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Conserved domains on  [gi|1805791161|ref|NP_001365192|]
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probable global transcription activator SNF2L1 isoform f [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000678)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
87-1034 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: 1205.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   87 MKADRAKRFEFLLKQTELFAHFIQPSaqKSPTSPLNMKLGRPRIK---KDEKQSLISAGDyrhrrteqeedeellseSRK 163
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGD--QSASAKKAKGRGRHASKlteEEEDEEYLKEEE-----------------DGL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  164 TSNVCIRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKST 243
Cdd:PLN03142   152 GGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKST 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  244 LHNWMNEFKRWVPSLRVICFVGDKDARAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 322
Cdd:PLN03142   231 LGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  323 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTD 402
Cdd:PLN03142   310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSD 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  403 VEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIV 482
Cdd:PLN03142   390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  483 SNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNAPNSSKFIFMLST 562
Cdd:PLN03142   468 ENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLST 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  563 RAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLID 642
Cdd:PLN03142   548 RAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAE 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  643 QQsnKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRnFRMDIEQSLYKFEGEDY 722
Cdd:PLN03142   628 QK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDD 704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  723 REKQKLGMVE-----WIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYR 796
Cdd:PLN03142   705 KDENKLDFKKivsdnWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLM 784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  797 K---------TIGYKVPRNPDIPNPALAQREEQKKIDgaepltpeeteekeklltQGFTNWTKRDFNQFIKANEKYGRDD 867
Cdd:PLN03142   785 QahqkgqlkdTIDVAEPEEPGDPLTAEEQEEKEQLLE------------------EGFSTWSRRDFNAFIRACEKYGRND 846
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  868 IDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKG 947
Cdd:PLN03142   847 IKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKG 926
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  948 KNYTEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEK 1026
Cdd:PLN03142   927 KLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARK 1003

                   ....*...
gi 1805791161 1027 KKRATKTP 1034
Cdd:PLN03142  1004 EKKLAKNA 1011
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
87-1034 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1205.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   87 MKADRAKRFEFLLKQTELFAHFIQPSaqKSPTSPLNMKLGRPRIK---KDEKQSLISAGDyrhrrteqeedeellseSRK 163
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGD--QSASAKKAKGRGRHASKlteEEEDEEYLKEEE-----------------DGL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  164 TSNVCIRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKST 243
Cdd:PLN03142   152 GGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKST 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  244 LHNWMNEFKRWVPSLRVICFVGDKDARAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 322
Cdd:PLN03142   231 LGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  323 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTD 402
Cdd:PLN03142   310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSD 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  403 VEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIV 482
Cdd:PLN03142   390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  483 SNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNAPNSSKFIFMLST 562
Cdd:PLN03142   468 ENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLST 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  563 RAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLID 642
Cdd:PLN03142   548 RAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAE 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  643 QQsnKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRnFRMDIEQSLYKFEGEDY 722
Cdd:PLN03142   628 QK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDD 704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  723 REKQKLGMVE-----WIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYR 796
Cdd:PLN03142   705 KDENKLDFKKivsdnWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLM 784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  797 K---------TIGYKVPRNPDIPNPALAQREEQKKIDgaepltpeeteekeklltQGFTNWTKRDFNQFIKANEKYGRDD 867
Cdd:PLN03142   785 QahqkgqlkdTIDVAEPEEPGDPLTAEEQEEKEQLLE------------------EGFSTWSRRDFNAFIRACEKYGRND 846
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  868 IDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKG 947
Cdd:PLN03142   847 IKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKG 926
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  948 KNYTEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEK 1026
Cdd:PLN03142   927 KLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARK 1003

                   ....*...
gi 1805791161 1027 KKRATKTP 1034
Cdd:PLN03142  1004 EKKLAKNA 1011
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
168-400 2.16e-164

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: 482.60  E-value: 2.16e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  168 CIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 247
Cdd:cd18065      1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  248 MNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 327
Cdd:cd18065     81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805791161  328 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 400
Cdd:cd18065    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
180-634 4.61e-152

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 467.78  E-value: 4.61e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  180 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 259
Cdd:COG0553    239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 339
Cdd:COG0553    318 VLVLDGTRERAKGANPFE----DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  340 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 419
Cdd:COG0553    394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  420 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVSNSGKMVVLDKLLAKL 498
Cdd:COG0553    474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  499 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNApNSSKFIFMLSTRAGGLGINLASADVVI 578
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  579 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 634
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
186-466 2.75e-141

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: 424.79  E-value: 2.75e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  186 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 261
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  262 CFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 341
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  342 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 420
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1805791161  421 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 466
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
179-355 3.04e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 3.04e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   179 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 256
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   257 SLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 331
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 1805791161   332 STNRLLLTGTPLQNNLHELWALLN 355
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DpdE NF041062
protein DpdE;
206-408 1.68e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.83  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  206 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdaraafirdem 278
Cdd:NF041062   175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  279 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 347
Cdd:NF041062   228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  348 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 408
Cdd:NF041062   303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
87-1034 0e+00

