NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039798802|ref|XP_017174135|]
View 

probable global transcription activator SNF2L1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
86-1033 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: 1217.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   86 MKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEELLSESRKTSN 165
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLKEEEDGLGGS 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  166 VCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 245
Cdd:PLN03142   155 GGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  246 WMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSE 324
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSK 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  325 IVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEK 404
Cdd:PLN03142   313 TMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEK 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  405 SLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVGNS 484
Cdd:PLN03142   393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENS 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  485 GKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKFIFMLSTRAG 564
Cdd:PLN03142   471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAG 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  565 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQs 644
Cdd:PLN03142   551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQK- 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  645 nKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYKFEGEDYREK 724
Cdd:PLN03142   630 -TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDDKDE 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  725 QKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYRKTi 798
Cdd:PLN03142   708 NKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLMQA- 786
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  799 gykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKS 878
Cdd:PLN03142   787 --------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKT 858
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  879 PEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLI 958
Cdd:PLN03142   859 EEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFML 938
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798802  959 CMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEKKKRATKTP 1033
Cdd:PLN03142   939 CMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARKEKKLAKNA 1011
DBINO super family cl16460
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
52-109 4.13e-04

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


The actual alignment was detected with superfamily member pfam13892:

Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 41.37  E-value: 4.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802   52 KGEKKEKITSPFQLKLAAKASKSEkemdpeyEEKMKADR-AKRFEFLLKQTELFAHFIQ 109
Cdd:pfam13892   77 KNEKEERELRKRAEKEALEQAKKE-------EELREAKRqQRKLNFLITQTELYSHFMG 128
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
86-1033 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1217.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   86 MKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEELLSESRKTSN 165
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLKEEEDGLGGS 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  166 VCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 245
Cdd:PLN03142   155 GGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  246 WMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSE 324
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSK 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  325 IVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEK 404
Cdd:PLN03142   313 TMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEK 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  405 SLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVGNS 484
Cdd:PLN03142   393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENS 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  485 GKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKFIFMLSTRAG 564
Cdd:PLN03142   471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAG 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  565 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQs 644
Cdd:PLN03142   551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQK- 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  645 nKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYKFEGEDYREK 724
Cdd:PLN03142   630 -TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDDKDE 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  725 QKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYRKTi 798
Cdd:PLN03142   708 NKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLMQA- 786
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  799 gykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKS 878
Cdd:PLN03142   787 --------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKT 858
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  879 PEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLI 958
Cdd:PLN03142   859 EEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFML 938
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798802  959 CMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEKKKRATKTP 1033
Cdd:PLN03142   939 CMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARKEKKLAKNA 1011
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
167-399 5.63e-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: 5.63e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  167 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 246
Cdd:cd18065      1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  247 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 326
Cdd:cd18065     81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798802  327 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 399
Cdd:cd18065    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
179-633 6.29e-153

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 470.09  E-value: 6.29e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  179 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 258
Cdd:COG0553    239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDvRAAFIRDEmmpGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 338
Cdd:COG0553    318 VLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  339 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 418
Cdd:COG0553    394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  419 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVGNSGKMVALDKLLARI 497
Cdd:COG0553    474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  498 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApNSSKFIFMLSTRAGGLGINLASADVVI 577
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  578 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 633
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
185-465 4.03e-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: 4.03e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  185 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 260
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  261 CFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 340
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  341 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 419
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039798802  420 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 465
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
178-354 3.15e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.44  E-value: 3.15e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   178 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 255
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   256 SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 330
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 1039798802   331 STNRLLLTGTPLQNNLHELWALLN 354
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DpdE NF041062
protein DpdE;
205-407 1.97e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.44  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  205 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdvraafirdem 277
Cdd:NF041062   175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  278 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 346
Cdd:NF041062   228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  347 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 407
Cdd:NF041062   303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
52-109 4.13e-04

