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Conserved domains on  [gi|17540630|ref|NP_502137|]
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Transcription termination factor 2 [Caenorhabditis elegans]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1067 8.04e-129

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 408.07  E-value: 8.04e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  458 TELTDTPKGFKLELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvv 537
Cdd:COG0553  229 EALESLPAGLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP--------------- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  538 keqglipsngTLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKqRDIDARRLARYDVVITTFNLIAneliekirtks 617
Cdd:COG0553  293 ----------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTRE-RAKGANPFEDADLVITSYGLLR----------- 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  618 kaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYS 697
Cdd:COG0553  349 ----------------------RDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWS 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  698 LVRFLRirP--FSDDKYWKE----SIMPMKPIMADRVNLLTKNLLLRRTKDQTcavtnqkLVQLPPKNVEVHELELDGDE 771
Cdd:COG0553  407 LLDFLN--PglLGSLKAFRErfarPIEKGDEEALERLRRLLRPFLLRRTKEDV-------LKDLPEKTEETLYVELTPEQ 477
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  772 AQAYEimmeAAKKFVKKLLQDSNDMKNHGFIprrnrragkegevqnpfnfgprdlaagsnfekmscvLMLLLRLRQACVH 851
Cdd:COG0553  478 RALYE----AVLEYLRRELEGAEGIRRRGLI------------------------------------LAALTRLRQICSH 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  852 FNItktgvdmdafsliggdnaeeanvddlneLLEKTMNMTLGNGdneerdkprattrifdpdylscKIKNTLEIVENIME 931
Cdd:COG0553  518 PAL----------------------------LLEEGAELSGRSA----------------------KLEALLELLEELLA 547
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  932 KKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFnREKGGARVMLLSLAAGGVGLNLTGGNHLVMV 1011
Cdd:COG0553  548 EGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHY 626
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630 1012 DLHWNPALEQQAFDRIYRMGQKKDVFIHRLVTKGTIEQRVVMLQKDKVALASSVLD 1067
Cdd:COG0553  627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1067 8.04e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 408.07  E-value: 8.04e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  458 TELTDTPKGFKLELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvv 537
Cdd:COG0553  229 EALESLPAGLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP--------------- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  538 keqglipsngTLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKqRDIDARRLARYDVVITTFNLIAneliekirtks 617
Cdd:COG0553  293 ----------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTRE-RAKGANPFEDADLVITSYGLLR----------- 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  618 kaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYS 697
Cdd:COG0553  349 ----------------------RDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWS 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  698 LVRFLRirP--FSDDKYWKE----SIMPMKPIMADRVNLLTKNLLLRRTKDQTcavtnqkLVQLPPKNVEVHELELDGDE 771
Cdd:COG0553  407 LLDFLN--PglLGSLKAFRErfarPIEKGDEEALERLRRLLRPFLLRRTKEDV-------LKDLPEKTEETLYVELTPEQ 477
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  772 AQAYEimmeAAKKFVKKLLQDSNDMKNHGFIprrnrragkegevqnpfnfgprdlaagsnfekmscvLMLLLRLRQACVH 851
Cdd:COG0553  478 RALYE----AVLEYLRRELEGAEGIRRRGLI------------------------------------LAALTRLRQICSH 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  852 FNItktgvdmdafsliggdnaeeanvddlneLLEKTMNMTLGNGdneerdkprattrifdpdylscKIKNTLEIVENIME 931
Cdd:COG0553  518 PAL----------------------------LLEEGAELSGRSA----------------------KLEALLELLEELLA 547
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  932 KKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFnREKGGARVMLLSLAAGGVGLNLTGGNHLVMV 1011
Cdd:COG0553  548 EGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHY 626
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630 1012 DLHWNPALEQQAFDRIYRMGQKKDVFIHRLVTKGTIEQRVVMLQKDKVALASSVLD 1067
Cdd:COG0553  627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
471-739 2.44e-84

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: 273.01  E-value: 2.44e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRetqpqpGGILADDMGLGKTLSMISLIAHQKAARRARREDGNDDKDKEKRKVVkeqglipSNGTLI 550
Cdd:cd18008    1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSDPKKLYL-------SKTTLI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDSVLSTYMFHGtkKQRDIDARRLARYDVVITTFNLIANELiekirTKSKADDSSDGESdsn 630
Cdd:cd18008   68 VVPLSLLSQWKDEIEKHTKPGSLKVYVYHG--SKRIKSIEELSDYDIVITTYGTLASEF-----PKNKKGGGRDSKE--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  631 htgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSDD 710
Cdd:cd18008  138 ---------KEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDY 208
                        250       260       270
                 ....*....|....*....|....*....|...
gi 17540630  711 KYWKESIMPM----KPIMADRVNLLTKNLLLRR 739
Cdd:cd18008  209 PWFNSDISKPfsknDRKALERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
474-851 4.15e-68

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: 230.26  E-value: 4.15e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    474 HQKAGLTWMRWRETQPQPGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGLIPSNGTLIVAP 553
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLY-----------------------LKHVDKNWGGPTLIVVP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    554 ASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDI---DARRLARYDVVITTFNLIaneliekirtkskaddssdgesdsn 630
Cdd:pfam00176   58 LSLLHNWMNEFERWVSPPALRVVVLHGNKRPQERwknDPNFLADFDVVITTYETL------------------------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    631 htgirravGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSDD 710
Cdd:pfam00176  113 --------RKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSL 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    711 KYWKE--SIMPMKPIMADRVNLL---TKNLLLRRTKDQTCAvtnqklvQLPPKNVEVHELELDGDEAQAYeimmeaakkf 785
Cdd:pfam00176  185 STFRNwfDRPIERGGGKKGVSRLhklLKPFLLRRTKKDVEK-------SLPPKVEYILFCRLSKLQRKLY---------- 247
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630    786 vkkllqdsndmknHGFIPRRNRRAGKEGEvqnpfnfgprdlaagSNFEKMSCVLMLLLRLRQACVH 851
Cdd:pfam00176  248 -------------QTFLLKKDLNAIKTGE---------------GGREIKASLLNILMRLRKICNH 285
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-1066 2.68e-42