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 1205.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   87 MKADRAKRFEFLLKQTELFAHFIQPSaqKSPTSPLNMKLGRPRIK---KDEKQSLISAGDyrhrrteqeedeellseSRK 163
Cdd:PLN03142    91 MNNKGKGRLKYLLQQTEIFAHFAKGD--QSASAKKAKGRGRHASKlteEEEDEEYLKEEE-----------------DGL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  164 TSNVCIRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKST 243
Cdd:PLN03142   152 GGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKST 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  244 LHNWMNEFKRWVPSLRVICFVGDKDARAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 322
Cdd:PLN03142   231 LGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  323 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTD 402
Cdd:PLN03142   310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSD 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  403 VEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIV 482
Cdd:PLN03142   390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  483 SNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNAPNSSKFIFMLST 562
Cdd:PLN03142   468 ENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLST 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  563 RAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLID 642
Cdd:PLN03142   548 RAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAE 627
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  643 QQsnKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRnFRMDIEQSLYKFEGEDY 722
Cdd:PLN03142   628 QK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMDDTAELYDFDDEDD 704
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  723 REKQKLGMVE-----WIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFF-PPRLFELLEKEILYYR 796
Cdd:PLN03142   705 KDENKLDFKKivsdnWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQRLTELYEKEVRYLM 784
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  797 K---------TIGYKVPRNPDIPNPALAQREEQKKIDgaepltpeeteekeklltQGFTNWTKRDFNQFIKANEKYGRDD 867
Cdd:PLN03142   785 QahqkgqlkdTIDVAEPEEPGDPLTAEEQEEKEQLLE------------------EGFSTWSRRDFNAFIRACEKYGRND 846
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  868 IDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKG 947
Cdd:PLN03142   847 IKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYGQNKG 926
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  948 KNYTEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERER-AEK 1026
Cdd:PLN03142   927 KLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERERqARK 1003

                   ....*...
gi 1805791161 1027 KKRATKTP 1034
Cdd:PLN03142  1004 EKKLAKNA 1011
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
168-400 2.16e-164

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: 482.60  E-value: 2.16e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  168 CIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 247
Cdd:cd18065      1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  248 MNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 327
Cdd:cd18065     81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805791161  328 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 400
Cdd:cd18065    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
168-411 4.70e-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: 464.14  E-value: 4.70e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  168 CIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 247
Cdd:cd18064      1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  248 MNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 327
Cdd:cd18064     81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  328 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSL 407
Cdd:cd18064    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                   ....
gi 1805791161  408 PPKK 411
Cdd:cd18064    241 PPKK 244
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
180-400 1.38e-155

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: 459.48  E-value: 1.38e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  180 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 259
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 339
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791161  340 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD-QKLVERLHAVLKPFLLRRIK 400
Cdd:cd17997    161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnQEVVQRLHKVLRPFLLRRIK 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
180-634 4.61e-152

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 467.78  E-value: 4.61e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  180 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 259
Cdd:COG0553    239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLT 339
Cdd:COG0553    318 VLVLDGTRERAKGANPFE----DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  340 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 419
Cdd:COG0553    394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  420 SKMQREWYTKILMK-DIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVSNSGKMVVLDKLLAKL 498
Cdd:COG0553    474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  499 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNApNSSKFIFMLSTRAGGLGINLASADVVI 578
Cdd:COG0553    546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  579 LYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 634
Cdd:COG0553    625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
186-466 2.75e-141

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: 424.79  E-value: 2.75e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  186 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 261
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  262 CFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGT 341
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  342 PLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQ-KLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 420
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1805791161  421 KMQREWY-TKILMKDIDVLNSSGKMDK--MRLLNILMQLRKCCNHPYLF 466
Cdd:pfam00176  241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
180-400 8.28e-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: 313.92  E-value: 8.28e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  180 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 259
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAfIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV-REFKSTNRLLL 338
Cdd:cd17996     81 KIVYKGTPDVRKK-LQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805791161  339 TGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT---------KNCLGDQK---LVERLHAVLKPFLLRRIK 400
Cdd:cd17996    160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvKIELNEEEtllIIRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
180-400 1.79e-95

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: 302.38  E-value: 1.79e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  180 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 259
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAFIRDEMMP----GEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNR 335
Cdd:cd18009     80 VLLYHGTKEERERLRKKIMKRegtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  336 LLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD---------TKNCLGD---QKLVERLHAVLKPFLLRRIK 400
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 ...
183-398 1.18e-89

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: 286.17  E-value: 1.18e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 342
Cdd:cd18003     81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805791161  343 LQNNLHELWALLNFLLPDVFNSADDFDSWFD-------TKNCLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18003    161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
183-362 1.16e-88

