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Conserved domains on  [gi|189535029|ref|XP_687332|]
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helicase ARIP4 isoform X2 [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12785142)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as human DNA excision repair protein ERCC-6-like and DNA repair and recombination protein RAD54-like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
281-557 2.36e-157

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: 473.53  E-value: 2.36e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLW 360
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 LPAAEALPpdtdpqQVLPRTFKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLlslkksfvtgrkrkskkpagp 440
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 viidldeedrqqelmkaieralsRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 189535029  521 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYR 557
Cdd:cd18069   191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
185-887 1.40e-95

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 323.33  E-value: 1.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  185 LDSSGDEGEEKEAPPPPLPDHRDDVIELSSGDEGDALRISSEEEEDRSLTPGTEESSGSHINDSLNQPDSQGRVLININH 264
Cdd:COG0553   142 LAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDA 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  265 PAEEEDLFLAPQLARAVK----PHQIGGIRFLYdnlveSLERYktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKT 340
Cdd:COG0553   222 FRLRRLREALESLPAGLKatlrPYQLEGAAWLL-----FLRRL----GLGGLLADDMGLGKTIQALALLLELKERGLARP 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  341 VLAIVPVNTLQNWLAEFNLWLPaaealppdtdpqqvlprTFKVHILNDEHKttvaRAKVVEDWtGDGGVLLMGYEMYRll 420
Cdd:COG0553   293 VLIVAPTSLVGNWQRELAKFAP-----------------GLRVLVLDGTRE----RAKGANPF-EDADLVITSYGLLR-- 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  421 slkksfvtgrkrkskkpagpviidldeedRQQELMKAIEralsrpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVL 500
Cdd:COG0553   349 -----------------------------RDIELLAAVD-------WDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  501 TGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstPQDVQLMRyrshvlhSLLEGFVQRR-GHDVLRh 579
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD-----EEALERLR-------RLLRPFLLRRtKEDVLK- 459
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  580 QLPPKEEHVILVRLSRLQRALYTEFMNRFREAGNSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANE 650
Cdd:COG0553   460 DLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEG 525
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  651 QDLDLDdlnsssgtrcsapgiksktsdaansrqmsvghlnplqekanqvityewakevmtnyqtgvlenSAKMVLLFYLI 730
Cdd:COG0553   526 AELSGR---------------------------------------------------------------SAKLEALLELL 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  731 DETVARGDKILVFSQSLSTLTVIEDFLSRRpmpiqtetgthnwvrNINYYRLDGSTSASERERLINQFNDPANtqAWVFL 810
Cdd:COG0553   543 EELLAEGEKVLVFSQFTDTLDLLEERLEER---------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFL 605
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029  811 LSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCHIYRLVCDFTLEKKIYDRQVSKQGMSDRVVD 887
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PHA03378 super family cl33729
EBNA-3B; Provisional
911-1161 1.32e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  911 PDPAELQPNNEMET----VIQQACVMYPHLLTKPPFHHESllmdrkemkltkAEKRAAKKSYEDEKRASVPYqRPSYAHY 986
Cdd:PHA03378  569 LGPLQIQPLTSPTTsqlaSSAPSYAQTPWPVPHPSQTPEP------------PTTQSHIPETSAPRQWPMPL-RPIPMRP 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  987 ------------YPASDQRLTNIPAFSQRNWRPPPHLEEKPV----ASVRPVQSTPIPMMPrqvPMGVPSsstgfPVNYL 1050
Cdd:PHA03378  636 lrmqpitfnvlvFPTPHQPPQVEITPYKPTWTQIGHIPYQPSptgaNTMLPIQWAPGTMQP---PPRAPT-----PMRPP 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029 1051 QKAGVYVQRVVTTTDIVIPGSNSSTDVQARIGAgesihvirgskgtyirTNDGRIFAIRSGKPRPPEGGATASREDCGPP 1130
Cdd:PHA03378  708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAA----------------PGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                         250       260       270
                  ....*....|....*....|....*....|.
gi 189535029 1131 lhsvsnGRASPQEPKRLTPEALPRPSSRESP 1161
Cdd:PHA03378  772 ------GAPTPQPPPQAPPAPQQRPRGAPTP 796
 
Name Accession Description Interval E-value
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
281-557 2.36e-157

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: 473.53  E-value: 2.36e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLW 360
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 LPAAEALPpdtdpqQVLPRTFKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLlslkksfvtgrkrkskkpagp 440
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 viidldeedrqqelmkaieralsRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 189535029  521 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYR 557
Cdd:cd18069   191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
185-887 1.40e-95

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 323.33  E-value: 1.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  185 LDSSGDEGEEKEAPPPPLPDHRDDVIELSSGDEGDALRISSEEEEDRSLTPGTEESSGSHINDSLNQPDSQGRVLININH 264
Cdd:COG0553   142 LAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDA 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  265 PAEEEDLFLAPQLARAVK----PHQIGGIRFLYdnlveSLERYktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKT 340
Cdd:COG0553   222 FRLRRLREALESLPAGLKatlrPYQLEGAAWLL-----FLRRL----GLGGLLADDMGLGKTIQALALLLELKERGLARP 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  341 VLAIVPVNTLQNWLAEFNLWLPaaealppdtdpqqvlprTFKVHILNDEHKttvaRAKVVEDWtGDGGVLLMGYEMYRll 420
Cdd:COG0553   293 VLIVAPTSLVGNWQRELAKFAP-----------------GLRVLVLDGTRE----RAKGANPF-EDADLVITSYGLLR-- 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  421 slkksfvtgrkrkskkpagpviidldeedRQQELMKAIEralsrpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVL 500
Cdd:COG0553   349 -----------------------------RDIELLAAVD-------WDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  501 TGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstPQDVQLMRyrshvlhSLLEGFVQRR-GHDVLRh 579
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD-----EEALERLR-------RLLRPFLLRRtKEDVLK- 459
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  580 QLPPKEEHVILVRLSRLQRALYTEFMNRFREAGNSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANE 650
Cdd:COG0553   460 DLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEG 525
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  651 QDLDLDdlnsssgtrcsapgiksktsdaansrqmsvghlnplqekanqvityewakevmtnyqtgvlenSAKMVLLFYLI 730
Cdd:COG0553   526 AELSGR---------------------------------------------------------------SAKLEALLELL 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  731 DETVARGDKILVFSQSLSTLTVIEDFLSRRpmpiqtetgthnwvrNINYYRLDGSTSASERERLINQFNDPANtqAWVFL 810
Cdd:COG0553   543 EELLAEGEKVLVFSQFTDTLDLLEERLEER---------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFL 605
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029  811 LSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCHIYRLVCDFTLEKKIYDRQVSKQGMSDRVVD 887
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
284-638 9.72e-62

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: 212.93  E-value: 9.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   284 HQIGGIRFLYDnlvesleRYkTSSGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTvLAIVPVNTLQNWLAEFNLW 360
Cdd:pfam00176    1 YQIEGVNWMLS-------LE-NNLGRGGILADEMGLGKTLQTISLLLYLKHVdknWGGPT-LIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   361 lpaaeALPPDTdpqqvlpRTFKVHILNDEHKTTVARAKVVEDWtgdgGVLLMGYEMYRllslkksfvtgrKRKSKkpagp 440
Cdd:pfam00176   72 -----VSPPAL-------RVVVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR------------KHKEL----- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   441 viidldeedrqqelmkaieraLSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:pfam00176  119 ---------------------LKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLR 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   521 PDFLGTRQEFSNMFERPILNGQcidstpqdvqlMRYRSHVLHSLLEGFVQRRGHDVLRHQLPPKEEHVILVRLSRLQRAL 600
Cdd:pfam00176  178 PGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKL 246
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 189535029   601 YTEFMnRFRE--AGNSGWLGLNPLKAFCVCC----KIWNHPDVL 638
Cdd:pfam00176  247 YQTFL-LKKDlnAIKTGEGGREIKASLLNILmrlrKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
225-878 1.34e-55