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 41.37  E-value: 4.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802   52 KGEKKEKITSPFQLKLAAKASKSEkemdpeyEEKMKADR-AKRFEFLLKQTELFAHFIQ 109
Cdd:pfam13892   77 KNEKEERELRKRAEKEALEQAKKE-------EELREAKRqQRKLNFLITQTELYSHFMG 128
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
86-1033 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1217.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   86 MKADRAKRFEFLLKQTELFAHFIQPSAQKsptsplNMKLARPRVKKDDKQSlisvgdyrhrRTEQEEDEELLSESRKTSN 165
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGDQSA------SAKKAKGRGRHASKLT----------EEEEDEEYLKEEEDGLGGS 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  166 VCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 245
Cdd:PLN03142   155 GGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  246 WMNEFKRWVPSLRVICFVGDKDVRAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSE 324
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSK 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  325 IVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEK 404
Cdd:PLN03142   313 TMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEK 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  405 SLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVGNS 484
Cdd:PLN03142   393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENS 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  485 GKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPNSSKFIFMLSTRAG 564
Cdd:PLN03142   471 GKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAG 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  565 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQs 644
Cdd:PLN03142   551 GLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQK- 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  645 nKLAKEEMLQMIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnFRMDLEQSLYKFEGEDYREK 724
Cdd:PLN03142   630 -TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDDKDE 707
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  725 QKLG-----TVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYRKTi 798
Cdd:PLN03142   708 NKLDfkkivSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLMQA- 786
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  799 gykvprnpEIPNPAIAQREEQKKIDGAEPLTPQETEEKDKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKS 878
Cdd:PLN03142   787 --------HQKGQLKDTIDVAEPEEPGDPLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKT 858
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  879 PEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLI 958
Cdd:PLN03142   859 EEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKGKLYNEECDRFML 938
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798802  959 CMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEKKKRATKTP 1033
Cdd:PLN03142   939 CMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARKEKKLAKNA 1011
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
167-399 5.63e-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: 5.63e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  167 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 246
Cdd:cd18065      1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  247 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 326
Cdd:cd18065     81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798802  327 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 399
Cdd:cd18065    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
167-410 1.32e-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: 465.68  E-value: 1.32e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  167 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 246
Cdd:cd18064      1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  247 MNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 326
Cdd:cd18064     81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  327 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSL 406
Cdd:cd18064    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                   ....
gi 1039798802  407 PPKK 410
Cdd:cd18064    241 PPKK 244
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
179-399 1.82e-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: 461.41  E-value: 1.82e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  179 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 258
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 338
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039798802  339 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD-QKLVERLHAVLKPFLLRRIK 399
Cdd:cd17997    161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnQEVVQRLHKVLRPFLLRRIK 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
179-633 6.29e-153

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 470.09  E-value: 6.29e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  179 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 258
Cdd:COG0553    239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDvRAAFIRDEmmpGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 338
Cdd:COG0553    318 VLVLDGTRE-RAKGANPF---EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  339 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 418
Cdd:COG0553    394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  419 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVGNSGKMVALDKLLARI 497
Cdd:COG0553    474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  498 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApNSSKFIFMLSTRAGGLGINLASADVVI 577
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  578 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 633
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
185-465 4.03e-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: 4.03e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  185 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 260
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  261 CFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 340
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  341 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 419
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039798802  420 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 465
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
179-399 1.92e-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: 1.92e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  179 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 258
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDVRAAfIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV-REFKSTNRLLL 337
Cdd:cd17996     81 KIVYKGTPDVRKK-LQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039798802  338 TGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT---------KNCLGDQK---LVERLHAVLKPFLLRRIK 399
Cdd:cd17996    160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvKIELNEEEtllIIRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
179-399 7.69e-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: 303.15  E-value: 7.69e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  179 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 258
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDVRAAFIRDEMMP----GEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNR 334
Cdd:cd18009     80 VLLYHGTKEERERLRKKIMKRegtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  335 LLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD---------TKNCLGD---QKLVERLHAVLKPFLLRRIK 399
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 ...
182-397 4.60e-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: 287.33  E-value: 4.60e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 341
Cdd:cd18003     81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798802  342 LQNNLHELWALLNFLLPDVFNSADDFDSWFD-------TKNCLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18003    161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
182-361 2.13e-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: 280.99  E-value: 2.13e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEmMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 341
Cdd:cd17919     81 YHGSQRERAQIRAKE-KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                          170       180
                   ....*....|....*....|
gi 1039798802  342 LQNNLHELWALLNFLLPDVF 361
Cdd:cd17919    160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
182-397 2.31e-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: 266.14  E-value: 2.31e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAfIRD-EMMPG-----EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 335
Cdd:cd17993     82 YLGDIKSRDT-IREyEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039798802  336 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNclgdQKLVERLHAVLKPFLLRR 397
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; ...
182-397 2.49e-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: 2.49e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPsLRVIC 261
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAaFIRD-EMM-----------PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF 329
Cdd:cd17995     80 YHGSGESRQ-IIQQyEMYfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  330 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-DTKNclGDQklVERLHAVLKPFLLRR 397
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, ...
182-397 1.22e-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: 242.34  E-value: 1.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 341
Cdd:cd18006     81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  342 LQNNLHELWALLNFLLPDVF--NSADDFDSWF-DTKNclgDQKLVERLHAVLKPFLLRR 397
Cdd:cd18006    161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDD---ESETVEELHLLLQPFLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
182-397 4.62e-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: 241.25  E-value: 4.62e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVG---DKDVRAAFIRDEMMPGE---WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 335
Cdd:cd18002     81 YWGnpkDRKVLRKFWDRKNLYTRdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  336 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--DTKNCLG-----DQKLVERLHAVLKPFLLRR 397
Cdd:cd18002    161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAEnktglNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
166-399 8.58e-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: 8.58e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  166 VCVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 245
Cdd:cd18062      8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  246 WMNEFKRWVPSLRVICFVGDKDVRAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 325
Cdd:cd18062     88 WVYEFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  326 VR-EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFL 394
Cdd:cd18062    167 LNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFL 246