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 168.44  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   458 TELTDTPKGFKLELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKaarrarredgnddkdkEKRKVv 537
Cdd:PLN03142  157 TRLLVQPSCIKGKMRDYQLAGLNWL-IRLYENGINGILADEMGLGKTLQTISLLGYLH----------------EYRGI- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   538 keqglipSNGTLIVAPASLIHQWDAEIDRRLddSVLSTYMFHGTKKQRDIDARRL---ARYDVVITTFNLIAneliekir 614
Cdd:PLN03142  219 -------TGPHMVVAPKSTLGNWMNEIRRFC--PVLRAVKFHGNPEERAHQREELlvaGKFDVCVTSFEMAI-------- 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   615 tkskaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:PLN03142  282 -------------------------KEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   695 LYSLVRFLRIRPFSDDKYWKESI-MPMKPIMADRVNLLTKNL---LLRRTKDQTcavtnQKlvQLPPKNVEVHELEldgd 770
Cdd:PLN03142  337 LWALLNFLLPEIFSSAETFDEWFqISGENDQQEVVQQLHKVLrpfLLRRLKSDV-----EK--GLPPKKETILKVG---- 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   771 eaqayeiMMEAAKKFVKKLLQDSNDMKNHGFIPRRnrragkegevqnpfnfgprdlaagsnfekmscVLMLLLRLRQACV 850
Cdd:PLN03142  406 -------MSQMQKQYYKALLQKDLDVVNAGGERKR--------------------------------LLNIAMQLRKCCN 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   851 H---FNITKTGVdmdafSLIGGDNaeeanvddlneLLEKTMNMTLgngdneeRDKprattrifdpdylsckikntleIVE 927
Cdd:PLN03142  447 HpylFQGAEPGP-----PYTTGEH-----------LVENSGKMVL-------LDK----------------------LLP 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   928 NIMEKKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFNREKGGARVMLLSLAAGGVGLNLTGGNH 1007
Cdd:PLN03142  482 KLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADI 561
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17540630  1008 LVMVDLHWNPALEQQAFDRIYRMGQKKDVFIHRLVTKGTIEQRVVMLQKDKVALASSVL 1066
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXDc smart00487
DEAD-like helicases superfamily;
463-712 1.05e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 88.32  E-value: 1.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     463 TPKGFKLELMPHQKAGLTWMRWRETqpqpGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvvkeqgl 542
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR----DVILAAPTGSGKTLAALLPALEALKRGKGGR-------------------- 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     543 ipsngTLIVAP-ASLIHQWDAEIDRRLDDSVL-STYMFHGTKKQRDIDARRLARYDVVITTFNLIANELIEKIRTKSKad 620
Cdd:smart00487   57 -----VLVLVPtRELAEQWAEELKKLGPSLGLkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSN-- 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     621 dssdgesdsnhtgirravgkddsvlaqicWSRVILDEAHTIKN--RQSLASKAVCRL-SAFSRWCLSGTP---IHNNLWD 694
Cdd:smart00487  130 -----------------------------VDLVILDEAHRLLDggFGDQLEKLLKLLpKNVQLLLLSATPpeeIENLLEL 180
                           250
                    ....*....|....*...
gi 17540630     695 LYSLVRFLRIRPFSDDKY 712
Cdd:smart00487  181 FLNDPVFIDVGFTPLEPI 198
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1067 8.04e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 408.07  E-value: 8.04e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  458 TELTDTPKGFKLELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvv 537
Cdd:COG0553  229 EALESLPAGLKATLRPYQLEGAAWL-LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP--------------- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  538 keqglipsngTLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKqRDIDARRLARYDVVITTFNLIAneliekirtks 617
Cdd:COG0553  293 ----------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTRE-RAKGANPFEDADLVITSYGLLR----------- 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  618 kaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYS 697
Cdd:COG0553  349 ----------------------RDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWS 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  698 LVRFLRirP--FSDDKYWKE----SIMPMKPIMADRVNLLTKNLLLRRTKDQTcavtnqkLVQLPPKNVEVHELELDGDE 771
Cdd:COG0553  407 LLDFLN--PglLGSLKAFRErfarPIEKGDEEALERLRRLLRPFLLRRTKEDV-------LKDLPEKTEETLYVELTPEQ 477
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  772 AQAYEimmeAAKKFVKKLLQDSNDMKNHGFIprrnrragkegevqnpfnfgprdlaagsnfekmscvLMLLLRLRQACVH 851
Cdd:COG0553  478 RALYE----AVLEYLRRELEGAEGIRRRGLI------------------------------------LAALTRLRQICSH 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  852 FNItktgvdmdafsliggdnaeeanvddlneLLEKTMNMTLGNGdneerdkprattrifdpdylscKIKNTLEIVENIME 931
Cdd:COG0553  518 PAL----------------------------LLEEGAELSGRSA----------------------KLEALLELLEELLA 547
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  932 KKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFnREKGGARVMLLSLAAGGVGLNLTGGNHLVMV 1011
Cdd:COG0553  548 EGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHY 626
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630 1012 DLHWNPALEQQAFDRIYRMGQKKDVFIHRLVTKGTIEQRVVMLQKDKVALASSVLD 1067
Cdd:COG0553  627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
471-739 2.44e-84

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: 273.01  E-value: 2.44e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRetqpqpGGILADDMGLGKTLSMISLIAHQKAARRARREDGNDDKDKEKRKVVkeqglipSNGTLI 550
Cdd:cd18008    1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSDPKKLYL-------SKTTLI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDSVLSTYMFHGtkKQRDIDARRLARYDVVITTFNLIANELiekirTKSKADDSSDGESdsn 630
Cdd:cd18008   68 VVPLSLLSQWKDEIEKHTKPGSLKVYVYHG--SKRIKSIEELSDYDIVITTYGTLASEF-----PKNKKGGGRDSKE--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  631 htgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSDD 710
Cdd:cd18008  138 ---------KEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDY 208
                        250       260       270
                 ....*....|....*....|....*....|...
gi 17540630  711 KYWKESIMPM----KPIMADRVNLLTKNLLLRR 739
Cdd:cd18008  209 PWFNSDISKPfsknDRKALERLQALLKPILLRR 241
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
471-739 2.24e-81

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: 265.11  E-value: 2.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRARR-EDGNDDKDKEKRKvvkEQGLIPSNGTL 549
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEeEKEKALTEWESKK---DSTLVPSAGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTkkQRDIDARRLARYDVVITTFNLIANEliekIRTKSKADDSsdgesds 629
Cdd:cd18072   78 VVCPASLVHQWKNEVESRVASNKLRVCLYHGP--NRERIGEVLRDYDIVITTYSLVAKE----IPTYKEESRS------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  630 nhtgirravgkddSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSD 709
Cdd:cd18072  145 -------------SPLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDD 211
                        250       260       270
                 ....*....|....*....|....*....|
gi 17540630  710 DKYWKESIMPMKPIMADRVNLLTKNLLLRR 739
Cdd:cd18072  212 LKVWKKQVDNKSRKGGERLNILTKSLLLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
474-851 4.15e-68

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: 230.26  E-value: 4.15e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    474 HQKAGLTWMRWRETQPQPGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGLIPSNGTLIVAP 553
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLY-----------------------LKHVDKNWGGPTLIVVP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    554 ASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDI---DARRLARYDVVITTFNLIaneliekirtkskaddssdgesdsn 630
Cdd:pfam00176   58 LSLLHNWMNEFERWVSPPALRVVVLHGNKRPQERwknDPNFLADFDVVITTYETL------------------------- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    631 htgirravGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSDD 710
Cdd:pfam00176  113 --------RKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSL 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    711 KYWKE--SIMPMKPIMADRVNLL---TKNLLLRRTKDQTCAvtnqklvQLPPKNVEVHELELDGDEAQAYeimmeaakkf 785
Cdd:pfam00176  185 STFRNwfDRPIERGGGKKGVSRLhklLKPFLLRRTKKDVEK-------SLPPKVEYILFCRLSKLQRKLY---------- 247
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630    786 vkkllqdsndmknHGFIPRRNRRAGKEGEvqnpfnfgprdlaagSNFEKMSCVLMLLLRLRQACVH 851
Cdd:pfam00176  248 -------------QTFLLKKDLNAIKTGE---------------GGREIKASLLNILMRLRKICNH 285
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
471-739 7.00e-56