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 281.76  E-value: 1.16e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEmMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 342
Cdd:cd17919     81 YHGSQRERAQIRAKE-KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                          170       180
                   ....*....|....*....|
gi 1805791161  343 LQNNLHELWALLNFLLPDVF 362
Cdd:cd17919    160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
183-398 1.37e-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: 266.91  E-value: 1.37e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAfIRD-EMMPG-----EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 336
Cdd:cd17993     82 YLGDIKSRDT-IREyEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791161  337 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNclgdQKLVERLHAVLKPFLLRR 398
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; ...
183-398 9.88e-78

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: 253.71  E-value: 9.88e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPsLRVIC 262
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAaFIRD-EMM-----------PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF 330
Cdd:cd17995     80 YHGSGESRQ-IIQQyEMYfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  331 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-DTKNclGDQklVERLHAVLKPFLLRR 398
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, ...
183-398 1.57e-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: 241.96  E-value: 1.57e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 342
Cdd:cd18006     81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  343 LQNNLHELWALLNFLLPDVF--NSADDFDSWF-DTKNclgDQKLVERLHAVLKPFLLRR 398
Cdd:cd18006    161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDD---ESETVEELHLLLQPFLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
183-398 4.80e-72

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: 238.56  E-value: 4.80e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAA---FIRDEMMPGE---WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRL 336
Cdd:cd18002     81 YWGNPKDRKVlrkFWDRKNLYTRdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  337 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--DTKNCLG-----DQKLVERLHAVLKPFLLRR 398
Cdd:cd18002    161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAEnktglNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
170-400 3.44e-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: 237.25  E-value: 3.44e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  170 RFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 249
Cdd:cd18062     11 KVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  250 EFKRWVPSLRVICFVGDKDARAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVR- 328
Cdd:cd18062     91 EFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  329 EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 398
Cdd:cd18062    170 HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 249

                   ..
gi 1805791161  399 IK 400
Cdd:cd18062    250 LK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
181-400 6.62e-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: 6.62e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  181 GPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRV 260
Cdd:cd18012      3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  261 ICFVGDKDARAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTG 340
Cdd:cd18012     82 LVIHGTKRKREKLRALE----DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805791161  341 TPLQNNLHELWALLNFLLPDVFNSADDF-DSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 400
Cdd:cd18012    158 TPIENHLGELWSIFDFLNPGLLGSYKRFkKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
170-400 1.78e-68

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: 229.56  E-value: 1.78e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  170 RFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 249
Cdd:cd18063     11 RVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  250 EFKRWVPSLRVICFVGDKDARAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVR- 328
Cdd:cd18063     91 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  329 EFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 398
Cdd:cd18063    170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 249

                   ..
gi 1805791161  399 IK 400
Cdd:cd18063    250 LK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
175-398 5.76e-67

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: 224.88  E-value: 5.76e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  175 PSYVKGG--PLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 252
Cdd:cd18054     11 PSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  253 RWVPSLRVICFVGDKDARAAfIRDEmmpgEW----------DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 322
Cdd:cd18054     91 IWAPEINVVVYIGDLMSRNT-IREY----EWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805791161  323 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18054    166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
183-362 1.07e-62

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: 210.70  E-value: 1.07e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARaAFIRDEMMPG--EWDVCVTSYEMVI---KEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLL 337
Cdd:cd17998     80 YYGSQEER-KHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                          170       180
                   ....*....|....*....|....*
gi 1805791161  338 LTGTPLQNNLHELWALLNFLLPDVF 362
Cdd:cd17998    159 LTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
479-611 1.85e-62

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 208.10  E-value: 1.85e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  479 EHIVSnsGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNAPnSSKFIF 558
Cdd:cd18793      6 EEVVS--GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVF 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1805791161  559 MLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLI 611
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; ...
183-398 1.21e-56

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: 194.20  E-value: 1.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKdaraafirdemmpgewdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTP 342
Cdd:cd17994     81 YVGDH-----------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1805791161  343 LQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd17994    144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
175-398 1.44e-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: 1.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  175 PSYVKGGP---LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEF 251
Cdd:cd18053     10 PSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  252 KRWVPSLRVICFVGDKDARAAFIRDEMMPGE-----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 326
Cdd:cd18053     90 QTWAPQMNAVVYLGDINSRNMIRTHEWMHPQtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKT 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791161  327 VREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18053    170 LIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
183-398 1.60e-54

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: 189.48  E-value: 1.60e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRN------IPGPHMVLVPKSTLHNWMNEFKRWVP 256
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  257 --SLRVICFVGDKDARAafiRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTN 334
Cdd:cd17999     80 naFLKPLAYVGPPQERR---RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805791161  335 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQKL----VERLHAVLKPFLLRR 398
Cdd:cd17999    157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrDSKASAKEQEAgalaLEALHKQVLPFLLRR 232
SLIDE pfam09111
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ...
901-1015 1.20e-53