                   ....*
gi 1039798802  395 LRRIK 399
Cdd:cd18062    247 LRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
169-399 6.07e-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: 6.07e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  169 RFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 248
Cdd:cd18063     11 RVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  249 EFKRWVPSLRVICFVGDKDVRAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVR- 327
Cdd:cd18063     91 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  328 EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 397
Cdd:cd18063    170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 249

                   ..
gi 1039798802  398 IK 399
Cdd:cd18063    250 LK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
180-399 6.64e-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: 6.64e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  180 GPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRV 259
Cdd:cd18012      3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  260 ICFVGDKDVRAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTG 339
Cdd:cd18012     82 LVIHGTKRKREKLRALE----DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039798802  340 TPLQNNLHELWALLNFLLPDVFNSADDF-DSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 399
Cdd:cd18012    158 TPIENHLGELWSIFDFLNPGLLGSYKRFkKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
168-397 1.14e-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: 1.14e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  168 VRFEVSPSYVKGG--PLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 245
Cdd:cd18054      5 VALKKQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  246 WMNEFKRWVPSLRVICFVGDKDVRAAfIRDEmmpgEW----------DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 315
Cdd:cd18054     85 WQREFEIWAPEINVVVYIGDLMSRNT-IREY----EWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  316 KNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLL 395
Cdd:cd18054    160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLL 235

