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Conserved domains on  [gi|126090612|ref|NP_109655|]
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helicase ARIP4 [Mus musculus]

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 ...
271-547 4.21e-156

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: 470.84  E-value: 4.21e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  351 LPAPEALPadskpeEVQPRFFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLltlkkslatsrpkktkkrshp 430
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 126090612  511 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18069   191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 1.76e-90

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 1.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKEYAAPIPTVPLEFLPEEIVLRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553    87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEEDEEEEKGGTHVNDALNQHDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNm 349
Cdd:COG0553   243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA- 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 wlpapealpadskpeevqpRFF---KVHILNDEHKtvasRAKvTADWVSEGGVLLMGYEMyrlltlkkslatsrpkktkk 426
Cdd:COG0553   311 -------------------KFApglRVLVLDGTRE----RAK-GANPFEDADLVITSYGL-------------------- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  427 rshpviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:COG0553   347 -----------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  507 DFVRPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQI 586
Cdd:COG0553   409 DFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  587 QRDLYTQFMDRFRDCGTSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANEQDLDVEelgsagtsarc 657
Cdd:COG0553   477 QRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR----------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  658 pphgtkvkgedsalpssmgeatnskflqgvgfnpfqergnnivtyewakelltnyqtgvlenSPKMVLLFHLIEESVKLG 737
Cdd:COG0553   532 --------------------------------------------------------------SAKLEALLELLEELLAEG 549
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  738 DKILVFSQSLSTLALIEEFLGKRdmpclpgaegqgtqkwvrNVSYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTR 817
Cdd:COG0553   550 EKVLVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLK 609
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126090612  818 AGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553   610 AGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1112-1445 2.54e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1112 SDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPEGLARPvspdsPEIISELQQYADVAAARES 1191
Cdd:PHA03247 2657 APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-----HALVSATPLPPGPAAARQA 2731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1192 RQSSPSVSAALPGPPGQLMDNSTipgTALGTEPclgghclnssllVTGQPSGGRHPVLDLRGHKRKLATPSVTQESVRRR 1271
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGP---ARPARPP------------TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1272 SrkghLPAPVQPYEHGYPVSGGFAMPPVSLN--HNLTTPFTSQAGENSLFMGSNPSYYQLSNLLA---DARLVFPVTTDP 1346
Cdd:PHA03247 2797 S----LPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApggDVRRRPPSRSPA 2872
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1347 LVPAGPVSSSSTATSVTASNPS---FMLNPSVPGMLPSYSLPfSQPLLSEPRMFAPFPSPGLPSNLSRGVSVYPGYMSPH 1423
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVSRStesFALPPDQPERPPQPQAP-PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951
                         330       340
                  ....*....|....*....|..
gi 126090612 1424 AGYPAGGLLRSQVPPFDSHEVA 1445
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVA 2973
 
Name Accession Description Interval E-value
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
271-547 4.21e-156

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: 470.84  E-value: 4.21e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  351 LPAPEALPadskpeEVQPRFFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLltlkkslatsrpkktkkrshp 430
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 126090612  511 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18069   191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 1.76e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 1.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKEYAAPIPTVPLEFLPEEIVLRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553    87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEEDEEEEKGGTHVNDALNQHDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNm 349
Cdd:COG0553   243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA- 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 wlpapealpadskpeevqpRFF---KVHILNDEHKtvasRAKvTADWVSEGGVLLMGYEMyrlltlkkslatsrpkktkk 426
Cdd:COG0553   311 -------------------KFApglRVLVLDGTRE----RAK-GANPFEDADLVITSYGL-------------------- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  427 rshpviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:COG0553   347 -----------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  507 DFVRPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQI 586
Cdd:COG0553   409 DFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  587 QRDLYTQFMDRFRDCGTSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANEQDLDVEelgsagtsarc 657
Cdd:COG0553   477 QRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR----------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  658 pphgtkvkgedsalpssmgeatnskflqgvgfnpfqergnnivtyewakelltnyqtgvlenSPKMVLLFHLIEESVKLG 737
Cdd:COG0553   532 --------------------------------------------------------------SAKLEALLELLEELLAEG 549
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  738 DKILVFSQSLSTLALIEEFLGKRdmpclpgaegqgtqkwvrNVSYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTR 817
Cdd:COG0553   550 EKVLVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLK 609
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126090612  818 AGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553   610 AGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
274-628 3.44e-59

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: 205.61  E-value: 3.44e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   274 HQIGGIRFLYdnlveSLERFktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP--AKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:pfam00176    1 YQIEGVNWML-----SLENN---LGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   352 pAPEALPAdskpeevqprfFKVHILNDEHKTVASRAKVTADWvsegGVLLMGYEMYRlltlkkslatsrpkktkkrSHPV 431
Cdd:pfam00176   73 -SPPALRV-----------VVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR-------------------KHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   432 IIDldeedrQQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:pfam00176  118 LLK------KVHWHR-------------IVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   512 DFLGTRQEFSNMFERPILNGQcidstpqdvrlMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQIQRDLY 591
Cdd:pfam00176  179 GPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLY 247
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 126090612   592 TQFMdRFRDcgtsGWLGLNPLKAFCVCC----------KIWNHPDVL 628
Cdd:pfam00176  248 QTFL-LKKD----LNAIKTGEGGREIKAsllnilmrlrKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-865 1.57e-51

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: 177.67  E-value: 1.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  720 SPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRdmpclpgaegqgtqkwvrNVSYFRLDGSTPAFERERLIN 799
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER------------------GIKYLRLDGSTSSKERQKLVD 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126090612  800 QFNDPSNLTtwLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLV 865
Cdd:cd18793    72 RFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
274-881 1.31e-48