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: 182.34  E-value: 1.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  901 EKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTS-KGKNYTEEEDRFLICMLHKMGFDRENVYEELRQC 979
Cdd:pfam09111    1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYPPNnKGKTYTEEEDRFLLCMLYKYGYGNEDLYEKIKQE 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1805791161  980 VRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKEN 1015
Cdd:pfam09111   81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
183-359 2.10e-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: 2.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVI- 261
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  262 -----CFVGDKDARAAFIRDEMM----PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKS 332
Cdd:cd18000     81 lhssgSGTGSEEKLGSIERKSQLirkvVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                          170       180
                   ....*....|....*....|....*..
gi 1805791161  333 TNRLLLTGTPLQNNLHELWALLNFLLP 359
Cdd:cd18000    161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
183-398 3.94e-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: 177.13  E-value: 3.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARA-------------------AFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 323
Cdd:cd18055     81 YTGDKDSRAiirenefsfddnavkggkkAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  324 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
183-398 9.87e-50

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: 176.02  E-value: 9.87e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVG-DKDARaafiRDEMM--PGEWDVCVTSYEMVIKEKSVF-----KKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTN 334
Cdd:cd18001     80 FHGtSKKER----ERNLEriQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKN 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  335 RLLLTGTPLQNNLHELWALLNFLLP-DVFNSADDFDSWFDT-------KNCLGDQK-----LVERLHAVLKPFLLRR 398
Cdd:cd18001    156 RIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENpitrgrdKDATQGEKalgseVAENLRQIIKPYFLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
183-398 3.68e-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: 171.70  E-value: 3.68e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISlyeNGvnGILADEMGLGKTLQTIAL-LGYLKHYRNIPGPHM----------------VLVPKSTLH 245
Cdd:cd18008      1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  246 NWMNEFKR--WVPSLRVICFVGDKdaRAAFIRDemmPGEWDVCVTSYEMV----------------IKEKSVFKKFHWRY 307
Cdd:cd18008     76 QWKDEIEKhtKPGSLKVYVYHGSK--RIKSIEE---LSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  308 LVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSaddfDSWFDTKNCL----GDQKL 383
Cdd:cd18008    151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGD----YPWFNSDISKpfskNDRKA 226
                          250
                   ....*....|....*
gi 1805791161  384 VERLHAVLKPFLLRR 398
Cdd:cd18008    227 LERLQALLKPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
183-398 9.91e-48

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: 170.64  E-value: 9.91e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKH--------YRNIP------------GPHMVLVPKS 242
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPrfkkkppassakKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  243 TLHNWMNEFKRWvPSLRVICFVGDKDARAAFIRdeMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 322
Cdd:cd18005     81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGR--LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  323 LSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKN--CLGDQKLVErLHA 389
Cdd:cd18005    158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSepikrgqrhtaTARelRLGRKRKQE-LAV 236

                   ....*....
gi 1805791161  390 VLKPFLLRR 398
Cdd:cd18005    237 KLSKFFLRR 245
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
183-398 1.04e-47

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


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 169.84  E-value: 1.04e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 262
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEM---------MPGEW--DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 331
Cdd:cd18058     79 YHGSQISRQMIQQYEMyyrdeqgnpLSGIFkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  332 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
183-398 1.58e-47

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


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 169.47  E-value: 1.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 323
Cdd:cd18057     81 YTGDKESRSVIRENEFsfednairsgkkvfrMKKEaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  324 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
183-398 3.47e-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: 165.62  E-value: 3.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 262
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 323
Cdd:cd18056     81 YVGDKDSRAIIRENEFsfednairggkkasrMKKEasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  324 SEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD---IAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
183-398 1.78e-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: 163.30  E-value: 1.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 262
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEM---------MPG--EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 331
Cdd:cd18060     79 YHGSLASRQMIQQYEMyckdsrgrlIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  332 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
183-398 3.69e-43

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 156.73  E-value: 3.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 262
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEM---------MPGEWD--VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 331
Cdd:cd18059     79 YHGSQASRRTIQLYEMyfkdpqgrvIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  332 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
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 ...
183-372 5.88e-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: 153.60  E-value: 5.88e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLIS-LYENGVNG------ILADEMGLGKTLQTIALL-GYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRW 254
Cdd:cd18007      1 LKPHQVEGVRFLWSnLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  255 VPSLRVICFV-------GDKDARAAFIRDEMMPGewDVCVTSYEM---VIKEKSVFKKFHWRY-----------LVIDEA 313
Cdd:cd18007     80 LPPDLRPLLVlvslsasKRADARLRKINKWHKEG--GVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEG 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  314 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 372
Cdd:cd18007    158 HRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
183-398 1.79e-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: 152.44  E-value: 1.79e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLislYE--------NGVNGILADEMGLGKTLQTIALL-GYLKHYRNIPGPH---MVLVPKSTLHNWMNE 250
Cdd:cd18004      1 LRPHQREGVQFL---YDcltgrrgyGGGGAILADEMGLGKTLQAIALVwTLLKQGPYGKPTAkkaLIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  251 FKRWVPSLRVICFV--GDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVI-DEAHRIKNEKSKLSEIV 327
Cdd:cd18004     78 FDKWLGLRRIKVVTadGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  328 REFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT-------KNC------LGDQKLvERLHAVLKPF 394
Cdd:cd18004    158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdPDAseedkeLGAERS-QELSELTSRF 236

