:PLN03142  158 RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   453 EFALWAPSISAFLYDGSKEKRTEIRAR-IAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGT 531
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   532 gYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgsASLTDEEEllIINRLHHVIRPFLLRRK 611
Cdd:PLN03142  317 -FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI-------SGENDQQE--VVQQLHKVLRPFLLRRL 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   612 KSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGnGKSKSLQNLTMQLRKCCNHPYLFVGADYN--MCKKPE 689
Cdd:PLN03142  387 KSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG-GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTGEH 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   690 IVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLL 769
Cdd:PLN03142  466 LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLL 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   770 STRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLF 849
Cdd:PLN03142  546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL 625
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 30687235   850 --NTTSTAQDRREML----EEIMSKGTSSLgedvpSEREINRLAARTEEE 893
Cdd:PLN03142  626 aeQKTVNKDELLQMVrygaEMVFSSKDSTI-----TDEDIDRIIAKGEEA 670
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
898-964 7.07e-12

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


:

Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 61.51  E-value: 7.07e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30687235    898 EQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDK----TNAKNHFGslTGKRKRKEAVYSDSLSDLQWM 964
Cdd:pfam14619    1 ERRREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKedkeELDEQVYG--RGKRKRKEVSYSDGLTEEQWL 69
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
373-893 6.64e-177

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 544.78  E-value: 6.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   373 KVTKQPSLLQGgELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWEN 452
Cdd:PLN03142  158 RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   453 EFALWAPSISAFLYDGSKEKRTEIRAR-IAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGT 531
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   532 gYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgsASLTDEEEllIINRLHHVIRPFLLRRK 611
Cdd:PLN03142  317 -FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI-------SGENDQQE--VVQQLHKVLRPFLLRRL 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   612 KSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGnGKSKSLQNLTMQLRKCCNHPYLFVGADYN--MCKKPE 689
Cdd:PLN03142  387 KSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG-GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTGEH 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   690 IVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLL 769
Cdd:PLN03142  466 LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLL 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   770 STRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLF 849
Cdd:PLN03142  546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL 625
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 30687235   850 --NTTSTAQDRREML----EEIMSKGTSSLgedvpSEREINRLAARTEEE 893
Cdd:PLN03142  626 aeQKTVNKDELLQMVrygaEMVFSSKDSTI-----TDEDIDRIIAKGEEA 670
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
301-845 1.74e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 425.02  E-value: 1.74e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  301 LGAAVQRQKDAKLSENTKLLKGSESDLSDVDAPEDVLPAQDIEIIDSDNNDDSNDLLEGERQFNLAIHSIQEKVTKQPSL 380
Cdd:COG0553  158 LLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAG 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  381 LQGgELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDlHGPHLILAPKAVLPNWENEFALWAPS 460
Cdd:COG0553  238 LKA-TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLVGNWQRELAKFAPG 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  461 ISAFLYDGSKEkRTEIRARIAggKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECA---LAKTLgtgyRIKR 537
Cdd:COG0553  316 LRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKrakAVRAL----KARH 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  538 RLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAEcgsaslTDEEELliiNRLHHVIRPFLLRRKKSEVEK 617
Cdd:COG0553  389 RLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEK------GDEEAL---ERLRRLLRPFLLRRTKEDVLK 459
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  618 FLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGNGKSKSLQNLT--MQLRKCCNHPYLFVGadynmcKKPEIVRASG 695
Cdd:COG0553  460 DLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAalTRLRQICSHPALLLE------EGAELSGRSA 533
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  696 KFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFmFLLSTRAGG 775
Cdd:COG0553  534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGG 612
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  776 LGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQ 845
Cdd:COG0553  613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
383-612 9.78e-124

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: 377.48  E-value: 9.78e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  383 GGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSIS 462
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  463 AFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTGYRIKRRLLLT 542
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30687235  543 GTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSAS---LTDEEELLIINRLHHVIRPFLLRRKK 612
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkieLNEEETLLIIRRLHKVLRPFLLRRLK 233
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-677 8.02e-103

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: 324.25  E-value: 8.02e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    389 YQLEGLQWMVSLYNNDY-NGILADEMGLGKTIQTIALIAYLLESKDLHG-PHLILAPKAVLPNWENEFALWA--PSISAF 464
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    465 LYDGSKEKR-TEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLLLTG 543
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS-LKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    544 TPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSAsltdeeelLIINRLHHVIRPFLLRRKKSEVEKFLPGKT 623
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK--------KGVSRLHKLLKPFLLRRTKKDVEKSLPPKV 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 30687235    624 QVILKCDMSAWQKLYYKQVT---DVGRVGL-HSGNGKSKSLQNLTMQLRKCCNHPYLF 677
Cdd:pfam00176  232 EYILFCRLSKLQRKLYQTFLlkkDLNAIKTgEGGREIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
385-562 5.18e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.06  E-value: 5.18e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235     385 ELRSYQLEGLQWMVSLYNNdynGILADEMGLGKTIQTIALIAYLLeSKDLHGPHLILAP-KAVLPNWENEFALWAPS--- 460
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPtRELAEQWAEELKKLGPSlgl 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235     461 ISAFLYDGskEKRTEIRARIAGGKFNVLITHYDLIMRD--KAFLKKIDWNYMIVDEGHRLKN--HECALAKTLGTGYRIK 536
Cdd:smart00487   84 KVVGLYGG--DSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNV 161
                           170       180
                    ....*....|....*....|....*....
gi 30687235     537 RRLLLTGTP---IQNSLQELWSLLNFLLP 562
Cdd:smart00487  162 QLLLLSATPpeeIENLLELFLNDPVFIDV 190
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
898-964 7.07e-12

