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Conserved domains on  [gi|1016080529|ref|NP_001309185|]
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helicase ARIP4 isoform a [Homo sapiens]

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 7.36e-158

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: 475.46  E-value: 7.36e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 LPPPEALPadnkpeEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshp 430
Cdd:cd18069     81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069    134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1016080529  511 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18069    191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 5.70e-91

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 310.62  E-value: 5.70e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553     87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553    167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:COG0553    243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAK 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPpealpadnkpeevqprfFKVHILNDEHKtmasRAKvMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrsh 429
Cdd:COG0553    312 FAPG-----------------LRVLVLDGTRE----RAK-GANPFEDADLVITSYGL----------------------- 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  430 pviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:COG0553    347 --------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFL 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  510 RPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRD 589
Cdd:COG0553    412 NPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRA 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  590 LYTQFMDRFRDCGSSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkesLANEQDLDVEelgsagtsarcppq 660
Cdd:COG0553    480 LYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR-------------- 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  661 gtkgkgedstlassmgeatnskflqgvgfnpfqergnnivtyewakdlltnyqtgvlenSPKMVLLFHLIEESVKLGDKI 740
Cdd:COG0553    532 -----------------------------------------------------------SAKLEALLELLEELLAEGEKV 552
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  741 LVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTRAGC 820
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLKAGG 612
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  821 LGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1106-1414 8.97e-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: 40.69  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1106 GTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQ--GPSCESTSNGRHSASSPKAPDPEGLARPVSPdspeiiselqqya 1183
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLA------------- 2813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1184 dvAAARESRQSSPSTnaALPGPPAQLMDSSAVPGTALGTEPRLGGHCLnssllvtgqPCGDrhpvLDLRGHKRKLATPPA 1263
Cdd:PHA03247  2814 --PAAALPPAASPAG--PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---------PGGD----VRRRPPSRSPAAKPA 2876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1264 AqeSSRRRSRKGHLPAPVQPYEhgypvsgGFAMPPVSLNHNLTTPFTSQAgenslfmgSTPSYYQLSNLLADARlvfPVT 1343
Cdd:PHA03247  2877 A--PARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPP---PPP 2936
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529 1344 TDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGilpsySLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMS 1414
Cdd:PHA03247  2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG-----RVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
 
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 7.36e-158

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: 475.46  E-value: 7.36e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 LPPPEALPadnkpeEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshp 430
Cdd:cd18069     81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069    134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1016080529  511 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18069    191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 5.70e-91

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 310.62  E-value: 5.70e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553     87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553    167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:COG0553    243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAK 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPpealpadnkpeevqprfFKVHILNDEHKtmasRAKvMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrsh 429
Cdd:COG0553    312 FAPG-----------------LRVLVLDGTRE----RAK-GANPFEDADLVITSYGL----------------------- 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  430 pviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:COG0553    347 --------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFL 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  510 RPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRD 589
Cdd:COG0553    412 NPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRA 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  590 LYTQFMDRFRDCGSSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkesLANEQDLDVEelgsagtsarcppq 660
Cdd:COG0553    480 LYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR-------------- 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  661 gtkgkgedstlassmgeatnskflqgvgfnpfqergnnivtyewakdlltnyqtgvlenSPKMVLLFHLIEESVKLGDKI 740
Cdd:COG0553    532 -----------------------------------------------------------SAKLEALLELLEELLAEGEKV 552
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  741 LVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTRAGC 820
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLKAGG 612
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  821 LGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
274-628 3.45e-60

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 208.69  E-value: 3.45e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  274 HQIGGIRFLYdnlveSLERFktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP--AKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:pfam00176    1 YQIEGVNWML-----SLENN---LGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 PPPeALPAdnkpeevqprfFKVHILNDEHKTMASRAKVMADWvsegGVLLMGYEMYRlltlkksfatgrpkktkkrSHPV 431
Cdd:pfam00176   73 SPP-ALRV-----------VVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR-------------------KHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  432 IIDldeedrQQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:pfam00176  118 LLK------KVHWHR-------------IVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  512 DFLGTRQEFSNMFERPILNGQcidstpqdvrlMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRDLY 591
Cdd:pfam00176  179 GPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLY 247
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1016080529  592 TQFMDrfrdcGSSGWLGLNPLKAFCVCC----------KIWNHPDVL 628
Cdd:pfam00176  248 QTFLL-----KKDLNAIKTGEGGREIKAsllnilmrlrKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-865 9.03e-52

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 178.44  E-value: 9.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  720 SPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLIN 799
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER------------------GIKYLRLDGSTSSKERQKLVD 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016080529  800 QFNDPSNLTtwLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLV 865
Cdd:cd18793     72 RFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
274-881 3.72e-48

