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Conserved domains on  [gi|595582135|ref|NP_001277637|]
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probable global transcription activator SNF2L1 isoform 2 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000678)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
2-1061 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1222.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    2 EPDTATEAATVAVSDARATVVVVEDEQPGpstfkEEGAAAAATEGTTATEKGEKKekitspfQLKLAAKASKSEKEMDPE 81
Cdd:PLN03142   14 DEEELEAVARSAGSDSDDDEVPAEDEDED-----EEDDEEAESPAKAEISKREKA-------RLKELKKQKKQEIQKILE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   82 YEEKMVNMPLKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEEL 161
Cdd:PLN03142   82 QQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  162 LSESRKTSNVCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMV 241
Cdd:PLN03142  146 EEEDGLGGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  242 LVPKSTLHNWMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 320
Cdd:PLN03142  225 VAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  321 KNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLL 400
Cdd:PLN03142  304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  401 RRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYT 480
Cdd:PLN03142  384 RRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  481 TDEHIVGNSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKF 560
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  561 IFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQ 640
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  641 QGRLIDQQsnKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYK 720
Cdd:PLN03142  622 QGRLAEQK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYD 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  721 FEGEDYREKQKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEK 794
Cdd:PLN03142  699 FDDEDDKDENKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEK 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  795 EILYYRKTigykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDN 874
Cdd:PLN03142  779 EVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKS 849
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  875 IAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNY 954
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLY 929
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  955 TEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRA 1034
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKK 1006
                        1050      1060
                  ....*....|....*....|....*..
gi 595582135 1035 TKTPMSQKRKAESATESSGRKDVKKVK 1061
Cdd:PLN03142 1007 LAKNATPSKRPSGRQANESPSSLKKRK 1033
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
2-1061 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1222.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    2 EPDTATEAATVAVSDARATVVVVEDEQPGpstfkEEGAAAAATEGTTATEKGEKKekitspfQLKLAAKASKSEKEMDPE 81
Cdd:PLN03142   14 DEEELEAVARSAGSDSDDDEVPAEDEDED-----EEDDEEAESPAKAEISKREKA-------RLKELKKQKKQEIQKILE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   82 YEEKMVNMPLKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEEL 161
Cdd:PLN03142   82 QQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  162 LSESRKTSNVCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMV 241
Cdd:PLN03142  146 EEEDGLGGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  242 LVPKSTLHNWMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 320
Cdd:PLN03142  225 VAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  321 KNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLL 400
Cdd:PLN03142  304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  401 RRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYT 480
Cdd:PLN03142  384 RRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  481 TDEHIVGNSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKF 560
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  561 IFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQ 640
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  641 QGRLIDQQsnKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYK 720
Cdd:PLN03142  622 QGRLAEQK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYD 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  721 FEGEDYREKQKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEK 794
Cdd:PLN03142  699 FDDEDDKDENKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEK 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  795 EILYYRKTigykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDN 874
Cdd:PLN03142  779 EVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKS 849
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  875 IAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNY 954
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLY 929
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  955 TEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRA 1034
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKK 1006
                        1050      1060
                  ....*....|....*....|....*..
gi 595582135 1035 TKTPMSQKRKAESATESSGRKDVKKVK 1061
Cdd:PLN03142 1007 LAKNATPSKRPSGRQANESPSSLKKRK 1033
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
172-404 9.50e-165

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: 484.14  E-value: 9.50e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  172 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 251
Cdd:cd18065     1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  252 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 331
Cdd:cd18065    81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582135  332 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 404
Cdd:cd18065   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
184-638 6.37e-153

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 470.48  E-value: 6.37e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  184 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 263
Cdd:COG0553   239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDvRAAFIRDEmmpGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 343
Cdd:COG0553   318 VLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  344 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 423
Cdd:COG0553   394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  424 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVGNSGKMVALDKLLARI 502
Cdd:COG0553   474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  503 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApNSSKFIFMLSTRAGGLGINLASADVVI 582
Cdd:COG0553   546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  583 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 638
Cdd:COG0553   625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
190-470 5.86e-142