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 211.58  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  225 SEEEEDRSLTPGTEESSGSHINDSL-NQPDS-QGRVlininhpaeeedlflapqlaravKPHQIGGIRF---LYDNlves 299
Cdd:PLN03142  135 TEEEEDEEYLKEEEDGLGGSGGTRLlVQPSCiKGKM-----------------------RDYQLAGLNWlirLYEN---- 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  300 leryktssGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTVlaIVPVNTLQNWLAEFNLWLPaaealppdtdpqqV 376
Cdd:PLN03142  188 --------GINGILADEMGLGKTLQTISLLGYLHEYrgiTGPHMV--VAPKSTLGNWMNEIRRFCP-------------V 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  377 LpRTFKVHILNDEhkttvaRAKVVEDWTGDGG--VLLMGYEMyrllslkksfvtGRKRKSkkpagpviidldeedrqqel 454
Cdd:PLN03142  245 L-RAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM------------AIKEKT-------------------- 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  455 mkaierALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:PLN03142  286 ------ALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  535 ERPILNGQcidstpQDVqlmryrSHVLHSLLEGFVQRRGHDVLRHQLPPKEEHVILVRLSRLQRALYTEFMNRFREAGNS 614
Cdd:PLN03142  360 QISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  615 GwlG-----LNPLKAFCVCCkiwNHPdVLYEALQkenlaneqdldlddlnsssgtrcsaPGIKSKTSDaansrqmsvgHL 689
Cdd:PLN03142  428 G--GerkrlLNIAMQLRKCC---NHP-YLFQGAE-------------------------PGPPYTTGE----------HL 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  690 nplqekanqvityewakevmtnyqtgvLENSAKMVLLFYLIDETVARGDKILVFSQSLSTLTVIEDFLSrrpmpiqtetg 769
Cdd:PLN03142  467 ---------------------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLM----------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  770 thnwVRNINYYRLDGSTSASERERLINQFNDPaNTQAWVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYR 849
Cdd:PLN03142  509 ----YRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHR 583
                         650       660
                  ....*....|....*....|....*....
gi 189535029  850 YGQRKPCHIYRLVCDFTLEKKIYDRQVSK 878
Cdd:PLN03142  584 IGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-862 1.04e-52

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: 181.14  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  720 SAKMVLLFYLIDETVARGDKILVFSQSLSTLTVIEDFLSRRpmpiqtetgthnwvrNINYYRLDGSTSASERERLINQFN 799
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER---------------GIKYLRLDGSTSSKERQKLVDRFN 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189535029  800 DPANTQawVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCHIYRLV 862
Cdd:cd18793    75 EDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
721-851 3.37e-20

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: 87.27  E-value: 3.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   721 AKMVLLFYLIDEtvARGDKILVFSQSLSTLTviEDFLSRRpmpiqtetgthnwvRNINYYRLDGSTSASERERLINQFND 800
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEK--------------EGIKVARLHGDLSQEEREEILEDFRK 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 189535029   801 PANTqawvFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 851
Cdd:pfam00271   63 GKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
775-851 2.09e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.10  E-value: 2.09e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029    775 RNINYYRLDGSTSASERERLINQFNDPANtqawVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 851
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKI----KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
283-524 1.08e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 62.51  E-value: 1.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    283 PHQIGGIRFLYDNLvesleryktssgFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTL-QNWLAEFNLWL 361
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    362 PaaealppdtdpqqvlPRTFKVHILNDEHKTTVARAKVVEdwtGDGGVLLMGYEmyRLLSLKKsfvtgrkrkskkpagpv 441
Cdd:smart00487   79 P---------------SLGLKVVGLYGGDSKREQLRKLES---GKTDILVTTPG--RLLDLLE----------------- 121
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    442 iidldeedrqqelmkaiERALSRPGPDVVICDEGHRIKNchASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 513
Cdd:smart00487  122 -----------------NDKLSLSNVDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 189535029    514 CMVDFVRPDFL 524
Cdd:smart00487  183 NDPVFIDVGFT 193
PHA03378 PHA03378
EBNA-3B; Provisional
911-1161 1.32e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  911 PDPAELQPNNEMET----VIQQACVMYPHLLTKPPFHHESllmdrkemkltkAEKRAAKKSYEDEKRASVPYqRPSYAHY 986
Cdd:PHA03378  569 LGPLQIQPLTSPTTsqlaSSAPSYAQTPWPVPHPSQTPEP------------PTTQSHIPETSAPRQWPMPL-RPIPMRP 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  987 ------------YPASDQRLTNIPAFSQRNWRPPPHLEEKPV----ASVRPVQSTPIPMMPrqvPMGVPSsstgfPVNYL 1050
Cdd:PHA03378  636 lrmqpitfnvlvFPTPHQPPQVEITPYKPTWTQIGHIPYQPSptgaNTMLPIQWAPGTMQP---PPRAPT-----PMRPP 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029 1051 QKAGVYVQRVVTTTDIVIPGSNSSTDVQARIGAgesihvirgskgtyirTNDGRIFAIRSGKPRPPEGGATASREDCGPP 1130
Cdd:PHA03378  708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAA----------------PGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                         250       260       270
                  ....*....|....*....|....*....|.
gi 189535029 1131 lhsvsnGRASPQEPKRLTPEALPRPSSRESP 1161
Cdd:PHA03378  772 ------GAPTPQPPPQAPPAPQQRPRGAPTP 796
 
Name Accession Description Interval E-value
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
281-557 2.36e-157

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: 473.53  E-value: 2.36e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLW 360
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 LPAAEALPpdtdpqQVLPRTFKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLlslkksfvtgrkrkskkpagp 440
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 viidldeedrqqelmkaieralsRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 189535029  521 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYR 557
Cdd:cd18069   191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
281-557 1.90e-110

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: 348.51  E-value: 1.90e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESleRYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHT-GAKTVLAIVPVNTLQNWLAEFNL 359
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAApRRSRPLVLCPASTLYNWEDEFKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WLPaaealpPDTDPqqvlprtFKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLLSLKKSFVTGRKRKSkkpag 439
Cdd:cd18007    79 WLP------PDLRP-------LLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNATTDPRLKQEF----- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  440 pviidldeedrqqelmkaiERALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 519
Cdd:cd18007   141 -------------------IAALLDPGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 189535029  520 RPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYR 557
Cdd:cd18007   202 RPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLMLKR 239
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
185-887 1.40e-95