                   ....
gi 1805791161  395 LLRR 398
Cdd:cd18004    237 ILRR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
183-398 1.26e-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: 146.69  E-value: 1.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 262
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDKDARAAFIRDEMM-----------PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFK 331
Cdd:cd18061     79 YHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805791161  332 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
183-398 3.69e-34

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 130.40  E-value: 3.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLIslyENGVNGILADEMGLGKTLQTIALLGYLKHYrnipGPHMVLVPKSTLHNWMNEFKRWVPSL---R 259
Cdd:cd18010      1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARaafirdemMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS-EIVREFKSTNR-LL 337
Cdd:cd18010     74 IQVIVKSKDGL--------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTkAALPLLKRAKRvIL 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805791161  338 LTGTPLQNNLHELWALLNFLLPDVFNSADDFDS-----------WFDTknclGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18010    146 LSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfgWDYS----GSSNLEELHLLLLATIMIRR 213
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
204-398 1.89e-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: 123.74  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  204 GILADEMGLGKTLQTIALLGYLKHYRN---------------------IP-GPHMVLVPKSTLHNWMNEFKRWVPS--LR 259
Cdd:cd18072     23 GILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASnkLR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVG-DKDARAAFIRDemmpgeWDVCVTSYEMVIKE---------KSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRE 329
Cdd:cd18072    103 VCLYHGpNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  330 FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDqklvERLHAVLKPFLLRR 398
Cdd:cd18072    177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
DEXDc smart00487
DEAD-like helicases superfamily;
179-355 3.04e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 121.83  E-value: 3.04e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   179 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 256
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   257 SLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVREF-K 331
Cdd:smart00487   80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
                           170       180
                    ....*....|....*....|....
gi 1805791161   332 STNRLLLTGTPLQNNLHELWALLN 355
Cdd:smart00487  160 NVQLLLLSATPPEEIENLLELFLN 183
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
199-398 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 1805791161  199 ENGVNGILADEMGLGKTLQTIALLgylkhyrnIPGPHMVLVPKSTLHNWMNEFKRWVPS--LRVICFVGdkdarAAFIRD 276
Cdd:cd18071     46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHG-----GERNRD 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  277 EMMPGEWDVCVTSYEMVIKEKSV-----FKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELW 351
Cdd:cd18071    113 PKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1805791161  352 ALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRR 398
Cdd:cd18071    193 SLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
486-600 1.27e-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: 1.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  486 GKMVVLDKLLAKlkEQGSRVLIFSQMTRLLDIlEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNapnSSKFIFMLSTRAG 565
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1805791161  566 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIG 600
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
183-397 1.30e-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: 118.60  E-value: 1.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLyengvNGILADEMGLGKTLQTIALLgyLKHYRN--------IPGPHMVLVP-----------KST 243
Cdd:cd18070      1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPdndldaadDDSDEMVCCPdclvaetpvssKAT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  244 L--------HNWMNEFKRWVP-SLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKE------------KSVFKK 302
Cdd:cd18070     74 LivcpsailAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTElhyaeanrsnrrRRRQKR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  303 F----------HWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFdsWF 372
Cdd:cd18070    154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWW--AR 231
                          250       260
                   ....*....|....*....|....*
gi 1805791161  373 DTKNCLGDQKLVERLHAVLKPFLLR 397
Cdd:cd18070    232 VLIRPQGRNKAREPLAALLKELLWR 256
HAND pfam09110
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ...
746-826 2.72e-29

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: 112.65  E-value: 2.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  746 AVDAYFREALRVSEPK---IPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRnPDIPNPALA------- 815
Cdd:pfam09110    1 SVDNYYKDVLGTGGKKsttKPKAPRAPKQINIQDHQFFPPRLKELQEKEQLYYKKKIGYKVTL-DDGKEEDGEefeeere 79
                           90
                   ....*....|...
gi 1805791161  816 --QREEQKKIDGA 826
Cdd:pfam09110   80 akRKLEQEEIDNA 92
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
183-398 1.33e-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: 112.25  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYL---KHYRNIP--GPHMVLVPKSTLHNWMNEFK 252
Cdd:cd18066      1 LRPHQREGIEFLyecvMGMRVNERFGaILADEMGLGKTLQCISLIWTLlrqGPYGGKPviKRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  253 RWVPSLRVICFVGDKDARaafIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKS 332
Cdd:cd18066     81 KWLGSERIKVFTVDQDHK---VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791161  333 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-------------TKNCLGDQKLVErLHAVLKPFLLRR 398
Cdd:cd18066    158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepivrsreptatpEEKKLGEARAAE-LTRLTGLFILRR 235
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
183-373 5.44e-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: 107.21  E-value: 5.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLislYEN------------GVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMN 249
Cdd:cd18069      1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  250 EFKRWVPSLRVICFVGDKDARAAFIRDEM--------MPGEWD----VCVTSYEMvikeksvfkkFHWR----YLVIDEA 313
Cdd:cd18069     76 EFNKWLPPPEALPNVRPRPFKVFILNDEHkttaarakVIEDWVkdggVLLMGYEM----------FRLRpgpdVVICDEG 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  314 HRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD 373
Cdd:cd18069    146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
183-398 1.15e-25