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: 427.10  E-value: 5.86e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   190 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 265
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   266 CFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 345
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   346 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 424
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 595582135   425 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 470
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
183-359 2.74e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 2.74e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    183 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 260
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    261 SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 335
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 595582135    336 STNRLLLTGTPLQNNLHELWALLN 359
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DpdE NF041062
protein DpdE;
210-412 1.83e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.83  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  210 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdvraafirdem 282
Cdd:NF041062  175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  283 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 351
Cdd:NF041062  228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  352 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 412
Cdd:NF041062  303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
2-1061 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1222.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    2 EPDTATEAATVAVSDARATVVVVEDEQPGpstfkEEGAAAAATEGTTATEKGEKKekitspfQLKLAAKASKSEKEMDPE 81
Cdd:PLN03142   14 DEEELEAVARSAGSDSDDDEVPAEDEDED-----EEDDEEAESPAKAEISKREKA-------RLKELKKQKKQEIQKILE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   82 YEEKMVNMPLKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEEL 161
Cdd:PLN03142   82 QQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  162 LSESRKTSNVCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMV 241
Cdd:PLN03142  146 EEEDGLGGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMV 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  242 LVPKSTLHNWMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 320
Cdd:PLN03142  225 VAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  321 KNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLL 400
Cdd:PLN03142  304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  401 RRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYT 480
Cdd:PLN03142  384 RRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  481 TDEHIVGNSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKF 560
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  561 IFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQ 640
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  641 QGRLIDQQsnKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYK 720
Cdd:PLN03142  622 QGRLAEQK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYD 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  721 FEGEDYREKQKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEK 794
Cdd:PLN03142  699 FDDEDDKDENKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEK 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  795 EILYYRKTigykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDN 874
Cdd:PLN03142  779 EVRYLMQA---------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKS 849
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  875 IAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNY 954
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLY 929
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  955 TEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRA 1034
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERQARKEKK 1006
                        1050      1060
                  ....*....|....*....|....*..
gi 595582135 1035 TKTPMSQKRKAESATESSGRKDVKKVK 1061
Cdd:PLN03142 1007 LAKNATPSKRPSGRQANESPSSLKKRK 1033
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
172-404 9.50e-165

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: 484.14  E-value: 9.50e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  172 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 251
Cdd:cd18065     1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  252 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 331
Cdd:cd18065    81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582135  332 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 404
Cdd:cd18065   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
172-415 2.52e-157

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: 465.29  E-value: 2.52e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  172 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 251
Cdd:cd18064     1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  252 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 331
Cdd:cd18064    81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  332 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSL 411
Cdd:cd18064   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                  ....
gi 595582135  412 PPKK 415
Cdd:cd18064   241 PPKK 244
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
184-404 2.14e-156

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: 461.79  E-value: 2.14e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  184 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 263
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 343
Cdd:cd17997    81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595582135  344 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD-QKLVERLHAVLKPFLLRRIK 404
Cdd:cd17997   161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnQEVVQRLHKVLRPFLLRRIK 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
184-638 6.37e-153

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 470.48  E-value: 6.37e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  184 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 263
Cdd:COG0553   239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDvRAAFIRDEmmpGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 343
Cdd:COG0553   318 VLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  344 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 423
Cdd:COG0553   394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  424 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVGNSGKMVALDKLLARI 502
Cdd:COG0553   474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  503 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApNSSKFIFMLSTRAGGLGINLASADVVI 582
Cdd:COG0553   546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  583 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 638
Cdd:COG0553   625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
190-470 5.86e-142

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: 427.10  E-value: 5.86e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   190 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 265
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   266 CFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 345
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   346 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 424
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 595582135   425 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 470
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
184-404 2.37e-100

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: 315.46  E-value: 2.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  184 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 263
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDVRAAfIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV-REFKSTNRLLL 342
Cdd:cd17996    81 KIVYKGTPDVRKK-LQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 595582135  343 TGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT---------KNCLGDQK---LVERLHAVLKPFLLRRIK 404
Cdd:cd17996   160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvKIELNEEEtllIIRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
184-404 8.91e-96

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: 303.54  E-value: 8.91e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  184 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 263
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDVRAAFIRDEMMP----GEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNR 339
Cdd:cd18009    80 VLLYHGTKEERERLRKKIMKRegtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  340 LLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD---------TKNCLGD---QKLVERLHAVLKPFLLRRIK 404
Cdd:cd18009   160 LLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaaDISNLSEereQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
187-402 4.20e-90

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: 287.71  E-value: 4.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 346
Cdd:cd18003    81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582135  347 LQNNLHELWALLNFLLPDVFNSADDFDSWFD-------TKNCLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18003   161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
187-366 1.88e-88

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: 281.76  E-value: 1.88e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEmMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 346
Cdd:cd17919    81 YHGSQRERAQIRAKE-KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                         170       180
                  ....*....|....*....|
gi 595582135  347 LQNNLHELWALLNFLLPDVF 366
Cdd:cd17919   160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
187-402 2.15e-82

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: 266.53  E-value: 2.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAfIRD-EMMPG-----EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 340
Cdd:cd17993    82 YLGDIKSRDT-IREyEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595582135  341 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNclgdQKLVERLHAVLKPFLLRR 402
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQ----EKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
187-402 2.36e-77