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 323.33  E-value: 1.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  185 LDSSGDEGEEKEAPPPPLPDHRDDVIELSSGDEGDALRISSEEEEDRSLTPGTEESSGSHINDSLNQPDSQGRVLININH 264
Cdd:COG0553   142 LAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDA 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  265 PAEEEDLFLAPQLARAVK----PHQIGGIRFLYdnlveSLERYktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKT 340
Cdd:COG0553   222 FRLRRLREALESLPAGLKatlrPYQLEGAAWLL-----FLRRL----GLGGLLADDMGLGKTIQALALLLELKERGLARP 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  341 VLAIVPVNTLQNWLAEFNLWLPaaealppdtdpqqvlprTFKVHILNDEHKttvaRAKVVEDWtGDGGVLLMGYEMYRll 420
Cdd:COG0553   293 VLIVAPTSLVGNWQRELAKFAP-----------------GLRVLVLDGTRE----RAKGANPF-EDADLVITSYGLLR-- 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  421 slkksfvtgrkrkskkpagpviidldeedRQQELMKAIEralsrpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVL 500
Cdd:COG0553   349 -----------------------------RDIELLAAVD-------WDLVILDEAQHIKNPATKRAKAVRALKARHRLAL 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  501 TGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstPQDVQLMRyrshvlhSLLEGFVQRR-GHDVLRh 579
Cdd:COG0553   393 TGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD-----EEALERLR-------RLLRPFLLRRtKEDVLK- 459
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  580 QLPPKEEHVILVRLSRLQRALYTEFMNRFREAGNSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANE 650
Cdd:COG0553   460 DLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEG 525
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  651 QDLDLDdlnsssgtrcsapgiksktsdaansrqmsvghlnplqekanqvityewakevmtnyqtgvlenSAKMVLLFYLI 730
Cdd:COG0553   526 AELSGR---------------------------------------------------------------SAKLEALLELL 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  731 DETVARGDKILVFSQSLSTLTVIEDFLSRRpmpiqtetgthnwvrNINYYRLDGSTSASERERLINQFNDPANtqAWVFL 810
Cdd:COG0553   543 EELLAEGEKVLVFSQFTDTLDLLEERLEER---------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFL 605
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029  811 LSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCHIYRLVCDFTLEKKIYDRQVSKQGMSDRVVD 887
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
281-557 1.27e-81

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: 268.29  E-value: 1.27e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTVLAIVPVNTLQNWLAEF 357
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCeklENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  358 NLWLPAAEalppDTDpqqvlprTFKVHILnDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLLSlkksfvTGRKRKSKKP 437
Cdd:cd18068    81 EKWQEGLK----DEE-------KIEVNEL-ATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILA------QERNVKSREK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 AgpviidldeedrQQELMKAieraLSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 517
Cdd:cd18068   143 L------------KEIFNKA----LVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVN 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 189535029  518 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYR 557
Cdd:cd18068   207 FVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDVRVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
284-638 9.72e-62

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: 212.93  E-value: 9.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   284 HQIGGIRFLYDnlvesleRYkTSSGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTvLAIVPVNTLQNWLAEFNLW 360
Cdd:pfam00176    1 YQIEGVNWMLS-------LE-NNLGRGGILADEMGLGKTLQTISLLLYLKHVdknWGGPT-LIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   361 lpaaeALPPDTdpqqvlpRTFKVHILNDEHKTTVARAKVVEDWtgdgGVLLMGYEMYRllslkksfvtgrKRKSKkpagp 440
Cdd:pfam00176   72 -----VSPPAL-------RVVVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR------------KHKEL----- 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   441 viidldeedrqqelmkaieraLSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:pfam00176  119 ---------------------LKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLR 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   521 PDFLGTRQEFSNMFERPILNGQcidstpqdvqlMRYRSHVLHSLLEGFVQRRGHDVLRHQLPPKEEHVILVRLSRLQRAL 600
Cdd:pfam00176  178 PGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKL 246
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 189535029   601 YTEFMnRFRE--AGNSGWLGLNPLKAFCVCC----KIWNHPDVL 638
Cdd:pfam00176  247 YQTFL-LKKDlnAIKTGEGGREIKASLLNILmrlrKICNHPGLI 289
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
283-572 2.69e-59

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: 204.06  E-value: 2.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLYDnlveSLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHT-----GAKTVLAIVPVNTLQNWLAEF 357
Cdd:cd18004     3 PHQREGVQFLYD----CLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGpygkpTAKKALIVCPSSLVGNWKAEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  358 NLWLPaaealppdtdpqqvlPRTFKVHILNDEHKTTVArAKVVEDWTGDGGVLLMGYEMYRLLSlkksfvtgrkrkskkp 437
Cdd:cd18004    79 DKWLG---------------LRRIKVVTADGNAKDVKA-SLDFFSSASTYPVLIISYETLRRHA---------------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 agpviidldeedrqQELMKAIeralsrpGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 517
Cdd:cd18004   127 --------------EKLSKKI-------SIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVD 185
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 189535029  518 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18004   186 FVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
225-878 1.34e-55

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 211.58  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  225 SEEEEDRSLTPGTEESSGSHINDSL-NQPDS-QGRVlininhpaeeedlflapqlaravKPHQIGGIRF---LYDNlves 299
Cdd:PLN03142  135 TEEEEDEEYLKEEEDGLGGSGGTRLlVQPSCiKGKM-----------------------RDYQLAGLNWlirLYEN---- 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  300 leryktssGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTVlaIVPVNTLQNWLAEFNLWLPaaealppdtdpqqV 376
Cdd:PLN03142  188 --------GINGILADEMGLGKTLQTISLLGYLHEYrgiTGPHMV--VAPKSTLGNWMNEIRRFCP-------------V 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  377 LpRTFKVHILNDEhkttvaRAKVVEDWTGDGG--VLLMGYEMyrllslkksfvtGRKRKSkkpagpviidldeedrqqel 454
Cdd:PLN03142  245 L-RAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM------------AIKEKT-------------------- 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  455 mkaierALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:PLN03142  286 ------ALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  535 ERPILNGQcidstpQDVqlmryrSHVLHSLLEGFVQRRGHDVLRHQLPPKEEHVILVRLSRLQRALYTEFMNRFREAGNS 614
Cdd:PLN03142  360 QISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  615 GwlG-----LNPLKAFCVCCkiwNHPdVLYEALQkenlaneqdldlddlnsssgtrcsaPGIKSKTSDaansrqmsvgHL 689
Cdd:PLN03142  428 G--GerkrlLNIAMQLRKCC---NHP-YLFQGAE-------------------------PGPPYTTGE----------HL 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  690 nplqekanqvityewakevmtnyqtgvLENSAKMVLLFYLIDETVARGDKILVFSQSLSTLTVIEDFLSrrpmpiqtetg 769
Cdd:PLN03142  467 ---------------------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLM----------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  770 thnwVRNINYYRLDGSTSASERERLINQFNDPaNTQAWVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYR 849
Cdd:PLN03142  509 ----YRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHR 583
                         650       660
                  ....*....|....*....|....*....
gi 189535029  850 YGQRKPCHIYRLVCDFTLEKKIYDRQVSK 878
Cdd:PLN03142  584 IGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-862 1.04e-52

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: 181.14  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  720 SAKMVLLFYLIDETVARGDKILVFSQSLSTLTVIEDFLSRRpmpiqtetgthnwvrNINYYRLDGSTSASERERLINQFN 799
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER---------------GIKYLRLDGSTSSKERQKLVDRFN 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189535029  800 DPANTQawVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQRKPCHIYRLV 862
Cdd:cd18793    75 EDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
282-524 2.14e-46