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: 193.84  E-value: 7.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQPQP----------------------------GGILADDMGLGKTLSMISLIAHQKaarrarr 522
Cdd:cd18071    1 LLPHQKQALAWMVSRENSQDLppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLILANF------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  523 edgnddkdkekrkvvkeqglipsngTLIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRdiDARRLARYDVVITTF 602
Cdd:cd18071   74 -------------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNR--DPKLLSKYDIVLTTY 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  603 NLIANELiekirtkskaddssdgesdsnhtgirraVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWC 682
Cdd:cd18071  127 NTLASDF----------------------------GAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWV 178
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17540630  683 LSGTPIHNNLWDLYSLVRFLRIRPFSDDKYWKESImpMKPI-MADRVNL-----LTKNLLLRR 739
Cdd:cd18071  179 LTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLI--QRPLtMGDPTGLkrlqvLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
471-715 7.60e-55

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 191.40  E-value: 7.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWretqpqPGGILADDMGLGKTLSMISLI-AHQKAARRARREDGNDDKDKEKRKVVKEQGLIPSNGTL 549
Cdd:cd18070    1 LLPYQRRAVNWMLV------PGGILADEMGLGKTVEVLALIlLHPRPDNDLDAADDDSDEMVCCPDCLVAETPVSSKATL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSvLSTYMFHGTKKQ---RDIDARRLARYDVVITTFNLIANELIEKIRtkskaddssdge 626
Cdd:cd18070   75 IVCPSAILAQWLDEINRHVPSS-LKVLTYQGVKKDgalASPAPEILAEYDIVVTTYDVLRTELHYAEA------------ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  627 sdsNHTGIRRAVGK----DDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18070  142 ---NRSNRRRRRQKryeaPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFL 218
                        250
                 ....*....|...
gi 17540630  703 RIRPFSDDKYWKE 715
Cdd:cd18070  219 GVEPFCDSDWWAR 231
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
915-1042 4.83e-51

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 175.74  E-value: 4.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  915 LSCKIKNTLEIVENIMEKKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFNrEKGGARVMLLSLA 994
Cdd:cd18793    9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFN-EDPDIRVFLLSTK 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17540630  995 AGGVGLNLTGGNHLVMVDLHWNPALEQQAFDRIYRMGQKKDVFIHRLV 1042
Cdd:cd18793   88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
471-702 2.36e-47

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: 167.36  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWREtQPQPGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvvkeqgliPsngTLI 550
Cdd:cd17919    1 LRPYQLEGLNFLLELY-ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERG---------------------P---VLV 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRDIDA--RRLARYDVVITTFNLIaneliekirtkskaddssdgesd 628
Cdd:cd17919   56 VCPLSVLENWEREFEKWTPD--LRVVVYHGSQRERAQIRakEKLDKFDVVLTTYETL----------------------- 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17540630  629 snhtgirravGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd17919  111 ----------RRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
467-741 8.03e-47

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: 166.97  E-value: 8.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  467 FKLELMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHQKAARRARredgnddkdkekrkvvkeqgliPSn 546
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHY-GLGGILADDMGLGKTLQTLALLLSRKEEGRKG----------------------PS- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  547 gtLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRDIDaRRLARYDVVITTFNLIANElIEKIRTKSkaddssdge 626
Cdd:cd18012   57 --LVVAPTSLIYNWEEEAAKFAPE--LKVLVIHGTKRKREKL-RALEDYDLVITSYGLLRRD-IELLKEVK--------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  627 sdsnhtgirravgkddsvlaqicWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL---- 702
Cdd:cd18012  122 -----------------------FHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLnpgl 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 17540630  703 --RIRPFSddKYWKESIMPMKPIMA-DRVNLLTKNLLLRRTK 741
Cdd:cd18012  179 lgSYKRFK--KRFAKPIEKDGDEEAlEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-1066 2.68e-42

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 168.44  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   458 TELTDTPKGFKLELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKaarrarredgnddkdkEKRKVv 537
Cdd:PLN03142  157 TRLLVQPSCIKGKMRDYQLAGLNWL-IRLYENGINGILADEMGLGKTLQTISLLGYLH----------------EYRGI- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   538 keqglipSNGTLIVAPASLIHQWDAEIDRRLddSVLSTYMFHGTKKQRDIDARRL---ARYDVVITTFNLIAneliekir 614
Cdd:PLN03142  219 -------TGPHMVVAPKSTLGNWMNEIRRFC--PVLRAVKFHGNPEERAHQREELlvaGKFDVCVTSFEMAI-------- 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   615 tkskaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:PLN03142  282 -------------------------KEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   695 LYSLVRFLRIRPFSDDKYWKESI-MPMKPIMADRVNLLTKNL---LLRRTKDQTcavtnQKlvQLPPKNVEVHELEldgd 770
Cdd:PLN03142  337 LWALLNFLLPEIFSSAETFDEWFqISGENDQQEVVQQLHKVLrpfLLRRLKSDV-----EK--GLPPKKETILKVG---- 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   771 eaqayeiMMEAAKKFVKKLLQDSNDMKNHGFIPRRnrragkegevqnpfnfgprdlaagsnfekmscVLMLLLRLRQACV 850
Cdd:PLN03142  406 -------MSQMQKQYYKALLQKDLDVVNAGGERKR--------------------------------LLNIAMQLRKCCN 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   851 H---FNITKTGVdmdafSLIGGDNaeeanvddlneLLEKTMNMTLgngdneeRDKprattrifdpdylsckikntleIVE 927
Cdd:PLN03142  447 HpylFQGAEPGP-----PYTTGEH-----------LVENSGKMVL-------LDK----------------------LLP 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630   928 NIMEKKEKVVIVSQWTSVLNLIEIHIKSSGFKYTSITGQVLVKDRQERVDSFNREKGGARVMLLSLAAGGVGLNLTGGNH 1007
Cdd:PLN03142  482 KLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADI 561
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17540630  1008 LVMVDLHWNPALEQQAFDRIYRMGQKKDVFIHRLVTKGTIEQRVVMLQKDKVALASSVL 1066
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
471-727 1.57e-36

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: 137.87  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAhqkaarrarredgnddKDKEKRKVVKEQGLIPSngtLI 550
Cdd:cd17999    1 LRPYQQEGINWLAFLNKY-NLHGILCDDMGLGKTLQTLCILA----------------SDHHKRANSFNSENLPS---LV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIDARRLARYDVVITTFNLIANeliekirtkskaddssdgesdsn 630
Cdd:cd17999   61 VCPPTLVGHWVAEIKKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRN----------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  631 htgirravgkDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSDD 710
Cdd:cd17999  118 ----------DIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTE 187
                        250
                 ....*....|....*..
gi 17540630  711 KYWKESImpMKPIMADR 727
Cdd:cd17999  188 KQFQRRF--LKPILASR 202
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
471-698 4.54e-35