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 61.51  E-value: 7.07e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30687235    898 EQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDK----TNAKNHFGslTGKRKRKEAVYSDSLSDLQWM 964
Cdd:pfam14619    1 ERRREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKedkeELDEQVYG--RGKRKRKEVSYSDGLTEEQWL 69
DpdE NF041062
protein DpdE;
409-573 6.36e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 53.82  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   409 LADEMGLGKTIQTIALI-AYLLESKDLHGphLILAPKAVLPNWenefalwapsisaflydgskekRTEIRARIAGGKF-- 485
Cdd:NF041062  175 LADEVGLGKTIEAGLVIrQHLLDNPDARV--LVLVPDALVRQW----------------------RRELRDKFFLDDFpg 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   486 -NVLITHYDLIMRDKAFLKKIDwnYMIVDEGHRLKNHECALAKTLGTGYR--------IKRRLLLTGTPIQNSLQELWSL 556
Cdd:NF041062  231 aRVRVLSHEEPERWEPLLDAPD--LLVVDEAHQLARLAWSGDPPERARYRelaalahaAPRLLLLSATPVLGNEETFLAL 308
                         170
                  ....*....|....*....
gi 30687235   557 LNFLLPHIF--NSIHNFEE 573
Cdd:NF041062  309 LHLLDPDLYplDDLEAFRE 327
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
373-893 6.64e-177

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 544.78  E-value: 6.64e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   373 KVTKQPSLLQGgELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWEN 452
Cdd:PLN03142  158 RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   453 EFALWAPSISAFLYDGSKEKRTEIRAR-IAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGT 531
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   532 gYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgsASLTDEEEllIINRLHHVIRPFLLRRK 611
Cdd:PLN03142  317 -FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI-------SGENDQQE--VVQQLHKVLRPFLLRRL 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   612 KSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGnGKSKSLQNLTMQLRKCCNHPYLFVGADYN--MCKKPE 689
Cdd:PLN03142  387 KSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG-GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTGEH 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   690 IVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLL 769
Cdd:PLN03142  466 LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLL 545
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   770 STRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLF 849
Cdd:PLN03142  546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL 625
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 30687235   850 --NTTSTAQDRREML----EEIMSKGTSSLgedvpSEREINRLAARTEEE 893
Cdd:PLN03142  626 aeQKTVNKDELLQMVrygaEMVFSSKDSTI-----TDEDIDRIIAKGEEA 670
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
301-845 1.74e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 425.02  E-value: 1.74e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  301 LGAAVQRQKDAKLSENTKLLKGSESDLSDVDAPEDVLPAQDIEIIDSDNNDDSNDLLEGERQFNLAIHSIQEKVTKQPSL 380
Cdd:COG0553  158 LLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAG 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  381 LQGgELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDlHGPHLILAPKAVLPNWENEFALWAPS 460
Cdd:COG0553  238 LKA-TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLVGNWQRELAKFAPG 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  461 ISAFLYDGSKEkRTEIRARIAggKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECA---LAKTLgtgyRIKR 537
Cdd:COG0553  316 LRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKrakAVRAL----KARH 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  538 RLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAEcgsaslTDEEELliiNRLHHVIRPFLLRRKKSEVEK 617
Cdd:COG0553  389 RLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEK------GDEEAL---ERLRRLLRPFLLRRTKEDVLK 459
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  618 FLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGNGKSKSLQNLT--MQLRKCCNHPYLFVGadynmcKKPEIVRASG 695
Cdd:COG0553  460 DLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAalTRLRQICSHPALLLE------EGAELSGRSA 533
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  696 KFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFmFLLSTRAGG 775
Cdd:COG0553  534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGG 612
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  776 LGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQ 845
Cdd:COG0553  613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
383-612 9.78e-124

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: 377.48  E-value: 9.78e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  383 GGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSIS 462
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  463 AFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTGYRIKRRLLLT 542
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30687235  543 GTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSAS---LTDEEELLIINRLHHVIRPFLLRRKK 612
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkieLNEEETLLIIRRLHKVLRPFLLRRLK 233
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-677 8.02e-103

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: 324.25  E-value: 8.02e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    389 YQLEGLQWMVSLYNNDY-NGILADEMGLGKTIQTIALIAYLLESKDLHG-PHLILAPKAVLPNWENEFALWA--PSISAF 464
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    465 LYDGSKEKR-TEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLLLTG 543
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS-LKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    544 TPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSAsltdeeelLIINRLHHVIRPFLLRRKKSEVEKFLPGKT 623
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK--------KGVSRLHKLLKPFLLRRTKKDVEKSLPPKV 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 30687235    624 QVILKCDMSAWQKLYYKQVT---DVGRVGL-HSGNGKSKSLQNLTMQLRKCCNHPYLF 677
Cdd:pfam00176  232 EYILFCRLSKLQRKLYQTFLlkkDLNAIKTgEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
368-612 3.73e-95

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: 302.37  E-value: 3.73e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  368 HSIQEKVTKQPSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVL 447
Cdd:cd18063    6 HAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  448 PNWENEFALWAPSISAFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAK 527
Cdd:cd18063   86 SNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  528 TLGTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGS-ASLTDEEELLIINRLHHVIRPF 606
Cdd:cd18063  166 VLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGErVDLNEEETILIIRRLHKVLRPF 245