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: 164.66  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFLydnlvesLERYKTssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKT-VLAIVPVNTLQNWLAEFNLW 360
Cdd:cd17919     2 RPYQLEGLNFL-------LELYEN--GPGGILADEMGLGKTLQAIAFLAYLLKEGKERGpVLVVCPLSVLENWEREFEKW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 LPaaealppdtdpqqvlprTFKVHILNDEHKTTVARAKVVedWTGDGGVLLMGYEMYRLLSlkksfvtgrkrkskkpagp 440
Cdd:cd17919    73 TP-----------------DLRVVVYHGSQRERAQIRAKE--KLDKFDVVLTTYETLRRDK------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 viidldeedrqqelmkaieRALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:cd17919   115 -------------------ASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLD 175

                  ....
gi 189535029  521 PDFL 524
Cdd:cd17919   176 PPFL 179
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
282-572 1.52e-40

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: 150.61  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFLYDNLVEsleryktssGFGCILAHSMGLGKTLQVISFIDVLLRHTG---------------------AKT 340
Cdd:cd18005     2 RDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLGKTGtrrdrennrprfkkkppassaKKP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  341 VLAIVPVNTLQNWLAEFNLWlpaaealppdtdpqqvlpRTFKVHILNDEHKTTV--ARAKvvedwTGDGGVLLMGYEMYR 418
Cdd:cd18005    73 VLIVAPLSVLYNWKDELDTW------------------GHFEVGVYHGSRKDDEleGRLK-----AGRLEVVVTTYDTLR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  419 LlslkksfvtgrkrkskkpagpviiDLDEedrqqelmkaieraLSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRV 498
Cdd:cd18005   130 R------------------------CIDS--------------LNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRI 171
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189535029  499 VLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18005   172 GLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR 245
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
281-572 3.27e-40

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: 149.23  E-value: 3.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYdnlvESLERYKTSSGFGCILAHSMGLGKTLQVISFIDVLLR--HTGAKTV----LAIVPVNTLQNWL 354
Cdd:cd18066     1 LRPHQREGIEFLY----ECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRqgPYGGKPVikraLIVTPGSLVKNWK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  355 AEFNLWLPAAEalppdtdpqqvlprtFKVHILNDEHKttvarakvVEDWTGDG--GVLLMGYEMyrLLslkksfvtgrkr 432
Cdd:cd18066    77 KEFQKWLGSER---------------IKVFTVDQDHK--------VEEFIASPlySVLIISYEM--LL------------ 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  433 kskkpagpviidldeedRQQELMKAIERalsrpgpDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEY 512
Cdd:cd18066   120 -----------------RSLDQISKLNF-------DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEF 175
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  513 WCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18066   176 FALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
281-572 3.70e-40

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: 149.16  E-value: 3.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLVESLERyktsSGFGCILAHSMGLGKTLQVISFIDVLLRHT-GAKTVL--AIV--PVNTLQNWLA 355
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIR----GSHGCIMADEMGLGKTLQCITLMWTLLRQSpQCKPEIdkAIVvsPSSLVKNWAN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  356 EFNLWLPaaealpPDTDPQQVLPRTFKVHILNDEHKTTVARAKVVEDwtgdggVLLMGYEMYRLlslkksfvtgrkrksk 435
Cdd:cd18067    77 ELGKWLG------GRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP------VLIISYETFRL---------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  436 kpagpviidldeedrQQELMKAIERALsrpgpdvVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 515
Cdd:cd18067   129 ---------------HVEVLQKGEVGL-------VICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSL 186
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029  516 VDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18067   187 VNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
283-572 1.66e-37

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: 141.35  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLYdnlveSLEryktSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLWLP 362
Cdd:cd18001     3 PHQREGVAWLW-----SLH----DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  363 AAealppdtdpqqvlpRTFKVHILNdehktTVARAKVVEDWTGDGGVLLMGYEMYRllslkksfvtgrkRKSKkpagpvi 442
Cdd:cd18001    74 GL--------------RVKVFHGTS-----KKERERNLERIQRGGGVLLTTYGMVL-------------SNTE------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  443 iDLDEEDRQQELMkaieralsrpgpDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP- 521
Cdd:cd18001   115 -QLSADDHDEFKW------------DYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNg 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189535029  522 DFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18001   182 SLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
283-524 1.79e-31

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: 122.43  E-value: 1.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLYDnlvesleryKTSSGFGCILAHSMGLGKTLQVISFIDVL-LRHTGAKTVLAIVPVNTLQNWLAEFNLWL 361
Cdd:cd18000     3 KYQQTGVQWLWE---------LHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  362 PAAealppdtdpqqvlpRTFKVH------ILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRLLSlkksfvtgrkrksk 435
Cdd:cd18000    74 PPF--------------RVVVLHssgsgtGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHK-------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  436 kpagpviidldeedrqqelmkaieRALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 515
Cdd:cd18000   126 ------------------------DLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSL 181

                  ....*....
gi 189535029  516 VDFVRPDFL 524
Cdd:cd18000   182 FDFVFPPYL 190
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
283-572 3.21e-31

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: 122.67  E-value: 3.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLYdnlveSLERYktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLWLP 362
Cdd:cd18012     7 PYQKEGFNWLS-----FLRHY----GLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  363 aaealppdtdpqqvlprTFKVHILNDehkttVARAKVVEDWTGDGGVLLMGYEMYRllslkksfvtgrkrkskkpagpvi 442
Cdd:cd18012    78 -----------------ELKVLVIHG-----TKRKREKLRALEDYDLVITSYGLLR------------------------ 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  443 idldeedRQQELMKAIERalsrpgpDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPD 522
Cdd:cd18012   112 -------RDIELLKEVKF-------HYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPG 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 189535029  523 FLGTRQEFSNMFERPILNGQCIDSTPQdvqlmryrshvLHSLLEGFVQRR 572
Cdd:cd18012   178 LLGSYKRFKKRFAKPIEKDGDEEALEE-----------LKKLISPFILRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
312-572 1.13e-30

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: 121.27  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  312 ILAHSMGLGKTLQVISFIDVLLRHTG-AKTVLAIVPVNTLQNWLAEFNLWLPaaealppdtdpqqvLPRTFKVHILNDEH 390
Cdd:cd17997    26 ILADEMGLGKTLQTISLLGYLKHYKNiNGPHLIIVPKSTLDNWMREFKRWCP--------------SLRVVVLIGDKEER 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 KTTVARAKVVEDWTgdggVLLMGYEMyrllslkksfvtgrkrkskkpagpVIIDldeedrqqelmkaiERALSRPGPDVV 470
Cdd:cd17997    92 ADIIRDVLLPGKFD----VCITSYEM------------------------VIKE--------------KTVLKKFNWRYI 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  471 ICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCIDSTPQD 550
Cdd:cd17997   130 IIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN----VNNCDDDNQEV 205
                         250       260
                  ....*....|....*....|..
gi 189535029  551 VQLmryrshvLHSLLEGFVQRR 572
Cdd:cd17997   206 VQR-------LHKVLRPFLLRR 220
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
282-572 3.66e-30

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: 120.18  E-value: 3.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGI---RFLYDNlvesleryktssGFGCILAHSMGLGKTLQVISFIdVLLRHTGAK-TVLAIVPVNTLQNWLAEF 357
Cdd:cd18009     5 RPYQLEGMewlRMLWEN------------GINGILADEMGLGKTIQTIALL-AHLRERGVWgPFLVIAPLSTLPNWVNEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  358 NLWLPAAEALppdtdpqqvlprtfKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMYRllslkksfvtgrkrkskkp 437
Cdd:cd18009    72 ARFTPSVPVL--------------LYHGTKEERERLRKKIMKREGTLQDFPVVVTSYEIAM------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 agpviidldeEDRQqelmkaierALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 517
Cdd:cd18009   119 ----------RDRK---------ALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLN 179
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 189535029  518 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRYRSHVLHSLLEGFVQRR 572
Cdd:cd18009   180 FLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRR 234
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
282-572 2.77e-28