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: 134.04  E-value: 4.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQPQpGGILADDMGLGKTLSMISLIAhqkaarRARREDGNDDKDKEKRKVVKEQGLIPSNG--T 548
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGR-GGILGDDMGLGKTVQVIAFLA------AVLGKTGTRRDRENNRPRFKKKPPASSAKkpV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRlddSVLSTYMFHGTKKQRDIDAR-RLARYDVVITTFNLIANELiekirtkskaddssdges 627
Cdd:cd18005   74 LIVAPLSVLYNWKDELDTW---GHFEVGVYHGSRKDDELEGRlKAGRLEVVVTTYDTLRRCI------------------ 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17540630  628 dsnhtgirravgkddSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSL 698
Cdd:cd18005  133 ---------------DSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCL 188
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
471-702 9.66e-28

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: 112.46  E-value: 9.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISL---IAHQKAARRArredgnddkdkekrkvvkeqglipsng 547
Cdd:cd18001    1 LYPHQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAFlsgMFDSGLIKSV--------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  548 tLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGT-KKQRDIDARRLAR-YDVVITTFNLIaneliekirtkskaddssdg 625
Cdd:cd18001   53 -LVVMPTSLIPHWVKEFAKWTPG--LRVKVFHGTsKKERERNLERIQRgGGVLLTTYGMV-------------------- 109
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17540630  626 esdSNHTGIRRAVGKDDSVlaqicWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18001  110 ---LSNTEQLSADDHDEFK-----WDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
471-701 3.75e-27

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: 109.72  E-value: 3.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvvkeqgliPSngtLI 550
Cdd:cd18000    1 LFKYQQTGVQWL-WELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLG---------------------PS---LI 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDR---RLDDSVL---STYMFHGTKKQRDIDARRLAR-----YDVVITTFnlianeliEKIRTKSKA 619
Cdd:cd18000   56 VCPATVLKQWVKEFHRwwpPFRVVVLhssGSGTGSEEKLGSIERKSQLIRkvvgdGGILITTY--------EGFRKHKDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  620 ddssdgesdsnhtgirravgkddsvLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLV 699
Cdd:cd18000  128 -------------------------LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLF 182

                 ..
gi 17540630  700 RF 701
Cdd:cd18000  183 DF 184
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
470-741 4.28e-27

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: 110.49  E-value: 4.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  470 ELMPHQKAGLTWMRwreTQPQPG--GILADDMGLGKTLSMISLIAHQKaarrarredgnddkdkEKRKVvkeqglipsNG 547
Cdd:cd17997    3 TMRDYQIRGLNWLI---SLFENGinGILADEMGLGKTLQTISLLGYLK----------------HYKNI---------NG 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  548 T-LIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQR-DIDARRL--ARYDVVITTFNLIANELiekirtkskaddss 623
Cdd:cd17997   55 PhLIIVPKSTLDNWMREFKRWCPS--LRVVVLIGDKEERaDIIRDVLlpGKFDVCITSYEMVIKEK-------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  624 dgesdsnhtgirravgkddSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLR 703
Cdd:cd17997  119 -------------------TVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLL 179
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 17540630  704 IRPFSD----DKYWK-ESIMPMKPIMADRVNLLTKNLLLRRTK 741
Cdd:cd17997  180 PDVFTSsedfDEWFNvNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
471-739 2.43e-26

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: 108.10  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHQkaarrarredgnddkdkekRKVVKEQGLIpsngt 548
Cdd:cd17995    1 LRDYQLEGVNWLlfNWYNRR---NCILADEMGLGKTIQSIAFLEHL-------------------YQVEGIRGPF----- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDDSVLstyMFHGTKKQRDID--------------ARRLARYDVVITTFNLIaneliekir 614
Cdd:cd17995   54 LVIAPLSTIPNWQREFETWTDMNVV---VYHGSGESRQIIqqyemyfkdaqgrkKKGVYKFDVLITTYEMV--------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  615 tkskaddssdgesdsnhtgirravGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:cd17995  122 ------------------------IADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEE 177
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 17540630  695 LYSLVRFLRIRPFSDDKYWKESIMPMKPimADRVNLLTKNL---LLRR 739
Cdd:cd17995  178 LWSLLNFLEPEKFPSSEEFLEEFGDLKT--AEQVEKLQALLkpyMLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
471-709 3.57e-24

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: 102.46  E-value: 3.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRwreTQPQPG--GILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGLI-Psng 547
Cdd:cd18009    4 MRPYQLEGMEWLR---MLWENGinGILADEMGLGKTIQTIALLAH-----------------------LRERGVWgP--- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  548 TLIVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRDIDAR-------RLARYDVVITTFNLIANeliekirtkskad 620
Cdd:cd18009   55 FLVIAPLSTLPNWVNEFARFTPS--VPVLLYHGTKEERERLRKkimkregTLQDFPVVVTSYEIAMR------------- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  621 dssdgesdsnhtgirravgkDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVR 700
Cdd:cd18009  120 --------------------DRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLN 179

                 ....*....
gi 17540630  701 FLRIRPFSD 709
Cdd:cd18009  180 FLLPDVFDD 188
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
471-707 2.16e-23

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: 98.61  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGlipSNGT-L 549
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQK-KLSGILADEMGLGKTIQVIAFLAY-----------------------LKEIG---IPGPhL 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYmfHGTKKQ----RDIDARRLARYDVVITTFNLIANELIEKirtkskaddssdg 625
Cdd:cd17998   54 VVVPSSTLDNWLREFKRWCPSLKVEPY--YGSQEErkhlRYDILKGLEDFDVIVTTYNLATSNPDDR------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  626 esdsnhtgirravgkddSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIR 705
Cdd:cd17998  119 -----------------SFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181

                 ..
gi 17540630  706 PF 707
Cdd:cd17998  182 PF 183
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
471-739 5.18e-23

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: 99.28  E-value: 5.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM----RWRETQPQPGGILADDMGLGKTLSMISLIAhqkaarrarredgnddkdkekrKVVK--EQGLIP 544
Cdd:cd18004    1 LRPHQREGVQFLydclTGRRGYGGGGAILADEMGLGKTLQAIALVW----------------------TLLKqgPYGKPT 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  545 SNGTLIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKK--QRDIDARRLA-RYDVVIT---TFNLIANELIEKIRTksk 618
Cdd:cd18004   59 AKKALIVCPSSLVGNWKAEFDKWLGLRRIKVVTADGNAKdvKASLDFFSSAsTYPVLIIsyeTLRRHAEKLSKKISI--- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  619 addssdgesdsnhtgirravgkdDSVlaqICwsrvilDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSL 698
Cdd:cd18004  136 -----------------------DLL---IC------DEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFAL 183
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17540630  699 VRFLRIRPFSDDKYWKEsiMPMKPIM------------------ADRVNLLTKNLLLRR 739
Cdd:cd18004  184 VDFVNPGILGSLASFRK--VFEEPILrsrdpdaseedkelgaerSQELSELTSRFILRR 240
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
471-739 1.20e-22