                 ....*.
gi 30687235  607 LLRRKK 612
Cdd:cd18063  246 LLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
368-612 7.41e-94

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: 298.88  E-value: 7.41e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  368 HSIQEKVTKQPSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVL 447
Cdd:cd18062    6 HAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  448 PNWENEFALWAPSISAFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAK 527
Cdd:cd18062   86 SNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  528 TLGTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGS-ASLTDEEELLIINRLHHVIRPF 606
Cdd:cd18062  166 VLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEkVDLNEEETILIIRRLHKVLRPF 245

                 ....*.
gi 30687235  607 LLRRKK 612
Cdd:cd18062  246 LLRRLK 251
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
383-612 2.19e-92

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: 294.29  E-value: 2.19e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  383 GGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLEsKDLHGPHLILAPKAVLPNWENEFALWAPSIS 462
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  463 AFLYDGSKEKRTEIRARI-----AGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKR 537
Cdd:cd18009   80 VLLYHGTKEERERLRKKImkregTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT-FNSDN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  538 RLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNtpFAECGSAS-----LTDEEELLIINRLHHVIRPFLLRRKK 612
Cdd:cd18009  159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFD--FSSLSDNAadisnLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
383-612 3.09e-89

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: 285.37  E-value: 3.09e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  383 GGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSIS 462
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  463 AFLYDGSKEKRTEI-RARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLLL 541
Cdd:cd17997   81 VVVLIGDKEERADIiRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRL-FNSRNRLLL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30687235  542 TGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgSASLTDEEELliINRLHHVIRPFLLRRKK 612
Cdd:cd17997  160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV------NNCDDDNQEV--VQRLHKVLRPFLLRRIK 222
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
386-565 1.84e-81

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 262.50  E-value: 1.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRIKRRLLLTGTP 545
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKAL-KALRAKRRLLLTGTP 159
                        170       180
                 ....*....|....*....|
gi 30687235  546 IQNSLQELWSLLNFLLPHIF 565
Cdd:cd17919  160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
385-610 5.97e-78

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: 254.59  E-value: 5.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  385 ELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAF 464
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  465 LYDGSKEKRTEIR---------ARIaggKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRI 535
Cdd:cd17993   81 VYLGDIKSRDTIReyefyfsqtKKL---KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEAL-KEFKT 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30687235  536 KRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEwfntpfaecgsasLTDEEELLIINRLHHVIRPFLLRR 610
Cdd:cd17993  157 NNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE-------------EHDEEQEKGIADLHKELEPFILRR 218
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
386-610 2.15e-76

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: 250.35  E-value: 2.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRARIAG-GKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLLLTGT 544
Cdd:cd18003   81 YYGSAKERKLKRQGWMKpNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30687235  545 PIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIinRLHHVIRPFLLRR 610
Cdd:cd18003  160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGSQEENEELVR--RLHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
378-622 1.34e-72

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: 240.72  E-value: 1.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  378 PSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALW 457
Cdd:cd18064    8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  458 APSISAFLYDGSKEKRTE-IRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIK 536
Cdd:cd18064   88 VPTLRAVCLIGDKDQRAAfVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE-FKTT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  537 RRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgSASLTDEEellIINRLHHVIRPFLLRRKKSEVE 616
Cdd:cd18064  167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT------NNCLGDQK---LVERLHMVLRPFLLRRIKADVE 237

                 ....*.
gi 30687235  617 KFLPGK 622
Cdd:cd18064  238 KSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
378-612 7.37e-71

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: 235.68  E-value: 7.37e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  378 PSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALW 457
Cdd:cd18065    8 PSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  458 APSISAFLYDGSKEKRTE-IRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIK 536
Cdd:cd18065   88 VPSLRAVCLIGDKDARAAfIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE-FKTT 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30687235  537 RRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTpfaecgSASLTDEEellIINRLHHVIRPFLLRRKK 612
Cdd:cd18065  167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT------KNCLGDQK---LVERLHAVLKPFLLRRIK 233
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
386-610 6.22e-69

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: 229.83  E-value: 6.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPsISAFL 465
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIR----------ARIAGG--KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgY 533
Cdd:cd17995   80 YHGSGESRQIIQqyemyfkdaqGRKKKGvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKK-L 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd17995  159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---------GDLKTAEQ---VEKLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
386-610 2.39e-66

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: 222.77  E-value: 2.39e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRA-------RIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRIKRR 538
Cdd:cd18002   81 YWGNPKDRKVLRKfwdrknlYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30687235  539 LLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPF-AECGSASLTDEEELliiNRLHHVIRPFLLRR 610
Cdd:cd18002  160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIeSHAENKTGLNEHQL---KRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
376-610 1.66e-65

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: 221.03  E-value: 1.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  376 KQPSLL--QGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENE 453
Cdd:cd18054    9 KQPSYIggENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  454 FALWAPSISAFLYDGSKEKRTEIR------ARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAK 527
Cdd:cd18054   89 FEIWAPEINVVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  528 TLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPfAECGSASltdeeelliinrLHHVIRPFL 607
Cdd:cd18054  169 TL-IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKG-RENGYQS------------LHKVLEPFL 234

                 ...
gi 30687235  608 LRR 610
Cdd:cd18054  235 LRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
384-612 4.22e-64