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: 114.77  E-value: 2.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRF---LYDNLVESleryktssgfgcILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEF 357
Cdd:cd17996     5 KEYQLKGLQWmvsLYNNNLNG------------ILADEMGLGKTIQTISLITYLMEKKKNNgPYLVIVPLSTLSNWVSEF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  358 NLWLPaaealppdtdpqqvlprtfKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEmYRLlslkksfvtgrKRKSKkp 437
Cdd:cd17996    73 EKWAP-------------------SVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYE-YII-----------KDKPL-- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 agpviidldeedrqqelmkaieraLSRPGPDVVICDEGHRIKNCHASTSQALKN-IRSRRRVVLTGYPLQNNLIEYWCMV 516
Cdd:cd17996   120 ------------------------LSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALL 175
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189535029  517 DFVRPDFLGTRQEFSNMFERPILN--GQCIDSTPQDVQLMRYRShvLHSLLEGFVQRR 572
Cdd:cd17996   176 NFLLPKIFKSCKTFEQWFNTPFANtgEQVKIELNEEETLLIIRR--LHKVLRPFLLRR 231
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
282-521 3.36e-26

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: 107.09  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFLydNLVeslerYKtsSGFGCILAHSMGLGKTLQVISFIDVLLR--HTGAKtvLAIVPVNTLQNWLAEFNL 359
Cdd:cd17998     2 KDYQLIGLNWL--NLL-----YQ--KKLSGILADEMGLGKTIQVIAFLAYLKEigIPGPH--LVVVPSSTLDNWLREFKR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WLPAAEALPPDTDPQQvlprtfKVHILNDEHKTtvarakvVEDWTgdggVLLMGYEMyrllslkksfVTGRKrkskkpag 439
Cdd:cd17998    71 WCPSLKVEPYYGSQEE------RKHLRYDILKG-------LEDFD----VIVTTYNL----------ATSNP-------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  440 pviidldeEDRqqelmkaieRALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 519
Cdd:cd17998   116 --------DDR---------SFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178

                  ..
gi 189535029  520 RP 521
Cdd:cd17998   179 MP 180
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
310-534 4.61e-23

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: 99.24  E-value: 4.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  310 GCILAHSMGLGKTLQVISFIDVLlRHTGAK--TVLAIVPVNTLQNWLAEFNLWlpaaealppdtdpqqvlprtfkvhiln 387
Cdd:cd17995    21 NCILADEMGLGKTIQSIAFLEHL-YQVEGIrgPFLVIAPLSTIPNWQREFETW--------------------------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  388 dehktTVARAKVVEDwTGDGGVLLMGYEMYrllslkksFVTGRKRKSKKPAGPVIIDLDEEDrqqeLMKAIErALSRPGP 467
Cdd:cd17995    73 -----TDMNVVVYHG-SGESRQIIQQYEMY--------FKDAQGRKKKGVYKFDVLITTYEM----VIADAE-ELRKIPW 133
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029  468 DVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:cd17995   134 RVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
312-572 8.18e-22

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 95.50  E-value: 8.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  312 ILAHSMGLGKTLQVISfidvLLRHTGA-KTV----LAIVPVNTLQNWLAEFNLWLPAaealppdtdpqqvlprtFKVHIL 386
Cdd:cd18003    23 ILADEMGLGKTIQTIA----LLAHLACeKGNwgphLIVVPTSVMLNWEMEFKRWCPG-----------------FKILTY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  387 NDEHKTtvaRAKVVEDWTGDGG--VLLMGYEMyrLLSLKKSFvtgrKRKSKKpagpviidldeedrqqelmkaieralsr 464
Cdd:cd18003    82 YGSAKE---RKLKRQGWMKPNSfhVCITSYQL--VVQDHQVF----KRKKWK---------------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  465 pgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPiLNGQCI 544
Cdd:cd18003   125 ----YLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSE 199
                         250       260
                  ....*....|....*....|....*...
gi 189535029  545 DSTPQDVQLMRYrshvLHSLLEGFVQRR 572
Cdd:cd18003   200 GSQEENEELVRR----LHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
307-585 1.80e-20

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: 92.42  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  307 SGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTVLaiVPVNTLQNWLAEFNLWLPAAEALPPDTDPQQvlprtfkv 383
Cdd:cd18064    33 NGINGILADEMGLGKTLQTISLLGYMKHYrniPGPHMVL--VPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQ-------- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  384 hilndehkttvaRAKVVED--WTGDGGVLLMGYEMyrLLSLKKSFVTGRKRkskkpagpviidldeedrqqelmkaiera 461
Cdd:cd18064   103 ------------RAAFVRDvlLPGEWDVCVTSYEM--LIKEKSVFKKFNWR----------------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  462 lsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNG 541
Cdd:cd18064   140 -------YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD----TN 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 189535029  542 QCIDstpqDVQLMRYrshvLHSLLEGFVQRRGHDVLRHQLPPKE 585
Cdd:cd18064   209 NCLG----DQKLVER----LHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
312-572 2.58e-20

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: 92.05  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  312 ILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNLWLPAAEALPPDTDPqqvlprtfkvhilndeh 390
Cdd:cd18063    46 ILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTP----------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 ktTVARAKVVEDWTGDGGVLLMGYEMyrllslkksfvtgrkrkskkpagpVIIDldeedrqqelmkaiERALSRPGPDVV 470
Cdd:cd18063   109 --AMRRSLVPQLRSGKFNVLLTTYEY------------------------IIKD--------------KHILAKIRWKYM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  471 ICDEGHRIKNCHASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTP 548
Cdd:cd18063   149 IVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNE 228
                         250       260
                  ....*....|....*....|....
gi 189535029  549 QDVQLMRYRshvLHSLLEGFVQRR 572
Cdd:cd18063   229 EETILIIRR---LHKVLRPFLLRR 249
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
309-572 2.83e-20

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: 91.58  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  309 FGCILAHSMGLGKTLQVISFI------------------DVLLRHTGAKTVLAIVPVNTLQNWLAEFNlwlpaaealppd 370
Cdd:cd18008    15 RGGILADEMGLGKTIQALALIlatrpqdpkipeeleensSDPKKLYLSKTTLIVVPLSLLSQWKDEIE------------ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  371 tdpQQVLPRTFKVHILndeHKTTvaRAKVVEDWTG-DggVLLMGYEMyrllsLKKSFvtgrkRKSKKPAGpviidLDEED 449
Cdd:cd18008    83 ---KHTKPGSLKVYVY---HGSK--RIKSIEELSDyD--IVITTYGT-----LASEF-----PKNKKGGG-----RDSKE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  450 RQQELMKAIE--RalsrpgpdvVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTR 527
Cdd:cd18008   138 KEASPLHRIRwyR---------VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDY 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 189535029  528 QEFSNMFERPILNGQcidstpqdvqlmRYRSHVLHSLLEGFVQRR 572
Cdd:cd18008   209 PWFNSDISKPFSKND------------RKALERLQALLKPILLRR 241
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
721-851 3.37e-20