                   ..
gi 1039798802  396 RR 397
Cdd:cd18054    236 RR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
182-361 7.07e-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: 7.07e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRaAFIRDEMMPG--EWDVCVTSYEMVI---KEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLL 336
Cdd:cd17998     80 YYGSQEER-KHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                          170       180
                   ....*....|....*....|....*
gi 1039798802  337 LTGTPLQNNLHELWALLNFLLPDVF 361
Cdd:cd17998    159 LTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
478-610 2.13e-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: 207.71  E-value: 2.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  478 EHIVgnSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNAPnSSKFIF 557
Cdd:cd18793      6 EEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVF 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039798802  558 MLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLI 610
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; ...
182-397 5.79e-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: 194.97  E-value: 5.79e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKdvraafirdemmpgewdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 341
Cdd:cd17994     81 YVGDH-----------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798802  342 LQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd17994    144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
168-397 1.49e-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: 192.57  E-value: 1.49e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  168 VRFEVSPSYVKGGP---LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLH 244
Cdd:cd18053      4 VALKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  245 NWMNEFKRWVPSLRVICFVGDKDVRAAFIRDEMMPGE-----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEK 319
Cdd:cd18053     84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039798802  320 SKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLLRR 397
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 ...
182-397 9.61e-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: 9.61e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRN------IPGPHMVLVPKSTLHNWMNEFKRWVP 255
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  256 --SLRVICFVGDKDVRAafiRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTN 333
Cdd:cd17999     80 naFLKPLAYVGPPQERR---RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798802  334 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQKL----VERLHAVLKPFLLRR 397
Cdd:cd17999    157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrDSKASAKEQEAgalaLEALHKQVLPFLLRR 232
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
900-1014 5.87e-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: 183.49  E-value: 5.87e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  900 EKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTS-KGKNYTEEEDRFLICMLHKMGFDRENVYEELRQC 978
Cdd:pfam09111    1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYPPNnKGKTYTEEEDRFLLCMLYKYGYGNEDLYEKIKQE 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039798802  979 VRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKEN 1014
Cdd:pfam09111   81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
182-358 2.13e-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: 2.13e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVI- 260
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  261 -----CFVGDKD-----VRAAFIRDEMMPgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 330
Cdd:cd18000     81 lhssgSGTGSEEklgsiERKSQLIRKVVG-DGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                          170       180
                   ....*....|....*....|....*...
gi 1039798802  331 STNRLLLTGTPLQNNLHELWALLNFLLP 358
Cdd:cd18000    160 TPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
182-397 7.90e-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: 7.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRA-------------------AFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 322
Cdd:cd18055     81 YTGDKDSRAiirenefsfddnavkggkkAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  323 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
182-397 1.24e-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: 1.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKdvRAAFIRD-EMMPGEWDVCVTSYEMVIKEKSVF-----KKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 335
Cdd:cd18001     80 FHGTS--KKERERNlERIQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRI 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  336 LLTGTPLQNNLHELWALLNFLLP-DVFNSADDFDSWFDT-------KNCLGDQK-----LVERLHAVLKPFLLRR 397
Cdd:cd18001    158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENpitrgrdKDATQGEKalgseVAENLRQIIKPYFLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
182-397 2.03e-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: 2.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISlyeNGvnGILADEMGLGKTLQTIAL-LGYLKHYRNIPGPHM----------------VLVPKSTLH 244
Cdd:cd18008      1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  245 NWMNEFKR--WVPSLRVICFVGDKdvRAAFIRDemmPGEWDVCVTSYEMV----------------IKEKSVFKKFHWRY 306
Cdd:cd18008     76 QWKDEIEKhtKPGSLKVYVYHGSK--RIKSIEE---LSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  307 LVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSaddfDSWFDTKNCL----GDQKL 382
Cdd:cd18008    151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGD----YPWFNSDISKpfskNDRKA 226
                          250
                   ....*....|....*
gi 1039798802  383 VERLHAVLKPFLLRR 397
Cdd:cd18008    227 LERLQALLKPILLRR 241
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
182-397 1.37e-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: 169.45  E-value: 1.37e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 261
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEM---------MPGEW--DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 330
Cdd:cd18058     79 YHGSQISRQMIQQYEMyyrdeqgnpLSGIFkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  331 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
182-397 3.07e-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: 168.70  E-value: 3.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 322
Cdd:cd18057     81 YTGDKESRSVIRENEFsfednairsgkkvfrMKKEaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  323 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
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 ...
182-397 3.65e-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: 169.10  E-value: 3.65e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKH--------YRNIP------------GPHMVLVPKS 241
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPrfkkkppassakKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  242 TLHNWMNEFKRWvPSLRVICFVGDKDVRAAFIRdeMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 321
Cdd:cd18005     81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGR--LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  322 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKN--CLGDQKLVErLHA 388
Cdd:cd18005    158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSepikrgqrhtaTARelRLGRKRKQE-LAV 236

                   ....*....
gi 1039798802  389 VLKPFLLRR 397
Cdd:cd18005    237 KLSKFFLRR 245
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
182-397 7.29e-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: 7.29e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 261
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 322
Cdd:cd18056     81 YVGDKDSRAIIRENEFsfednairggkkasrMKKEasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  323 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD---IAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
182-397 2.30e-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: 2.30e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 261
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEM---------MPG--EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 330
Cdd:cd18060     79 YHGSLASRQMIQQYEMyckdsrgrlIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  331 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
182-397 7.24e-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: 155.96  E-value: 7.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 261
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEM---------MPGEWD--VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 330
Cdd:cd18059     79 YHGSQASRRTIQLYEMyfkdpqgrvIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  331 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
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 ...
182-371 4.89e-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: 4.89e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLIS-LYENGVNG------ILADEMGLGKTLQTIALL-GYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRW 253
Cdd:cd18007      1 LKPHQVEGVRFLWSnLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  254 -----VPSLRVICFVGDKDVRAAF--IRDEMMPGewDVCVTSYEM---VIKEKSVFKKFHWRY-----------LVIDEA 312
Cdd:cd18007     80 lppdlRPLLVLVSLSASKRADARLrkINKWHKEG--GVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEG 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  313 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 371
Cdd:cd18007    158 HRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
182-397 1.23e-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: 1.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLislYE--------NGVNGILADEMGLGKTLQTIALL-GYLKHYRNIPGPH---MVLVPKSTLHNWMNE 249
Cdd:cd18004      1 LRPHQREGVQFL---YDcltgrrgyGGGGAILADEMGLGKTLQAIALVwTLLKQGPYGKPTAkkaLIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  250 FKRWVPSLRVICFV--GDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVI-DEAHRIKNEKSKLSEIV 326
Cdd:cd18004     78 FDKWLGLRRIKVVTadGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  327 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT-------KNC------LGDQKLvERLHAVLKPF 393
Cdd:cd18004    158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdPDAseedkeLGAERS-QELSELTSRF 236