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: 252.94  E-value: 2.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPsLRVIC 266
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAaFIRD-EMM-----------PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF 334
Cdd:cd17995    80 YHGSGESRQ-IIQQyEMYfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  335 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-DTKNclGDQklVERLHAVLKPFLLRR 402
Cdd:cd17995   159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFgDLKT--AEQ--VEKLQALLKPYMLRR 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
187-402 1.13e-73

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: 242.73  E-value: 1.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 346
Cdd:cd18006    81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  347 LQNNLHELWALLNFLLPDVF--NSADDFDSWF-DTKNclgDQKLVERLHAVLKPFLLRR 402
Cdd:cd18006   161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDD---ESETVEELHLLLQPFLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
187-402 4.92e-73

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: 241.64  E-value: 4.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVG---DKDVRAAFIRDEMMPGE---WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 340
Cdd:cd18002    81 YWGnpkDRKVLRKFWDRKNLYTRdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  341 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--DTKNCLG-----DQKLVERLHAVLKPFLLRR 402
Cdd:cd18002   161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAEnktglNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
171-404 9.57e-71

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: 236.09  E-value: 9.57e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  171 VCVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 250
Cdd:cd18062     8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  251 WMNEFKRWVPSLRVICFVGDKDVRAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 330
Cdd:cd18062    88 WVYEFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  331 VR-EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFL 399
Cdd:cd18062   167 LNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFL 246

                  ....*
gi 595582135  400 LRRIK 404
Cdd:cd18062   247 LRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
174-404 6.96e-69

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: 230.72  E-value: 6.96e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  174 RFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 253
Cdd:cd18063    11 RVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  254 EFKRWVPSLRVICFVGDKDVRAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVR- 332
Cdd:cd18063    91 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  333 EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 402
Cdd:cd18063   170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 249

                  ..
gi 595582135  403 IK 404
Cdd:cd18063   250 LK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
185-404 7.23e-69

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: 229.37  E-value: 7.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  185 GPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRV 264
Cdd:cd18012     3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  265 ICFVGDKDVRAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTG 344
Cdd:cd18012    82 LVIHGTKRKREKLRALE----DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 595582135  345 TPLQNNLHELWALLNFLLPDVFNSADDF-DSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 404
Cdd:cd18012   158 TPIENHLGELWSIFDFLNPGLLGSYKRFkKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
173-402 1.28e-66

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: 224.11  E-value: 1.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  173 VRFEVSPSYVKGG--PLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 250
Cdd:cd18054     5 VALKKQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  251 WMNEFKRWVPSLRVICFVGDKDVRAAfIRDEmmpgEW----------DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 320
Cdd:cd18054    85 WQREFEIWAPEINVVVYIGDLMSRNT-IREY----EWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  321 KNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLL 400
Cdd:cd18054   160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLL 235

                  ..
gi 595582135  401 RR 402
Cdd:cd18054   236 RR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
187-366 7.23e-63

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: 211.47  E-value: 7.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRaAFIRDEMMPG--EWDVCVTSYEMVI---KEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLL 341
Cdd:cd17998    80 YYGSQEER-KHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                         170       180
                  ....*....|....*....|....*
gi 595582135  342 LTGTPLQNNLHELWALLNFLLPDVF 366
Cdd:cd17998   159 LTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
483-615 1.98e-62

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: 208.10  E-value: 1.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  483 EHIVgnSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPnSSKFIF 562
Cdd:cd18793     6 EEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVF 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 595582135  563 MLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLI 615
Cdd:cd18793    83 LLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
187-402 4.49e-57

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: 195.35  E-value: 4.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKdvraafirdemmpgewdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 346
Cdd:cd17994    81 YVGDH-----------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 595582135  347 LQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd17994   144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
173-402 1.36e-55

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: 192.96  E-value: 1.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  173 VRFEVSPSYVKGGP---LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLH 249
Cdd:cd18053     4 VALKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  250 NWMNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGE-----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEK 324
Cdd:cd18053    84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 595582135  325 SKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18053   164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
187-402 9.18e-55

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: 190.25  E-value: 9.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRN------IPGPHMVLVPKSTLHNWMNEFKRWVP 260
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  261 --SLRVICFVGDKDVRAafiRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTN 338
Cdd:cd17999    80 naFLKPLAYVGPPQERR---RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 595582135  339 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQKL----VERLHAVLKPFLLRR 402
Cdd:cd17999   157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrDSKASAKEQEAgalaLEALHKQVLPFLLRR 232
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
905-1019 6.93e-54

SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three alpha-helices. It has a role in DNA binding, contacting DNA target sites similar to c-Myb (pfam00249) repeats or homeodomains.