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: 87.27  E-value: 3.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029   721 AKMVLLFYLIDEtvARGDKILVFSQSLSTLTviEDFLSRRpmpiqtetgthnwvRNINYYRLDGSTSASERERLINQFND 800
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEK--------------EGIKVARLHGDLSQEEREEILEDFRK 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 189535029   801 PANTqawvFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 851
Cdd:pfam00271   63 GKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
281-572 3.72e-20

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: 91.64  E-value: 3.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFL---YDNlvesleryktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAE 356
Cdd:cd18062    24 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWVYE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  357 FNLWLPAAEALPPDTDPqqvlprtfkvhilndehktTVARAKVVEDWTGDGGVLLMGYEMyrllslkksfvtgrkrkskk 436
Cdd:cd18062    92 FDKWAPSVVKVSYKGSP-------------------AARRAFVPQLRSGKFNVLLTTYEY-------------------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  437 pagpVIIDldeedrqqelmkaiERALSRPGPDVVICDEGHRIKNCHASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCM 515
Cdd:cd18062   133 ----IIKD--------------KQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWAL 194
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189535029  516 VDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTPQDVQLMRYRshvLHSLLEGFVQRR 572
Cdd:cd18062   195 LNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR---LHKVLRPFLLRR 249
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
282-546 1.28e-19

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: 89.33  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFLydnlvESLERYKTSSgfgcILAHSMGLGKTLQVISFI--DVLLRHTGAKT----VLAIVPVNTLQNWLA 355
Cdd:cd17999     2 RPYQQEGINWL-----AFLNKYNLHG----ILCDDMGLGKTLQTLCILasDHHKRANSFNSenlpSLVVCPPTLVGHWVA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  356 EFNLWLPaaealppdtdpQQVLprtfKVHILndeHKTTVARAKVVEDwTGDGGVLLMGYEMYRLLS---LKKSFvtgrkr 432
Cdd:cd17999    73 EIKKYFP-----------NAFL----KPLAY---VGPPQERRRLREQ-GEKHNVIVASYDVLRNDIevlTKIEW------ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  433 kskkpagpviidldeedrqqelmkaieralsrpgpDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEY 512
Cdd:cd17999   128 -----------------------------------NYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLEL 172
                         250       260       270
                  ....*....|....*....|....*....|....
gi 189535029  513 WCMVDFVRPDFLGTRQEFSNMFERPILngQCIDS 546
Cdd:cd17999   173 WSLFDFLMPGYLGTEKQFQRRFLKPIL--ASRDS 204
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
283-535 6.44e-19

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: 86.34  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLydnlvesleRYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNLWL 361
Cdd:cd17994     3 PYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMWA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  362 PaaealppdtdpqqvlprtfkvhilnDEHKTTvarakvvedWTGDgGVLLMGYEMyrllslkksfvtgrkrkskkpagpV 441
Cdd:cd17994    74 P-------------------------DFYVVT---------YVGD-HVLLTSYEL------------------------I 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  442 IIDldeedrqQELMKAIERAlsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 521
Cdd:cd17994    95 SID-------QAILGSIDWA-------VLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
                         250
                  ....*....|....
gi 189535029  522 DFLGTRQEFSNMFE 535
Cdd:cd17994   161 ERFNNLQGFLEEFA 174
HELICc smart00490
helicase superfamily c-terminal domain;
775-851 2.09e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.10  E-value: 2.09e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189535029    775 RNINYYRLDGSTSASERERLINQFNDPANtqawVFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 851
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKI----KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
281-572 4.30e-18

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: 84.86  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYdNLVESleryktssGFGCILAHSMGLGKTLQVISFIDVLLRHTGA-KTVLAIVPVNTLQNWLAEFNL 359
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQ--------GINGILADEMGLGKTVQSIAVLAHLAEEHNIwGPFLVIAPASTLHNWQQEISR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WLPAAEALPPDTDPQQvlpRTFKVHILNDEHKTTvarakvvedwtGDGG--VLLMGYEMyrllslkksfvtgrkrkskkp 437
Cdd:cd18002    72 FVPQFKVLPYWGNPKD---RKVLRKFWDRKNLYT-----------RDAPfhVVITSYQL--------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 agpVIIDldeedrqqelmkaiERALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 517
Cdd:cd18002   117 ---VVQD--------------EKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLH 179
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 189535029  518 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVQLMRyrshvLHSLLEGFVQRR 572
Cdd:cd18002   180 FIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKR-----LHMILKPFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
311-572 6.91e-18

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: 83.94  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  311 CILAHSMGLGKTLQVISFIDVLL-RHTGAKTVLAIVPVNTLQNWLAEFNLWLPAaealppdtdpqqvlprtfkvhiLNde 389
Cdd:cd17993    23 GILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWAPD----------------------MN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  390 hkttvarakvVEDWTGDGGV--LLMGYEMYrllslkksfvTGRKRKSKKPAGPVIIDLDEEDRQQelmkaieraLSRPGP 467
Cdd:cd17993    79 ----------VIVYLGDIKSrdTIREYEFY----------FSQTKKLKFNVLLTTYEIILKDKAF---------LGSIKW 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  468 DVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFsnmferpilngqciDST 547
Cdd:cd17993   130 QYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF--------------EEE 195
                         250       260
                  ....*....|....*....|....*
gi 189535029  548 PQDVQLMRYRShvLHSLLEGFVQRR 572
Cdd:cd17993   196 HDEEQEKGIAD--LHKELEPFILRR 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
312-572 7.29e-18

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: 84.67  E-value: 7.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  312 ILAHSMGLGKTLQVISFIDVLL-RHTGAKTVLAIVPVNTLQNWLAEFNLWLPAAEALppdtdpqqvlprtfkVHILNDEH 390
Cdd:cd18054    43 ILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV---------------VYIGDLMS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 KTTVARAKVVEDWTG--DGGVLLMGYEMYrllsLKKSFVTGrkrkskkpagpviidldeedrqqelmkAIERALsrpgpd 468
Cdd:cd18054   108 RNTIREYEWIHSQTKrlKFNALITTYEIL----LKDKTVLG---------------------------SINWAF------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  469 vVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGqcidstp 548
Cdd:cd18054   151 -LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG------- 222
                         250       260
                  ....*....|....*....|....
gi 189535029  549 qdvqlmrYRShvLHSLLEGFVQRR 572
Cdd:cd18054   223 -------YQS--LHKVLEPFLLRR 237
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
307-572 1.00e-17

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: 83.91  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  307 SGFGCILAHSMGLGKTLQVISFIDVLLRH---TGAKTVLaiVPVNTLQNWLAEFNLWLPAAEAlppdtdpqqvlprtfkV 383
Cdd:cd18065    33 NGVNGILADEMGLGKTLQTIALLGYLKHYrniPGPHMVL--VPKSTLHNWMNEFKRWVPSLRA----------------V 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  384 HILNDEHkttvARAKVVED--WTGDGGVLLMGYEMyrLLSLKKSFVTGRKRkskkpagpviidldeedrqqelmkaiera 461
Cdd:cd18065    95 CLIGDKD----ARAAFIRDvmMPGEWDVCVTSYEM--VIKEKSVFKKFNWR----------------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  462 lsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNG 541
Cdd:cd18065   140 -------YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD----TK 208
                         250       260       270
                  ....*....|....*....|....*....|.
gi 189535029  542 QCIDstpqDVQLMRYrshvLHSLLEGFVQRR 572
Cdd:cd18065   209 NCLG----DQKLVER----LHAVLKPFLLRR 231
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
281-572 1.13e-16