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: 216.28  E-value: 4.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  384 GELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLhGPHLILAPKAVLPNWENEFALWAPSISA 463
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRK-GPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  464 FLYDGSKEKRTEIRARiagGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLLLTG 543
Cdd:cd18012   82 LVIHGTKRKREKLRAL---EDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKA-LKADHRLALTG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30687235  544 TPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPfaecgSASLTDEEELliiNRLHHVIRPFLLRRKK 612
Cdd:cd18012  158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP-----IEKDGDEEAL---EELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
386-610 3.35e-61

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: 208.06  E-value: 3.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRARI-AGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRIKRRLLLTGT 544
Cdd:cd18006   81 YMGDKEKRLDLQQDIkSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTL-SEFSVDFRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30687235  545 PIQNSLQELWSLLNFLLPHIFNSihNFEEWFNTPFAECGSASLTDEEelliinrLHHVIRPFLLRR 610
Cdd:cd18006  160 PIQNSLQELYALLSFIEPNVFPK--DKLDDFIKAYSETDDESETVEE-------LHLLLQPFLLRR 216
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
386-565 1.88e-59

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: 201.84  E-value: 1.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDlHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRARIAGG--KFNVLITHYDLIM---RDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgYRIKRRLL 540
Cdd:cd17998   80 YYGSQEERKHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
                        170       180
                 ....*....|....*....|....*
gi 30687235  541 LTGTPIQNSLQELWSLLNFLLPHIF 565
Cdd:cd17998  159 LTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
694-820 1.25e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.54  E-value: 1.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  694 SGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPyFMFLLSTRA 773
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30687235  774 GGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLV 820
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
386-610 3.54e-55

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: 189.96  E-value: 3.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSkekrteirariaggkfNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRIKRRLLLTGTP 545
Cdd:cd17994   81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRIL-NSYKIGYKLLLTGTP 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30687235  546 IQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERFNNLQGFLEEF---------ADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
386-610 7.03e-54

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: 187.94  E-value: 7.03e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLynNDYN--GILADEMGLGKTIQTIALIA---YLLES--KDLHGPHLILAPKAVLPNWENEFALWA 458
Cdd:cd17999    1 LRPYQQEGINWLAFL--NKYNlhGILCDDMGLGKTLQTLCILAsdhHKRANsfNSENLPSLVVCPPTLVGHWVAEIKKYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  459 P--SISAFLYDGSKEKRTEIRARiaGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGYRIK 536
Cdd:cd17999   79 PnaFLKPLAYVGPPQERRRLREQ--GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKAN 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  537 RRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSA---SLTDEEELLIINRLHHVIRPFLLRR 610
Cdd:cd17999  156 HRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSkasAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
376-610 3.23e-53

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: 186.02  E-value: 3.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  376 KQPSLLQGGE---LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWEN 452
Cdd:cd18053    8 KQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  453 EFALWAPSISAFLYDGSKEKRTEIRA------RIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALA 526
Cdd:cd18053   88 EIQTWAPQMNAVVYLGDINSRNMIRThewmhpQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  527 KTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPfAECGSASltdeeelliinrLHHVIRPF 606
Cdd:cd18053  168 KTL-IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKG-REYGYAS------------LHKELEPF 233

                 ....
gi 30687235  607 LLRR 610
Cdd:cd18053  234 LLRR 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
386-610 7.94e-53

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: 184.88  E-value: 7.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPhLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDG-SKEKRTEIRARIAGGkFNVLITHYDLIMRDKAFLKKID-----WNYMIVDEGHRLKNHECALAKTLgTGYRIKRRL 539
Cdd:cd18001   80 FHGtSKKERERNLERIQRG-GGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSL-REIPAKNRI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30687235  540 LLTGTPIQNSLQELWSLLNFLLPH-IFNSIHNFEEWFNTPFAECGSASLTDEEELL---IINRLHHVIRPFLLRR 610
Cdd:cd18001  158 ILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALgseVAENLRQIIKPYFLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
386-610 2.40e-50

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: 177.90  E-value: 2.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRAR--------IAGG------------KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECAL 525
Cdd:cd18055   81 YTGDKDSRAIIRENefsfddnaVKGGkkafkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  526 AKTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRP 605
Cdd:cd18055  161 FRVL-NGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ---IKKLHDLLGP 227

                 ....*
gi 30687235  606 FLLRR 610
Cdd:cd18055  228 HMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
386-610 1.38e-48

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: 172.56  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIR--------------------ARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECAL 525
Cdd:cd18057   81 YTGDKESRSVIRenefsfednairsgkkvfrmKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  526 AKTLGTgYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRP 605
Cdd:cd18057  161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ---IKKLHDLLGP 227

                 ....*
gi 30687235  606 FLLRR 610
Cdd:cd18057  228 HMLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
386-562 1.96e-47

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: 167.89  E-value: 1.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 ------YDGSKEK-----RTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKN--HECALA-KTLGT 531
Cdd:cd18000   81 lhssgsGTGSEEKlgsieRKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNpdAEITLAcKQLRT 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 30687235  532 GYRIkrrlLLTGTPIQNSLQELWSLLNFLLP 562
Cdd:cd18000  161 PHRL----ILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
386-610 3.83e-47

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: 168.30  E-value: 3.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLeSKDLHGPHLILAPKAVLPNWENEFALWApSISAFL 465
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRT-----EIRARIAGG-------KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgY 533
Cdd:cd18058   79 YHGSQISRQmiqqyEMYYRDEQGnplsgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL-M 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd18058  158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF---------GDLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
386-610 4.66e-47