Pssm-ID: 462681 [Multi-domain]  Cd Length: 116  Bit Score: 183.11  E-value: 6.93e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   905 EKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTS-KGKNYTEEEDRFLICMLHKMGFDRENVYEELRQC 983
Cdd:pfam09111    1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYPPNnKGKTYTEEEDRFLLCMLYKYGYGNEDLYEKIKQE 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 595582135   984 VRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKEN 1019
Cdd:pfam09111   81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
187-363 2.22e-52

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: 182.14  E-value: 2.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVI- 265
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  266 -----CFVGDKD-----VRAAFIRDEMMPgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 335
Cdd:cd18000    81 lhssgSGTGSEEklgsiERKSQLIRKVVG-DGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                         170       180
                  ....*....|....*....|....*...
gi 595582135  336 STNRLLLTGTPLQNNLHELWALLNFLLP 363
Cdd:cd18000   160 TPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
187-402 8.18e-50

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 176.36  E-value: 8.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRA-------------------AFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 327
Cdd:cd18055    81 YTGDKDSRAiirenefsfddnavkggkkAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  328 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
187-402 1.32e-49

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: 175.64  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKdvRAAFIRD-EMMPGEWDVCVTSYEMVIKEKSVF-----KKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 340
Cdd:cd18001    80 FHGTS--KKERERNlERIQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  341 LLTGTPLQNNLHELWALLNFLLP-DVFNSADDFDSWFDT-------KNCLGDQK-----LVERLHAVLKPFLLRR 402
Cdd:cd18001   158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENpitrgrdKDATQGEKalgseVAENLRQIIKPYFLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
187-402 2.18e-48

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: 172.47  E-value: 2.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISlyeNGvnGILADEMGLGKTLQTIAL-LGYLKHYRNIPGPHM----------------VLVPKSTLH 249
Cdd:cd18008     1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  250 NWMNEFKR--WVPSLRVICFVGDKdvRAAFIRDemmPGEWDVCVTSYEMV----------------IKEKSVFKKFHWRY 311
Cdd:cd18008    76 QWKDEIEKhtKPGSLKVYVYHGSK--RIKSIEE---LSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  312 LVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSaddfDSWFDTKNCL----GDQKL 387
Cdd:cd18008   151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGD----YPWFNSDISKpfskNDRKA 226
                         250
                  ....*....|....*
gi 595582135  388 VERLHAVLKPFLLRR 402
Cdd:cd18008   227 LERLQALLKPILLRR 241
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
187-402 1.03e-47

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


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 169.84  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 266
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEM---------MPGEW--DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 335
Cdd:cd18058    79 YHGSQISRQMIQQYEMyyrdeqgnpLSGIFkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  336 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
187-402 2.36e-47

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: 169.09  E-value: 2.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 327
Cdd:cd18057    81 YTGDKESRSVIRENEFsfednairsgkkvfrMKKEaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  328 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
187-402 4.78e-47

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


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 168.71  E-value: 4.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKH--------YRNIP------------GPHMVLVPKS 246
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPrfkkkppassakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  247 TLHNWMNEFKRWvPSLRVICFVGDKDVRAAFIRdeMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 326
Cdd:cd18005    81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGR--LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  327 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKN--CLGDQKLVErLHA 393
Cdd:cd18005   158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSepikrgqrhtaTARelRLGRKRKQE-LAV 236

                  ....*....
gi 595582135  394 VLKPFLLRR 402
Cdd:cd18005   237 KLSKFFLRR 245
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
187-402 6.48e-46

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: 164.85  E-value: 6.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 266
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 327
Cdd:cd18056    81 YVGDKDSRAIIRENEFsfednairggkkasrMKKEasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  328 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD---IAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
187-402 2.37e-45

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: 162.92  E-value: 2.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 266
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEM---------MPG--EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 335
Cdd:cd18060    79 YHGSLASRQMIQQYEMyckdsrgrlIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  336 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
187-402 5.66e-43

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: 156.35  E-value: 5.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 266
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEM---------MPGEWD--VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 335
Cdd:cd18059    79 YHGSQASRRTIQLYEMyfkdpqgrvIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  336 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
187-376 4.97e-42

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: 153.99  E-value: 4.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLIS-LYENGVNG------ILADEMGLGKTLQTIALL-GYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRW 258
Cdd:cd18007     1 LKPHQVEGVRFLWSnLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  259 -----VPSLRVICFVGDKDVRAAF--IRDEMMPGewDVCVTSYEM---VIKEKSVFKKFHWRY-----------LVIDEA 317
Cdd:cd18007    80 lppdlRPLLVLVSLSASKRADARLrkINKWHKEG--GVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  318 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 376
Cdd:cd18007   158 HRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
187-402 1.33e-41