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: 106.79  E-value: 1.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH----MVLVPKSTLHNWMNEFKR 253
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  254 WVPSlRVICFVGDKDARAAFIRDEMMPGEWD-------VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 326
Cdd:cd18067     81 WLGG-RLQPLAIDGGSKKEIDRKLVQWASQQgrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  327 VREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVErLHAVLKP 393
Cdd:cd18067    160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadasEKERQLGEEKLQE-LISIVNR 238

                   ....*
gi 1805791161  394 FLLRR 398
Cdd:cd18067    239 CIIRR 243
HELICc smart00490
helicase superfamily c-terminal domain;
516-600 1.36e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.13  E-value: 1.36e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161   516 DILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNapnSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDR 595
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1805791161   596 AHRIG 600
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
201-372 3.00e-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: 105.74  E-value: 3.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  201 GVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLV--PKSTLHNWMNEFKRWVP------SLRV--ICFVGDKDAR 270
Cdd:cd18068     28 GSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVvcPLNTVLNWLNEFEKWQEglkdeeKIEVneLATYKRPQER 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  271 AafirdeMMPGEWD----VCVTSYEMV--------IKEKSVFKKFHWRYL--------VIDEAHRIKNEKSKLSEIVREF 330
Cdd:cd18068    108 S------YKLQRWQeeggVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1805791161  331 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 372
Cdd:cd18068    182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
183-398 7.37e-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: 100.44  E-value: 7.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVngILADEMGLGKTLQTIALLGYLKhYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 262
Cdd:cd18011      1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  263 FVGDkDARAAFIRDEMMPGEWDVCVTSYEMV---IKEKSVFKKFHWRYLVIDEAHRIKN----EKSKLSEIVREF--KST 333
Cdd:cd18011     77 LDRE-TAAQLRRLIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRAR 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  334 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtknclgdqklVERLHAVLKPFLLRR 398
Cdd:cd18011    156 HVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR-------------LDGLREVLAKVLLRR 207
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
181-756 1.00e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.69  E-value: 1.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  181 GPLRDYQIRGLN-WLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIpgphMVLVPKSTL-HNWMNEFKRWvpsL 258
Cdd:COG1061     79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELlEQWAEELRRF---L 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  259 RVICFVGDKDARaafirdemmpgEWDVCVTSYEMVIKEKSVFK-KFHWRYLVIDEAHRIKNEksKLSEIVREFKSTNRLL 337
Cdd:COG1061    152 GDPLAGGGKKDS-----------DAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLG 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  338 LTGTPL-QNNLHELWALLNFLLPDVfnsaddfdSWfdtknclgdQKLVERlhAVLKPFLLRRIKTDVEkslppkKEIKIY 416
Cdd:COG1061    219 LTATPFrSDGREILLFLFDGIVYEY--------SL---------KEAIED--GYLAPPEYYGIRVDLT------DERAEY 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  417 LGLSkmqrEWYTKILMKDidvlnssgkmdkmrllnilmqlrkccnhpylfdgaepgppyttdehivsNSGKMVVLDKLLA 496
Cdd:COG1061    274 DALS----ERLREALAAD-------------------------------------------------AERKDKILRELLR 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  497 KLKEQGsRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFNApnsSKFIFMLSTRAGGLGINLASADV 576
Cdd:COG1061    301 EHPDDR-KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDV 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  577 VILYDSDWNPQVDLQAMDRAHRIGQ-KKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQ 655
Cdd:COG1061    377 AILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALE 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  656 MIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYREKQKLGMVEWIE 735
Cdd:COG1061    457 VKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLL 536
                          570       580
                   ....*....|....*....|.
gi 1805791161  736 PPKRERKANYAVDAYFREALR 756
Cdd:COG1061    537 ELLELLAALLRLEELAALLLK 557
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
183-357 4.31e-16