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 189.63  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  274 HQIGGIRF---LYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVL--FR-----HtpaktvLAIVPVNTLQNW 343
Cdd:PLN03142  173 YQLAGLNWlirLYEN------------GINGILADEMGLGKTLQTISLLGYLheYRgitgpH------MVVAPKSTLGNW 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  344 LAEFNMWLPAPealpadskpeevqpRFFKVHILNDEhktvasRAKVTADWVSEGG--VLLMGYEMyrllTLKKslatsrp 421
Cdd:PLN03142  235 MNEIRRFCPVL--------------RAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM----AIKE------- 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  422 KKTKKRSHpviidldeedrqqeFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIE 501
Cdd:PLN03142  284 KTALKRFS--------------WR-------------YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  502 YWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstpQDVrlmryrSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILV 581
Cdd:PLN03142  337 LWALLNFLLPEIFSSAETFDEWFQISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKV 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  582 RLSQIQRDLYTQFMDRFRDCGTSGwlG-----LNPLKAFCVCCkiwNHPDVLYEAlqkenlaneqdldveELGsagtsar 656
Cdd:PLN03142  405 GMSQMQKQYYKALLQKDLDVVNAG--GerkrlLNIAMQLRKCC---NHPYLFQGA---------------EPG------- 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  657 cPPHGTkvkgedsalpssmgeatnskflqgvgfnpfqerGNNIVtyewakelltnyqtgvlENSPKMVLLFHLIEESVKL 736
Cdd:PLN03142  458 -PPYTT---------------------------------GEHLV-----------------ENSGKMVLLDKLLPKLKER 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  737 GDKILVFSQSLSTLALIEEFLgkrdmpclpgaegqgtqkWVRNVSYFRLDGSTPAFERERLINQFNDPsNLTTWLFLLST 816
Cdd:PLN03142  487 DSRVLIFSQMTRLLDILEDYL------------------MYRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLST 547
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126090612  817 RAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISK 881
Cdd:PLN03142  548 RAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
722-854 8.66e-19

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: 83.03  E-value: 8.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   722 KMVLLFHLIEEsvKLGDKILVFSQSLSTLAliEEFLGKRdmpclpgaegqgtqkwvRNVSYFRLDGSTPAFERERLINQF 801
Cdd:pfam00271    2 KLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEK-----------------EGIKVARLHGDLSQEEREEILEDF 60
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 126090612   802 NDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:pfam00271   61 RKGKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
778-854 4.49e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.25  E-value: 4.49e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126090612    778 RNVSYFRLDGSTPAFERERLINQFNDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
273-514 5.28e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 60.58  E-value: 5.28e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    273 PHQIGGIRFLYDNLveslerfktssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTL-QNWLAEFNMWL 351
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    352 PapealpadskpeevqPRFFKVHILNDEHKTVASRAKVTADwvsEGGVLLMGYEMYRLLTLKKSLATSRpkktkkrshpv 431
Cdd:smart00487   79 P---------------SLGLKVVGLYGGDSKREQLRKLESG---KTDILVTTPGRLLDLLENDKLSLSN----------- 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    432 iidldeedrqqefrrefekalcrpgPDVVICDEGHRIKNcqASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 503
Cdd:smart00487  130 -------------------------VDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 126090612    504 CMVDFVRPDFL 514
Cdd:smart00487  183 NDPVFIDVGFT 193
PHA03247 PHA03247
large tegument protein UL36; Provisional
1112-1445 2.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1112 SDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPEGLARPvspdsPEIISELQQYADVAAARES 1191
Cdd:PHA03247 2657 APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-----HALVSATPLPPGPAAARQA 2731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1192 RQSSPSVSAALPGPPGQLMDNSTipgTALGTEPclgghclnssllVTGQPSGGRHPVLDLRGHKRKLATPSVTQESVRRR 1271
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGP---ARPARPP------------TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1272 SrkghLPAPVQPYEHGYPVSGGFAMPPVSLN--HNLTTPFTSQAGENSLFMGSNPSYYQLSNLLA---DARLVFPVTTDP 1346
Cdd:PHA03247 2797 S----LPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApggDVRRRPPSRSPA 2872
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1347 LVPAGPVSSSSTATSVTASNPS---FMLNPSVPGMLPSYSLPfSQPLLSEPRMFAPFPSPGLPSNLSRGVSVYPGYMSPH 1423
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVSRStesFALPPDQPERPPQPQAP-PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951
                         330       340
                  ....*....|....*....|..
gi 126090612 1424 AGYPAGGLLRSQVPPFDSHEVA 1445
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVA 2973
 
Name Accession Description Interval E-value
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
271-547 4.21e-156

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: 470.84  E-value: 4.21e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  351 LPAPEALPadskpeEVQPRFFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLltlkkslatsrpkktkkrshp 430
Cdd:cd18069    81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069   134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 126090612  511 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
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 ...
271-547 2.12e-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: 2.12e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 WLPaPEALPadskpeevqprfFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLLTLKKSlatsrpkkTKKRSH 429
Cdd:cd18007    79 WLP-PDLRP------------LLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT--------TDPRLK 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  430 pviidldeedrqqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd18007   138 ----------------QEFIAALLDPGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 126090612  510 RPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18007   202 RPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLMLKR 239
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 1.76e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 1.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKEYAAPIPTVPLEFLPEEIVLRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553    87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEEDEEEEKGGTHVNDALNQHDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNm 349
Cdd:COG0553   243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELA- 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 wlpapealpadskpeevqpRFF---KVHILNDEHKtvasRAKvTADWVSEGGVLLMGYEMyrlltlkkslatsrpkktkk 426
Cdd:COG0553   311 -------------------KFApglRVLVLDGTRE----RAK-GANPFEDADLVITSYGL-------------------- 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  427 rshpviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:COG0553   347 -----------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLL 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  507 DFVRPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQI 586
Cdd:COG0553   409 DFLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  587 QRDLYTQFMDRFRDCGTSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkenLANEQDLDVEelgsagtsarc 657
Cdd:COG0553   477 QRALYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR----------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  658 pphgtkvkgedsalpssmgeatnskflqgvgfnpfqergnnivtyewakelltnyqtgvlenSPKMVLLFHLIEESVKLG 737
Cdd:COG0553   532 --------------------------------------------------------------SAKLEALLELLEELLAEG 549
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  738 DKILVFSQSLSTLALIEEFLGKRdmpclpgaegqgtqkwvrNVSYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTR 817
Cdd:COG0553   550 EKVLVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLK 609
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126090612  818 AGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553   610 AGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
271-547 8.99e-83

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: 271.76  E-value: 8.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP---AKTVLAIVPVNTLQNWLAEF 347
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKlenFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  348 NMWLpapealpADSKPEEVqprfFKVHILnDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLLTLKKSlatsrPKKTKKR 427
Cdd:cd18068    81 EKWQ-------EGLKDEEK----IEVNEL-ATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERN-----VKSREKL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  428 shpviidldeedrqqefRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18068   144 -----------------KEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVN 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 126090612  508 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18068   207 FVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDVRVMKKR 246
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
273-562 7.87e-60