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: 152.83  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLislYE--------NGVNGILADEMGLGKTLQTIALL-GYLKHYRNIPGPH---MVLVPKSTLHNWMNE 254
Cdd:cd18004     1 LRPHQREGVQFL---YDcltgrrgyGGGGAILADEMGLGKTLQAIALVwTLLKQGPYGKPTAkkaLIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  255 FKRWVPSLRVICFV--GDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVI-DEAHRIKNEKSKLSEIV 331
Cdd:cd18004    78 FDKWLGLRRIKVVTadGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  332 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT-------KNC------LGDQKLvERLHAVLKPF 398
Cdd:cd18004   158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdPDAseedkeLGAERS-QELSELTSRF 236

                  ....
gi 595582135  399 LLRR 402
Cdd:cd18004   237 ILRR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
187-402 1.49e-39

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 146.30  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 266
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDKDVRAAFIRDEMMPGE-----------WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 335
Cdd:cd18061    79 YHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 595582135  336 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
750-848 1.27e-38

HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of which (H2, H3, H4) form an L-like configuration. Helix H2 runs antiparallel to helices H3 and H4, packing closely against helix H4, whilst helix H1 reposes in the concave surface formed by these three helices and runs perpendicular to them. The domain confers DNA and nucleosome binding properties to the protein.


Pssm-ID: 430414  Cd Length: 110  Bit Score: 139.23  E-value: 1.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   750 AVDAYFREALRVSEPK---IPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRN------PEIPNPAIA- 819
Cdd:pfam09110    1 SVDNYYKDVLGTGGKKsttKPKAPRAPKQINIQDHQFFPPRLKELQEKEQLYYKKKIGYKVTLDdgkeedGEEFEEEREa 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 595582135   820 -QREEQKKIDGAEPLTPQETEEKDKLLTQG 848
Cdd:pfam09110   81 kRKLEQEEIDNAEPLTEEEEAEKEELLSEG 110
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
187-402 4.00e-34

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: 130.40  E-value: 4.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLIslyENGVNGILADEMGLGKTLQTIALLGYLKHYrnipGPHMVLVPKSTLHNWMNEFKRWVPSL---R 263
Cdd:cd18010     1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDVRaafirdemMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS-EIVREFKSTNR-LL 341
Cdd:cd18010    74 IQVIVKSKDGL--------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTkAALPLLKRAKRvIL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 595582135  342 LTGTPLQNNLHELWALLNFLLPDVFNSADDFDS-----------WFDTknclGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18010   146 LSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfgWDYS----GSSNLEELHLLLLATIMIRR 213
DEXDc smart00487
DEAD-like helicases superfamily;
183-359 2.74e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 2.74e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    183 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 260
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    261 SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 335
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 595582135    336 STNRLLLTGTPLQNNLHELWALLN 359
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
208-402 2.94e-31

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: 122.97  E-value: 2.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  208 GILADEMGLGKTLQTIALLGYLKHYRN---------------------IP-GPHMVLVPKSTLHNWMNEFKRWVPS--LR 263
Cdd:cd18072    23 GILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASnkLR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVG-DKDVRAAFIRDemmpgeWDVCVTSYEMVIKE---------KSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRE 333
Cdd:cd18072   103 VCLYHGpNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  334 FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDqklvERLHAVLKPFLLRR 402
Cdd:cd18072   177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
203-402 4.59e-31

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: 122.58  E-value: 4.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  203 ENGVNGILADEMGLGKTLQTIALLgylkhyrnIPGPHMVLVPKSTLHNWMNEFKRWVPS--LRVICFVGdkdvrAAFIRD 280
Cdd:cd18071    46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHG-----GERNRD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  281 EMMPGEWDVCVTSYEMVIKEKSV-----FKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELW 355
Cdd:cd18071   113 PKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 595582135  356 ALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRR 402
Cdd:cd18071   193 SLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
490-604 1.32e-30

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: 116.54  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   490 GKMVALDKLLAriKEQGSRVLIFSQMTRLLDIlEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNapnSSKFIFMLSTRAG 569
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 595582135   570 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIG 604
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
187-401 1.13e-29

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: 118.99  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLyengvNGILADEMGLGKTLQTIALLgyLKHYRN--------IPGPHMVLVP-----------KST 247
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPdndldaadDDSDEMVCCPdclvaetpvssKAT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  248 L--------HNWMNEFKRWVP-SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKE------------KSVFKK 306
Cdd:cd18070    74 LivcpsailAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTElhyaeanrsnrrRRRQKR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  307 F----------HWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFdsWF 376
Cdd:cd18070   154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWW--AR 231
                         250       260
                  ....*....|....*....|....*
gi 595582135  377 DTKNCLGDQKLVERLHAVLKPFLLR 401
Cdd:cd18070   232 VLIRPQGRNKAREPLAALLKELLWR 256
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
187-402 2.23e-27