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: 80.56  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLydnlvesLERYKTssGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNL 359
Cdd:cd18006     1 LRPYQLEGVNWL-------LQCRAE--QHGCILGDEMGLGKTCQTISLLWYLAGRLKLLgPFLVLCPLSVLDNWKEELNR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WLPAAEALPPDTDPQQVLPRTFKVHILNDEHkttvarakvvedwtgdggVLLMGYEMyrllslkksfvtgrkrkskkpag 439
Cdd:cd18006    72 FAPDLSVITYMGDKEKRLDLQQDIKSTNRFH------------------VLLTTYEI----------------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  440 pVIIDldeedrqQELMKAIERAlsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 519
Cdd:cd18006   111 -CLKD-------ASFLKSFPWA-------SLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFI 175
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 189535029  520 RPDFLG--TRQEFSNMFERpilngqcIDSTPQDVQlmryrshVLHSLLEGFVQRR 572
Cdd:cd18006   176 EPNVFPkdKLDDFIKAYSE-------TDDESETVE-------ELHLLLQPFLLRR 216
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
281-534 1.55e-14

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: 74.72  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLydnlvesleRYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNL 359
Cdd:cd18057     1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WlpaaealppdtdpqqvLPRTFKVHILNDEHKTTVARAKvveDWTGDGGVLLMGYEMYRLlslkksfvtgrKRKSKKPAG 439
Cdd:cd18057    72 W----------------APDFYVVTYTGDKESRSVIREN---EFSFEDNAIRSGKKVFRM-----------KKEAQIKFH 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  440 PVIIDLDEEDRQQELMKAIERAlsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 519
Cdd:cd18057   122 VLLTSYELITIDQAILGSIEWA-------CLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFL 194
                         250
                  ....*....|....*
gi 189535029  520 RPDFLGTRQEFSNMF 534
Cdd:cd18057   195 TPERFNNLEGFLEEF 209
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
307-541 2.24e-14

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: 74.43  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  307 SGFGCILAHSMGLGKTLQVISFIdvllrhtGAKTVLAIVPVNTLQNWLAEFNlwlpaaealppdtdpQQVLPRTFKVHIL 386
Cdd:cd18071    47 LVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFE---------------EHVKPGQLKVYTY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  387 NDEHKTTVARakvvedwtgdggvLLMGYEM----YRLLSLKKSfvtgrkrksKKPAGPViidldeedrqqelmKAIE--R 460
Cdd:cd18071   105 HGGERNRDPK-------------LLSKYDIvlttYNTLASDFG---------AKGDSPL--------------HTINwlR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  461 alsrpgpdvVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILN 540
Cdd:cd18071   149 ---------VVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM 219

                  .
gi 189535029  541 G 541
Cdd:cd18071   220 G 220
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
282-530 1.57e-13

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: 72.00  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFL--YDNLVESLERYKTS--SGFGCILAHSMGLGKTLQVISFIDVLL-RHTGAKTVLAIVPVNTLQNWLAE 356
Cdd:cd18053     9 QPSYIGGHEGLelRDYQLNGLNWLAHSwcKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  357 FNLWLPAAEALP--PDTDPQQVLPRTFKVHilndehkTTVARAKVvedwtgdgGVLLMGYEmyrLLSLKKSFVTGrkrks 434
Cdd:cd18053    89 IQTWAPQMNAVVylGDINSRNMIRTHEWMH-------PQTKRLKF--------NILLTTYE---ILLKDKSFLGG----- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  435 kkpagpviidldeedrqqelmkaIERALsrpgpdvVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 514
Cdd:cd18053   146 -----------------------LNWAF-------IGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWS 195
                         250
                  ....*....|....*.
gi 189535029  515 MVDFVRPDFLGTRQEF 530
Cdd:cd18053   196 LLHFIMPEKFSSWEDF 211
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
302-533 5.13e-13

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: 70.04  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  302 RYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNLWLPAAEAL--PPDTDPQQVLP 378
Cdd:cd18055    13 RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKgPFLVSAPLSTIINWEREFQMWAPDFYVVtyTGDKDSRAIIR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  379 R---TFKVHILNDEHKTTVARAKVVEDWTgdggVLLMGYEMyrllslkksfvtgrkrkskkpagpVIIDldeedrqQELM 455
Cdd:cd18055    93 EnefSFDDNAVKGGKKAFKMKREAQVKFH----VLLTSYEL------------------------VTID-------QAAL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  456 KAIERAlsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFL----GTRQEFS 531
Cdd:cd18055   138 GSIRWA-------CLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFA 210

                  ..
gi 189535029  532 NM 533
Cdd:cd18055   211 DI 212
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
311-534 1.20e-12

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: 68.93  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  311 CILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLWlpaaealppdTDPQQVLprtfkvhilndEH 390
Cdd:cd18060    22 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTW----------TEMNTIV-----------YH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 KTTVARAkvvedwtgdggvLLMGYEMYrllslkksfvtgrkrkSKKPAGPVIIDLDEEDrqqELMKAIERALSrPGPDV- 469
Cdd:cd18060    81 GSLASRQ------------MIQQYEMY----------------CKDSRGRLIPGAYKFD---ALITTFEMILS-DCPELr 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189535029  470 ------VICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:cd18060   129 eiewrcVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
281-533 1.24e-12

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: 68.94  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLydnlvesleRYKTSSGFGCILAHSMGLGKTLQVISFIDVLLRHTGAK-TVLAIVPVNTLQNWLAEFNL 359
Cdd:cd18056     1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  360 WLPAAEALP--PDTDPQQVLpRTFKVHILNDEHKTTVARAKVVEDWTGDGGVLLMGYEMyrllslkksfvtgrkrkskkp 437
Cdd:cd18056    72 WAPDMYVVTyvGDKDSRAII-RENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYEL--------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  438 agpVIIDLdeedrqqELMKAIERAlsrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 517
Cdd:cd18056   130 ---ITIDM-------AILGSIDWA-------CLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLN 192
                         250       260
                  ....*....|....*....|
gi 189535029  518 FVRPDFL----GTRQEFSNM 533
Cdd:cd18056   193 FLTPERFhnleGFLEEFADI 212
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
311-534 1.73e-12

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: 68.53  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  311 CILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLWlpaaealppdTDPQQVLprtfkvhilndEH 390
Cdd:cd18058    22 CILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTW----------TEMNAIV-----------YH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 KTTVARAkvvedwtgdggvLLMGYEMYRllslkksfvtgrkRKSKKPAGPVIIDLDEEDRQQELMKAIERALSRPGPDVV 470
Cdd:cd18058    81 GSQISRQ------------MIQQYEMYY-------------RDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCV 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189535029  471 ICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:cd18058   136 IIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
311-534 3.57e-12

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: 67.34  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  311 CILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLWlpaaealppdTDPQQVLprtfkvhilndEH 390
Cdd:cd18061    22 CILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTW----------TDLNVVV-----------YH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  391 KTTVARAkvvedwtgdggvLLMGYEMYrllslkksfvtgrkrkSKKPAGPVIidlDEEDRQQELMKAIERALSRPGP--- 467
Cdd:cd18061    81 GSLISRQ------------MIQQYEMY----------------FRDSQGRII---RGAYRFQAIITTFEMILGGCPElna 129
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  468 ---DVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 534
Cdd:cd18061   130 idwRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
282-530 1.43e-11