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: 205.60  E-value: 7.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIGGIRFLYDnlveSLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-----AKTVLAIVPVNTLQNWLAEF 347
Cdd:cd18004     3 PHQREGVQFLYD----CLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPygkptAKKALIVCPSSLVGNWKAEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  348 NMWLP----APEALPADSKPEEVQPRFFkvhilndehkTVASRAKVtadwvseggvLLMGYEMyrlltlkkslatsrpkk 423
Cdd:cd18004    79 DKWLGlrriKVVTADGNAKDVKASLDFF----------SSASTYPV----------LIISYET----------------- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  424 tkkrshpviidldeedrqqeFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYW 503
Cdd:cd18004   122 --------------------LRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFF 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 126090612  504 CMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18004   182 ALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
274-628 3.44e-59

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: 205.61  E-value: 3.44e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   274 HQIGGIRFLYdnlveSLERFktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP--AKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:pfam00176    1 YQIEGVNWML-----SLENN---LGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   352 pAPEALPAdskpeevqprfFKVHILNDEHKTVASRAKVTADWvsegGVLLMGYEMYRlltlkkslatsrpkktkkrSHPV 431
Cdd:pfam00176   73 -SPPALRV-----------VVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR-------------------KHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   432 IIDldeedrQQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:pfam00176  118 LLK------KVHWHR-------------IVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   512 DFLGTRQEFSNMFERPILNGQcidstpqdvrlMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQIQRDLY 591
Cdd:pfam00176  179 GPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLY 247
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 126090612   592 TQFMdRFRDcgtsGWLGLNPLKAFCVCC----------KIWNHPDVL 628
Cdd:pfam00176  248 QTFL-LKKD----LNAIKTGEGGREIKAsllnilmrlrKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-865 1.57e-51

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: 177.67  E-value: 1.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  720 SPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRdmpclpgaegqgtqkwvrNVSYFRLDGSTPAFERERLIN 799
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER------------------GIKYLRLDGSTSSKERQKLVD 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126090612  800 QFNDPSNLTtwLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLV 865
Cdd:cd18793    72 RFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
272-514 3.02e-49

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: 173.14  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFLYDNLveslerfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKT-VLAIVPVNTLQNWLAEFNMW 350
Cdd:cd17919     2 RPYQLEGLNFLLELY---------ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGpVLVVCPLSVLENWEREFEKW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  351 LPapealpadskpeevqprFFKVHILndeHKTVASRAKVTAD-WVSEGGVLLMGYEMYRLLTlkkslatsrpkktkkrsh 429
Cdd:cd17919    73 TP-----------------DLRVVVY---HGSQRERAQIRAKeKLDKFDVVLTTYETLRRDK------------------ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  430 pviidldeedrqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd17919   115 --------------------ASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174

                  ....*
gi 126090612  510 RPDFL 514
Cdd:cd17919   175 DPPFL 179
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
274-881 1.31e-48

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 189.63  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  274 HQIGGIRF---LYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVL--FR-----HtpaktvLAIVPVNTLQNW 343
Cdd:PLN03142  173 YQLAGLNWlirLYEN------------GINGILADEMGLGKTLQTISLLGYLheYRgitgpH------MVVAPKSTLGNW 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  344 LAEFNMWLPAPealpadskpeevqpRFFKVHILNDEhktvasRAKVTADWVSEGG--VLLMGYEMyrllTLKKslatsrp 421
Cdd:PLN03142  235 MNEIRRFCPVL--------------RAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM----AIKE------- 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  422 KKTKKRSHpviidldeedrqqeFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIE 501
Cdd:PLN03142  284 KTALKRFS--------------WR-------------YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  502 YWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstpQDVrlmryrSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILV 581
Cdd:PLN03142  337 LWALLNFLLPEIFSSAETFDEWFQISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKV 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  582 RLSQIQRDLYTQFMDRFRDCGTSGwlG-----LNPLKAFCVCCkiwNHPDVLYEAlqkenlaneqdldveELGsagtsar 656
Cdd:PLN03142  405 GMSQMQKQYYKALLQKDLDVVNAG--GerkrlLNIAMQLRKCC---NHPYLFQGA---------------EPG------- 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  657 cPPHGTkvkgedsalpssmgeatnskflqgvgfnpfqerGNNIVtyewakelltnyqtgvlENSPKMVLLFHLIEESVKL 736
Cdd:PLN03142  458 -PPYTT---------------------------------GEHLV-----------------ENSGKMVLLDKLLPKLKER 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  737 GDKILVFSQSLSTLALIEEFLgkrdmpclpgaegqgtqkWVRNVSYFRLDGSTPAFERERLINQFNDPsNLTTWLFLLST 816
Cdd:PLN03142  487 DSRVLIFSQMTRLLDILEDYL------------------MYRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLST 547
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126090612  817 RAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISK 881
Cdd:PLN03142  548 RAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
271-562 2.22e-42

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: 155.71  E-value: 2.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYDNLVESLERfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVL--AIV--PVNTLQNWLA 345
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIR----GSHGCIMADEMGLGKTLQCITLMWTLLRQSPqCKPEIdkAIVvsPSSLVKNWAN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  346 EFNMWL-PAPEALPADSKPEEvqprffkvhilNDEHKTVAsrakvtadWVSEGG------VLLMGYEMYRLltlkkslat 418
Cdd:cd18067    77 ELGKWLgGRLQPLAIDGGSKK-----------EIDRKLVQ--------WASQQGrrvstpVLIISYETFRL--------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  419 srpkktkkrshpviidldeedrqqefrreFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNN 498
Cdd:cd18067   129 -----------------------------HVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQND 179
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126090612  499 LIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18067   180 LSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
272-562 5.91e-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: 148.68  E-value: 5.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFLYDNLVEslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHT---------------------PAKT 330
Cdd:cd18005     2 RDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkkkppassAKKP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  331 VLAIVPVNTLQNWLAEFNMWlpapealpadskpeevqpRFFKVHILNDEHKTVASRAKVTADWVSeggVLLMGYEMYRLl 410
Cdd:cd18005    73 VLIVAPLSVLYNWKDELDTW------------------GHFEVGVYHGSRKDDELEGRLKAGRLE---VVVTTYDTLRR- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  411 tlkkslatsrpkktkkrshpviiDLDEEDrQQEFrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVL 490
Cdd:cd18005   131 -----------------------CIDSLN-SINW-------------SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGL 173
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126090612  491 TGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18005   174 TGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR 245
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
271-562 6.20e-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: 148.45  E-value: 6.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYdnlvESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP------AKTVLAIVPVNTLQNWL 344
Cdd:cd18066     1 LRPHQREGIEFLY----ECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPyggkpvIKRALIVTPGSLVKNWK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  345 AEFNMWLPAPEalpadskpeevqprfFKVHILNDEHKTvasRAKVTADWVSeggVLLMGYEMyrlltLKKSLatsrpkkt 424
Cdd:cd18066    77 KEFQKWLGSER---------------IKVFTVDQDHKV---EEFIASPLYS---VLIISYEM-----LLRSL-------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  425 kkrshpviidldEEDRQQEFrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 504
Cdd:cd18066   123 ------------DQISKLNF-------------DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFA 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 126090612  505 MVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18066   178 LIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
273-562 5.68e-39