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 188.09  E-value: 3.72e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  274 HQIGGIRF---LYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVL--FR-----HtpaktvLAIVPVNTLQNW 343
Cdd:PLN03142   173 YQLAGLNWlirLYEN------------GINGILADEMGLGKTLQTISLLGYLheYRgitgpH------MVVAPKSTLGNW 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  344 LAEFNMWLPppealpadnkpeevQPRFFKVHILNDEhktmasRAKVMADWVSEGG--VLLMGYEMyrllTLKKsfatgrp 421
Cdd:PLN03142   235 MNEIRRFCP--------------VLRAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM----AIKE------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  422 KKTKKRSHpviidldeedrqqeFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIE 501
Cdd:PLN03142   284 KTALKRFS--------------WR-------------YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  502 YWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstpQDVrlmryrSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILV 581
Cdd:PLN03142   337 LWALLNFLLPEIFSSAETFDEWFQISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKV 404
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  582 RLSKIQRDLYtqfmdrfrdcgssgwlglnplKAfcvcckiwnhpdvlyeALQKeslaneqdlDVEELGSAGTSARCppqg 661
Cdd:PLN03142   405 GMSQMQKQYY---------------------KA----------------LLQK---------DLDVVNAGGERKRL---- 434
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  662 tkgkgedSTLASSMGEATNSKFL-QGVGFNPfqergnnivtyewakdlltNYQTG--VLENSPKMVLLFHLIEESVKLGD 738
Cdd:PLN03142   435 -------LNIAMQLRKCCNHPYLfQGAEPGP-------------------PYTTGehLVENSGKMVLLDKLLPKLKERDS 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  739 KILVFSQSLSTLALIEEFLgkrevpcppgtegqgaqkWVRNISYFRLDGSTPAFERERLINQFNDPsNLTTWLFLLSTRA 818
Cdd:PLN03142   489 RVLIFSQMTRLLDILEDYL------------------MYRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRA 549
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016080529  819 GCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISK 881
Cdd:PLN03142   550 GGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
722-854 2.86e-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: 84.57  E-value: 2.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  722 KMVLLFHLIEEsvKLGDKILVFSQSLSTLAliEEFLGKREvpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQF 801
Cdd:pfam00271    2 KLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKE-----------------GIKVARLHGDLSQEEREEILEDF 60
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1016080529  802 NDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:pfam00271   61 RKGKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
778-854 1.80e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.41  E-value: 1.80e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016080529   778 RNISYFRLDGSTPAFERERLINQFNDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
273-514 1.41e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.43  E-value: 1.41e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   273 PHQIGGIRFLYDNLveslerfktssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTL-QNWLAEFNMWL 351
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   352 PPPealpadnkpeevqprFFKVHILNDEHKTMASRAKVMADwvsEGGVLLMGYEmyRLLTLKKsfatgrpkktkkrshpv 431
Cdd:smart00487   79 PSL---------------GLKVVGLYGGDSKREQLRKLESG---KTDILVTTPG--RLLDLLE----------------- 121
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   432 iidldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNcqASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 503
Cdd:smart00487  122 -----------------NDKLSLSNVDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 1016080529   504 CMVDFVRPDFL 514
Cdd:smart00487  183 NDPVFIDVGFT 193
PHA03247 PHA03247
large tegument protein UL36; Provisional
1106-1414 8.97e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1106 GTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQ--GPSCESTSNGRHSASSPKAPDPEGLARPVSPdspeiiselqqya 1183
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLA------------- 2813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1184 dvAAARESRQSSPSTnaALPGPPAQLMDSSAVPGTALGTEPRLGGHCLnssllvtgqPCGDrhpvLDLRGHKRKLATPPA 1263
Cdd:PHA03247  2814 --PAAALPPAASPAG--PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---------PGGD----VRRRPPSRSPAAKPA 2876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1264 AqeSSRRRSRKGHLPAPVQPYEhgypvsgGFAMPPVSLNHNLTTPFTSQAgenslfmgSTPSYYQLSNLLADARlvfPVT 1343
Cdd:PHA03247  2877 A--PARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPP---PPP 2936
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529 1344 TDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGilpsySLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMS 1414
Cdd:PHA03247  2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG-----RVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
 
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 7.36e-158

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: 475.46  E-value: 7.36e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 350
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 LPPPEALPadnkpeEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshp 430
Cdd:cd18069     81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  431 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18069    134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1016080529  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 4.38e-111

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: 350.44  E-value: 4.38e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18007      1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPpEALPadnkpeevqprfFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTLKKSfatgrpkkTKKRSH 429
Cdd:cd18007     79 WLPP-DLRP------------LLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT--------TDPRLK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  430 pviidldeedrqqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd18007    138 ----------------QEFIAALLDPGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1016080529  510 RPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18007    202 RPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLMLKR 239
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
110-890 5.70e-91

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 310.62  E-value: 5.70e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  110 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSS 189
Cdd:COG0553     87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  190 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALgrVLVNLNHPPEEENVFLAPQLar 269
Cdd:COG0553    167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  270 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:COG0553    243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAK 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPpealpadnkpeevqprfFKVHILNDEHKtmasRAKvMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrsh 429
Cdd:COG0553    312 FAPG-----------------LRVLVLDGTRE----RAK-GANPFEDADLVITSYGL----------------------- 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  430 pviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:COG0553    347 --------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFL 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  510 RPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRD 589
Cdd:COG0553    412 NPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRA 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  590 LYTQFMDRFRDCGSSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkesLANEQDLDVEelgsagtsarcppq 660
Cdd:COG0553    480 LYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR-------------- 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  661 gtkgkgedstlassmgeatnskflqgvgfnpfqergnnivtyewakdlltnyqtgvlenSPKMVLLFHLIEESVKLGDKI 740
Cdd:COG0553    532 -----------------------------------------------------------SAKLEALLELLEELLAEGEKV 552
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  741 LVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTRAGC 820
Cdd:COG0553    553 LVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLKAGG 612
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  821 LGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVD 890
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
271-547 8.08e-84

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: 274.46  E-value: 8.08e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP---AKTVLAIVPVNTLQNWLAEF 347
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKlenFSRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  348 NMWLpppealpADNKPEEVqprfFKVHILnDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTlkksfaTGRPKKTKKR 427
Cdd:cd18068     81 EKWQ-------EGLKDEEK----IEVNEL-ATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILA------QERNVKSREK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  428 ShpviidldeedrqqefRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18068    143 L----------------KEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVN 206
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1016080529  508 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 547
Cdd:cd18068    207 FVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDVRVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
274-628 3.45e-60

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 208.69  E-value: 3.45e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  274 HQIGGIRFLYdnlveSLERFktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP--AKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:pfam00176    1 YQIEGVNWML-----SLENN---LGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 PPPeALPAdnkpeevqprfFKVHILNDEHKTMASRAKVMADWvsegGVLLMGYEMYRlltlkksfatgrpkktkkrSHPV 431
Cdd:pfam00176   73 SPP-ALRV-----------VVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR-------------------KHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  432 IIDldeedrQQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:pfam00176  118 LLK------KVHWHR-------------IVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  512 DFLGTRQEFSNMFERPILNGQcidstpqdvrlMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRDLY 591
Cdd:pfam00176  179 GPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLY 247
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1016080529  592 TQFMDrfrdcGSSGWLGLNPLKAFCVCC----------KIWNHPDVL 628
Cdd:pfam00176  248 QTFLL-----KKDLNAIKTGEGGREIKAsllnilmrlrKICNHPGLI 289
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
273-562 4.00e-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: 206.37  E-value: 4.00e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIGGIRFLYDnlveSLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-----AKTVLAIVPVNTLQNWLAEF 347
Cdd:cd18004      3 PHQREGVQFLYD----CLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPygkptAKKALIVCPSSLVGNWKAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  348 NMWLPP----PEALPADNKPEEVQPRFFkvhilndehkTMASRAKVmadwvseggvLLMGYEMyrlltlkksfatgrpkk 423
Cdd:cd18004     79 DKWLGLrrikVVTADGNAKDVKASLDFF----------SSASTYPV----------LIISYET----------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  424 tkkrshpviidldeedrqqeFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYW 503
Cdd:cd18004    122 --------------------LRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFF 181
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016080529  504 CMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18004    182 ALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
720-865 9.03e-52

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 178.44  E-value: 9.03e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  720 SPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLIN 799
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER------------------GIKYLRLDGSTSSKERQKLVD 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016080529  800 QFNDPSNLTtwLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLV 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 1.84e-48

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: 170.82  E-value: 1.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFLYDNLveslerfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKT-VLAIVPVNTLQNWLAEFNMW 350
Cdd:cd17919      2 RPYQLEGLNFLLELY---------ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGpVLVVCPLSVLENWEREFEKW 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 LPPpealpadnkpeevqprfFKVHILndeHKTMASRAKVMAD-WVSEGGVLLMGYEMYRLLTlkksfatgrpkktkkrsh 429
Cdd:cd17919     73 TPD-----------------LRVVVY---HGSQRERAQIRAKeKLDKFDVVLTTYETLRRDK------------------ 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  430 pviidldeedrqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd17919    115 --------------------ASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174

                   ....*
gi 1016080529  510 RPDFL 514
Cdd:cd17919    175 DPPFL 179
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
274-881 3.72e-48

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 188.09  E-value: 3.72e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  274 HQIGGIRF---LYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVL--FR-----HtpaktvLAIVPVNTLQNW 343
Cdd:PLN03142   173 YQLAGLNWlirLYEN------------GINGILADEMGLGKTLQTISLLGYLheYRgitgpH------MVVAPKSTLGNW 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  344 LAEFNMWLPppealpadnkpeevQPRFFKVHILNDEhktmasRAKVMADWVSEGG--VLLMGYEMyrllTLKKsfatgrp 421
Cdd:PLN03142   235 MNEIRRFCP--------------VLRAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM----AIKE------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  422 KKTKKRSHpviidldeedrqqeFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIE 501
Cdd:PLN03142   284 KTALKRFS--------------WR-------------YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  502 YWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstpQDVrlmryrSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILV 581
Cdd:PLN03142   337 LWALLNFLLPEIFSSAETFDEWFQISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKV 404
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  582 RLSKIQRDLYtqfmdrfrdcgssgwlglnplKAfcvcckiwnhpdvlyeALQKeslaneqdlDVEELGSAGTSARCppqg 661
Cdd:PLN03142   405 GMSQMQKQYY---------------------KA----------------LLQK---------DLDVVNAGGERKRL---- 434
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  662 tkgkgedSTLASSMGEATNSKFL-QGVGFNPfqergnnivtyewakdlltNYQTG--VLENSPKMVLLFHLIEESVKLGD 738
Cdd:PLN03142   435 -------LNIAMQLRKCCNHPYLfQGAEPGP-------------------PYTTGehLVENSGKMVLLDKLLPKLKERDS 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  739 KILVFSQSLSTLALIEEFLgkrevpcppgtegqgaqkWVRNISYFRLDGSTPAFERERLINQFNDPsNLTTWLFLLSTRA 818
Cdd:PLN03142   489 RVLIFSQMTRLLDILEDYL------------------MYRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRA 549
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016080529  819 GCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISK 881
Cdd:PLN03142   550 GGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
271-562 8.21e-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: 154.16  E-value: 8.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYDNLVESLERfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVL--AIV--PVNTLQNWLA 345
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIR----GSHGCIMADEMGLGKTLQCITLMWTLLRQSPqCKPEIdkAIVvsPSSLVKNWAN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  346 EFNMWLPPpealpadnkpeEVQPRffkvhILNDEHKTMASRAKVmaDWVSEGG------VLLMGYEMYRLltlkksfatg 419
Cdd:cd18067     77 ELGKWLGG-----------RLQPL-----AIDGGSKKEIDRKLV--QWASQQGrrvstpVLIISYETFRL---------- 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  420 rpkktkkrshpviidldeedrqqefrreFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNL 499
Cdd:cd18067    129 ----------------------------HVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDL 180
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016080529  500 IEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 562
Cdd:cd18067    181 SEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
272-562 9.06e-41

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 150.99  E-value: 9.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFLYDNLVEslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHT---------------------PAKT 330
Cdd:cd18005      2 RDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkkkppassAKKP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  331 VLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevqpRFFKVHILNDEHKTMASRAKVMADWVSeggVLLMGYEMYRLl 410
Cdd:cd18005     73 VLIVAPLSVLYNWKDELDTW------------------GHFEVGVYHGSRKDDELEGRLKAGRLE---VVVTTYDTLRR- 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  411 tlkksfatgrpkktkkrshpviiDLDEEDrQQEFrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVL 490
Cdd:cd18005    131 -----------------------CIDSLN-SINW-------------SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGL 173
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016080529  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 3.41e-39

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: 146.14  E-value: 3.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYdnlvESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP------AKTVLAIVPVNTLQNWL 344
Cdd:cd18066      1 LRPHQREGIEFLY----ECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPyggkpvIKRALIVTPGSLVKNWK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  345 AEFNMWLpppealpadnKPEEVqprffKVHILNDEHKTmasRAKVMADWVSeggVLLMGYEMyrLLtlkksfatgrpkkt 424
Cdd:cd18066     77 KEFQKWL----------GSERI-----KVFTVDQDHKV---EEFIASPLYS---VLIISYEM--LL-------------- 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  425 kkRSHPVIIDLDEedrqqefrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 504
Cdd:cd18066    120 --RSLDQISKLNF--------------------DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFA 177
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016080529  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 6.63e-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: 145.21  E-value: 6.63e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIGGIRFLYdnlveSLErfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLP 352
Cdd:cd18001      3 PHQREGVAWLW-----SLH----DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  353 ppealpadnkpeevQPRFFKVHILNdehktMASRAKVMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrshpvi 432
Cdd:cd18001     74 --------------GLRVKVFHGTS-----KKERERNLERIQRGGGVLLTTYGM-------------------------- 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  433 IDLDEEDRQQEFRREFEKalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP- 511
Cdd:cd18001    109 VLSNTEQLSADDHDEFKW-------DYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNg 181
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1016080529  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 7.05e-32

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: 124.60  E-value: 7.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLP 352
Cdd:cd18012      7 PYQKEGFNWL---------SFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  353 PpealpadnkpeevqprfFKVHILNDehktmASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshpvi 432
Cdd:cd18012     78 E-----------------LKVLVIHG-----TKRKREKLRALEDYDLVITSYGLLRR----------------------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  433 idlDEEDRQQefrREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPD 512
Cdd:cd18012    113 ---DIELLKE---VKF---------HYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPG 177
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1016080529  513 FLGTRQEFSNMFERPILNGQCIDSTPQdvrlmryrshvLHSLLEGFVQRR 562
Cdd:cd18012    178 LLGSYKRFKKRFAKPIEKDGDEEALEE-----------LKKLISPFILRR 216
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
273-514 7.82e-32

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: 123.59  E-value: 7.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIGGIRFLYDnlveslerfKTSSGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd18000      3 KYQQTGVQWLWE---------LHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWW 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 PPpealpadnkpeevqprfFKVHIL--------NDEHKTMASRAKVMADWV-SEGGVLLMGYEMYRLLtlkksfatgrpk 422
Cdd:cd18000     74 PP-----------------FRVVVLhssgsgtgSEEKLGSIERKSQLIRKVvGDGGILITTYEGFRKH------------ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  423 ktkkrSHPVIidldeedrqqefRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEY 502
Cdd:cd18000    125 -----KDLLL------------NHNW---------QYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKEL 178
                          250
                   ....*....|..
gi 1016080529  503 WCMVDFVRPDFL 514
Cdd:cd18000    179 WSLFDFVFPPYL 190
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
302-562 1.64e-30

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 120.89  E-value: 1.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  302 ILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffKVHILNDE 379
Cdd:cd17997     26 ILADEMGLGKTLQTISLLGYLkhYKNINGPH-LIIVPKSTLDNWMREFKRWCPSLRVV--------------VLIGDKEE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  380 HKTMASRAKVMADWvsegGVLLMGYEMyrlltlkksfatgrpkktkkrshpVIIDldeedrqqefrrefEKALCRPGPDV 459
Cdd:cd17997     91 RADIIRDVLLPGKF----DVCITSYEM------------------------VIKE--------------KTVLKKFNWRY 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  460 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCIDstPQ 539
Cdd:cd17997    129 IIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN----VNNCDD--DN 202
                          250       260
                   ....*....|....*....|...
gi 1016080529  540 DVRLMRyrshvLHSLLEGFVQRR 562
Cdd:cd17997    203 QEVVQR-----LHKVLRPFLLRR 220
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
272-562 9.32e-30

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 119.03  E-value: 9.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGI---RFLYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN 348
Cdd:cd18009      5 RPYQLEGMewlRMLWEN------------GINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  349 MWLPPPEALpadnkpeevqprffKVHILNDEHKTMasRAKVMadwvseggvllmgyemyrlltlkksfatgrPKKTKKRS 428
Cdd:cd18009     73 RFTPSVPVL--------------LYHGTKEERERL--RKKIM------------------------------KREGTLQD 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  429 HPVIIDLDE---EDRqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd18009    107 FPVVVTSYEiamRDR---------KALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSL 177
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016080529  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 1.04e-27

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: 112.85  E-value: 1.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRF---LYDNLVESlerfktssgfgcILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEF 347
Cdd:cd17996      5 KEYQLKGLQWmvsLYNNNLNG------------ILADEMGLGKTIQTISLITYLMEKKKNNgPYLVIVPLSTLSNWVSEF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  348 NMWLPPPEALPADNKPEeVQPRFFKVHIlndehktmasrakvmadwVSEGGVLLMGYEMyrllTLKKsfatgRPKKTKKR 427
Cdd:cd17996     73 EKWAPSVSKIVYKGTPD-VRKKLQSQIR------------------AGKFNVLLTTYEY----IIKD-----KPLLSKIK 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  428 SHPVIIDldeedrqqefrrefekalcrpgpdvvicdEGHRIKNCQASTSQALKN-IRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:cd17996    125 WKYMIID-----------------------------EGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALL 175
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016080529  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 7.36e-26

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 106.32  E-value: 7.36e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFLydNLVESlerfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd17998      2 KDYQLIGLNWL--NLLYQ-------KKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWC 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 PPPEALPADNKPEEvqprffKVHILNDEHKTmasrakvmadwVSEGGVLLMGYEMyrlltlkksfATGRPkktkkrshpv 431
Cdd:cd17998     73 PSLKVEPYYGSQEE------RKHLRYDILKG-----------LEDFDVIVTTYNL----------ATSNP---------- 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  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 7.51e-24

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: 101.56  E-value: 7.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  300 GCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPppealpadnkpeevqprffkvhiLND 378
Cdd:cd17995     21 NCILADEMGLGKTIQSIAFLEHLYqVEGIRGPFLVIAPLSTIPNWQREFETWTD-----------------------MNV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  379 --EHKTMASRAkvmadwvseggvLLMGYEMYRlltlkkSFATGRPKKTKKRSHpVIIDLDE---EDRQqefrrEFEKALC 453
Cdd:cd17995     78 vvYHGSGESRQ------------IIQQYEMYF------KDAQGRKKKGVYKFD-VLITTYEmviADAE-----ELRKIPW 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529  454 RpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd17995    134 R----VVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
299-562 1.18e-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: 95.82  E-value: 1.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  299 FGCILAHSMGLGKTLQVISFI------------------DVLFRHTPAKTVLAIVPVNTLQNWLAEFNMwlpppealpad 360
Cdd:cd18008     15 RGGILADEMGLGKTIQALALIlatrpqdpkipeeleensSDPKKLYLSKTTLIVVPLSLLSQWKDEIEK----------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  361 nkpeEVQPRFFKVHILndeHKtmASRAKVMADWvSEGGVLLMGYEmyrllTLKKSFATGRPKKTKKRSHPVIIDLdeedR 440
Cdd:cd18008     84 ----HTKPGSLKVYVY---HG--SKRIKSIEEL-SDYDIVITTYG-----TLASEFPKNKKGGGRDSKEKEASPL----H 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  441 QQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEF 520
Cdd:cd18008    145 RIRWYR-------------VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1016080529  521 snmferpilNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18008    212 ---------NSDISKPFSKNDRKALER---LQALLKPILLRR 241
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
302-562 1.39e-21

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


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 95.11  E-value: 1.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  302 ILAHSMGLGKTLQVISFIDVLFRHtpaKTV----LAIVPVNTLQNWLAEFNMWLPPpealpadnkpeevqprfFKVHILN 377
Cdd:cd18003     23 ILADEMGLGKTIQTIALLAHLACE---KGNwgphLIVVPTSVMLNWEMEFKRWCPG-----------------FKILTYY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  378 DEHKtmaSRAKVMADWVSEGG--VLLMGYEMyrlltlkksfatgrpkktkkrshpVIIDldeedrQQEFRREFEKALcrp 455
Cdd:cd18003     83 GSAK---ERKLKRQGWMKPNSfhVCITSYQL------------------------VVQD------HQVFKRKKWKYL--- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  456 gpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPiLNGQCID 535
Cdd:cd18003    127 -----ILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSEG 200
                          250       260
                   ....*....|....*....|....*..
gi 1016080529  536 STPQDVRLMRYrshvLHSLLEGFVQRR 562
Cdd:cd18003    201 SQEENEELVRR----LHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
297-575 3.46e-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: 91.65  E-value: 3.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  297 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEAlpadnkpeevqprffkVH 374
Cdd:cd18064     33 NGINGILADEMGLGKTLQTISLLGYMkhYRNIPGPH-MVLVPKSTLHNWMAEFKRWVPTLRA----------------VC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  375 ILNDEHKTMASRAKVMADwvSEGGVLLMGYEMyrLLTLKKSFatgrpKKTKKRshpviidldeedrqqefrrefekalcr 454
Cdd:cd18064     96 LIGDKDQRAAFVRDVLLP--GEWDVCVTSYEM--LIKEKSVF-----KKFNWR--------------------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  455 pgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCI 534
Cdd:cd18064    140 ----YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD----TNNCL 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1016080529  535 DstpqDVRLMRYrshvLHSLLEGFVQRRGHTVLKIHLPAKE 575
Cdd:cd18064    212 G----DQKLVER----LHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
272-536 3.88e-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: 3.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFLydnlvESLERFKTSSgfgcILAHSMGLGKTLQVISFIDVLFRHTPAKT------VLAIVPVNTLQNWLA 345
Cdd:cd17999      2 RPYQQEGINWL-----AFLNKYNLHG----ILCDDMGLGKTLQTLCILASDHHKRANSFnsenlpSLVVCPPTLVGHWVA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  346 EFNMWLPPPealpadnkpeevqprFFKVHILndeHKTMASRAKvMADWVSEGGVLLMGYEMYRlltlkksfatgrpkktk 425
Cdd:cd17999     73 EIKKYFPNA---------------FLKPLAY---VGPPQERRR-LREQGEKHNVIVASYDVLR----------------- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  426 krshpviidldeedRQQEFRREFEKALCrpgpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd17999    117 --------------NDIEVLTKIEWNYC-------VLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSL 175
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1016080529  506 VDFVRPDFLGTRQEFSNMFERPILngQCIDS 536
Cdd:cd17999    176 FDFLMPGYLGTEKQFQRRFLKPIL--ASRDS 204
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
722-854 2.86e-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: 84.57  E-value: 2.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  722 KMVLLFHLIEEsvKLGDKILVFSQSLSTLAliEEFLGKREvpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQF 801
Cdd:pfam00271    2 KLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKE-----------------GIKVARLHGDLSQEEREEILEDF 60
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1016080529  802 NDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:pfam00271   61 RKGKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
301-562 4.44e-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: 87.41  E-value: 4.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  301 CILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffkVHILNde 379
Cdd:cd17993     23 GILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI---------------VYLGD-- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  380 hktMASRAkvmadwvseggvLLMGYEMYrlltlkksfatgrPKKTKKRSHPVIIDLDE---EDRQ--QEFRREFekalcr 454
Cdd:cd17993     86 ---IKSRD------------TIREYEFY-------------FSQTKKLKFNVLLTTYEiilKDKAflGSIKWQY------ 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  455 pgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFsnmferpilngqci 534
Cdd:cd17993    132 -----LAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-------------- 192
                          250       260
                   ....*....|....*....|....*...
gi 1016080529  535 DSTPQDVRLMRYRShvLHSLLEGFVQRR 562
Cdd:cd17993    193 EEEHDEEQEKGIAD--LHKELEPFILRR 218
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
273-525 5.54e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 86.72  E-value: 5.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWl 351
Cdd:cd17994      3 PYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMW- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 pppealpadnkpeevQPRFFKVHILNDEhktmasrakvmadwvseggVLLMGYEmyrLLTLKKsfatgrpkktkkrshPV 431
Cdd:cd17994     73 ---------------APDFYVVTYVGDH-------------------VLLTSYE---LISIDQ---------------AI 100
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  432 IIDLDEEdrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 511
Cdd:cd17994    101 LGSIDWA--------------------VLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
                          250
                   ....*....|....
gi 1016080529  512 DFLGTRQEFSNMFE 525
Cdd:cd17994    161 ERFNNLQGFLEEFA 174
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
297-562 9.42e-19

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: 9.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  297 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEAlpadnkpeevqprffkVH 374
Cdd:cd18065     33 NGVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMNEFKRWVPSLRA----------------VC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  375 ILNDEHKTMASRAKVMADwvSEGGVLLMGYEMYrlltlkksfatgrpkktkkrshpviidLDEEDRQQEFRREFekalcr 454
Cdd:cd18065     96 LIGDKDARAAFIRDVMMP--GEWDVCVTSYEMV---------------------------IKEKSVFKKFNWRY------ 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  455 pgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCI 534
Cdd:cd18065    141 -----LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD----TKNCL 211
                          250       260
                   ....*....|....*....|....*...
gi 1016080529  535 DstpqDVRLMRYrshvLHSLLEGFVQRR 562
Cdd:cd18065    212 G----DQKLVER----LHAVLKPFLLRR 231
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
271-562 6.34e-18

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: 85.10  E-value: 6.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFL---YDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAE 346
Cdd:cd18062     24 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWVYE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  347 FNMWLPPPEALPADNKPEevqprffkvhilndehktmASRAKVMADWVSEGGVLLMGYEMyrLLTLKKSFATGRPKktkk 426
Cdd:cd18062     92 FDKWAPSVVKVSYKGSPA-------------------ARRAFVPQLRSGKFNVLLTTYEY--IIKDKQILAKIRWK---- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  427 rshpviidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCM 505
Cdd:cd18062    147 --------------------------------YMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWAL 194
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016080529  506 VDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18062    195 LNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR---LHKVLRPFLLRR 249
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
302-562 1.14e-17

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: 83.90  E-value: 1.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  302 ILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffkVHILNdeh 380
Cdd:cd18054     43 ILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV---------------VYIGD--- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  381 ktMASRAKVMA-DWVSEggvllmgyemyrlltlkksfatgrpkKTKKRSHPVIIDldeedrQQEFRREFEKALCRPGPDV 459
Cdd:cd18054    105 --LMSRNTIREyEWIHS--------------------------QTKRLKFNALIT------TYEILLKDKTVLGSINWAF 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  460 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGqcidstpq 539
Cdd:cd18054    151 LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-------- 222
                          250       260
                   ....*....|....*....|...
gi 1016080529  540 dvrlmrYRShvLHSLLEGFVQRR 562
Cdd:cd18054    223 ------YQS--LHKVLEPFLLRR 237
HELICc smart00490
helicase superfamily c-terminal domain;
778-854 1.80e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.41  E-value: 1.80e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016080529   778 RNISYFRLDGSTPAFERERLINQFNDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 854
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
302-562 1.91e-17

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: 83.57  E-value: 1.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  302 ILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWLPPpealpadnkpeevqprffkvhILNDEH 380
Cdd:cd18063     46 ILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYEFDKWAPS---------------------VVKISY 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  381 KTMASRAKVMADWVSEG--GVLLMGYEMyrLLTLKKSFATGRPKktkkrshpviidldeedrqqefrrefekalcrpgpd 458
Cdd:cd18063    105 KGTPAMRRSLVPQLRSGkfNVLLTTYEY--IIKDKHILAKIRWK------------------------------------ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  459 VVICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCIDS 536
Cdd:cd18063    147 YMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDL 226
                          250       260
                   ....*....|....*....|....*.
gi 1016080529  537 TPQDVRLMRYRshvLHSLLEGFVQRR 562
Cdd:cd18063    227 NEEETILIIRR---LHKVLRPFLLRR 249
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
271-562 4.31e-17

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: 82.17  E-value: 4.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLYdNLVESlerfktssGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQ--------GINGILADEMGLGKTVQSIAVLAHLAeEHNIWGPFLVIAPASTLHNWQQEISR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPPEALP--ADNKPEEVQPRFFkvhilndEHKTMASRAkvmadwvSEGGVLLMGYEMyrlltlkksfatgrpkktkkr 427
Cdd:cd18002     72 FVPQFKVLPywGNPKDRKVLRKFW-------DRKNLYTRD-------APFHVVITSYQL--------------------- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  428 shpVIIDldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18002    117 ---VVQD--------------EKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLH 179
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1016080529  508 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRyrshvLHSLLEGFVQRR 562
Cdd:cd18002    180 FIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKR-----LHMILKPFMLRR 229
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
271-524 1.24e-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: 80.88  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18057      1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEM 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WlpppealpadnkpeevQPRFFKVHILNDEHktmaSRAKVMADWVS-EGGVLLMGYEMYRLltlkksfatgrPKKTKKRS 428
Cdd:cd18057     72 W----------------APDFYVVTYTGDKE----SRSVIRENEFSfEDNAIRSGKKVFRM-----------KKEAQIKF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  429 HPVIIDLDEEDRQQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDF 508
Cdd:cd18057    121 HVLLTSYELITIDQAILGSIEWA-------CLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNF 193
                          250
                   ....*....|....*.
gi 1016080529  509 VRPDFLGTRQEFSNMF 524
Cdd:cd18057    194 LTPERFNNLEGFLEEF 209
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
271-562 1.48e-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: 80.17  E-value: 1.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLydnlvesLERFKTssGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18006      1 LRPYQLEGVNWL-------LQCRAE--QHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WLPPPEALPADNKPEEvqprffkvhilndehktmasRAKVMADWVSEG--GVLLMGYEMyrlltlkksfatgrpkktkkr 427
Cdd:cd18006     72 FAPDLSVITYMGDKEK--------------------RLDLQQDIKSTNrfHVLLTTYEI--------------------- 110
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  428 shpVIIDldeedrqQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 507
Cdd:cd18006    111 ---CLKD-------ASFLKSFPWA-------SLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLS 173
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016080529  508 FVRPDFLG--TRQEFSNMFERpilngqcIDSTPQDVRlmryrshVLHSLLEGFVQRR 562
Cdd:cd18006    174 FIEPNVFPkdKLDDFIKAYSE-------TDDESETVE-------ELHLLLQPFLLRR 216
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
297-531 3.34e-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: 76.74  E-value: 3.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  297 SGFGCILAHSMGLGKTLQVISFIdvLFRHTpaktvLAIVPVNTLQNWLAEFNmwlpppealpadnkpEEVQPRFFKVHIL 376
Cdd:cd18071     47 LVRGGILADDMGLGKTLTTISLI--LANFT-----LIVCPLSVLSNWETQFE---------------EHVKPGQLKVYTY 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  377 NDEHKTMAsrakvmADWVSEGGVLLMGYEmyrllTLKKSFATgrpkktkKRSHPViidldeedRQQEFRRefekalcrpg 456
Cdd:cd18071    105 HGGERNRD------PKLLSKYDIVLTTYN-----TLASDFGA-------KGDSPL--------HTINWLR---------- 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016080529  457 pdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNG 531
Cdd:cd18071    149 ---VVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMG 220
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
292-523 3.67e-15

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: 76.59  E-value: 3.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  292 RFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevQPRF 370
Cdd:cd18055     13 RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKgPFLVSAPLSTIINWEREFQMW----------------APDF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  371 FKVHILNDEHKTMASRAKVMA--DWVSEGGvllmgyemyrlltlKKSFATGRPKKTKkrSHPVIIDLDEEDRQQEFRREF 448
Cdd:cd18055     77 YVVTYTGDKDSRAIIRENEFSfdDNAVKGG--------------KKAFKMKREAQVK--FHVLLTSYELVTIDQAALGSI 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016080529  449 EKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFL----GTRQEFSNM 523
Cdd:cd18055    141 RWA-------CLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADI 212
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
272-520 1.76e-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: 74.70  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFL--YDNLVESLERFKTS--SGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAE 346
Cdd:cd18053      9 QPSYIGGHEGLelRDYQLNGLNWLAHSwcKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQRE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  347 FNMWLPPPEALpadnkpeeVQPRFFKVHILNDEHKTMASRAKVMadwvsEGGVLLMGYEmyrLLTLKKSFATGRPKKtkk 426
Cdd:cd18053     89 IQTWAPQMNAV--------VYLGDINSRNMIRTHEWMHPQTKRL-----KFNILLTTYE---ILLKDKSFLGGLNWA--- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  427 rshpviidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMV 506
Cdd:cd18053    150 --------------------------------FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLL 197
                          250
                   ....*....|....
gi 1016080529  507 DFVRPDFLGTRQEF 520
Cdd:cd18053    198 HFIMPEKFSSWEDF 211
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
301-524 2.71e-14

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: 73.91  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 380
Cdd:cd18059     22 CILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-------------TELNVVVY--------H 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  381 KTMASRAKVMAdwvseggvllmgYEMYRLLTlkksfaTGRPKKTKKRSHPVIIDLD------EEDRQQEFRrefekalcr 454
Cdd:cd18059     81 GSQASRRTIQL------------YEMYFKDP------QGRVIKGSYKFHAIITTFEmiltdcPELRNIPWR--------- 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  455 pgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18059    134 ----CVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
301-524 3.44e-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: 73.55  E-value: 3.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 380
Cdd:cd18060     22 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTW-------------TEMNTIVY--------H 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  381 KTMASRAkvmadwvseggvLLMGYEMYrlltLKKSFATGRPKKTK----KRSHPVIIDLDEEDRQQEFRrefekalcrpg 456
Cdd:cd18060     81 GSLASRQ------------MIQQYEMY----CKDSRGRLIPGAYKfdalITTFEMILSDCPELREIEWR----------- 133
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016080529  457 pdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18060    134 --CVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
272-520 1.76e-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: 71.08  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFlydnlveSLERfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPaktVLAIVPVNTLQNWLAEFNMWL 351
Cdd:cd18010      2 LPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAIAIAAYYREEWP---LLIVCPSSLRLTWADEIERWL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  352 PppealpadnkpeEVQPRffkvhilnDEHKTMASRAKVMADWvseGGVLLMGYEMyrLLTLKKSFATGRPKktkkrshpv 431
Cdd:cd18010     67 P------------SLPPD--------DIQVIVKSKDGLRDGD---AKVVIVSYDL--LRRLEKQLLARKFK--------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  432 iidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNI--RSRRRVVLTGYPLQNNLIEYWCMVDFV 509
Cdd:cd18010    113 ---------------------------VVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDAL 165
                          250
                   ....*....|.
gi 1016080529  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 2.24e-13

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: 71.23  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 380
Cdd:cd18058     22 CILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTW-------------TEMNAIVY--------H 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  381 KTMASRAkvmadwvseggvLLMGYEMYRlltlkkSFATGRPKKTKKRSHPVIIDLdeedrqqefrrEFEKALCrpgPDV- 459
Cdd:cd18058     81 GSQISRQ------------MIQQYEMYY------RDEQGNPLSGIFKFQVVITTF-----------EMILADC---PELk 128
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529  460 ------VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18058    129 kinwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
271-523 6.05e-13

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: 70.09  E-value: 6.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  271 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 349
Cdd:cd18056      1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEM 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  350 WlpppealpadnkpeevQPRFFKVHILNDEHktmaSRAKVMADWVS-EGGVLLMGYEMYRLltlkksfatgrPKKTKKRS 428
Cdd:cd18056     72 W----------------APDMYVVTYVGDKD----SRAIIRENEFSfEDNAIRGGKKASRM-----------KKEASVKF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  429 HPVIIDLDEEDRQQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDF 508
Cdd:cd18056    121 HVLLTSYELITIDMAILGSIDWA-------CLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNF 193
                          250
                   ....*....|....*....
gi 1016080529  509 VRPDFL----GTRQEFSNM 523
Cdd:cd18056    194 LTPERFhnleGFLEEFADI 212
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
301-524 1.53e-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: 65.80  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  301 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevqprffkVHI-LNDE 379
Cdd:cd18061     22 CILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTW----------------------TDLnVVVY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  380 HKTMASRAkvmadwvseggvLLMGYEMYrlltLKKSfaTGRPKKTKKRSHPVIIdldeedrqqefrrEFEKALCRPGP-- 457
Cdd:cd18061     80 HGSLISRQ------------MIQQYEMY----FRDS--QGRIIRGAYRFQAIIT-------------TFEMILGGCPEln 128
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529  458 ----DVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 524
Cdd:cd18061    129 aidwRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
273-544 3.20e-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: 61.54  E-value: 3.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  273 PHQIggirflyDNLVESLERFKtssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN--MW 350
Cdd:cd18011      3 PHQI-------DAVLRALRKPP----VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQdkFG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 LPPPEALPADNKPEEvqprffkvhilndehktmasrakvmadwvseggvllmgyemyrlltlkksfatGRPKKTKKRSHP 430
Cdd:cd18011     72 LPFLILDRETAAQLR-----------------------------------------------------RLIGNPFEEFPI 98
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  431 VIIDLDEEDRQqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQ----ALKNI--RSRRRVVLTGYPLQNNLIEYWC 504
Cdd:cd18011     99 VIVSLDLLKRS----EERRGLLLSEEWDLVVVDEAHKLRNSGGGKETkrykLGRLLakRARHVLLLTATPHNGKEEDFRA 174
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1016080529  505 MVDFVRPDFlgtrqefsnmFERPILNGQCIDSTPQDVRLM 544
Cdd:cd18011    175 LLSLLDPGR----------FAVLGRFLRLDGLREVLAKVL 204
DEXDc smart00487
DEAD-like helicases superfamily;
273-514 1.41e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.43  E-value: 1.41e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   273 PHQIGGIRFLYDNLveslerfktssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTL-QNWLAEFNMWL 351
Cdd:smart00487   11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   352 PPPealpadnkpeevqprFFKVHILNDEHKTMASRAKVMADwvsEGGVLLMGYEmyRLLTLKKsfatgrpkktkkrshpv 431
Cdd:smart00487   79 PSL---------------GLKVVGLYGGDSKREQLRKLESG---KTDILVTTPG--RLLDLLE----------------- 121
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529   432 iidldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNcqASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 503
Cdd:smart00487  122 -----------------NDKLSLSNVDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
                           250
                    ....*....|.
gi 1016080529   504 CMVDFVRPDFL 514
Cdd:smart00487  183 NDPVFIDVGFT 193
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
460-510 1.73e-06

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 50.94  E-value: 1.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1016080529  460 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 510
Cdd:cd18072    155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
272-509 4.00e-04

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 43.49  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  272 KPHQIGGIRFLYDNLVeslerfktssgfGCILAhSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQN-WLAEFNMW 350
Cdd:cd18013      2 HPYQKVAINFIIEHPY------------CGLFL-DMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  351 lpppealpadnkpeevqprffkvhilndEHktmasrakvmadwvseggvllmgyemyrLLTLKKSFATGRPKK----TKK 426
Cdd:cd18013     69 ----------------------------NH----------------------------LRNLTVSVAVGTERQrskaANT 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529  427 RSHPVIIDLDEED---RQQEFRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSR--RRVVLTGYPLQNNLIE 501
Cdd:cd18013     93 PADLYVINRENLKwlvNKSGDPWPF---------DMVVIDELSSFKSPRSKRFKALRKVRPVikRLIGLTGTPSPNGLMD 163

                   ....*...
gi 1016080529  502 YWCMVDFV 509
Cdd:cd18013    164 LWAQIALL 171
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
812-865 6.29e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.91  E-value: 6.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1016080529  812 FLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQkKPCYIYRLV 865
Cdd:cd18785     25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
1106-1414 8.97e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1106 GTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQ--GPSCESTSNGRHSASSPKAPDPEGLARPVSPdspeiiselqqya 1183
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLA------------- 2813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1184 dvAAARESRQSSPSTnaALPGPPAQLMDSSAVPGTALGTEPRLGGHCLnssllvtgqPCGDrhpvLDLRGHKRKLATPPA 1263
Cdd:PHA03247  2814 --PAAALPPAASPAG--PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---------PGGD----VRRRPPSRSPAAKPA 2876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016080529 1264 AqeSSRRRSRKGHLPAPVQPYEhgypvsgGFAMPPVSLNHNLTTPFTSQAgenslfmgSTPSYYQLSNLLADARlvfPVT 1343
Cdd:PHA03247  2877 A--PARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPP---PPP 2936
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016080529 1344 TDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGilpsySLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMS 1414
Cdd:PHA03247  2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG-----RVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
 
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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