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: 168.32  E-value: 4.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFL 465
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRAR--------IAGG------------KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECAL 525
Cdd:cd18056   81 YVGDKDSRAIIRENefsfednaIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  526 AKTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRP 605
Cdd:cd18056  161 FRVL-NGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF---------ADIAKEDQ---IKKLHDMLGP 227

                 ....*
gi 30687235  606 FLLRR 610
Cdd:cd18056  228 HMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
386-610 7.69e-47

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: 167.94  E-value: 7.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLL-------ESKDLH-------------GPHLILAPKA 445
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrDRENNRprfkkkppassakKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  446 VLPNWENEFALWApSISAFLYDGSKEKRtEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECAL 525
Cdd:cd18005   81 VLYNWKDELDTWG-HFEVGVYHGSRKDD-ELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  526 AKTLGTgYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVI-- 603
Cdd:cd18005  159 TQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAvk 237

                 ....*...
gi 30687235  604 -RPFLLRR 610
Cdd:cd18005  238 lSKFFLRR 245
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
386-610 3.16e-45

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: 162.51  E-value: 3.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIaYLLESKDLHGPHLILAPKAVLPNWENEFALWApSISAFL 465
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEIRA----------RIAGG--KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgY 533
Cdd:cd18059   79 YHGSQASRRTIQLyemyfkdpqgRVIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM-M 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd18059  158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---------GDLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
386-610 1.27e-44

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: 160.99  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLeSKDLHGPHLILAPKAVLPNWENEFALWApSISAFL 465
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEI----------RARIAGG--KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgY 533
Cdd:cd18060   79 YHGSLASRQMIqqyemyckdsRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH-M 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd18060  158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---------GDLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
386-610 6.06e-44

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: 159.76  E-value: 6.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVS--LYNNDYNG---ILADEMGLGKTIQTIALIAYLLESKDLHGPH----LILAPKAVLPNWENEFAL 456
Cdd:cd18004    1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  457 WAPS--ISAFLYDGSKEKR-TEIRARIAGGKFNVLITHYDLIMR-DKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTg 532
Cdd:cd18004   81 WLGLrrIKVVTADGNAKDVkASLDFFSSASTYPVLIISYETLRRhAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  533 YRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVIR---PFLLR 609
Cdd:cd18004  160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSEltsRFILR 239

                 .
gi 30687235  610 R 610
Cdd:cd18004  240 R 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
386-610 8.40e-43

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: 156.29  E-value: 8.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSlynndYNGILADEMGLGKTIQTIALIA---------------YLLESKDLHGPH--LILAPKAVLP 448
Cdd:cd18008    1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALALILatrpqdpkipeeleeNSSDPKKLYLSKttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  449 NWENEFA--LWAPSISAFLYDGSKEKRTEIRARiaggKFNVLITHYDLIMRD----------------KAFLKKIDWNYM 510
Cdd:cd18008   76 QWKDEIEkhTKPGSLKVYVYHGSKRIKSIEELS----DYDIVITTYGTLASEfpknkkgggrdskekeASPLHRIRWYRV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  511 IVDEGHRLKNHECALAK---TLgtgyRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFaecgsasl 587
Cdd:cd18008  152 ILDEAHNIKNRSTKTSRavcAL----KAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF-------- 219
                        250       260
                 ....*....|....*....|...
gi 30687235  588 tDEEELLIINRLHHVIRPFLLRR 610
Cdd:cd18008  220 -SKNDRKALERLQALLKPILLRR 241
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
386-610 4.89e-39

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: 144.76  E-value: 4.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESkDLHGPHLILAPKAVLPNWENEFALWApSISAFL 465
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  466 YDGSKEKRTEI----------RARIAGG--KFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTgY 533
Cdd:cd18061   79 YHGSLISRQMIqqyemyfrdsQGRIIRGayRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL-M 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFntpfaecgsASLTDEEElliINRLHHVIRPFLLRR 610
Cdd:cd18061  158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---------GDLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
386-610 2.35e-35

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: 134.59  E-value: 2.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQW-----MVSLYNNDYNGILADEMGLGKTIQTIALIAYLLE-----SKDLHGPHLILAPKAVLPNWENEFA 455
Cdd:cd18066    1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRqgpygGKPVIKRALIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  456 LWAPS--ISAFLYDGSKEkrteIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLgTGY 533
Cdd:cd18066   81 KWLGSerIKVFTVDQDHK----VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  534 RIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINR---LHHVIRPFLLRR 610
Cdd:cd18066  156 SCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaeLTRLTGLFILRR 235
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
386-594 1.15e-31

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: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWM-----VSLYNNDYNG--ILADEMGLGKTIQTIALI-AYLLESKDLHGPhLILAPKAVLPNWENEFALW 457
Cdd:cd18007    1 LKPHQVEGVRFLwsnlvGTDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  458 APSISAFLYDGSkEKRTEIRARIAGGKFN-------VLITHYDL--------------IMRDKAFLKKIDWNYMIVDEGH 516
Cdd:cd18007   80 LPPDLRPLLVLV-SLSASKRADARLRKINkwhkeggVLLIGYELfrnlasnattdprlKQEFIAALLDPGPDLLVLDEGH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  517 RLKNHECALAKTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAE--CGSASLTDEEELL 594
Cdd:cd18007  159 RLKNEKSQLSKAL-SKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAgqCVDSTEEDVRLML 237
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
386-610 4.05e-31