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: 78.55  E-value: 4.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLIslyENGVNGILADeMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTL-HNWMNEFKRW--VPSLR 259
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  260 VICFVGDKDARAAfirdeMMPGEWDVCVTSYEMVIK-EKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREF-KSTNRLL 337
Cdd:cd18013     76 VSVAVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                          170       180
                   ....*....|....*....|.
gi 1805791161  338 -LTGTPLQNNLHELWALLNFL 357
Cdd:cd18013    151 gLTGTPSPNGLMDLWAQIALL 171
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
183-342 7.33e-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: 7.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGL-NWLISLYENGvnGILADEMGLGKTLQTIALLGYLKhyrniPGPHMVLVP-KSTLHNWMNEFKRWVPSlRV 260
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGD-SS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  261 ICFVGdKDARAAFIrdemmpgEWDVCVTSYEMVIK-EKSVFKKFH-WRYLVIDEAHRIKNEKskLSEIVREFKSTNRLLL 338
Cdd:cd17926     73 IGLIG-GGKKKDFD-------DANVVVATYQSLSNlAEEEKDLFDqFGLLIVDEAHHLPAKT--FSEILKELNAKYRLGL 142

                   ....
gi 1805791161  339 TGTP 342
Cdd:cd17926    143 TATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
182-342 8.05e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 61.53  E-value: 8.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  182 PLRDYQIRGL-NWLISLYENGVNGILADEMGLGKTL---QTIALLGYLKHYRNIpgphMVLVP-KSTLHNWMNEFKRWVP 256
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLtaaKLIARLFKKGPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  257 SLRVIC--FVGDKDARaafirdemMPGEWDVCVTSYEMV----IKEKSVFKKFHWRYLVIDEAHRIKNEKSKlsEIVREF 330
Cdd:pfam04851   79 NYVEIGeiISGDKKDE--------SVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYF 148
                          170
                   ....*....|..
gi 1805791161  331 KSTNRLLLTGTP 342
Cdd:pfam04851  149 KPAFLLGLTATP 160
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
203-341 3.11e-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: 59.34  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  203 NGILADEMGLGKTLQ-TIALLGYLKHYRnipGPHMVLVPKSTL-HNWMNEFKRWV-PSLRVICFVGDKDARAAFIRDEmm 279
Cdd:cd00046      3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLRELFgPGIRVAVLVGGSSAEEREKNKL-- 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  280 pGEWDVCVTSYEMVIKEKSVFKKFH---WRYLVIDEAHRI-KNEKS----KLSEIVREFKSTNRLLLTGT 341
Cdd:cd00046     78 -GDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGalilDLAVRKAGLKNAQVILLSAT 146
DpdE NF041062
protein DpdE;
206-408 1.68e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 58.83  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  206 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdaraafirdem 278
Cdd:NF041062   175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  279 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI----KNEKSKLSEIVREFK----STNR-LLLTGTPLQNNL 347
Cdd:NF041062   228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahAAPRlLLLSATPVLGNE 302
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  348 HELWALLNFLLPDVFnSADDFDSwFDTKncLGDQKLVERLHAVLKP----FLLRRIKTDVEKSLP 408
Cdd:NF041062   303 ETFLALLHLLDPDLY-PLDDLEA-FRER--LEEREELGRLVLGLDPdnpnFLLRQALDELRALFP 363
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
491-724 2.16e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 58.20  E-value: 2.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  491 LDKLLAKLKEQ-----GSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHE--------EREEAIEAFNApnsSKFI 557
Cdd:COG1111    337 LSKLREILKEQlgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEgdkgltqkEQIEILERFRA---GEFN 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  558 FMLSTRAGGLGINLASADVVILYDSDWNPQVDLQamdRAHRIGQKKPVRVFRLITDNTVEE--RIVERAEIKLRLDSIVI 635
Cdd:COG1111    414 VLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEayYWSSRRKEKKMKSILKK 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  636 QQGRLIDQQSNKLAKEEmlqmirHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNfRMDIEQSLY 715
Cdd:COG1111    491 LKKLLDKQEKEKLKESA------QATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIV-STLAESLEL 563

                   ....*....
gi 1805791161  716 KFEGEDYRE 724
Cdd:COG1111    564 RELGEKVDD 572
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
847-886 3.67e-07