                   ....
gi 1039798802  394 LLRR 397
Cdd:cd18004    237 ILRR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
182-397 1.57e-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: 1.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 261
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDKDVRAAFIRDEMMPGE-----------WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 330
Cdd:cd18061     79 YHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798802  331 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
745-843 8.02e-39

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: 140.00  E-value: 8.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  745 AVDAYFREALRVSEPK---IPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRN------PEIPNPAIA- 814
Cdd:pfam09110    1 SVDNYYKDVLGTGGKKsttKPKAPRAPKQINIQDHQFFPPRLKELQEKEQLYYKKKIGYKVTLDdgkeedGEEFEEEREa 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1039798802  815 -QREEQKKIDGAEPLTPQETEEKDKLLTQG 843
Cdd:pfam09110   81 kRKLEQEEIDNAEPLTEEEEAEKEELLSEG 110
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
182-397 4.47e-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: 130.02  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLIslyENGVNGILADEMGLGKTLQTIALLGYLKHYrnipGPHMVLVPKSTLHNWMNEFKRWVPSL---R 258
Cdd:cd18010      1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDVRaafirdemMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS-EIVREFKSTNR-LL 336
Cdd:cd18010     74 IQVIVKSKDGL--------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTkAALPLLKRAKRvIL 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039798802  337 LTGTPLQNNLHELWALLNFLLPDVFNSADDFDS-----------WFDTknclGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18010    146 LSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfgWDYS----GSSNLEELHLLLLATIMIRR 213
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
203-397 2.00e-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: 123.36  E-value: 2.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  203 GILADEMGLGKTLQTIALLGYLKHYRN---------------------IP-GPHMVLVPKSTLHNWMNEFKRWVPS--LR 258
Cdd:cd18072     23 GILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASnkLR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVG-DKDVRAAFIRDemmpgeWDVCVTSYEMVIKE---------KSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRE 328
Cdd:cd18072    103 VCLYHGpNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  329 FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDqklvERLHAVLKPFLLRR 397
Cdd:cd18072    177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
DEXDc smart00487
DEAD-like helicases superfamily;
178-354 3.15e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.44  E-value: 3.15e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   178 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 255
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   256 SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 330
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 1039798802   331 STNRLLLTGTPLQNNLHELWALLN 354
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
198-397 4.49e-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: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  198 ENGVNGILADEMGLGKTLQTIALLgylkhyrnIPGPHMVLVPKSTLHNWMNEFKRWVPS--LRVICFVGdkdvrAAFIRD 275
Cdd:cd18071     46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHG-----GERNRD 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  276 EMMPGEWDVCVTSYEMVIKEKSV-----FKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELW 350
Cdd:cd18071    113 PKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039798802  351 ALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRR 397
Cdd:cd18071    193 SLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
485-599 1.33e-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: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  485 GKMVALDKLLAriKEQGSRVLIFSQMTRLLDIlEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNapnSSKFIFMLSTRAG 564
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039798802  565 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIG 599
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
182-396 1.16e-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: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLyengvNGILADEMGLGKTLQTIALLgyLKHYRN--------IPGPHMVLVP-----------KST 242
Cdd:cd18070      1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPdndldaadDDSDEMVCCPdclvaetpvssKAT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  243 L--------HNWMNEFKRWVP-SLRVICFVGDKDVRAAFIRDEMMPGEWDVCVTSYEMVIKE------------KSVFKK 301
Cdd:cd18070     74 LivcpsailAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTElhyaeanrsnrrRRRQKR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  302 F----------HWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFdsWF 371
Cdd:cd18070    154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWW--AR 231
                          250       260
                   ....*....|....*....|....*
gi 1039798802  372 DTKNCLGDQKLVERLHAVLKPFLLR 396
Cdd:cd18070    232 VLIRPQGRNKAREPLAALLKELLWR 256
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
182-397 2.18e-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: 2.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYL---KHYRNIP--GPHMVLVPKSTLHNWMNEFK 251
Cdd:cd18066      1 LRPHQREGIEFLyecvMGMRVNERFGaILADEMGLGKTLQCISLIWTLlrqGPYGGKPviKRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  252 RWVPSLRVICFVGDKDVRaafIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKS 331
Cdd:cd18066     81 KWLGSERIKVFTVDQDHK---VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  332 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-------------TKNCLGDQKLVErLHAVLKPFLLRR 397
Cdd:cd18066    158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepivrsreptatpEEKKLGEARAAE-LTRLTGLFILRR 235
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
182-372 2.16e-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: 108.36  E-value: 2.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLislYEN------------GVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMN 248
Cdd:cd18069      1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  249 EFKRWVPSLRVICFVGDKDVRAAFIRDEM--------MPGEWD----VCVTSYEMvikeksvfkkFHWR----YLVIDEA 312
Cdd:cd18069     76 EFNKWLPPPEALPNVRPRPFKVFILNDEHkttaarakVIEDWVkdggVLLMGYEM----------FRLRpgpdVVICDEG 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  313 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD 372
Cdd:cd18069    146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
182-397 6.99e-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: 6.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH----MVLVPKSTLHNWMNEFKR 252
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  253 WVPSlRVICFVGD---------KDVRAAFIRDEMMPGEwdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS 323
Cdd:cd18067     81 WLGG-RLQPLAIDggskkeidrKLVQWASQQGRRVSTP--VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  324 EIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVErLHAVL 390
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadasEKERQLGEEKLQE-LISIV 236