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: 145.59  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIGGIRFLYdnlveSLErfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLP 352
Cdd:cd18001     3 PHQREGVAWLW-----SLH----DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  353 APealpadskpeevqpRFFKVHILNdehktVASRAKVTADWVSEGGVLLMGYEMyrlltlkkslatsrpkktkkrshpvi 432
Cdd:cd18001    74 GL--------------RVKVFHGTS-----KKERERNLERIQRGGGVLLTTYGM-------------------------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  433 IDLDEEDRQQEFRREFEKalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP- 511
Cdd:cd18001   109 VLSNTEQLSADDHDEFKW-------DYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNg 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126090612  512 DFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18001   182 SLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
273-562 2.67e-33

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: 128.45  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlp 352
Cdd:cd18012     7 PYQKEGFNWL---------SFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKF-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  353 APEalpadskpeevqprfFKVHILndeHKTVASRAKVTAdwVSEGGVLLMGYEMYRLltlkkslatsrpkktkkrshpvi 432
Cdd:cd18012    76 APE---------------LKVLVI---HGTKRKREKLRA--LEDYDLVITSYGLLRR----------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  433 idlDEEDRQQefrREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPD 512
Cdd:cd18012   113 ---DIELLKE---VKF---------HYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPG 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 126090612  513 FLGTRQEFSNMFERPILNGQCIDSTPQdvrlmryrshvLHSLLEGFVQRR 562
Cdd:cd18012   178 LLGSYKRFKKRFAKPIEKDGDEEALEE-----------LKKLISPFILRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
302-562 1.12e-31

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: 123.97  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  302 ILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPAPEALpadskpeevqprffKVHILNDE 379
Cdd:cd17997    26 ILADEMGLGKTLQTISLLGYLkhYKNINGPH-LIIVPKSTLDNWMREFKRWCPSLRVV--------------VLIGDKEE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  380 HKTVASRAKVTADWvsegGVLLMGYEMyrlltlkkslatsrpkktkkrshpVIIDldeedrqqefrrefEKALCRPGPDV 459
Cdd:cd17997    91 RADIIRDVLLPGKF----DVCITSYEM------------------------VIKE--------------KTVLKKFNWRY 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  460 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCIDstPQ 539
Cdd:cd17997   129 IIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN----VNNCDD--DN 202
                         250       260
                  ....*....|....*....|...
gi 126090612  540 DVRLMRyrshvLHSLLEGFVQRR 562
Cdd:cd17997   203 QEVVQR-----LHKVLRPFLLRR 220
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
273-514 1.06e-30

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: 120.12  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIGGIRFLYDnlveslerfKTSSGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd18000     3 KYQQTGVQWLWE---------LHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  352 PapealpadskpeevqprFFKVHILNDEHKTVASRAKVTADW---------VSEGGVLLMGYEMYRLLtlkkslatsrpk 422
Cdd:cd18000    74 P-----------------PFRVVVLHSSGSGTGSEEKLGSIErksqlirkvVGDGGILITTYEGFRKH------------ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  423 ktkkrSHPVIidldeedrqqefRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEY 502
Cdd:cd18000   125 -----KDLLL------------NHNW---------QYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKEL 178
                         250
                  ....*....|..
gi 126090612  503 WCMVDFVRPDFL 514
Cdd:cd18000   179 WSLFDFVFPPYL 190
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
272-562 1.21e-29

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: 118.64  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGI---RFLYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN 348
Cdd:cd18009     5 RPYQLEGMewlRMLWEN------------GINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  349 MWLPAPEALpadskpeevqprffKVHILNDEHKTVAsrakvtadwvseggvllmgyemyrlltlkkslATSRPKKTKKRS 428
Cdd:cd18009    73 RFTPSVPVL--------------LYHGTKEERERLR--------------------------------KKIMKREGTLQD 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  429 HPVIIDLDE---EDRqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd18009   107 FPVVVTSYEiamRDR---------KALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSL 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 126090612  506 VDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18009   178 LNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRR 234
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
272-562 4.17e-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: 114.00  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRF---LYDNLVESlerfktssgfgcILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEF 347
Cdd:cd17996     5 KEYQLKGLQWmvsLYNNNLNG------------ILADEMGLGKTIQTISLITYLMEKKKNNgPYLVIVPLSTLSNWVSEF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  348 NMWLPAPEALPADSKPEeVQPRFFKVHIlndehktvasrakvtadwVSEGGVLLMGYEMyrllTLKKslatsRPKKTKKR 427
Cdd:cd17996    73 EKWAPSVSKIVYKGTPD-VRKKLQSQIR------------------AGKFNVLLTTYEY----IIKD-----KPLLSKIK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  428 SHPVIIDldeedrqqefrrefekalcrpgpdvvicdEGHRIKNCQASTSQALKN-IRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:cd17996   125 WKYMIID-----------------------------EGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALL 175
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 126090612  507 DFVRPDFLGTRQEFSNMFERPILN--GQCIDSTPQDVRLMRYRShvLHSLLEGFVQRR 562
Cdd:cd17996   176 NFLLPKIFKSCKTFEQWFNTPFANtgEQVKIELNEEETLLIIRR--LHKVLRPFLLRR 231
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
272-511 6.18e-27