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: 111.48  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYL---KHYRNIP--GPHMVLVPKSTLHNWMNEFK 256
Cdd:cd18066     1 LRPHQREGIEFLyecvMGMRVNERFGaILADEMGLGKTLQCISLIWTLlrqGPYGGKPviKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  257 RWVPSLRVICFVGDKDVRaafIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKS 336
Cdd:cd18066    81 KWLGSERIKVFTVDQDHK---VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  337 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-------------TKNCLGDQKLVErLHAVLKPFLLRR 402
Cdd:cd18066   158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepivrsreptatpEEKKLGEARAAE-LTRLTGLFILRR 235
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
187-377 2.13e-26

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: 108.75  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLislYEN------------GVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMN 253
Cdd:cd18069     1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  254 EFKRWVPSLRVICFVGDKDVRAAFIRDEM--------MPGEWD----VCVTSYEMvikeksvfkkFHWR----YLVIDEA 317
Cdd:cd18069    76 EFNKWLPPPEALPNVRPRPFKVFILNDEHkttaarakVIEDWVkdggVLLMGYEM----------FRLRpgpdVVICDEG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  318 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD 377
Cdd:cd18069   146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
187-402 8.18e-26

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: 107.56  E-value: 8.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH----MVLVPKSTLHNWMNEFKR 257
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  258 WVPSlRVICFVGD---------KDVRAAFIRDEMMPGEwdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS 328
Cdd:cd18067    81 WLGG-RLQPLAIDggskkeidrKLVQWASQQGRRVSTP--VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  329 EIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVErLHAVL 395
Cdd:cd18067   158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadasEKERQLGEEKLQE-LISIV 236

                  ....*..
gi 595582135  396 KPFLLRR 402
Cdd:cd18067   237 NRCIIRR 243
HELICc smart00490
helicase superfamily c-terminal domain;
520-604 1.87e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 100.75  E-value: 1.87e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135    520 DILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNapnSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDR 599
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 595582135    600 AHRIG 604
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
205-376 4.76e-25

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: 105.36  E-value: 4.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  205 GVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLV--PKSTLHNWMNEFKRWVP------SLRV--ICFVGDKDVR 274
Cdd:cd18068    28 GSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVvcPLNTVLNWLNEFEKWQEglkdeeKIEVneLATYKRPQER 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  275 AafirdeMMPGEWD----VCVTSYEMV--------IKEKSVFKKFHWRYL--------VIDEAHRIKNEKSKLSEIVREF 334
Cdd:cd18068   108 S------YKLQRWQeeggVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 595582135  335 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 376
Cdd:cd18068   182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
187-402 6.22e-24

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: 100.83  E-value: 6.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVngILADEMGLGKTLQTIALLGYLKhYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 266
Cdd:cd18011     1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  267 FVGDkDVRAAFIRDEMMPGEWDVCVTSYEMV---IKEKSVFKKFHWRYLVIDEAHRIKN----EKSKLSEIVREF--KST 337
Cdd:cd18011    77 LDRE-TAAQLRRLIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRAR 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  338 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtknclgdqklVERLHAVLKPFLLRR 402
Cdd:cd18011   156 HVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR-------------LDGLREVLAKVLLRR 207
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
185-760 3.61e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 83.15  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  185 GPLRDYQIRGLN-WLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIpgphMVLVPKSTL-HNWMNEFKRWvpsL 262
Cdd:COG1061    79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELlEQWAEELRRF---L 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  263 RVICFVGDKDvraafirdemmPGEWDVCVTSYEMVIKEKSVFK-KFHWRYLVIDEAHRIKNEksKLSEIVREFKSTNRLL 341
Cdd:COG1061   152 GDPLAGGGKK-----------DSDAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  342 LTGTPL-QNNLHELWALLNFLLPDVfnsaddfdSWfdtknclgdQKLVERlhAVLKPFLLRRIKTDVEkslppkKEIKIY 420
Cdd:COG1061   219 LTATPFrSDGREILLFLFDGIVYEY--------SL---------KEAIED--GYLAPPEYYGIRVDLT------DERAEY 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  421 LGLSkmqrEWYTKILMKDidvlnssgkmdkmrllnilmqlrkccnhpylfdgaepgppyttdehivgNSGKMVALDKLLA 500
Cdd:COG1061   274 DALS----ERLREALAAD-------------------------------------------------AERKDKILRELLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  501 RIKEQGsRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApnsSKFIFMLSTRAGGLGINLASADV 580
Cdd:COG1061   301 EHPDDR-KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDV 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  581 VILYDSDWNPQVDLQAMDRAHRIGQ-KKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQ 659
Cdd:COG1061   377 AILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALE 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  660 MIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRNFRMDLEQSLYKFEGEDYREKQKLGTVEWIE 739
Cdd:COG1061   457 VKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLL 536
                         570       580
                  ....*....|....*....|.
gi 595582135  740 PPKRERKANYAVDAYFREALR 760
Cdd:COG1061   537 ELLELLAALLRLEELAALLLK 557
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
187-361 1.42e-15