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: 122.58  E-value: 4.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWM----VSLYNNDYNG-ILADEMGLGKTIQTIALIAYLL----ESKDLHGPHLILAPKAVLPNWENEFAL 456
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  457 W-APSISAFLYDGSKEKRTEIR----ARIAGGKFN--VLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTL 529
Cdd:cd18067   81 WlGGRLQPLAIDGGSKKEIDRKlvqwASQQGRRVStpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  530 gTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVI---RPF 606
Cdd:cd18067  161 -DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELIsivNRC 239

                 ....
gi 30687235  607 LLRR 610
Cdd:cd18067  240 IIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
385-562 5.18e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.06  E-value: 5.18e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235     385 ELRSYQLEGLQWMVSLYNNdynGILADEMGLGKTIQTIALIAYLLeSKDLHGPHLILAP-KAVLPNWENEFALWAPS--- 460
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPtRELAEQWAEELKKLGPSlgl 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235     461 ISAFLYDGskEKRTEIRARIAGGKFNVLITHYDLIMRD--KAFLKKIDWNYMIVDEGHRLKN--HECALAKTLGTGYRIK 536
Cdd:smart00487   84 KVVGLYGG--DSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNV 161
                           170       180
                    ....*....|....*....|....*....
gi 30687235     537 RRLLLTGTP---IQNSLQELWSLLNFLLP 562
Cdd:smart00487  162 QLLLLSATPpeeIENLLELFLNDPVFIDV 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
386-610 1.66e-30

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 120.00  E-value: 1.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSlynndYNG--ILADEMGLGKTIQTIALIAYLLESkdlhGPHLILAPKAVLPNWENEFALWAPSISA 463
Cdd:cd18010    1 LLPFQREGVCFALR-----RGGrvLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLPP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  464 ---FLYDGSKEKRTEIRARIaggkfnvLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGT-GYRIKRRL 539
Cdd:cd18010   72 ddiQVIVKSKDGLRDGDAKV-------VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPlLKRAKRVI 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30687235  540 LLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEE-----WFNTPFAECGSASLTDEEELLIINRlhhvirpFLLRR 610
Cdd:cd18010  145 LLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaaKQGGFGWDYSGSSNLEELHLLLLAT-------IMIRR 213
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
695-809 1.26e-28

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: 110.76  E-value: 1.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    695 GKFELLDRLLPKLKkaGHRILLFSQMTRLIDLlEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPyfmFLLSTRAG 774
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30687235    775 GLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIG 809
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
386-560 1.80e-27

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: 112.18  E-value: 1.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNND-------------YN----------------GILADEMGLGKTIQTIALIaylleskdLHG 436
Cdd:cd18071    1 LLPHQKQALAWMVSRENSQdlppfweeavglfLNtitnfsqkkrpelvrgGILADDMGLGKTLTTISLI--------LAN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  437 PHLILAPKAVLPNWENEFA--LWAPSISAFLYDGSKEKRTEIRAriagGKFNVLITHYDLIMRDKAF-----LKKIDWNY 509
Cdd:cd18071   73 FTLIVCPLSVLSNWETQFEehVKPGQLKVYTYHGGERNRDPKLL----SKYDIVLTTYNTLASDFGAkgdspLHTINWLR 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30687235  510 MIVDEGHRLKNHECALAKTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFL 560
Cdd:cd18071  149 VVLDEGHQIRNPNAQQTKAV-LNLSSERRWVLTGTPIQNSPKDLGSLLSFL 198
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
386-589 1.97e-23

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: 100.73  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWM---------VSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPH--LILAPKAVLPNWENEF 454
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSrvLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  455 ALWAPSI----SAFLYDGSKEKRTEIRARIAGGKFN---VLITHYDLIM-----RDKAFLKKIDWNYM-----------I 511
Cdd:cd18068   81 EKWQEGLkdeeKIEVNELATYKRPQERSYKLQRWQEeggVMIIGYDMYRilaqeRNVKSREKLKEIFNkalvdpgpdfvV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  512 VDEGHRLKNHECALAKTLgTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPF--AECGSASLTD 589
Cdd:cd18068  161 CDEGHILKNEASAVSKAM-NSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIqnGQCADSTLVD 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
408-568 3.75e-23

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: 98.52  E-value: 3.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  408 ILADEMGLGKTIQTIALIAYLLESkDLHGPHLILAPKAVLPNWENEfaLWA-PSISAFLYDGSKEKRTEIRARIAGGKFN 486
Cdd:cd18011   21 LLADEVGLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDE--LQDkFGLPFLILDRETAAQLRRLIGNPFEEFP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  487 VLITHYDLIMRDK---AFLKKIDWNYMIVDEGHRLKNHECA-------LAKTLGTgyRIKRRLLLTGTPIQNSLQELWSL 556
Cdd:cd18011   98 IVIVSLDLLKRSEerrGLLLSEEWDLVVVDEAHKLRNSGGGketkrykLGRLLAK--RARHVLLLTATPHNGKEEDFRAL 175
                        170
                 ....*....|..
gi 30687235  557 LNFLLPHIFNSI 568
Cdd:cd18011  176 LSLLDPGRFAVL 187
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
386-578 1.43e-22