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: 97.51  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM-RWRETQPqpGGILADDMGLGKTLSMISLIAHQKAarrarredgnddKDKEKRKVvkeqglipsngtL 549
Cdd:cd18006    1 LRPYQLEGVNWLlQCRAEQH--GCILGDEMGLGKTCQTISLLWYLAG------------RLKLLGPF------------L 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYMfhGTKKQR-DI--DARRLARYDVVITTFNLianeliekirtkskaddssdge 626
Cdd:cd18006   55 VLCPLSVLDNWKEELNRFAPDLSVITYM--GDKEKRlDLqqDIKSTNRFHVLLTTYEI---------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  627 sdsnhtgirraVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRP 706
Cdd:cd18006  111 -----------CLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNV 179
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 17540630  707 FSDD------KYWKEsiMPMKPIMADRVNLLTKNLLLRR 739
Cdd:cd18006  180 FPKDklddfiKAYSE--TDDESETVEELHLLLQPFLLRR 216
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
471-706 5.17e-22

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: 96.21  E-value: 5.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMrWR------ETQPQPGG-ILADDMGLGKTLSMISLI-AHQKAARRARRedgnddkdkekrkvvkeqgl 542
Cdd:cd18007    1 LKPHQVEGVRFL-WSnlvgtdVGSDEGGGcILAHTMGLGKTLQVITFLhTYLAAAPRRSR-------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  543 ipsngTLIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIDARRLARYD------VVITTFNLIANeLIEKIRTK 616
Cdd:cd18007   60 -----PLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKRADARLRKINKwhkeggVLLIGYELFRN-LASNATTD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  617 SKADDSSDGESDSNHTGIrravgkddsvlaqicwsrVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLY 696
Cdd:cd18007  134 PRLKQEFIAALLDPGPDL------------------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYW 195
                        250
                 ....*....|
gi 17540630  697 SLVRFlrIRP 706
Cdd:cd18007  196 TMVDF--ARP 203
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
471-739 7.45e-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: 92.42  E-value: 7.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRwRETQPQPGGILADDMGLGKTLSMISLIAHQKAarrarrEDGNddkdkekrkvvkeQGliPSngtLI 550
Cdd:cd18003    1 LREYQHIGLDWLA-TLYEKNLNGILADEMGLGKTIQTIALLAHLAC------EKGN-------------WG--PH---LI 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDSVLSTYMfhGTKKQRdidarRLAR--------YDVVITTFNLianeliekirtkskadds 622
Cdd:cd18003   56 VVPTSVMLNWEMEFKRWCPGFKILTYY--GSAKER-----KLKRqgwmkpnsFHVCITSYQL------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  623 sdgesdsnhtgirraVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18003  111 ---------------VVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFL 175
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 17540630  703 RIRPFSDDKYWKESIM-PMKPIM----------ADRVNLLTKNLLLRR 739
Cdd:cd18003  176 MPHIFQSHQEFKEWFSnPLTAMSegsqeeneelVRRLHKVLRPFLLRR 223
DEXDc smart00487
DEAD-like helicases superfamily;
463-712 1.05e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 88.32  E-value: 1.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     463 TPKGFKLELMPHQKAGLTWMRWRETqpqpGGILADDMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvvkeqgl 542
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR----DVILAAPTGSGKTLAALLPALEALKRGKGGR-------------------- 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     543 ipsngTLIVAP-ASLIHQWDAEIDRRLDDSVL-STYMFHGTKKQRDIDARRLARYDVVITTFNLIANELIEKIRTKSKad 620
Cdd:smart00487   57 -----VLVLVPtRELAEQWAEELKKLGPSLGLkVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSN-- 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     621 dssdgesdsnhtgirravgkddsvlaqicWSRVILDEAHTIKN--RQSLASKAVCRL-SAFSRWCLSGTP---IHNNLWD 694
Cdd:smart00487  130 -----------------------------VDLVILDEAHRLLDggFGDQLEKLLKLLpKNVQLLLLSATPpeeIENLLEL 180
                           250
                    ....*....|....*...
gi 17540630     695 LYSLVRFLRIRPFSDDKY 712
Cdd:smart00487  181 FLNDPVFIDVGFTPLEPI 198
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
471-739 9.55e-19

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: 86.40  E-value: 9.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkVVKEQGLIpsNGTLI 550
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQ-GINGILADEMGLGKTVQSIAVLAH----------------------LAEEHNIW--GPFLV 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRDI-----DARRLARYD----VVITTFNLIAneliekirtkskadd 621
Cdd:cd18002   56 IAPASTLHNWQQEISRFVPQ--FKVLPYWGNPKDRKVlrkfwDRKNLYTRDapfhVVITSYQLVV--------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  622 ssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRF 701
Cdd:cd18002  119 ------------------QDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHF 180
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 17540630  702 LRIRPF-SDDKY--W--------KESIMPMKPIMADRVNLLTKNLLLRR 739
Cdd:cd18002  181 IMPTLFdSHDEFneWfskdieshAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
471-702 1.15e-18

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: 85.42  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTwmrwRETQPQPGG-ILADDMGLGKTLSMIsLIAHQKAARRarredgnddkdkEKRKVvkeqglipsngtL 549
Cdd:cd18011    1 PLPHQIDAVL----RALRKPPVRlLLADEVGLGKTIEAG-LIIKELLLRG------------DAKRV------------L 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIdARRLARYDVVITtfnlianeliekirtkskaddssdgesds 629
Cdd:cd18011   52 ILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLI-GNPFEEFPIVIV----------------------------- 101
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17540630  630 nHTGIRRAVGKDDSVLAQICWSRVILDEAHTIKNRQ----SLASKAVCRLSAFSRWC--LSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18011  102 -SLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLAKRARHVllLTATPHNGKEEDFRALLSLL 179
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
458-741 1.65e-18

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: 86.26  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  458 TELTDTPKGFKL-ELMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRarredgnddkdkekrkv 536
Cdd:cd18064    2 TRFEDSPSYVKWgKLRDYQVRGLNWL-ISLYENGINGILADEMGLGKTLQTISLLGYMKHYRN----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  537 vkeqglIPSNgTLIVAPASLIHQWDAEIDRRLddSVLSTYMFHGTKKQRDIDARRL---ARYDVVITTFNLIAnelieki 613
Cdd:cd18064   64 ------IPGP-HMVLVPKSTLHNWMAEFKRWV--PTLRAVCLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLI------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  614 rtkskaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLW 693
Cdd:cd18064  128 --------------------------KEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLH 181
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17540630  694 DLYSLVRFLRIRPFSD----DKYWKESIMPMKPIMADRVNLLTKNLLLRRTK 741
Cdd:cd18064  182 ELWALLNFLLPDVFNSaedfDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIK 233
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
471-702 2.66e-18