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: 65.30  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFlydnlveSLERyktssGFGCILAHSMGLGKTLQVISFIDVLlRHTGAktVLAIVPVNTLQNWLAEFNLWL 361
Cdd:cd18010     2 LPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAIAIAAYY-REEWP--LLIVCPSSLRLTWADEIERWL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  362 PaaEALPPDtdpqqvlprtfkVHILNDEHkttvarakvvEDW-TGDGGVLLMGYEMYRLLSLKKSfvtgrKRKSKkpagp 440
Cdd:cd18010    67 P--SLPPDD------------IQVIVKSK----------DGLrDGDAKVVIVSYDLLRRLEKQLL-----ARKFK----- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 viidldeedrqqelmkaieralsrpgpdVVICDEGHRIKNCHASTSQALKNI--RSRRRVVLTGYPLQNNLIEYWCMVDF 518
Cdd:cd18010   113 ----------------------------VVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDA 164
                         250
                  ....*....|..
gi 189535029  519 VRPDFLGTRQEF 530
Cdd:cd18010   165 LDPKLFGRFHDF 176
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
281-534 3.52e-11

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: 64.67  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  281 VKPHQIGGIRFLYDNLveslerYKTSSgfgCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAEFNLW 360
Cdd:cd18059     1 LREYQLEGVNWLLFNW------YNTRN---CILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTW 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 lpaaealppdTDPQQVLprtfkvhilndEHKTTVARAKVvedwtgdggvllMGYEMYrllslkksfvtgrkrkSKKPAGP 440
Cdd:cd18059    72 ----------TELNVVV-----------YHGSQASRRTI------------QLYEMY----------------FKDPQGR 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  441 VIidlDEEDRQQELMKAIERALS-----RPGP-DVVICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 514
Cdd:cd18059   103 VI---KGSYKFHAIITTFEMILTdcpelRNIPwRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFS 179
                         250       260
                  ....*....|....*....|
gi 189535029  515 MVDFVRPDFLGTRQEFSNMF 534
Cdd:cd18059   180 LLHFLEPSRFPSETTFMQEF 199
DEXDc smart00487
DEAD-like helicases superfamily;
283-524 1.08e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 62.51  E-value: 1.08e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    283 PHQIGGIRFLYDNLvesleryktssgFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTL-QNWLAEFNLWL 361
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    362 PaaealppdtdpqqvlPRTFKVHILNDEHKTTVARAKVVEdwtGDGGVLLMGYEmyRLLSLKKsfvtgrkrkskkpagpv 441
Cdd:smart00487   79 P---------------SLGLKVVGLYGGDSKREQLRKLES---GKTDILVTTPG--RLLDLLE----------------- 121
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029    442 iidldeedrqqelmkaiERALSRPGPDVVICDEGHRIKNchASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 513
Cdd:smart00487  122 -----------------NDKLSLSNVDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 189535029    514 CMVDFVRPDFL 524
Cdd:smart00487  183 NDPVFIDVGFT 193
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
283-536 3.80e-09

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: 58.07  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  283 PHQIGGIRFLYDNLVesleryktssgFGCILAHSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQNWLAE----FN 358
Cdd:cd18011     3 PHQIDAVLRALRKPP-----------VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDElqdkFG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  359 LwlpaaealppdtdpQQVLPRTFKVHILNDEHKTTVARAKVvedwtgdggvllmgyemyrllslkksfvtgrkrkskkpa 438
Cdd:cd18011    72 L--------------PFLILDRETAAQLRRLIGNPFEEFPI--------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  439 gpVIIDLDEEDRQQELmkaiERALSRPGPDVVICDEGHRIKNCHASTSQ----ALKNI--RSRRRVVLTGYPLQNNLIEY 512
Cdd:cd18011    99 --VIVSLDLLKRSEER----RGLLLSEEWDLVVVDEAHKLRNSGGGKETkrykLGRLLakRARHVLLLTATPHNGKEEDF 172
                         250       260       270
                  ....*....|....*....|....*....|....
gi 189535029  513 WCMVDFVRPDF----------LGTRQEFSNMFER 536
Cdd:cd18011   173 RALLSLLDPGRfavlgrflrlDGLREVLAKVLLR 206
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
470-520 3.07e-06

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: 50.17  E-value: 3.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189535029  470 VICDEGHRIKNCHASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 520
Cdd:cd18072   155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
282-519 5.90e-04

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: 43.11  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  282 KPHQIGGIRFLYDNLVesleryktssgfGCILAhSMGLGKTLQVISFIDVLLRHTGAKTVLAIVPVNTLQN-WLAEFNLW 360
Cdd:cd18013     2 HPYQKVAINFIIEHPY------------CGLFL-DMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  361 lpaaealppdtdpqqvlprtfkvhilndEHkttvarakvvedwtgdggvllmgyemyrLLSLKKSFVTGRKRK----SKK 436
Cdd:cd18013    69 ----------------------------NH----------------------------LRNLTVSVAVGTERQrskaANT 92
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  437 PAGPVIIDLDEEDrqqelmKAIERALSRPGPDVVICDEGHRIKNCHASTSQALKNIRSR--RRVVLTGYPLQNNLIEYWC 514
Cdd:cd18013    93 PADLYVINRENLK------WLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVRPVikRLIGLTGTPSPNGLMDLWA 166

                  ....*
gi 189535029  515 MVDFV 519
Cdd:cd18013   167 QIALL 171
PHA03378 PHA03378
EBNA-3B; Provisional
911-1161 1.32e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  911 PDPAELQPNNEMET----VIQQACVMYPHLLTKPPFHHESllmdrkemkltkAEKRAAKKSYEDEKRASVPYqRPSYAHY 986
Cdd:PHA03378  569 LGPLQIQPLTSPTTsqlaSSAPSYAQTPWPVPHPSQTPEP------------PTTQSHIPETSAPRQWPMPL-RPIPMRP 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  987 ------------YPASDQRLTNIPAFSQRNWRPPPHLEEKPV----ASVRPVQSTPIPMMPrqvPMGVPSsstgfPVNYL 1050
Cdd:PHA03378  636 lrmqpitfnvlvFPTPHQPPQVEITPYKPTWTQIGHIPYQPSptgaNTMLPIQWAPGTMQP---PPRAPT-----PMRPP 707
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029 1051 QKAGVYVQRVVTTTDIVIPGSNSSTDVQARIGAgesihvirgskgtyirTNDGRIFAIRSGKPRPPEGGATASREDCGPP 1130
Cdd:PHA03378  708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAA----------------PGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                         250       260       270
                  ....*....|....*....|....*....|.
gi 189535029 1131 lhsvsnGRASPQEPKRLTPEALPRPSSRESP 1161
Cdd:PHA03378  772 ------GAPTPQPPPQAPPAPQQRPRGAPTP 796
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
718-798 6.94e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.77  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189535029  718 ENSAKMVLLFYLIDETvARGDKILVFSQSLSTLTVIedflSRRpmpiqtetgthnwvrnINYYRLDGSTSASERERLINQ 797
Cdd:cd18789    31 MNPNKLRALEELLKRH-EQGDKIIVFTDNVEALYRY----AKR----------------LLKPFITGETPQSEREEILQN 89

                  .
gi 189535029  798 F 798
Cdd:cd18789    90 F 90
 
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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