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


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 47.57  E-value: 3.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1805791161  847 NWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 886
Cdd:cd00167      1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRER 40
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
845-886 1.22e-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: 1.22e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1805791161   845 FTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 886
Cdd:smart00717    1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRER 42
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
211-342 5.09e-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: 47.62  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  211 GLGKTLqtIALLGYLKH-YRNIPGPH-MVLVPKSTL-HNWMNEFKRW--VPSLRVICFVG--DKDARAAFIRDEmmpgew 283
Cdd:pfam00270   24 GSGKTL--AFLLPALEAlDKLDNGPQaLVLAPTRELaEQIYEELKKLgkGLGLKVASLLGgdSRKEQLEKLKGP------ 95
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805791161  284 DVCVTSYEMV---IKEKSVFKKFhwRYLVIDEAHRIKNE--KSKLSEIVREF-KSTNRLLLTGTP 342
Cdd:pfam00270   96 DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMgfGPDLEEILRRLpKKRQILLLSATL 158
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
553-611 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 1805791161  553 SSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQkKPVRVFRLI 611
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 ...
183-342 2.16e-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: 46.02  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  183 LRDYQIRGLNWLISLYENGVNGILAdEM--GLGKTlqTIALLGYLKHYRNIPGPH-MVLVPKSTL-HNWMNEFKRWVPSL 258
Cdd:cd18032      1 PRYYQQEAIEALEEAREKGQRRALL-VMatGTGKT--YTAAFLIKRLLEANRKKRiLFLAHREELlEQAERSFKEVLPDG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  259 RVICFVGDKDAraafirdemmPGEWDVCVTSYEMVIKEK--SVFKKFHWRYLVIDEAHRikNEKSKLSEIVREFKSTNRL 336
Cdd:cd18032     78 SFGNLKGGKKK----------PDDARVVFATVQTLNKRKrlEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLL 145

                   ....*.
gi 1805791161  337 LLTGTP 342
Cdd:cd18032    146 GLTATP 151
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
206-368 6.55e-05

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 47.14  E-value: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  206 LADEMGLGKTLQTiallGYLKHYRNIPGPH---MVLVPKSTLHNWMNEFKRWVpSLRVICFvgDKDARAAFIRDEMMPGE 282
Cdd:PRK04914   174 LADEVGLGKTIEA----GMIIHQQLLTGRAervLILVPETLQHQWLVEMLRRF-NLRFSLF--DEERYAEAQHDADNPFE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  283 WDVCV-TSYEMVIKEKSVFKKF---HWRYLVIDEAHRIKNEKSKLSeivREF--------KSTNRLLLTGTPLQNNLHEL 350
Cdd:PRK04914   247 TEQLViCSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHLVWSEEAPS---REYqvveqlaeVIPGVLLLTATPEQLGQESH 323
                          170
                   ....*....|....*...
gi 1805791161  351 WALLNFLLPDVFNSADDF 368
Cdd:PRK04914   324 FARLRLLDPDRFHDYEAF 341
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
482-578 1.17e-04

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: 43.39  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  482 VSNSGKMVVLDKLLAKLkEQGSRVLIFSQMtrlLDILEDYCMWRGYEYcrLDGQTPHEEREEAIEAFNApNSSKFIFmlS 561
Cdd:cd18789     30 AMNPNKLRALEELLKRH-EQGDKIIVFTDN---VEALYRYAKRLLKPF--ITGETPQSEREEILQNFRE-GEYNTLV--V 100
                           90
                   ....*....|....*..
gi 1805791161  562 TRAGGLGINLASADVVI 578
Cdd:cd18789    101 SKVGDEGIDLPEANVAI 117
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
480-581 3.14e-04

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: 41.72  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  480 HIVSNSGKMVVLDKLLaKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFnapNSSKFIFM 559
Cdd:cd18787      6 VVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKF---RSGKVRVL 81
                           90       100
                   ....*....|....*....|....*.
gi 1805791161  560 LST----RagglGINLASADVVILYD 581
Cdd:cd18787     82 VATdvaaR----GLDIPGVDHVINYD 103
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
84-110 1.15e-03

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: 40.21  E-value: 1.15e-03
                           10        20
                   ....*....|....*....|....*...
gi 1805791161   84 EEKMKADR-AKRFEFLLKQTELFAHFIQ 110
Cdd:pfam13892  101 EELREAKRqQRKLNFLITQTELYSHFMG 128
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
198-320 1.43e-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: 40.78  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  198 YENGVNGILADEMGLGKTLqtIALLGYLKHYRNiPGPHMVLVPKSTLHNW-MNEFKRW-VPSLRVICFVGDKDARAAFIr 275
Cdd:cd18028     14 LLKGENLLISIPTASGKTL--IAEMAMVNTLLE-GGKALYLVPLRALASEkYEEFKKLeEIGLKVGISTGDYDEDDEWL- 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1805791161  276 demmpGEWDVCVTSYEmviKEKSVFK-KFHW----RYLVIDEAHRIKNEK 320
Cdd:cd18028     90 -----GDYDIIVATYE---KFDSLLRhSPSWlrdvGVVVVDEIHLISDEE 131
PTZ00110 PTZ00110
helicase; Provisional
481-601 6.51e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 40.53  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791161  481 IVSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREEAIEAFnapNSSKFIFML 560
Cdd:PTZ00110   356 VVEEHEKRGKLKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEF---KTGKSPIMI 432
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1805791161  561 STRAGGLGINLASADVVILYDSdwnPQvdlQAMDRAHRIGQ 601
Cdd:PTZ00110   433 ATDVASRGLDVKDVKYVINFDF---PN---QIEDYVHRIGR 467
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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