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: 85.11  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHQKaarrarredgnddkdkEKRKVvkeqglipsNGT-L 549
Cdd:cd17996    4 LKEYQLKGLQWMVSLYNN-NLNGILADEMGLGKTIQTISLITYLM----------------EKKKN---------NGPyL 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRD--IDARRLARYDVVITTFNLIAneliekirtkskaddssdges 627
Cdd:cd17996   58 VIVPLSTLSNWVSEFEKWAPS--VSKIVYKGTPDVRKklQSQIRAGKFNVLLTTYEYII--------------------- 114
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17540630  628 dsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQS-LASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd17996  115 ------------KDKPLLSKIKWKYMIIDEGHRMKNAQSkLTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFL 178
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
470-702 6.06e-18

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 83.94  E-value: 6.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  470 ELMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHqkaARRARREDGnddkdkekrkvvkeqgliPsng 547
Cdd:cd17993    1 ELRDYQLTGLNWLahSWCKGN---NGILADEMGLGKTVQTISFLSY---LFHSQQQYG------------------P--- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  548 TLIVAPASLIHQWDAEIDRRLDDSVLSTYMfhGTKKQRDI--------DARRLARYDVVITTFNLIAneliekirtkska 619
Cdd:cd17993   54 FLVVVPLSTMPAWQREFAKWAPDMNVIVYL--GDIKSRDTireyefyfSQTKKLKFNVLLTTYEIIL------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  620 ddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLV 699
Cdd:cd17993  119 --------------------KDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALL 178

                 ...
gi 17540630  700 RFL 702
Cdd:cd17993  179 HFL 181
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
918-1031 1.76e-17

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: 79.18  E-value: 1.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630    918 KIKNTLEIVENimEKKEKVVIVSQWTSVLNlIEIHIKSSGFKYTSITGQVLVKDRQERVDSFNRekgGARVMLLSLAAGG 997
Cdd:pfam00271    2 KLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 17540630    998 VGLNLTGGNHLVMVDLHWNPALEQQAFDRIYRMG 1031
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
471-703 3.84e-17

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: 81.48  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTW-MRWRetqpqpGGIL-ADDMGLGKTLSMISLIAHQKAarrarredgnddkdkekrkvvkEQGLipsngt 548
Cdd:cd18010    1 LLPFQREGVCFaLRRG------GRVLiADEMGLGKTVQAIAIAAYYRE----------------------EWPL------ 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDD-SVLSTYMFHGTKkqrdiDARRLARYDVVITTFNLianeliekirtkskaddssdges 627
Cdd:cd18010   47 LIVCPSSLRLTWADEIERWLPSlPPDDIQVIVKSK-----DGLRDGDAKVVIVSYDL----------------------- 98
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17540630  628 dsnhtgirraVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWC--LSGTPIHNNLWDLYSLVRFLR 703
Cdd:cd18010   99 ----------LRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVilLSGTPALSRPIELFTQLDALD 166
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
471-741 2.76e-15

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: 76.59  E-value: 2.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMrWRETQPQPGGILADDMGLGKTLSMISLIAHQKAARRarredgnddkdkekrkvvkeqglIPSNGTLI 550
Cdd:cd18065   16 LRDYQVRGLNWM-ISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRN-----------------------IPGPHMVL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 VaPASLIHQWDAEIDRRLDDsvLSTYMFHGTKKQRDI---DARRLARYDVVITTFNLIAneliekirtkskaddssdges 627
Cdd:cd18065   72 V-PKSTLHNWMNEFKRWVPS--LRAVCLIGDKDARAAfirDVMMPGEWDVCVTSYEMVI--------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  628 dsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPF 707
Cdd:cd18065  128 ------------KEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVF 195
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 17540630  708 SD----DKYWKESIMPMKPIMADRVNLLTKNLLLRRTK 741
Cdd:cd18065  196 NSaddfDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
HELICc smart00490
helicase superfamily c-terminal domain;
949-1031 5.32e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.09  E-value: 5.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630     949 IEIHIKSSGFKYTSITGQVLVKDRQERVDSFNRekgGARVMLLSLAAGGVGLNLTGGNHLVMVDLHWNPALEQQAFDRIY 1028
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                    ...
gi 17540630    1029 RMG 1031
Cdd:smart00490   80 RAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
471-703 2.31e-14

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: 74.15  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--------RWRETQPQPGGILADDMGLGKTLSMISLIahqkaarrarredgnddkdkekRKVVKEQGL 542
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslKKTKKSPGSGCILAHCMGLGKTLQVVTFL----------------------HTVLLCEKL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  543 IPSNGTLIVAPASLIHQW---------DAEIDRRLDDSVLSTYmfhgtkkqRDIDARRLARYD------VVITTFNL--- 604
Cdd:cd18068   59 ENFSRVLVVCPLNTVLNWlnefekwqeGLKDEEKIEVNELATY--------KRPQERSYKLQRwqeeggVMIIGYDMyri 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  605 IANELIEKIRTKSKADdssdgesdsnhtgIRRAV---GKDdsvlaqicwsRVILDEAHTIKNRQSLASKAVCRLSAFSRW 681
Cdd:cd18068  131 LAQERNVKSREKLKEI-------------FNKALvdpGPD----------FVVCDEGHILKNEASAVSKAMNSIRTKRRI 187
                        250       260
                 ....*....|....*....|..
gi 17540630  682 CLSGTPIHNNLWDLYSLVRFLR 703
Cdd:cd18068  188 VLTGTPLQNNLIEYHCMVNFVK 209
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
466-715 3.08e-14

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: 73.50  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  466 GFKLELMPHQKAGLTWM--RWRETQPQpggILADDMGLGKTLSMISLIA---HQkaarrarredgnddkdkekrkvvkEQ 540
Cdd:cd18054   16 GENLELRDYQLEGLNWLahSWCKNNSV---ILADEMGLGKTIQTISFLSylfHQ------------------------HQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  541 GLIPsngTLIVAPASLIHQWDAEIDRRLDDSVLSTYM--FHGTKKQRDID-----ARRLaRYDVVITTFNLIAnelieki 613
Cdd:cd18054   69 LYGP---FLLVVPLSTLTSWQREFEIWAPEINVVVYIgdLMSRNTIREYEwihsqTKRL-KFNALITTYEILL------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  614 rtkskaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLW 693
Cdd:cd18054  138 --------------------------KDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLK 191
                        250       260
                 ....*....|....*....|..
gi 17540630  694 DLYSLVRFLRIRPFsddKYWKE 715
Cdd:cd18054  192 ELWSLLHFIMPEKF---EFWED 210
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
471-701 3.35e-14

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: 73.34  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTW-------MRWRETQpqpGGILADDMGLGKTLSMISLIAhqkaarRARREDGNDDKDKEKRkvvkeqgli 543
Cdd:cd18066    1 LRPHQREGIEFlyecvmgMRVNERF---GAILADEMGLGKTLQCISLIW------TLLRQGPYGGKPVIKR--------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  544 psngTLIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIDARRLarYDVVITTFNLIANEL--IEKIRtkskadd 621
Cdd:cd18066   63 ----ALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPL--YSVLIISYEMLLRSLdqISKLN------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  622 ssdgesdsnhtgirravgkddsvlaqicWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRF 701
Cdd:cd18066  130 ----------------------------FDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF 181
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
471-739 4.21e-13