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: 77.00  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLIslyENGVNGILADeMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTL-HNWMNEFKRW--VPSLR 263
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  264 VICFVGDKDVRAAfirdeMMPGEWDVCVTSYEMVIK-EKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF-KSTNRLL 341
Cdd:cd18013    76 VSVAVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                         170       180
                  ....*....|....*....|.
gi 595582135  342 -LTGTPLQNNLHELWALLNFL 361
Cdd:cd18013   151 gLTGTPSPNGLMDLWAQIALL 171
ResIII pfam04851
Type III restriction enzyme, res subunit;
186-346 4.08e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 62.30  E-value: 4.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   186 PLRDYQIRGL-NWLISLYENGVNGILADEMGLGKTL---QTIALLGYLKHYRNIpgphMVLVP-KSTLHNWMNEFKRWVP 260
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLtaaKLIARLFKKGPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   261 SLRVIC--FVGDKDVRaafirdemMPGEWDVCVTSYEMV----IKEKSVFKKFHWRYLVIDEAHRIKNEKSKlsEIVREF 334
Cdd:pfam04851   79 NYVEIGeiISGDKKDE--------SVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYF 148
                          170
                   ....*....|..
gi 595582135   335 KSTNRLLLTGTP 346
Cdd:pfam04851  149 KPAFLLGLTATP 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
187-346 6.86e-11

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 61.17  E-value: 6.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGL-NWLISLYENGvnGILADEMGLGKTLQTIALLGYLKhyrniPGPHMVLVP-KSTLHNWMNEFKRWVPSlRV 264
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGD-SS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  265 ICFVGDKDVRAAFIRDemmpgewdVCVTSYEMVIK-EKSVFKKFH-WRYLVIDEAHRIKNEKskLSEIVREFKSTNRLLL 342
Cdd:cd17926    73 IGLIGGGKKKDFDDAN--------VVVATYQSLSNlAEEEKDLFDqFGLLIVDEAHHLPAKT--FSEILKELNAKYRLGL 142

                  ....
gi 595582135  343 TGTP 346
Cdd:cd17926   143 TATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
207-345 7.06e-10

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: 58.57  E-value: 7.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  207 NGILADEMGLGKTLQ-TIALLGYLKHYRnipGPHMVLVPKSTL-HNWMNEFKRWV-PSLRVICFVGDKDVRAAFIRDEmm 283
Cdd:cd00046     3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLRELFgPGIRVAVLVGGSSAEEREKNKL-- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  284 pGEWDVCVTSYEMVIKEKSVFKKFH---WRYLVIDEAHRI-KNEKS----KLSEIVREFKSTNRLLLTGT 345
Cdd:cd00046    78 -GDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGalilDLAVRKAGLKNAQVILLSAT 146
DpdE NF041062
protein DpdE;
210-412 1.83e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.83  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  210 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdvraafirdem 282
Cdd:NF041062  175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  283 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 351
Cdd:NF041062  228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 595582135  352 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 412
Cdd:NF041062  303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
491-725 6.42e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.66  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  491 KMVALDKLLARI--KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHE--------EREEAIDAFNApnsSKF 560
Cdd:COG1111   336 KLSKLREILKEQlgTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEgdkgltqkEQIEILERFRA---GEF 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  561 IFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQamdRAHRIGQKKPVRVFRLITDNTVEE--RIVERAEIKLRLDSIV 638
Cdd:COG1111   413 NVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEayYWSSRRKEKKMKSILK 489
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  639 IQQGRLIDQQSNKLAKEEmlqmirHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnfRMDLEQSL 718
Cdd:COG1111   490 KLKKLLDKQEKEKLKESA------QATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVI--VSTLAESL 561

                  ....*..
gi 595582135  719 YKFEGED 725
Cdd:COG1111   562 ELRELGE 568
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
851-890 3.67e-07

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 47.57  E-value: 3.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 595582135  851 NWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 890
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRER 40
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
849-890 1.28e-06

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 46.06  E-value: 1.28e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 595582135    849 FTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 890
Cdd:smart00717    1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRER 42
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
215-346 2.97e-06