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: 97.58  E-value: 1.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMvslYNN------DYNG------ILADEMGLGKTIQTIALIAYLLESKDLHGPhLILAPKAVLPNWENE 453
Cdd:cd18069    1 LKPHQIGGIRFL---YDNiiesleRYKGssgfgcILAHSMGLGKTLQVISFLDVLLRHTGAKTV-LAIVPVNTLQNWLSE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  454 FALWAPSISA------------FLYDGSKEKRTEIRA----RIAGGkfnVLITHYDLimrdkaFLKKIDWNYMIVDEGHR 517
Cdd:cd18069   77 FNKWLPPPEAlpnvrprpfkvfILNDEHKTTAARAKViedwVKDGG---VLLMGYEM------FRLRPGPDVVICDEGHR 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30687235  518 LKNHECALAKTLGTgYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTP 578
Cdd:cd18069  148 IKNCHASTSQALKN-IRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERP 207
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
386-610 1.19e-21

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 95.24  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYN-NDYNGILADEMGLGKTIQTIALIAY--------------LLESKDLH--------GPHLILA 442
Cdd:cd18072    1 LLLHQKQALAWLLWRERqKPRGGILADDMGLGKTLTMIALILAqkntqnrkeeekekALTEWESKkdstlvpsAGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  443 PKAVLPNWENEFALWAPS--ISAFLYDG-SKEKRTEIRARiaggkFNVLITHYDLIMRDKAFLKK---------IDWNYM 510
Cdd:cd18072   81 PASLVHQWKNEVESRVASnkLRVCLYHGpNRERIGEVLRD-----YDIVITTYSLVAKEIPTYKEesrssplfrIAWARI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  511 IVDEGHRLKNH--ECALAKTlgtGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGsaslt 588
Cdd:cd18072  156 ILDEAHNIKNPkvQASIAVC---KLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----- 227
                        250       260
                 ....*....|....*....|..
gi 30687235  589 deeelliiNRLHHVIRPFLLRR 610
Cdd:cd18072  228 --------ERLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
725-809 2.51e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.81  E-value: 2.51e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235     725 DLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPyfmFLLSTRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDR 804
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 30687235     805 AHRIG 809
Cdd:smart00490   78 AGRAG 82
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
386-560 5.04e-19

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: 87.02  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSlynNDYNGILADeMGLGKTIQTIALIAYLLESkDLHGPHLILAPKAVLPN-WENEFALWA--PSIS 462
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLD-DFTRRVLVIAPLRVARStWPDEVEKWNhlRNLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  463 AFLYDGSKEKRTeiraRIAGGKFNVLITHYDLIMR-DKAFLKKIDWNYMIVDEGHRLKNHECALAKTL-GTGYRIKRRLL 540
Cdd:cd18013   76 VSVAVGTERQRS----KAANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALrKVRPVIKRLIG 151
                        170       180
                 ....*....|....*....|
gi 30687235  541 LTGTPIQNSLQELWSLLNFL 560
Cdd:cd18013  152 LTGTPSPNGLMDLWAQIALL 171
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
386-565 6.13e-18

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: 84.70  E-value: 6.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLynndyNGILADEMGLGKTIQTIALI------------AYLLESKDLHGPH-------------LI 440
Cdd:cd18070    1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDclvaetpvsskatLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  441 LAPKAVLPNWENEFALWAP-SISAFLYDGSKE---KRTEIRARIAggKFNVLITHYDLI--------------------- 495
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKdgaLASPAPEILA--EYDIVVTTYDVLrtelhyaeanrsnrrrrrqkr 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30687235  496 -MRDKAFLKKIDWNYMIVDEGHRLknhECALAKTLGTGYRIKR--RLLLTGTPIQNSLQELWSLLNFLLPHIF 565
Cdd:cd18070  154 yEAPPSPLVLVEWWRVCLDEAQMV---ESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFLGVEPF 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
386-545 4.75e-12

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 64.63  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMVSLYNNDYnGILADEMGLGKTIQTIALIAYLLEskdlhGPHLILAPKAVLPN-WENEFALWAPSISAF 464
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR-GILVLPTGSGKTLTALALIAYLKE-----LRTLIVVPTDALLDqWKERFEDFLGDSSIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  465 LYDGSKEKRTEIRariaggkfNVLITHYDLIMRDKAFLKKI--DWNYMIVDEGHRLKnhecalAKTLG---TGYRIKRRL 539
Cdd:cd17926   75 LIGGGKKKDFDDA--------NVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLP------AKTFSeilKELNAKYRL 140

                 ....*.
gi 30687235  540 LLTGTP 545
Cdd:cd17926  141 GLTATP 146
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
898-964 7.07e-12

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 61.51  E-value: 7.07e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30687235    898 EQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDK----TNAKNHFGslTGKRKRKEAVYSDSLSDLQWM 964
Cdd:pfam14619    1 ERRREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKedkeELDEQVYG--RGKRKRKEVSYSDGLTEEQWL 69
ResIII pfam04851
Type III restriction enzyme, res subunit;
385-546 1.86e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    385 ELRSYQLEGLQ-WMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESkdLHGPH-LILAP-KAVLPNWENEFALWAPSi 461
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKK--GPIKKvLFLVPrKDLLEQALEEFKKFLPN- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    462 saflYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRD--KAFLKKID--WNYMIVDEGHRL--KNHECALAKtlgtgYRI 535
Cdd:pfam04851   80 ----YVEIGEIISGDKKDESVDDNKIVVTTIQSLYKAleLASLELLPdfFDVIIIDEAHRSgaSSYRNILEY-----FKP 150
                          170
                   ....*....|.
gi 30687235    536 KRRLLLTGTPI 546
Cdd:pfam04851  151 AFLLGLTATPE 161
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
405-544 1.94e-08