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: 109.40  E-value: 6.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFLydNLVESlerfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd17998     2 KDYQLIGLNWL--NLLYQ-------KKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  352 PAPEALPADSKPEEvqprffKVHILNDEHKtvasrakvtadwvseggvllmGYEMYRLLTLKKSLATSRPkktkkrshpv 431
Cdd:cd17998    73 PSLKVEPYYGSQEE------RKHLRYDILK---------------------GLEDFDVIVTTYNLATSNP---------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  432 iidldeEDRQQEFRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:cd17998   116 ------DDRSFFKRLKL---------NYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
300-524 1.43e-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: 100.79  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  300 GCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPApEALpadskpeevqprffkVHilnd 378
Cdd:cd17995    21 NCILADEMGLGKTIQSIAFLEHLYqVEGIRGPFLVIAPLSTIPNWQREFETWTDM-NVV---------------VY---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  379 eHKTVASRAkvtadwvseggvLLMGYEMYRlltlkkSLATSRPKKTKKRSHpVIIDLDE---EDRQqefrrEFEKALCRp 455
Cdd:cd17995    81 -HGSGESRQ------------IIQQYEMYF------KDAQGRKKKGVYKFD-VLITTYEmviADAE-----ELRKIPWR- 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126090612  456 gpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd17995   135 ---VVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
302-562 2.05e-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: 97.42  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  302 ILAHSMGLGKTLQVISFIDVLFRHtpaKTV----LAIVPVNTLQNWLAEFNMWLPApealpadskpeevqprfFKVHILN 377
Cdd:cd18003    23 ILADEMGLGKTIQTIALLAHLACE---KGNwgphLIVVPTSVMLNWEMEFKRWCPG-----------------FKILTYY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  378 DEHKtvaSRAKVTADWVSEGG--VLLMGYEMyrlltlkkslatsrpkktkkrshpVIIDldeedrQQEFRREFEKALcrp 455
Cdd:cd18003    83 GSAK---ERKLKRQGWMKPNSfhVCITSYQL------------------------VVQD------HQVFKRKKWKYL--- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  456 gpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPiLNGQCID 535
Cdd:cd18003   127 -----ILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSEG 200
                         250       260
                  ....*....|....*....|....*..
gi 126090612  536 STPQDVRLMRYrshvLHSLLEGFVQRR 562
Cdd:cd18003   201 SQEENEELVRR----LHKVLRPFLLRR 223
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
299-562 2.53e-21

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: 94.66  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  299 FGCILAHSMGLGKTLQVISFI------------------DVLFRHTPAKTVLAIVPVNTLQNWLAEFNMwlpapealpad 360
Cdd:cd18008    15 RGGILADEMGLGKTIQALALIlatrpqdpkipeeleensSDPKKLYLSKTTLIVVPLSLLSQWKDEIEK----------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  361 skpeEVQPRFFKVHILndeHKtvASRAKVTADWvSEGGVLLMGYEmyrllTLKKSLATSRPKKTKKRSHPVIIDLdeedR 440
Cdd:cd18008    84 ----HTKPGSLKVYVY---HG--SKRIKSIEEL-SDYDIVITTYG-----TLASEFPKNKKGGGRDSKEKEASPL----H 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  441 QQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEF 520
Cdd:cd18008   145 RIRWYR-------------VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 126090612  521 snmferpilNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18008   212 ---------NSDISKPFSKNDRKALER---LQALLKPILLRR 241
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
272-536 4.18e-20

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: 90.87  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFLydnlvESLERFKTSSgfgcILAHSMGLGKTLQVISFIDVLFRHTPAKT------VLAIVPVNTLQNWLA 345
Cdd:cd17999     2 RPYQQEGINWL-----AFLNKYNLHG----ILCDDMGLGKTLQTLCILASDHHKRANSFnsenlpSLVVCPPTLVGHWVA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  346 EFNMWLPAPealpadskpeevqprFFKVHILndeHKTVASRAKVTADwVSEGGVLLMGYEMYRlltlkkslatsrpkktk 425
Cdd:cd17999    73 EIKKYFPNA---------------FLKPLAY---VGPPQERRRLREQ-GEKHNVIVASYDVLR----------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  426 krshpviidldeedRQQEFRREFEKALCrpgpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd17999   117 --------------NDIEVLTKIEWNYC-------VLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSL 175
                         250       260       270
                  ....*....|....*....|....*....|.
gi 126090612  506 VDFVRPDFLGTRQEFSNMFERPILngQCIDS 536
Cdd:cd17999   176 FDFLMPGYLGTEKQFQRRFLKPIL--ASRDS 204
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
297-575 4.47e-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: 91.27  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  297 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPAPEAlpadskpeevqprffkVH 374
Cdd:cd18064    33 NGINGILADEMGLGKTLQTISLLGYMkhYRNIPGPH-MVLVPKSTLHNWMAEFKRWVPTLRA----------------VC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  375 ILNDEHKtvasRAKVTADWV--SEGGVLLMGYEMyrlLTLKKSLatsrpkktkkrshpviidldeedrqqefrreFEKAL 452
Cdd:cd18064    96 LIGDKDQ----RAAFVRDVLlpGEWDVCVTSYEM---LIKEKSV-------------------------------FKKFN 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  453 CRpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQ 532
Cdd:cd18064   138 WR----YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD----TNN 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 126090612  533 CIDstpqDVRLMRYrshvLHSLLEGFVQRRGHTVLKIHLPAKE 575
Cdd:cd18064   210 CLG----DQKLVER----LHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
273-525 5.70e-20

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: 89.42  E-value: 5.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWl 351
Cdd:cd17994     3 PYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMW- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  352 papealpadskpeevQPRFFKVHILNDEhktvasrakvtadwvseggVLLMGYEmyrLLTLKKSLATSrpkktkkrshpv 431
Cdd:cd17994    73 ---------------APDFYVVTYVGDH-------------------VLLTSYE---LISIDQAILGS------------ 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  432 iIDLdeedrqqefrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:cd17994   104 -IDW----------------------AVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
                         250
                  ....*....|....
gi 126090612  512 DFLGTRQEFSNMFE 525
Cdd:cd17994   161 ERFNNLQGFLEEFA 174
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
301-562 1.47e-19

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: 88.95  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  301 CILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPAPEALpadskpeevqprffkVHILNde 379
Cdd:cd17993    23 GILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI---------------VYLGD-- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  380 hktVASRAkvtadwvseggvLLMGYEMYrlltlkkslatsrPKKTKKRSHPVIIDLDE---EDRQ--QEFRREFekalcr 454
Cdd:cd17993    86 ---IKSRD------------TIREYEFY-------------FSQTKKLKFNVLLTTYEiilKDKAflGSIKWQY------ 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  455 pgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFsnmferpilngqci 534
Cdd:cd17993   132 -----LAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-------------- 192
                         250       260
                  ....*....|....*....|....*...
gi 126090612  535 DSTPQDVRLMRYRShvLHSLLEGFVQRR 562
Cdd:cd17993   193 EEEHDEEQEKGIAD--LHKELEPFILRR 218
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
271-562 3.12e-19