                   ....*..
gi 1039798802  391 KPFLLRR 397
Cdd:cd18067    237 NRCIIRR 243
HELICc smart00490
helicase superfamily c-terminal domain;
515-599 1.96e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 100.75  E-value: 1.96e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802   515 DILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNapnSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDR 594
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1039798802   595 AHRIG 599
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
200-371 3.99e-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: 3.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  200 GVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLV--PKSTLHNWMNEFKRWVP------SLRV--ICFVGDKDVR 269
Cdd:cd18068     28 GSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVvcPLNTVLNWLNEFEKWQEglkdeeKIEVneLATYKRPQER 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  270 AafirdeMMPGEWD----VCVTSYEMV--------IKEKSVFKKFHWRYL--------VIDEAHRIKNEKSKLSEIVREF 329
Cdd:cd18068    108 S------YKLQRWQeeggVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039798802  330 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 371
Cdd:cd18068    182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
182-397 6.50e-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: 6.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVngILADEMGLGKTLQTIALLGYLKhYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 261
Cdd:cd18011      1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  262 FVGDkDVRAAFIRDEMMPGEWDVCVTSYEMV---IKEKSVFKKFHWRYLVIDEAHRIKN----EKSKLSEIVREF--KST 332
Cdd:cd18011     77 LDRE-TAAQLRRLIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRAR 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  333 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtknclgdqklVERLHAVLKPFLLRR 397
Cdd:cd18011    156 HVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR-------------LDGLREVLAKVLLRR 207
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
180-755 4.21e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 82.77  E-value: 4.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  180 GPLRDYQIRGLN-WLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIpgphMVLVPKSTL-HNWMNEFKRWvpsL 257
Cdd:COG1061     79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELlEQWAEELRRF---L 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  258 RVICFVGDKDvraafirdemmPGEWDVCVTSYEMVIKEKSVFK-KFHWRYLVIDEAHRIKNEksKLSEIVREFKSTNRLL 336
Cdd:COG1061    152 GDPLAGGGKK-----------DSDAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLG 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  337 LTGTPL-QNNLHELWALLNFLLPDVfnsaddfdSWfdtknclgdQKLVERlhAVLKPFLLRRIKTDVEkslppkKEIKIY 415
Cdd:COG1061    219 LTATPFrSDGREILLFLFDGIVYEY--------SL---------KEAIED--GYLAPPEYYGIRVDLT------DERAEY 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  416 LGLSkmqrEWYTKILMKDidvlnssgkmdkmrllnilmqlrkccnhpylfdgaepgppyttdehivgNSGKMVALDKLLA 495
Cdd:COG1061    274 DALS----ERLREALAAD-------------------------------------------------AERKDKILRELLR 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  496 RIKEQGsRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFNApnsSKFIFMLSTRAGGLGINLASADV 575
Cdd:COG1061    301 EHPDDR-KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDV 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  576 VILYDSDWNPQVDLQAMDRAHRIGQ-KKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQ 654
Cdd:COG1061    377 AILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALE 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  655 MIRHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRNFRMDLEQSLYKFEGEDYREKQKLGTVEWIE 734
Cdd:COG1061    457 VKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLL 536
                          570       580
                   ....*....|....*....|.
gi 1039798802  735 PPKRERKANYAVDAYFREALR 755
Cdd:COG1061    537 ELLELLAALLRLEELAALLLK 557
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
182-356 1.41e-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: 1.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLIslyENGVNGILADeMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTL-HNWMNEFKRW--VPSLR 258
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  259 VICFVGDKDVRAAfirdeMMPGEWDVCVTSYEMVIK-EKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF-KSTNRLL 336
Cdd:cd18013     76 VSVAVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                          170       180
                   ....*....|....*....|.
gi 1039798802  337 -LTGTPLQNNLHELWALLNFL 356
Cdd:cd18013    151 gLTGTPSPNGLMDLWAQIALL 171
ResIII pfam04851
Type III restriction enzyme, res subunit;
181-341 4.70e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 62.30  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  181 PLRDYQIRGL-NWLISLYENGVNGILADEMGLGKTL---QTIALLGYLKHYRNIpgphMVLVP-KSTLHNWMNEFKRWVP 255
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLtaaKLIARLFKKGPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  256 SLRVIC--FVGDKDVRaafirdemMPGEWDVCVTSYEMV----IKEKSVFKKFHWRYLVIDEAHRIKNEKSKlsEIVREF 329
Cdd:pfam04851   79 NYVEIGeiISGDKKDE--------SVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYF 148
                          170
                   ....*....|..
gi 1039798802  330 KSTNRLLLTGTP 341
Cdd:pfam04851  149 KPAFLLGLTATP 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
182-341 6.71e-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: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGL-NWLISLYENGvnGILADEMGLGKTLQTIALLGYLKhyrniPGPHMVLVP-KSTLHNWMNEFKRWVPSlRV 259
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGD-SS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  260 ICFVGDKDVRAAFIRDemmpgewdVCVTSYEMVIK-EKSVFKKFH-WRYLVIDEAHRIKNEKskLSEIVREFKSTNRLLL 337
Cdd:cd17926     73 IGLIGGGKKKDFDDAN--------VVVATYQSLSNlAEEEKDLFDqFGLLIVDEAHHLPAKT--FSEILKELNAKYRLGL 142