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 48.39  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135   215 GLGKTLqtIALLGYLKH-YRNIPGPH-MVLVPKSTL-HNWMNEFKRW--VPSLRVICFVGDKDVRAafIRDEMmpGEWDV 289
Cdd:pfam00270   24 GSGKTL--AFLLPALEAlDKLDNGPQaLVLAPTRELaEQIYEELKKLgkGLGLKVASLLGGDSRKE--QLEKL--KGPDI 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 595582135   290 CVTSYEMV---IKEKSVFKKFhwRYLVIDEAHRIKNE--KSKLSEIVREF-KSTNRLLLTGTP 346
Cdd:pfam00270   98 LVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMgfGPDLEEILRRLpKKRQILLLSATL 158
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
557-615 7.19e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.00  E-value: 7.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 595582135  557 SSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQkKPVRVFRLI 615
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
187-346 1.02e-05

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 46.79  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  187 LRDYQIRGLNWLISLYENGVNGILAdEM--GLGKTlqTIALLGYLKHYRNIPGPH-MVLVPKSTL-HNWMNEFKRWVPSL 262
Cdd:cd18032     1 PRYYQQEAIEALEEAREKGQRRALL-VMatGTGKT--YTAAFLIKRLLEANRKKRiLFLAHREELlEQAERSFKEVLPDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  263 RVICFVGDKDVraafirdemmPGEWDVCVTSYEMVIKEK--SVFKKFHWRYLVIDEAHRikNEKSKLSEIVREFKSTNRL 340
Cdd:cd18032    78 SFGNLKGGKKK----------PDDARVVFATVQTLNKRKrlEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLL 145

                  ....*.
gi 595582135  341 LLTGTP 346
Cdd:cd18032   146 GLTATP 151
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
210-372 5.15e-05

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 47.52  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  210 LADEMGLGKTLQTiallGYLKHYRNIPGPH---MVLVPKSTLHNWMNEFKRWVpSLRVICFvgDKDVRAAFIRDEMMPGE 286
Cdd:PRK04914  174 LADEVGLGKTIEA----GMIIHQQLLTGRAervLILVPETLQHQWLVEMLRRF-NLRFSLF--DEERYAEAQHDADNPFE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  287 WDVCV-TSYEMVIKEKSVFKKF---HWRYLVIDEAHRIKNEKSKLSeivREF--------KSTNRLLLTGTPLQNNLHEL 354
Cdd:PRK04914  247 TEQLViCSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHLVWSEEAPS---REYqvveqlaeVIPGVLLLTATPEQLGQESH 323
                         170
                  ....*....|....*...
gi 595582135  355 WALLNFLLPDVFNSADDF 372
Cdd:PRK04914  324 FARLRLLDPDRFHDYEAF 341
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
486-582 9.52e-05

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 43.78  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  486 VGNSGKMVALDKLLARiKEQGSRVLIFSQMTRLLdiledycmwrgYEYSR------LDGQTPHEEREEAIDAFNApNSSK 559
Cdd:cd18789    30 AMNPNKLRALEELLKR-HEQGDKIIVFTDNVEAL-----------YRYAKrllkpfITGETPQSEREEILQNFRE-GEYN 96
                          90       100
                  ....*....|....*....|...
gi 595582135  560 FIFmlSTRAGGLGINLASADVVI 582
Cdd:cd18789    97 TLV--VSKVGDEGIDLPEANVAI 117
PTZ00110 PTZ00110
helicase; Provisional
485-605 1.41e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 42.45  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  485 IVGNSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFnapNSSKFIFML 564
Cdd:PTZ00110  356 VVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEF---KTGKSPIMI 432
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 595582135  565 STRAGGLGINLASADVVILYDSdwnPQvdlQAMDRAHRIGQ 605
Cdd:PTZ00110  433 ATDVASRGLDVKDVKYVINFDF---PN---QIEDYVHRIGR 467
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
202-324 2.09e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 40.40  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  202 YENGVNGILADEMGLGKTLqtIALLGYLKHYRNiPGPHMVLVPKSTLHNW-MNEFKRW-VPSLRVICFVGDKDVRAAFIr 279
Cdd:cd18028    14 LLKGENLLISIPTASGKTL--IAEMAMVNTLLE-GGKALYLVPLRALASEkYEEFKKLeEIGLKVGISTGDYDEDDEWL- 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 595582135  280 demmpGEWDVCVTSYEmviKEKSVFK-KFHW----RYLVIDEAHRIKNEK 324
Cdd:cd18028    90 -----GDYDIIVATYE---KFDSLLRhSPSWlrdvGVVVVDEIHLISDEE 131
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
495-585 2.33e-03

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 39.41  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 595582135  495 LDKLLARIKEQGS--RVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFnapNSSKFIFMLST----Ra 568
Cdd:cd18787    14 KLLLLLLLLEKLKpgKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKF---RSGKVRVLVATdvaaR- 89
                          90
                  ....*....|....*..
gi 595582135  569 gglGINLASADVVILYD 585
Cdd:cd18787    90 ---GLDIPGVDHVINYD 103
 
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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