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: 88.95  E-value: 3.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFL---YDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAE 346
Cdd:cd18062    24 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWVYE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  347 FNMWLPAPEALPADSKPeevqprffkvhilndehktVASRAKVTADWVSEGGVLLMGYEMyrLLTLKKSLATSRPKktkk 426
Cdd:cd18062    92 FDKWAPSVVKVSYKGSP-------------------AARRAFVPQLRSGKFNVLLTTYEY--IIKDKQILAKIRWK---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  427 rshpviidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd18062   147 --------------------------------YMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWAL 194
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 126090612  506 VDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18062   195 LNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR---LHKVLRPFLLRR 249
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
722-854 8.66e-19

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: 83.03  E-value: 8.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612   722 KMVLLFHLIEEsvKLGDKILVFSQSLSTLAliEEFLGKRdmpclpgaegqgtqkwvRNVSYFRLDGSTPAFERERLINQF 801
Cdd:pfam00271    2 KLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEK-----------------EGIKVARLHGDLSQEEREEILEDF 60
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 126090612   802 NDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:pfam00271   61 RKGKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
297-562 1.03e-18

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: 87.00  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  297 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPAPEAlpadskpeevqprffkVH 374
Cdd:cd18065    33 NGVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMNEFKRWVPSLRA----------------VC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  375 ILNDEHktvaSRAKVTADWVSEG--GVLLMGYEMYrlltlkkslatsrpkktkkrshpviidLDEEDRQQEFRREFekal 452
Cdd:cd18065    96 LIGDKD----ARAAFIRDVMMPGewDVCVTSYEMV---------------------------IKEKSVFKKFNWRY---- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  453 crpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQ 532
Cdd:cd18065   141 -------LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD----TKN 209
                         250       260       270
                  ....*....|....*....|....*....|
gi 126090612  533 CIDstpqDVRLMRYrshvLHSLLEGFVQRR 562
Cdd:cd18065   210 CLG----DQKLVER----LHAVLKPFLLRR 231
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
302-562 1.42e-18

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: 87.04  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  302 ILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWLPAPEALPADSKPeevqprffkvhilndeh 380
Cdd:cd18063    46 ILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTP----------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  381 ktVASRAKVTADWVSEGGVLLMGYEMyrLLTLKKSLATSRPKktkkrshpviidldeedrqqefrrefekalcrpgpdVV 460
Cdd:cd18063   109 --AMRRSLVPQLRSGKFNVLLTTYEY--IIKDKHILAKIRWK------------------------------------YM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  461 ICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTP 538
Cdd:cd18063   149 IVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNE 228
                         250       260
                  ....*....|....*....|....
gi 126090612  539 QDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18063   229 EETILIIRR---LHKVLRPFLLRR 249
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
302-562 2.62e-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: 85.83  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  302 ILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPAPEALpadskpeevqprffkVHILNdeh 380
Cdd:cd18054    43 ILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV---------------VYIGD--- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  381 ktVASRAKVTA-DWVSEG------GVLLMGYEMyrLLTLKKSLATsrpkktkkrshpviidldeedrqqeFRREFekalc 453
Cdd:cd18054   105 --LMSRNTIREyEWIHSQtkrlkfNALITTYEI--LLKDKTVLGS-------------------------INWAF----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  454 rpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGqc 533
Cdd:cd18054   151 ------LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-- 222
                         250       260
                  ....*....|....*....|....*....
gi 126090612  534 idstpqdvrlmrYRShvLHSLLEGFVQRR 562
Cdd:cd18054   223 ------------YQS--LHKVLEPFLLRR 237
HELICc smart00490
helicase superfamily c-terminal domain;
778-854 4.49e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 77.25  E-value: 4.49e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126090612    778 RNVSYFRLDGSTPAFERERLINQFNDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
271-562 1.07e-16

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: 81.01  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLYdNLVESlerfktssGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQ--------GINGILADEMGLGKTVQSIAVLAHLAeEHNIWGPFLVIAPASTLHNWQQEISR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 WLPAPEALP--ADSKPEEVQPRFFkvhilndEHKTVASRAkvtadwvSEGGVLLMGYEMyrlltlkkslatsrpkktkkr 427
Cdd:cd18002    72 FVPQFKVLPywGNPKDRKVLRKFW-------DRKNLYTRD-------APFHVVITSYQL--------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  428 shpVIIDldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18002   117 ---VVQD--------------EKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLH 179
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 126090612  508 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRyrshvLHSLLEGFVQRR 562
Cdd:cd18002   180 FIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKR-----LHMILKPFMLRR 229
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
271-562 1.25e-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: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLydnlvesLERFKTssGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18006     1 LRPYQLEGVNWL-------LQCRAE--QHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 WLPAPEALPADSKPEEvqprffkvhilndehktvasRAKVTADWVSEG--GVLLMGYEMyrlltlkkslatsrpkktkkr 427
Cdd:cd18006    72 FAPDLSVITYMGDKEK--------------------RLDLQQDIKSTNrfHVLLTTYEI--------------------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  428 shpVIIDldeedrqQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18006   111 ---CLKD-------ASFLKSFPWA-------SLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLS 173
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 126090612  508 FVRPDFLG--TRQEFSNMFERpilngqcIDSTPQDVRlmryrshVLHSLLEGFVQRR 562
Cdd:cd18006   174 FIEPNVFPkdKLDDFIKAYSE-------TDDESETVE-------ELHLLLQPFLLRR 216
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
271-524 1.52e-16

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: 80.49  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18057     1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 WlpapealpadskpeevQPRFFKVHILNDEHktvaSRAKVTADWVS-EGGVLLMGYEMYRLltlkkslatsrPKKTKKRS 428
Cdd:cd18057    72 W----------------APDFYVVTYTGDKE----SRSVIRENEFSfEDNAIRSGKKVFRM-----------KKEAQIKF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  429 HPVIIDLDEEDRQQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDF 508
Cdd:cd18057   121 HVLLTSYELITIDQAILGSIEWA-------CLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNF 193
                         250
                  ....*....|....*.
gi 126090612  509 VRPDFLGTRQEFSNMF 524
Cdd:cd18057   194 LTPERFNNLEGFLEEF 209
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
297-531 1.83e-15

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: 77.51  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  297 SGFGCILAHSMGLGKTLQVISFIdvLFRHTpaktvLAIVPVNTLQNWLAEFNmwlpapealpadskpEEVQPRFFKVHIL 376
Cdd:cd18071    47 LVRGGILADDMGLGKTLTTISLI--LANFT-----LIVCPLSVLSNWETQFE---------------EHVKPGQLKVYTY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  377 NDEHKTVASRakvtadwvseggvLLMGYEMyrLLTLKKSLATsrpKKTKKRSHPViidldeedRQQEFRRefekalcrpg 456
Cdd:cd18071   105 HGGERNRDPK-------------LLSKYDI--VLTTYNTLAS---DFGAKGDSPL--------HTINWLR---------- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126090612  457 pdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNG 531
Cdd:cd18071   149 ---VVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMG 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
301-524 1.77e-14

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: 74.32  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLPAPEALpadskpeevqprffkvhilndEH 380
Cdd:cd18060    22 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIV---------------------YH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  381 KTVASRAkvtadwvseggvLLMGYEMYrlltLKKSLATSRPKKTK----KRSHPVIIDLDEEDRQQEFRrefekalcrpg 456
Cdd:cd18060    81 GSLASRQ------------MIQQYEMY----CKDSRGRLIPGAYKfdalITTFEMILSDCPELREIEWR----------- 133
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126090612  457 pdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18060   134 --CVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
272-520 2.69e-14

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: 74.32  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFL--YDNLVESLERFKTS--SGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAE 346
Cdd:cd18053     9 QPSYIGGHEGLelRDYQLNGLNWLAHSwcKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  347 FNMWLPAPEAlpadskpeevqprffkVHILNDehktVASRAKV-TADWVseggvllmgyemyrlltlkkslatsRPKKTK 425
Cdd:cd18053    89 IQTWAPQMNA----------------VVYLGD----INSRNMIrTHEWM-------------------------HPQTKR 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  426 KRSHPVIIDLDEEDRQQEFRREFEKALcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd18053   124 LKFNILLTTYEILLKDKSFLGGLNWAF-------IGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSL 196
                         250
                  ....*....|....*
gi 126090612  506 VDFVRPDFLGTRQEF 520
Cdd:cd18053   197 LHFIMPEKFSSWEDF 211
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
292-523 3.05e-14

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: 73.89  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  292 RFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWlpapealpadskpeevQPRF 370
Cdd:cd18055    13 RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKgPFLVSAPLSTIINWEREFQMW----------------APDF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  371 FKVHILNDEHktvaSRAKVTADWVSeggvllmgYEMYRLLTLKKSLATSRPKKTKkrSHPVIIDLDEEDRQQEFRREFEK 450
Cdd:cd18055    77 YVVTYTGDKD----SRAIIRENEFS--------FDDNAVKGGKKAFKMKREAQVK--FHVLLTSYELVTIDQAALGSIRW 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126090612  451 AlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFL----GTRQEFSNM 523
Cdd:cd18055   143 A-------CLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADI 212
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
271-523 5.63e-14

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: 73.18  E-value: 5.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  271 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18056     1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  350 WLPAPEALP----ADSKPEEVQPRF-FKVHILNDEHKtvASRAKVTADwvSEGGVLLMGYEmyrLLTLKKSLATSrpkkt 424
Cdd:cd18056    72 WAPDMYVVTyvgdKDSRAIIRENEFsFEDNAIRGGKK--ASRMKKEAS--VKFHVLLTSYE---LITIDMAILGS----- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  425 kkrshpviIDLdeedrqqefrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 504
Cdd:cd18056   140 --------IDW----------------------ACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFH 189
                         250       260
                  ....*....|....*....|...
gi 126090612  505 MVDFVRPDFL----GTRQEFSNM 523
Cdd:cd18056   190 LLNFLTPERFhnleGFLEEFADI 212
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
301-524 3.11e-13

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: 70.83  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpapealpadskpEEVQPRFFkvhilndeH 380
Cdd:cd18059    22 CILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-------------TELNVVVY--------H 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  381 KTVASRAKVTAdwvseggvllmgYEMYRLLTLKKSLATSRPKKTKKRSHPVIIDLDEEDRQQEFRrefekalcrpgpdVV 460
Cdd:cd18059    81 GSQASRRTIQL------------YEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWR-------------CV 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126090612  461 ICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18059   136 VIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
272-520 4.05e-13

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: 69.93  E-value: 4.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFlydnlveSLERfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPaktVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd18010     2 LPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAIAIAAYYREEWP---LLIVCPSSLRLTWADEIERWL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  352 PapealpadskpeEVQPRffkvhilnDEHKTVASRAKVTADWvseGGVLLMGYEMyrLLTLKKSLAtsrpkktkkrshpv 431
Cdd:cd18010    67 P------------SLPPD--------DIQVIVKSKDGLRDGD---AKVVIVSYDL--LRRLEKQLL-------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  432 iidldeedrQQEFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNI--RSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd18010   108 ---------ARKFK-------------VVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDAL 165
                         250
                  ....*....|.
gi 126090612  510 RPDFLGTRQEF 520
Cdd:cd18010   166 DPKLFGRFHDF 176
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
301-524 3.15e-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: 67.76  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpapealpadskpEEVQPRFFkvhilndeH 380
Cdd:cd18058    22 CILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTW-------------TEMNAIVY--------H 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  381 KTVASRAkvtadwvseggvLLMGYEMYRlltlkkSLATSRPKKTKKRSHPVIIDLdeedrqqefrrEFEKALCrpgPDV- 459
Cdd:cd18058    81 GSQISRQ------------MIQQYEMYY------RDEQGNPLSGIFKFQVVITTF-----------EMILADC---PELk 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126090612  460 ------VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18058   129 kinwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
301-524 3.19e-11

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: 64.64  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpapealpadskpeevqprffkVHI-LNDE 379
Cdd:cd18061    22 CILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTW----------------------TDLnVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  380 HKTVASRAkvtadwvseggvLLMGYEMYRLLTLKKSLATSRPKKTKKRSHPVIIDLDEEDRQQEFRrefekalcrpgpdV 459
Cdd:cd18061    80 HGSLISRQ------------MIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWR-------------C 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126090612  460 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18061   135 VIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
273-544 3.69e-10

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: 61.15  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  273 PHQIggirflyDNLVESLERFKtssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN--MW 350
Cdd:cd18011     3 PHQI-------DAVLRALRKPP----VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQdkFG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  351 LPAPEALPADSKPEEvqprffkvhilndehktvasrakvtadwvseggvllmgyemyrlltlkkslatSRPKKTKKRSHP 430
Cdd:cd18011    72 LPFLILDRETAAQLR-----------------------------------------------------RLIGNPFEEFPI 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  431 VIIDLDEEDRQqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQ----ALKNI--RSRRRVVLTGYPLQNNLIEYWC 504
Cdd:cd18011    99 VIVSLDLLKRS----EERRGLLLSEEWDLVVVDEAHKLRNSGGGKETkrykLGRLLakRARHVLLLTATPHNGKEEDFRA 174
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 126090612  505 MVDFVRPDFlgtrqefsnmFERPILNGQCIDSTPQDVRLM 544
Cdd:cd18011   175 LLSLLDPGR----------FAVLGRFLRLDGLREVLAKVL 204
DEXDc smart00487
DEAD-like helicases superfamily;
273-514 5.28e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 60.58  E-value: 5.28e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    273 PHQIGGIRFLYDNLveslerfktssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTL-QNWLAEFNMWL 351
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    352 PapealpadskpeevqPRFFKVHILNDEHKTVASRAKVTADwvsEGGVLLMGYEMYRLLTLKKSLATSRpkktkkrshpv 431
Cdd:smart00487   79 P---------------SLGLKVVGLYGGDSKREQLRKLESG---KTDILVTTPGRLLDLLENDKLSLSN----------- 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612    432 iidldeedrqqefrrefekalcrpgPDVVICDEGHRIKNcqASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 503
Cdd:smart00487  130 -------------------------VDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 126090612    504 CMVDFVRPDFL 514
Cdd:smart00487  183 NDPVFIDVGFT 193
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
300-510 1.13e-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: 51.33  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  300 GCILAHSMGLGKTLQVISFI------------------DVLFRH-----TPAKTVLAIVPVNTLQNWLAEFNmwlpapea 356
Cdd:cd18072    22 GGILADDMGLGKTLTMIALIlaqkntqnrkeeekekalTEWESKkdstlVPSAGTLVVCPASLVHQWKNEVE-------- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  357 lpadSKPEEVQPRFFKVHILNDEhktvaSRAKVTADWvsegGVLLMGYEmyrllTLKKSLATsrpKKTKKRSHPViidld 436
Cdd:cd18072    94 ----SRVASNKLRVCLYHGPNRE-----RIGEVLRDY----DIVITTYS-----LVAKEIPT---YKEESRSSPL----- 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126090612  437 eedrqqeFRREFEKalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18072   148 -------FRIAWAR---------IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
272-350 8.61e-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: 42.34  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612  272 KPHQIGGIRFLYDNLVeslerfktssgfGCILAhSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQN-WLAEFNMW 350
Cdd:cd18013     2 HPYQKVAINFIIEHPY------------CGLFL-DMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
1112-1445 2.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1112 SDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPEGLARPvspdsPEIISELQQYADVAAARES 1191
Cdd:PHA03247 2657 APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP-----HALVSATPLPPGPAAARQA 2731
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1192 RQSSPSVSAALPGPPGQLMDNSTipgTALGTEPclgghclnssllVTGQPSGGRHPVLDLRGHKRKLATPSVTQESVRRR 1271
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGP---ARPARPP------------TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1272 SrkghLPAPVQPYEHGYPVSGGFAMPPVSLN--HNLTTPFTSQAGENSLFMGSNPSYYQLSNLLA---DARLVFPVTTDP 1346
Cdd:PHA03247 2797 S----LPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApggDVRRRPPSRSPA 2872
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1347 LVPAGPVSSSSTATSVTASNPS---FMLNPSVPGMLPSYSLPfSQPLLSEPRMFAPFPSPGLPSNLSRGVSVYPGYMSPH 1423
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVSRStesFALPPDQPERPPQPQAP-PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAG 2951
                         330       340
                  ....*....|....*....|..
gi 126090612 1424 AGYPAGGLLRSQVPPFDSHEVA 1445
Cdd:PHA03247 2952 AGEPSGAVPQPWLGALVPGRVA 2973
PHA03247 PHA03247
large tegument protein UL36; Provisional
1106-1443 4.81e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1106 GTYIRTSDGRIFAVRATGKPKAPEDGRMAASGSQ--GPSLASTSNGRHSASSPKAPDPEGLARPVSPDSPEIiselqqya 1183
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL-------- 2818
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1184 dvaaaresrqsSPSVSAALPGPPgqlmdnstiPGTALGTEPCLGGHCLNSSLlvtgQPSGGRHPVLDLRghKRKLATPSV 1263
Cdd:PHA03247 2819 -----------PPAASPAGPLPP---------PTSAQPTAPPPPPGPPPPSL----PLGGSVAPGGDVR--RRPPSRSPA 2872
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1264 TQESVRRRSRKGHLPAPVQPyehgyPVSGGFAMPPVSLNHnlttPFTSQAGENSLFMGSNPSYYQLSNLLadarlvfPVT 1343
Cdd:PHA03247 2873 AKPAAPARPPVRRLARPAVS-----RSTESFALPPDQPER----PPQPQAPPPPQPQPQPPPPPQPQPPP-------PPP 2936
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1344 TDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGMLPSYSLPFSQPLLSEPrmfAPFPSPGLPSNLS-RGVSVYPGYMSP 1422
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE---APASSTPPLTGHSlSRVSSWASSLAL 3013
                         330       340
                  ....*....|....*....|...
gi 126090612 1423 H--AGYPAGGLLRSQVPPFDSHE 1443
Cdd:PHA03247 3014 HeeTDPPPVSLKQTLWPPDDTED 3036
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1112-1300 5.65e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1112 SDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPE------GLARPVSPDSPE-----IISELQ 1180
Cdd:PHA03307   79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPpaaspPAAGAS 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126090612 1181 QYADVAAARESRQSS---PSVSAALPGPPGQLMDNSTIPGTALGTEPCLGGHCLNSSLLVTGQPSGGRHPVLDlRGHKRK 1257
Cdd:PHA03307  159 PAAVASDAASSRQAAlplSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD-AGASSS 237
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 126090612 1258 LATPSVTQ------ESVRRRSRKGHLPAPVQPYEHGYPVSGGFAMPPVS 1300
Cdd:PHA03307  238 DSSSSESSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPAS 286
 
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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