                   ....
gi 1039798802  338 TGTP 341
Cdd:cd17926    143 TATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
202-340 6.91e-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: 6.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  202 NGILADEMGLGKTLQ-TIALLGYLKHYRnipGPHMVLVPKSTL-HNWMNEFKRWV-PSLRVICFVGDKDVRAAFIRDEmm 278
Cdd:cd00046      3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLRELFgPGIRVAVLVGGSSAEEREKNKL-- 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  279 pGEWDVCVTSYEMVIKEKSVFKKFH---WRYLVIDEAHRI-KNEKS----KLSEIVREFKSTNRLLLTGT 340
Cdd:cd00046     78 -GDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGalilDLAVRKAGLKNAQVILLSAT 146
DpdE NF041062
protein DpdE;
205-407 1.97e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.44  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  205 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdvraafirdem 277
Cdd:NF041062   175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  278 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 346
Cdd:NF041062   228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798802  347 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 407
Cdd:NF041062   303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
486-720 5.51e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.05  E-value: 5.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  486 KMVALDKLLARI--KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHE--------EREEAIDAFNApnsSKF 555
Cdd:COG1111    336 KLSKLREILKEQlgTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEgdkgltqkEQIEILERFRA---GEF 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  556 IFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQamdRAHRIGQKKPVRVFRLITDNTVEE--RIVERAEIKLRLDSIV 633
Cdd:COG1111    413 NVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEayYWSSRRKEKKMKSILK 489
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  634 IQQGRLIDQQSNKLAKEEmlqmirHGATHVFACKESELTDEDIVTILERGEKKTAEMNERMQKMGESSLRnfRMDLEQSL 713
Cdd:COG1111    490 KLKKLLDKQEKEKLKESA------QATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVI--VSTLAESL 561

                   ....*..
gi 1039798802  714 YKFEGED 720
Cdd:COG1111    562 ELRELGE 568
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
846-885 3.49e-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: 3.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1039798802  846 NWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 885
Cdd:cd00167      1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRER 40
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
844-885 1.15e-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: 1.15e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1039798802   844 FTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 885
Cdd:smart00717    1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRER 42
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
210-341 2.99e-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: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  210 GLGKTLqtIALLGYLKH-YRNIPGPH-MVLVPKSTL-HNWMNEFKRW--VPSLRVICFVGDKDVRAafIRDEMmpGEWDV 284
Cdd:pfam00270   24 GSGKTL--AFLLPALEAlDKLDNGPQaLVLAPTRELaEQIYEELKKLgkGLGLKVASLLGGDSRKE--QLEKL--KGPDI 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798802  285 CVTSYEMV---IKEKSVFKKFhwRYLVIDEAHRIKNE--KSKLSEIVREF-KSTNRLLLTGTP 341
Cdd:pfam00270   98 LVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMgfGPDLEEILRRLpKKRQILLLSATL 158
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
552-610 7.05e-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: 7.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802  552 SSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQkKPVRVFRLI 610
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 ...
182-341 1.14e-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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  182 LRDYQIRGLNWLISLYENGVNGILAdEM--GLGKTlqTIALLGYLKHYRNIPGPH-MVLVPKSTL-HNWMNEFKRWVPSL 257
Cdd:cd18032      1 PRYYQQEAIEALEEAREKGQRRALL-VMatGTGKT--YTAAFLIKRLLEANRKKRiLFLAHREELlEQAERSFKEVLPDG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  258 RVICFVGDKDVraafirdemmPGEWDVCVTSYEMVIKEK--SVFKKFHWRYLVIDEAHRikNEKSKLSEIVREFKSTNRL 335
Cdd:cd18032     78 SFGNLKGGKKK----------PDDARVVFATVQTLNKRKrlEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLL 145