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: 69.70  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHQKAArrarredgnddkdkekrkvvkeqGLipSNGT 548
Cdd:cd18060    1 LREYQLEGVNWLlfNWYNRQ---NCILADEMGLGKTIQSIAFLQEVYNV-----------------------GI--HGPF 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDdsvLSTYMFHGTKKQRDI----------DARRLA----RYDVVITTFNLIANELIEkir 614
Cdd:cd18060   53 LVIAPLSTITNWEREFNTWTE---MNTIVYHGSLASRQMiqqyemyckdSRGRLIpgayKFDALITTFEMILSDCPE--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  615 tkskaddssdgesdsnhtgirravgkddsvLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:cd18060  127 ------------------------------LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEE 176
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 17540630  695 LYSLVRFLRIRPFSDDKYWKESIMPMKP-IMADRVNLLTKNLLLRR 739
Cdd:cd18060  177 LFSLLHFLEPSQFPSESEFLKDFGDLKTeEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
471-709 6.60e-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: 69.32  E-value: 6.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQPQpGGILADDMGLGKTLSMISLIahqkaarRARREDGNddkdkekrkvvkeqglipSNGTLI 550
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGT-DTILADEMGLGKTVQTAVFL-------YSLYKEGH------------------SKGPFL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  551 V-APASLIHQWDAEIDRRLDDSVLSTYMfhgtkkqRDIDARRLARYDvvitTFNLIANelieKIRTKSKADDSSDGESDS 629
Cdd:cd18056   55 VsAPLSTIINWEREFEMWAPDMYVVTYV-------GDKDSRAIIREN----EFSFEDN----AIRGGKKASRMKKEASVK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  630 NHTGIR--RAVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPF 707
Cdd:cd18056  120 FHVLLTsyELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF 199

                 ..
gi 17540630  708 SD 709
Cdd:cd18056  200 HN 201
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
471-701 1.03e-12

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: 69.04  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMrWRETQPQP-----GGILADDMGLGKTLSMISLIAhqkaarrarredgnddkdkekrkVVKEQGLIPS 545
Cdd:cd18067    1 LRPHQREGVKFL-YRCVTGRRirgshGCIMADEMGLGKTLQCITLMW-----------------------TLLRQSPQCK 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  546 ---NGTLIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDI--------DARRLARYDVVIT--TFNLIANELiek 612
Cdd:cd18067   57 peiDKAIVVSPSSLVKNWANELGKWLGGRLQPLAIDGGSKKEIDRklvqwasqQGRRVSTPVLIISyeTFRLHVEVL--- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  613 irtkskaddssdgesdsnHTGirrAVGkddsvlaqicwsRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNL 692
Cdd:cd18067  134 ------------------QKG---EVG------------LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDL 180

                 ....*....
gi 17540630  693 WDLYSLVRF 701
Cdd:cd18067  181 SEYFSLVNF 189
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
471-739 1.35e-12

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 68.53  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAhqkaarrarredgnddkdkekrkvvkEQGLIPSNGT 548
Cdd:cd18058    1 LREYQLEGMNWLlfNWYNRK---NCILADEMGLGKTIQSITFLS--------------------------EIFLMGIRGP 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 -LIVAPASLIHQWDAEIDRRLDdsvLSTYMFHGTKKQRDI---------DARR-----LARYDVVITTFNLIANELIEki 613
Cdd:cd18058   52 fLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQISRQMiqqyemyyrDEQGnplsgIFKFQVVITTFEMILADCPE-- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  614 rtkskaddssdgesdsnhtgirravgkddsvLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLW 693
Cdd:cd18058  127 -------------------------------LKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 175
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17540630  694 DLYSLVRFLRIRPFSDDKYWKESIMPMKP-IMADRVNLLTKNLLLRR 739
Cdd:cd18058  176 ELFSLLNFLEPSQFPSETTFLEEFGDLKTeEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
471-709 1.53e-12

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: 68.55  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQPQpGGILADDMGLGKTLSMISLIahqkaarRARREDGNddkdkekrkvvkeqglipSNGT-L 549
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGT-DTILADEMGLGKTVQTIVFL-------YSLYKEGH------------------SKGPyL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYMfhGTKKQRDIdarrlarydVVITTFNLIANelieKIRTKSKADDSSDGESDS 629
Cdd:cd18057   55 VSAPLSTIINWEREFEMWAPDFYVVTYT--GDKESRSV---------IRENEFSFEDN----AIRSGKKVFRMKKEAQIK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  630 NHTGIR--RAVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPF 707
Cdd:cd18057  120 FHVLLTsyELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF 199

                 ..
gi 17540630  708 SD 709
Cdd:cd18057  200 NN 201
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
471-739 2.51e-12

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: 68.17  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHQKAARRArredgnddkdkekrkvvkeqglipsNGT-L 549
Cdd:cd18063   24 LKHYQLQGLEWMVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEHKRL-------------------------NGPyL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIDARRLARYDVVITTFNLIAneliekirtkskaddssdgesds 629
Cdd:cd18063   78 IIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYII----------------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  630 nhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAV-CRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFS 708
Cdd:cd18063  135 ----------KDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFK 204
                        250       260       270
                 ....*....|....*....|....*....|...
gi 17540630  709 DDKYWKESIMPMKPIMADRVNLLTKN--LLLRR 739
Cdd:cd18063  205 SCSTFEQWFNAPFAMTGERVDLNEEEtiLIIRR 237
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
471-709 8.17e-12

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: 65.54  E-value: 8.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIahqkaarrarredgnddkdkekRKVVKEQGlipSNGT-L 549
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQ-GTDTILADEMGLGKTIQTIVFL----------------------YSLYKEGH---SKGPfL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  550 IVAPASLIHQWDAEIDRRLDDSVLSTYmfHGTKkqrdidarrlarydVVITTFNLIAneliekirtkskaddssdgesds 629
Cdd:cd17994   55 VSAPLSTIINWEREFEMWAPDFYVVTY--VGDH--------------VLLTSYELIS----------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  630 nhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSD 709
Cdd:cd17994   96 ----------IDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNN 165
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
470-702 1.53e-11

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: 65.84  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  470 ELMPHQKAGLTWMRWRETQpQPGGILADDMGLGKTLSMISLIAHQKAARRArredgnddkdkekrkvvkeqglipsNGT- 548
Cdd:cd18062   23 VLKQYQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEHKRI-------------------------NGPf 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDDSVLSTYMFHGTKKQRDIDARRLARYDVVITTFNLIAneliekirtkskaddssdgesd 628
Cdd:cd18062   77 LIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYII---------------------- 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17540630  629 snhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAV-CRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18062  135 -----------KDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFL 198
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
469-715 7.93e-11

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: 63.53  E-value: 7.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  469 LELMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkVVKEQGLIpsN 546
Cdd:cd18053   19 LELRDYQLNGLNWLahSWCKGN---SCILADEMGLGKTIQTISFLNY----------------------LFHEHQLY--G 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  547 GTLIVAPASLIHQWDAEIdrRLDDSVLSTYMFHGTKKQRDI---------DARRLaRYDVVITTFNLIAneliekirtks 617
Cdd:cd18053   72 PFLLVVPLSTLTSWQREI--QTWAPQMNAVVYLGDINSRNMirthewmhpQTKRL-KFNILLTTYEILL----------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  618 kaddssdgesdsnhtgirravgKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYS 697
Cdd:cd18053  138 ----------------------KDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWS 195
                        250
                 ....*....|....*...
gi 17540630  698 LVRFLRIRPFSDDKYWKE 715
Cdd:cd18053  196 LLHFIMPEKFSSWEDFEE 213
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
474-709 8.99e-10

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: 60.41  E-value: 8.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  474 HQKAGLTWMRWRETQPQpGGILADDMGLGKTLSMISLIahqkaarRARREDGNddkdkekrkvvkEQGLIpsngtLIVAP 553
Cdd:cd18055    4 YQLEGLNWLRFSWAQGT-DTILADEMGLGKTIQTIVFL-------YSLYKEGH------------TKGPF-----LVSAP 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  554 ASLIHQWDAEIDRRLDDSVLSTYMfhgtkkqRDIDARRLARYDvvitTFNLIANelieKIRTKSKADDSSDGESDSNHTG 633
Cdd:cd18055   59 LSTIINWEREFQMWAPDFYVVTYT-------GDKDSRAIIREN----EFSFDDN----AVKGGKKAFKMKREAQVKFHVL 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17540630  634 IR--RAVGKDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFLRIRPFSD 709
Cdd:cd18055  124 LTsyELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNN 201
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
471-739 1.26e-09

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: 59.66  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGLipSNGT 548
Cdd:cd18059    1 LREYQLEGVNWLlfNWYNTR---NCILADEMGLGKTIQSITFLYE-----------------------IYLKGI--HGPF 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDdsvLSTYMFHGTKKQR-----------DIDARRLA---RYDVVITTFNLIANELIEkir 614
Cdd:cd18059   53 LVIAPLSTIPNWEREFRTWTE---LNVVVYHGSQASRrtiqlyemyfkDPQGRVIKgsyKFHAIITTFEMILTDCPE--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  615 tkskaddssdgesdsnhtgirravgkddsvLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:cd18059  127 ------------------------------LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEE 176
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 17540630  695 LYSLVRFLRIRPFSDDKYWKESIMPMKP-IMADRVNLLTKNLLLRR 739
Cdd:cd18059  177 LFSLLHFLEPSRFPSETTFMQEFGDLKTeEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
471-739 2.90e-08

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: 55.40  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--RWRETQpqpGGILADDMGLGKTLSMISLIAHqkaarrarredgnddkdkekrkvVKEQGLipSNGT 548
Cdd:cd18061    1 LREYQLEGLNWLlfNWYNRR---NCILADEMGLGKTIQSITFLYE-----------------------ILLTGI--RGPF 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  549 LIVAPASLIHQWDAEIDRRLDDSVLstyMFHGT--KKQ---------RDIDARRLA---RYDVVITTFNLIANELIEkir 614
Cdd:cd18061   53 LIIAPLSTIANWEREFRTWTDLNVV---VYHGSliSRQmiqqyemyfRDSQGRIIRgayRFQAIITTFEMILGGCPE--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  615 tkskaddssdgesdsnhtgirravgkddsvLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWD 694
Cdd:cd18061  127 ------------------------------LNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEE 176
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 17540630  695 LYSLVRFLRIRPFSDDKYWKESIMPMKP-IMADRVNLLTKNLLLRR 739
Cdd:cd18061  177 LFSLLHFLEPLRFPSESTFMQEFGDLKTeEQVQKLQAILKPMMLRR 222
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
473-702 6.19e-07

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: 51.58  E-value: 6.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  473 PHQKAGltwMRWRETQPQpGGILADdMGLGKTLSMISLIAHQKAARRARRedgnddkdkekrkvvkeqglipsngTLIVA 552
Cdd:cd18013    3 PYQKVA---INFIIEHPY-CGLFLD-MGLGKTVTTLTALSDLQLDDFTRR-------------------------VLVIA 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  553 PASLI-HQWDAEIDR--RLDDSVLSTYMfhGTKKQRdidaRRLARYDVVITTFNLianELIEKIrtkskaddssdgesds 629
Cdd:cd18013   53 PLRVArSTWPDEVEKwnHLRNLTVSVAV--GTERQR----SKAANTPADLYVINR---ENLKWL---------------- 107
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17540630  630 nhtgirravgkDDSVLAQICWSRVILDEAHTIKNRQSLASKAVCRLSAFSRWC--LSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18013  108 -----------VNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLigLTGTPSPNGLMDLWAQIALL 171
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
471-703 2.25e-06

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: 49.81  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  471 LMPHQKAGLTWM--------RWRETQPQPGGILADDMGLGKTLSMISLIahqKAARRArredgnddkdkekrkvvkeqgl 542
Cdd:cd18069    1 LKPHQIGGIRFLydniieslERYKGSSGFGCILAHSMGLGKTLQVISFL---DVLLRH---------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  543 IPSNGTLIVAPASLIHQWDAEIDRRLddsvlSTYMFHGTKKQRDIDARRLAryDVViTTFNLIANeLIEKIRTKSKADDS 622
Cdd:cd18069   56 TGAKTVLAIVPVNTLQNWLSEFNKWL-----PPPEALPNVRPRPFKVFILN--DEH-KTTAARAK-VIEDWVKDGGVLLM 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  623 sdgesdsNHTGIRRAVGKDdsvlaqicwsRVILDEAHTIKNRQSLASKAVCRLSAFSRWCLSGTPIHNNLWDLYSLVRFL 702
Cdd:cd18069  127 -------GYEMFRLRPGPD----------VVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFV 189

                 .
gi 17540630  703 R 703
Cdd:cd18069  190 R 190
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
491-659 5.31e-04

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 41.62  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  491 PGGILADDMGLGKTLsMISLIAHQKAARRARRedgnddkdkekrkvvkeqglipsngTLIVAP-ASLIHQWDAEIDRRLD 569
Cdd:cd00046    2 ENVLITAPTGSGKTL-AALLAALLLLLKKGKK-------------------------VLVLVPtKALALQTAERLRELFG 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540630  570 DSvLSTYMFHGTKKQRDIDARRLARYDVVITTfnlianelIEKIRTKSKADdssdgesdsnhtgiRRAVGKDdsvlaqic 649
Cdd:cd00046   56 PG-IRVAVLVGGSSAEEREKNKLGDADIIIAT--------PDMLLNLLLRE--------------DRLFLKD-------- 104
                        170
                 ....*....|
gi 17540630  650 WSRVILDEAH 659
Cdd:cd00046  105 LKLIIVDEAH 114
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
979-1039 1.03e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 43.29  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17540630   979 FNREKGGARVMLLSlAAGGVGLNLTGGNHLVMVDLHWNPALEQQAFDRIYRMGQKKDVFIH 1039
Cdd:PRK04914  540 FADEEDGAQVLLCS-EIGSEGRNFQFASHLVLFDLPFNPDLLEQRIGRLDRIGQKHDIQIH 599
 
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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