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 54.33  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  405 YNGILADEMGLGKTIqtIALIAYLLESKDLHGPHLILAP-KAVLPNWENEF-ALWAPSISAFLYDGSKEKrtEIRARIAG 482
Cdd:cd00046    2 ENVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPtKALALQTAERLrELFGPGIRVAVLVGGSSA--EEREKNKL 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30687235  483 GKFNVLITHYDLIMRDKAFLKKI---DWNYMIVDEGHR-LKNHECALAKTLGTGYRIK---RRLLLTGT 544
Cdd:cd00046   78 GDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHAlLIDSRGALILDLAVRKAGLknaQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
384-545 2.18e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.11  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  384 GELRSYQLEGL-QWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLhgphLILAP-KAVLPNWENEFALWAPSI 461
Cdd:COG1061   79 FELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPrRELLEQWAEELRRFLGDP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  462 SAflYDGSKEKRteirariaggkFNVLITHYDLIMRdKAFLKKI--DWNYMIVDEGHRlknhecALAKTLGTG---YRIK 536
Cdd:COG1061  155 LA--GGGKKDSD-----------APITVATYQSLAR-RAHLDELgdRFGLVIIDEAHH------AGAPSYRRIleaFPAA 214

                 ....*....
gi 30687235  537 RRLLLTGTP 545
Cdd:COG1061  215 YRLGLTATP 223
DpdE NF041062
protein DpdE;
409-573 6.36e-07

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 53.82  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   409 LADEMGLGKTIQTIALI-AYLLESKDLHGphLILAPKAVLPNWenefalwapsisaflydgskekRTEIRARIAGGKF-- 485
Cdd:NF041062  175 LADEVGLGKTIEAGLVIrQHLLDNPDARV--LVLVPDALVRQW----------------------RRELRDKFFLDDFpg 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   486 -NVLITHYDLIMRDKAFLKKIDwnYMIVDEGHRLKNHECALAKTLGTGYR--------IKRRLLLTGTPIQNSLQELWSL 556
Cdd:NF041062  231 aRVRVLSHEEPERWEPLLDAPD--LLVVDEAHQLARLAWSGDPPERARYRelaalahaAPRLLLLSATPVLGNEETFLAL 308
                         170
                  ....*....|....*....
gi 30687235   557 LNFLLPHIF--NSIHNFEE 573
Cdd:NF041062  309 LHLLDPDLYplDDLEAFRE 327
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
764-812 6.73e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 42.31  E-value: 6.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 30687235  764 YFMFLLSTRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKK 812
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
PTZ00110 PTZ00110
helicase; Provisional
700-810 1.85e-04

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 45.53  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235   700 LDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPyfmFLLSTRAGGLGLN 779
Cdd:PTZ00110  366 LKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSP---IMIATDVASRGLD 442
                          90       100       110
                  ....*....|....*....|....*....|.
gi 30687235   780 LQTADTIIIFDsdwnpqMDQQAEDRAHRIGQ 810
Cdd:PTZ00110  443 VKDVKYVINFD------FPNQIEDYVHRIGR 467
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
414-548 1.38e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235    414 GLGKTIqtIALIAYL--LESKDLHGPHLILAP-----KAVLPNWENEFALWAPSISAfLYDGSKekRTEIRARIAGGkfN 486
Cdd:pfam00270   24 GSGKTL--AFLLPALeaLDKLDNGPQALVLAPtrelaEQIYEELKKLGKGLGLKVAS-LLGGDS--RKEQLEKLKGP--D 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687235    487 VLI-TH--YDLIMRDKAFLKKIdwNYMIVDEGHRL--KNHECALAKTLGTGYRIKRRLLLTGTPIQN 548
Cdd:pfam00270   97 ILVgTPgrLLDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATLPRN 161
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
742-836 1.95e-03

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.02  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  742 DGSTKTDQRGILlKQFNEPDspyFMFLLSTRAGGLGLNLQTADTIIIFDSDWNP-QMDQqaedRAHRIGQKKEVRVFVLV 820
Cdd:COG1111  393 KGLTQKEQIEIL-ERFRAGE---FNVLVATSVAEEGLDIPEVDLVIFYEPVPSEiRSIQ----RKGRTGRKREGRVVVLI 464
                         90
                 ....*....|....*.
gi 30687235  821 SIGSIEEVILERAKQK 836
Cdd:COG1111  465 AKGTRDEAYYWSSRRK 480
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
386-544 5.54e-03

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB 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 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 38.82  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  386 LRSYQLEGLQWMvslYNNDY--NGILADEMGLGKTIQTIALIAYLLESKdlhgphLILAPKAV-LPNWENEFALWAP--- 459
Cdd:cd18029    9 LRPYQEKALSKM---FGNGRarSGVIVLPCGAGKTLVGITAACTIKKST------LVLCTSAVsVEQWRRQFLDWTTidd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687235  460 -SISAFlydgSKEKRTEIRARIaggkfnVLITHYDLIMRDKA----------FLKKIDWNYMIVDEGHRLKNHecALAKT 528
Cdd:cd18029   80 eQIGRF----TSDKKEIFPEAG------VTVSTYSMLANTRKrspesekfmeFITEREWGLIILDEVHVVPAP--MFRRV 147
                        170
                 ....*....|....*.
gi 30687235  529 LGTgYRIKRRLLLTGT 544
Cdd:cd18029  148 LTL-QKAHCKLGLTAT 162
 
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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