                   ....*.
gi 1039798802  336 LLTGTP 341
Cdd:cd18032    146 GLTATP 151
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
205-367 5.25e-05

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 47.52  E-value: 5.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  205 LADEMGLGKTLQTiallGYLKHYRNIPGPH---MVLVPKSTLHNWMNEFKRWVpSLRVICFvgDKDVRAAFIRDEMMPGE 281
Cdd:PRK04914   174 LADEVGLGKTIEA----GMIIHQQLLTGRAervLILVPETLQHQWLVEMLRRF-NLRFSLF--DEERYAEAQHDADNPFE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  282 WDVCV-TSYEMVIKEKSVFKKF---HWRYLVIDEAHRIKNEKSKLSeivREF--------KSTNRLLLTGTPLQNNLHEL 349
Cdd:PRK04914   247 TEQLViCSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHLVWSEEAPS---REYqvveqlaeVIPGVLLLTATPEQLGQESH 323
                          170
                   ....*....|....*...
gi 1039798802  350 WALLNFLLPDVFNSADDF 367
Cdd:PRK04914   324 FARLRLLDPDRFHDYEAF 341
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
481-577 9.32e-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: 9.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  481 VGNSGKMVALDKLLARiKEQGSRVLIFSQMTRLLdiledycmwrgYEYSR------LDGQTPHEEREEAIDAFNApNSSK 554
Cdd:cd18789     30 AMNPNKLRALEELLKR-HEQGDKIIVFTDNVEAL-----------YRYAKrllkpfITGETPQSEREEILQNFRE-GEYN 96
                           90       100
                   ....*....|....*....|...
gi 1039798802  555 FIFmlSTRAGGLGINLASADVVI 577
Cdd:cd18789     97 TLV--VSKVGDEGIDLPEANVAI 117
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
52-109 4.13e-04

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 41.37  E-value: 4.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798802   52 KGEKKEKITSPFQLKLAAKASKSEkemdpeyEEKMKADR-AKRFEFLLKQTELFAHFIQ 109
Cdd:pfam13892   77 KNEKEERELRKRAEKEALEQAKKE-------EELREAKRqQRKLNFLITQTELYSHFMG 128
PTZ00110 PTZ00110
helicase; Provisional
480-600 1.42e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 42.45  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  480 IVGNSGKMVALDKLLARIKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFnapNSSKFIFML 559
Cdd:PTZ00110   356 VVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEF---KTGKSPIMI 432
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039798802  560 STRAGGLGINLASADVVILYDSdwnPQvdlQAMDRAHRIGQ 600
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 ...
197-319 2.05e-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: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  197 YENGVNGILADEMGLGKTLqtIALLGYLKHYRNiPGPHMVLVPKSTLHNW-MNEFKRW-VPSLRVICFVGDKDVRAAFIr 274
Cdd:cd18028     14 LLKGENLLISIPTASGKTL--IAEMAMVNTLLE-GGKALYLVPLRALASEkYEEFKKLeEIGLKVGISTGDYDEDDEWL- 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039798802  275 demmpGEWDVCVTSYEmviKEKSVFK-KFHW----RYLVIDEAHRIKNEK 319
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 ...
490-580 2.35e-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: 39.03  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798802  490 LDKLLARIKEQGS--RVLIFSQMTRLLDILEDYCMWRGYEYSRLDGQTPHEEREEAIDAFnapNSSKFIFMLST----Ra 563
Cdd:cd18787     14 KLLLLLLLLEKLKpgKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKF---RSGKVRVLVATdvaaR- 89
                           90
                   ....*....|....*..
gi 1039798802  564 gglGINLASADVVILYD 580
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH