|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
90-1072 |
0e+00 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 1198.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 90 MKADRAKRFEFLLKQTELFAHFIQPSaqKSPTSPLNMKLGRPRIK----KDDKQSLISVGDyrhrrteqeedeellsesR 165
Cdd:PLN03142 91 MNNKGKGRLKYLLQQTEIFAHFAKGD--QSASAKKAKGRGRHASKlteeEEDEEYLKEEED------------------G 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 166 KTSNVCVRFEVSPSYVKGgPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKS 245
Cdd:PLN03142 151 LGGSGGTRLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 246 TLHNWMNEFKRWVPSLRVICFVGDKDARAAfIRDEMM-PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKS 324
Cdd:PLN03142 230 TLGNWMNEIRRFCPVLRAVKFHGNPEERAH-QREELLvAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 325 KLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERLHTVLKPFLLRRIKT 404
Cdd:PLN03142 309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKS 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 405 DVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSAGkmDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHI 484
Cdd:PLN03142 389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGG--ERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 485 VSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREDkflevellgqreAIEAFN 564
Cdd:PLN03142 467 VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDA------------SIDAFN 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 565 IPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLR 644
Cdd:PLN03142 535 KPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 645 LDSIVIQQGRLIDQQsnKMAKEEMLQMIRHGATHVFASKESELTDEDITTLLERGEKKTAEMNERLQKMGESSLRnFRMD 724
Cdd:PLN03142 615 LDALVIQQGRLAEQK--TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIK-FKMD 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 725 IEQSLYKFEGEDYREKQKLGMVE-----WIEPPKRERKANYAVDAYFREALRVSEPKVPKAPRPPKQPNVQDFQFF-PPR 798
Cdd:PLN03142 692 DTAELYDFDDEDDKDENKLDFKKivsdnWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFnVQR 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 799 LFELLEKEILYYRK---------TIGYKVPRNPDIPNPAVAQREEQKKIDgaepltpeeteekeklltQGFTNWTKRDFN 869
Cdd:PLN03142 772 LTELYEKEVRYLMQahqkgqlkdTIDVAEPEEPGDPLTAEEQEEKEQLLE------------------EGFSTWSRRDFN 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 870 QFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAP 949
Cdd:PLN03142 834 AFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKELNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNP 913
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 950 FHQLRIQYGTSKGKNYTEEEDRFLICMLHKMGFDRenvYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKE 1029
Cdd:PLN03142 914 WLELKIQYGQNKGKLYNEECDRFMLCMVHKLGYGN---WDELKAAFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKE 990
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 529013608 1030 NMEIEERERAEKKKRATKTPMSQKRKAESATESSGKKDVKKVK 1072
Cdd:PLN03142 991 NQEYDERERQARKEKKLAKNATPSKRPSGRQANESPSSLKKRK 1033
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
171-403 |
2.00e-162 |
|
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: 478.36 E-value: 2.00e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 171 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 250
Cdd:cd18065 1 CVRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 251 MNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 330
Cdd:cd18065 81 MNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529013608 331 RDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERLHTVLKPFLLRRIK 403
Cdd:cd18065 161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
171-414 |
1.15e-155 |
|
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: 461.44 E-value: 1.15e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 171 CVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNW 250
Cdd:cd18064 1 CTRFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 251 MNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV 330
Cdd:cd18064 81 MAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 331 RDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERLHTVLKPFLLRRIKTDVEKSL 410
Cdd:cd18064 161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240
|
....
gi 529013608 411 PPKK 414
Cdd:cd18064 241 PPKK 244
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
183-403 |
5.71e-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: 458.71 E-value: 5.71e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 183 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 262
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLT 342
Cdd:cd17997 81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529013608 343 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGD-QKLVERLHTVLKPFLLRRIK 403
Cdd:cd17997 161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDnQEVVQRLHKVLRPFLLRRIK 222
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
183-649 |
4.25e-147 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 455.84 E-value: 4.25e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 183 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 262
Cdd:COG0553 239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLT 342
Cdd:COG0553 318 VLVLDGTRERAKGANPFE----DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 343 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERLHTVLKPFLLRRIKTDVEKSLPPKKEIKIYLGL 422
Cdd:COG0553 394 GTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 423 SKMQREWYTKILMK-DIDVLNSAGKMDKMRLLNILMQLRKCCNHPYLFDGaepgppytTDEHIVSNSGKMVVLDKLLAKL 501
Cdd:COG0553 474 TPEQRALYEAVLEYlRRELEGAEGIRRRGLILAALTRLRQICSHPALLLE--------EGAELSGRSAKLEALLELLEEL 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 502 KEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREdkflevellgqrEAIEAFNipNSSKF-IFMLSTRAG 580
Cdd:COG0553 546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERD------------ELVDRFQ--EGPEApVFLISLKAG 611
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 581 GLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRL-DSIV 649
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALaESVL 681
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
189-469 |
3.23e-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: 425.56 E-value: 3.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 189 YQIRGLNWLISLYEN-GVNGILADEMGLGKTLQTIALLGYLKHYRNIPG-PHMVLVPKSTLHNWMNEFKRWV--PSLRVI 264
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 265 CFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGT 344
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 345 PLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQ-KLVERLHTVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLS 423
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGkKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 529013608 424 KMQREWY-TKILMKDIDVLNSAGKMDK--MRLLNILMQLRKCCNHPYLF 469
Cdd:pfam00176 241 KLQRKLYqTFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
183-403 |
1.16e-99 |
|
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: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 183 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 262
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARAAfIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIV-RDFKSTNRLLL 341
Cdd:cd17996 81 KIVYKGTPDVRKK-LQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529013608 342 TGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT---------KNCLGDQK---LVERLHTVLKPFLLRRIK 403
Cdd:cd17996 160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfantgeqvKIELNEEEtllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
183-403 |
2.98e-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: 2.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 183 GGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 262
Cdd:cd18009 1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARAAFIRDEMMP----GEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNR 338
Cdd:cd18009 80 VLLYHGTKEERERLRKKIMKRegtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 339 LLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD---------TKNCLGD---QKLVERLHTVLKPFLLRRIK 403
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 ... |
186-401 |
3.77e-90 |
|
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350761 [Multi-domain] Cd Length: 223 Bit Score: 288.10 E-value: 3.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTP 345
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529013608 346 LQNNLHELWALLNFLLPDVFNSAEDFDSWFD-------TKNCLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
186-365 |
1.69e-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: 1.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEmMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTP 345
Cdd:cd17919 81 YHGSQRERAQIRAKE-KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
170 180
....*....|....*....|
gi 529013608 346 LQNNLHELWALLNFLLPDVF 365
Cdd:cd17919 160 LQNNLEELWALLDFLDPPFL 179
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
186-401 |
6.55e-83 |
|
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: 268.07 E-value: 6.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAfIRD-EMMPG-----EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRL 339
Cdd:cd17993 82 YLGDIKSRDT-IREyEFYFSqtkklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529013608 340 LLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNclgdQKLVERLHTVLKPFLLRR 401
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; ... |
186-401 |
3.06e-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: 255.64 E-value: 3.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPsLRVIC 265
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAaFIRD-EMM-----------PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDF 333
Cdd:cd17995 80 YHGSGESRQ-IIQQyEMYfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 334 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-DTKNclGDQklVERLHTVLKPFLLRR 401
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, ... |
186-401 |
1.06e-72 |
|
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: 240.03 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTP 345
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 346 LQNNLHELWALLNFLLPDVF--NSAEDFDSWF-DTKNclgDQKLVERLHTVLKPFLLRR 401
Cdd:cd18006 161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDD---ESETVEELHLLLQPFLLRR 216
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
186-401 |
1.10e-71 |
|
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: 237.79 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAA---FIRDEMMPGE---WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRL 339
Cdd:cd18002 81 YWGNPKDRKVlrkFWDRKNLYTRdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 340 LLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--DTKNCLG-----DQKLVERLHTVLKPFLLRR 401
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAEnktglNEHQLKRLHMILKPFMLRR 229
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
170-403 |
3.24e-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: 3.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 170 VCVRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 249
Cdd:cd18062 8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 250 WMNEFKRWVPSLRVICFVGDKDARAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 329
Cdd:cd18062 88 WVYEFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 330 VRD-FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQK----------LVERLHTVLKPFL 398
Cdd:cd18062 167 LNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFL 246
|
....*
gi 529013608 399 LRRIK 403
Cdd:cd18062 247 LRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
173-403 |
1.62e-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: 229.95 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 173 RFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 252
Cdd:cd18063 11 RVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 253 EFKRWVPSLRVICFVGDKDARAAFIrDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRD 332
Cdd:cd18063 91 EFDKWAPSVVKISYKGTPAMRRSLV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 333 -FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQK----------LVERLHTVLKPFLLRR 401
Cdd:cd18063 170 hYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERvdlneeetilIIRRLHKVLRPFLLRR 249
|
..
gi 529013608 402 IK 403
Cdd:cd18063 250 LK 251
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
184-403 |
2.52e-68 |
|
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: 227.83 E-value: 2.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 184 GPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRV 263
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 264 ICFVGDKDARAAFIRDEmmpgEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTG 343
Cdd:cd18012 82 LVIHGTKRKREKLRALE----DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529013608 344 TPLQNNLHELWALLNFLLPDVFNSAEDF-DSWFDTKNCLGDQKLVERLHTVLKPFLLRRIK 403
Cdd:cd18012 158 TPIENHLGELWSIFDFLNPGLLGSYKRFkKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
172-401 |
4.96e-68 |
|
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: 227.97 E-value: 4.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 172 VRFEVSPSYVKGG--PLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 249
Cdd:cd18054 5 VALKKQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 250 WMNEFKRWVPSLRVICFVGDKDARAAfIRDEmmpgEW----------DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRI 319
Cdd:cd18054 85 WQREFEIWAPEINVVVYIGDLMSRNT-IREY----EWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 320 KNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdtKNCLGDQKLVERLHTVLKPFLL 399
Cdd:cd18054 160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLL 235
|
..
gi 529013608 400 RR 401
Cdd:cd18054 236 RR 237
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
186-365 |
1.12e-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: 211.09 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARaAFIRDEMMPG--EWDVCVTSYEMVI---KEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLL 340
Cdd:cd17998 80 YYGSQEER-KHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
|
170 180
....*....|....*....|....*
gi 529013608 341 LTGTPLQNNLHELWALLNFLLPDVF 365
Cdd:cd17998 159 LTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
482-626 |
4.70e-59 |
|
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: 198.47 E-value: 4.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 482 EHIVSnsGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREdkflevellgqrEAIE 561
Cdd:cd18793 6 EEVVS--GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQ------------KLVD 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 562 AFNiPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLI 626
Cdd:cd18793 72 RFN-EDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
186-401 |
2.24e-57 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350752 [Multi-domain] Cd Length: 196 Bit Score: 196.51 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKdaraafirdemmpgewdVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTP 345
Cdd:cd17994 81 YVGDH-----------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 529013608 346 LQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd17994 144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 196
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
172-401 |
2.47e-56 |
|
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: 194.88 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 172 VRFEVSPSYVKGGP---LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLH 248
Cdd:cd18053 4 VALKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 249 NWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGE-----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEK 323
Cdd:cd18053 84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529013608 324 SKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdtKNCLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18053 164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE----EHGKGREYGYASLHKELEPFLLRR 237
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
186-401 |
8.53e-55 |
|
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350757 [Multi-domain] Cd Length: 232 Bit Score: 190.25 E-value: 8.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRN------IPGPHMVLVPKSTLHNWMNEFKRWVP 259
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 260 --SLRVICFVGDKDARAafiRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTN 337
Cdd:cd17999 80 naFLKPLAYVGPPQERR---RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529013608 338 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTKNCLGDQKL----VERLHTVLKPFLLRR 401
Cdd:cd17999 157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkpilasrDSKASAKEQEAgalaLEALHKQVLPFLLRR 232
|
|
| SLIDE |
pfam09111 |
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ... |
916-1030 |
1.09e-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: 182.72 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 916 EKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTS-KGKNYTEEEDRFLICMLHKMGFDRENVYEELRQC 994
Cdd:pfam09111 1 EKYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYPPNnKGKTYTEEEDRFLLCMLYKYGYGNEDLYEKIKQE 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 529013608 995 VRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKEN 1030
Cdd:pfam09111 81 IRESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
186-362 |
5.59e-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: 180.98 E-value: 5.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVI- 264
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 265 -----CFVGDKDARAAFIRDEMM----PGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKS 335
Cdd:cd18000 81 lhssgSGTGSEEKLGSIERKSQLirkvVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
|
170 180
....*....|....*....|....*..
gi 529013608 336 TNRLLLTGTPLQNNLHELWALLNFLLP 362
Cdd:cd18000 161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
186-401 |
7.77e-51 |
|
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: 179.05 E-value: 7.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARA-------------------AFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 326
Cdd:cd18055 81 YTGDKDSRAiirenefsfddnavkggkkAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 327 SEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18055 161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
186-401 |
2.70e-49 |
|
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350759 [Multi-domain] Cd Length: 232 Bit Score: 174.48 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVG-DKDARaafiRDEMM--PGEWDVCVTSYEMVIKEKSVF-----KKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTN 337
Cdd:cd18001 80 FHGtSKKER----ERNLEriQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 338 RLLLTGTPLQNNLHELWALLNFLLP-DVFNSAEDFDSWFDT-------KNCLGDQK-----LVERLHTVLKPFLLRR 401
Cdd:cd18001 156 RIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENpitrgrdKDATQGEKalgseVAENLRQIIKPYFLRR 232
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
186-401 |
1.34e-48 |
|
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350766 [Multi-domain] Cd Length: 241 Bit Score: 172.86 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISlyeNGvnGILADEMGLGKTLQTIAL-LGYLKHYRNIPGPHM----------------VLVPKSTLH 248
Cdd:cd18008 1 LLPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 249 NWMNEFKR--WVPSLRVICFVGDKdaRAAFIRDemmPGEWDVCVTSYEMV----------------IKEKSVFKKFHWRY 310
Cdd:cd18008 76 QWKDEIEKhtKPGSLKVYVYHGSK--RIKSIEE---LSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 311 LVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERL 390
Cdd:cd18008 151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERL 230
|
250
....*....|.
gi 529013608 391 HTVLKPFLLRR 401
Cdd:cd18008 231 QALLKPILLRR 241
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
186-401 |
4.26e-48 |
|
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: 171.40 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 326
Cdd:cd18057 81 YTGDKESRSVIRENEFsfednairsgkkvfrMKKEaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 327 SEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
186-401 |
1.19e-47 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350816 [Multi-domain] Cd Length: 222 Bit Score: 169.45 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 265
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEM---------MPGEW--DVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFK 334
Cdd:cd18058 79 YHGSQISRQMIQQYEMyyrdeqgnpLSGIFkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 335 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---LKTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
186-401 |
6.61e-47 |
|
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: 167.93 E-value: 6.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVIC 265
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKL 326
Cdd:cd18056 81 YVGDKDSRAIIRENEFsfednairggkkasrMKKEasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 327 SEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD---IAKEDQIKKLHDMLGPHMLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
186-401 |
8.57e-47 |
|
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350763 [Multi-domain] Cd Length: 245 Bit Score: 167.94 E-value: 8.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKH--------YRNIP------------GPHMVLVPKS 245
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPrfkkkppassakKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 246 TLHNWMNEFKRWvPSLRVICFVGDKDARAAFIRdeMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSK 325
Cdd:cd18005 81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGR--LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 326 LSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD-----------TKN--CLGDQKLVErLHT 392
Cdd:cd18005 158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSepikrgqrhtaTARelRLGRKRKQE-LAV 236
|
....*....
gi 529013608 393 VLKPFLLRR 401
Cdd:cd18005 237 KLSKFFLRR 245
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
186-401 |
2.69e-45 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350818 [Multi-domain] Cd Length: 222 Bit Score: 162.92 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 265
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEM---------MPG--EWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFK 334
Cdd:cd18060 79 YHGSLASRQMIQQYEMyckdsrgrlIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 335 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
186-401 |
9.56e-43 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 155.57 E-value: 9.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 265
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEM---------MPGEWD--VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFK 334
Cdd:cd18059 79 YHGSQASRRTIQLYEMyfkdpqgrvIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 335 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
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 ... |
186-375 |
1.03e-41 |
|
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: 153.22 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLIS-LYENGVNG------ILADEMGLGKTLQTIALL-GYLKHYRNIPGPhMVLVPKSTLHNWMNEFKRW 257
Cdd:cd18007 1 LKPHQVEGVRFLWSnLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 258 VPSLRVICFV-------GDKDARAAFIRDEMMPGewDVCVTSYEM---VIKEKSVFKKFHWRY-----------LVIDEA 316
Cdd:cd18007 80 LPPDLRPLLVlvslsasKRADARLRKINKWHKEG--GVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 317 HRIKNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF 375
Cdd:cd18007 158 HRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
186-401 |
2.86e-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: 152.05 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLislYE--------NGVNGILADEMGLGKTLQTIALL-GYLKHYRNIPGPH---MVLVPKSTLHNWMNE 253
Cdd:cd18004 1 LRPHQREGVQFL---YDcltgrrgyGGGGAILADEMGLGKTLQAIALVwTLLKQGPYGKPTAkkaLIVCPSSLVGNWKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 254 FKRWVPSLRVICFV--GDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVI-DEAHRIKNEKSKLSEIV 330
Cdd:cd18004 78 FDKWLGLRRIKVVTadGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 331 RDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT-------KNC------LGDQKLvERLHTVLKPF 397
Cdd:cd18004 158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrsrdPDAseedkeLGAERS-QELSELTSRF 236
|
....
gi 529013608 398 LLRR 401
Cdd:cd18004 237 ILRR 240
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
186-401 |
4.32e-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: 145.15 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 265
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDKDARAAFIRDEMMPGE-----------WDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFK 334
Cdd:cd18061 79 YHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529013608 335 STNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTkncLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
186-401 |
2.62e-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: 130.79 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLIslyENGVNGILADEMGLGKTLQTIALLGYLKHYrnipGPHMVLVPKSTLHNWMNEFKRWVPSL---R 262
Cdd:cd18010 1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARaafirdemMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLS-EIVRDFKSTNR-LL 340
Cdd:cd18010 74 IQVIVKSKDGL--------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTkAALPLLKRAKRvIL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529013608 341 LTGTPLQNNLHELWALLNFLLPDVFNSAEDFDS-----------WFDTknclGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18010 146 LSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfgWDYS----GSSNLEELHLLLLATIMIRR 213
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
207-401 |
6.86e-32 |
|
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: 124.90 E-value: 6.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 207 GILADEMGLGKTLQTIALLGYLKHYRN---------------------IP-GPHMVLVPKSTLHNWMNEFKRWVPS--LR 262
Cdd:cd18072 23 GILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASnkLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVG-DKDARAAFIRDemmpgeWDVCVTSYEMVIKE---------KSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRD 332
Cdd:cd18072 103 VCLYHGpNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 333 FKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTKNCLGDqklvERLHTVLKPFLLRR 401
Cdd:cd18072 177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
202-401 |
3.45e-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: 122.96 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 202 ENGVNGILADEMGLGKTLQTIALLgylkhyrnIPGPHMVLVPKSTLHNWMNEFKRWVPS--LRVICFVGdkdarAAFIRD 279
Cdd:cd18071 46 ELVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHG-----GERNRD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 280 EMMPGEWDVCVTSYEMVIKEKSV-----FKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELW 354
Cdd:cd18071 113 PKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 529013608 355 ALLNFLLPDVFNSAEDFDSWFDTKNCLGDQKLVERLHTVLKPFLLRR 401
Cdd:cd18071 193 SLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQVLMKQITLRR 239
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
182-358 |
3.66e-31 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 121.44 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 182 KGGPLRDYQIRGLNWLISLYENGvngILADEMGLGKTLQ-TIALLGYLKhyRNIPGPHMVLVP-KSTLHNWMNEFKRWVP 259
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAaLLPALEALK--RGKGGRVLVLVPtRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 260 SLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIK--EKSVFKKFHWRYLVIDEAHRIKNE--KSKLSEIVRDF-K 334
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLpK 159
|
170 180
....*....|....*....|....
gi 529013608 335 STNRLLLTGTPLQNNLHELWALLN 358
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLN 183
|
|
| HAND |
pfam09110 |
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ... |
761-841 |
8.48e-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: 111.49 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 761 AVDAYFREALRVSEPKV---PKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRNP---DIPNPAVAQRE- 833
Cdd:pfam09110 1 SVDNYYKDVLGTGGKKSttkPKAPRAPKQINIQDHQFFPPRLKELQEKEQLYYKKKIGYKVTLDDgkeEDGEEFEEEREa 80
|
90
....*....|..
gi 529013608 834 ----EQKKIDGA 841
Cdd:pfam09110 81 krklEQEEIDNA 92
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
186-400 |
1.75e-28 |
|
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: 115.52 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLyengvNGILADEMGLGKTLQTIALLgyLKHYRN--------IPGPHMVLVP-----------KST 246
Cdd:cd18070 1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPdndldaadDDSDEMVCCPdclvaetpvssKAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 247 L--------HNWMNEFKRWVP-SLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKE------------KSVFKK 305
Cdd:cd18070 74 LivcpsailAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTElhyaeanrsnrrRRRQKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 306 F----------HWRYLVIDEAHRIKNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAedFDSWF 375
Cdd:cd18070 154 YeappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDS--DWWAR 231
|
250 260
....*....|....*....|....*
gi 529013608 376 DTKNCLGDQKLVERLHTVLKPFLLR 400
Cdd:cd18070 232 VLIRPQGRNKAREPLAALLKELLWR 256
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
186-401 |
9.54e-28 |
|
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: 112.63 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYL---KHYRNIP--GPHMVLVPKSTLHNWMNEFK 255
Cdd:cd18066 1 LRPHQREGIEFLyecvMGMRVNERFGaILADEMGLGKTLQCISLIWTLlrqGPYGGKPviKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 256 RWVPSLRVICFVGDKDARaafIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDFKS 335
Cdd:cd18066 81 KWLGSERIKVFTVDQDHK---VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 336 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD-------------TKNCLGDQKLVErLHTVLKPFLLRR 401
Cdd:cd18066 158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepivrsreptatpEEKKLGEARAAE-LTRLTGLFILRR 235
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
489-615 |
1.58e-27 |
|
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: 107.68 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 489 GKMVVLDKLLAKlkEQGSRVLIFSQMTRLLDIlEDYCMWRGYEYCRLDGQTPHEEREdkflevellgqrEAIEAFNipnS 568
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEERE------------EILEDFR---K 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 529013608 569 SKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIG 615
Cdd:pfam00271 63 GKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
186-401 |
2.56e-26 |
|
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350825 [Multi-domain] Cd Length: 243 Bit Score: 108.71 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWL----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH----MVLVPKSTLHNWMNEFKR 256
Cdd:cd18067 1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 257 WVPSlRVICFVGDKDARAAFIRDEMMPGEWD-------VCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEI 329
Cdd:cd18067 81 WLGG-RLQPLAIDGGSKKEIDRKLVQWASQQgrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 330 VRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-------------DTKNCLGDQKLVErLHTVLKP 396
Cdd:cd18067 160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdadasEKERQLGEEKLQE-LISIVNR 238
|
....*
gi 529013608 397 FLLRR 401
Cdd:cd18067 239 CIIRR 243
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
186-376 |
5.36e-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: 107.59 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLislYEN------------GVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMN 252
Cdd:cd18069 1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVL--LRHTGAKTvLAIVPVNTLQNWLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 253 EFKRWVPSLRVICFVGDKDARAAFIRDEM--------MPGEWD----VCVTSYEMvikeksvfkkFHWR----YLVIDEA 316
Cdd:cd18069 76 EFNKWLPPPEALPNVRPRPFKVFILNDEHkttaarakVIEDWVkdggVLLMGYEM----------FRLRpgpdVVICDEG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 317 HRIKNEKSKLSEIVRDFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD 376
Cdd:cd18069 146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
204-375 |
3.48e-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: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 204 GVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLV--PKSTLHNWMNEFKRWVP------SLRV--ICFVGDKDAR 273
Cdd:cd18068 28 GSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRVLVvcPLNTVLNWLNEFEKWQEglkdeeKIEVneLATYKRPQER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 274 AafirdeMMPGEWD----VCVTSYEMV--------IKEKSVFKKFHWRYL--------VIDEAHRIKNEKSKLSEIVRDF 333
Cdd:cd18068 108 S------YKLQRWQeeggVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 529013608 334 KSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF 375
Cdd:cd18068 182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
186-401 |
3.82e-23 |
|
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: 98.52 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVngILADEMGLGKTLQTIALLGYLKhYRNIPGPHMVLVPKSTLHNWMNEFKRWVpSLRVIC 265
Cdd:cd18011 1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 266 FVGDkDARAAFIRDEMMPGEWDVCVTSYEMV---IKEKSVFKKFHWRYLVIDEAHRIKN----EKSKLSEIVRDF--KST 336
Cdd:cd18011 77 LDRE-TAAQLRRLIGNPFEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 337 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdtknclgdqklVERLHTVLKPFLLRR 401
Cdd:cd18011 156 HVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR-------------LDGLREVLAKVLLRR 207
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
519-615 |
1.55e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.27 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 519 DILEDYCMWRGYEYCRLDGQTPHEEREdkflevellgqrEAIEAFNipnSSKFIFMLSTRAGGLGINLASADVVILYDSD 598
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEERE------------EILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLP 65
|
90
....*....|....*..
gi 529013608 599 WNPQVDLQAMDRAHRIG 615
Cdd:smart00490 66 WSPASYIQRIGRAGRAG 82
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
186-377 |
5.72e-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: 78.16 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLIslyENGVNGILADeMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTL-HNWMNEFKRW--VPSLR 262
Cdd:cd18013 1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 263 VICFVGDKDARAAfirdeMMPGEWDVCVTSYEMVIK-EKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVRDF-KSTNRLL 340
Cdd:cd18013 76 VSVAVGTERQRSK-----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 529013608 341 -LTGTPLQNNLHELWALLNFLlpDVFNSAEDF-----DSWFDT 377
Cdd:cd18013 151 gLTGTPSPNGLMDLWAQIALL--DQGERLGRSitayrERWFDP 191
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
184-771 |
1.59e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 74.68 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 184 GPLRDYQIRGLN-WLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIpgphMVLVPKSTL-HNWMNEFKRWvpsL 261
Cdd:COG1061 79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELlEQWAEELRRF---L 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 262 RVICFVGDKDARaafirdemmpgEWDVCVTSYEMVIKEKSVFK-KFHWRYLVIDEAHRIKNEksKLSEIVRDFKSTNRLL 340
Cdd:COG1061 152 GDPLAGGGKKDS-----------DAPITVATYQSLARRAHLDElGDRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 341 LTGTPL-QNNLHELWALLNFLLPDVfnsaedfdSWfdtknclgdQKLVERlhTVLKPFLLRRIKTDVEkslppkKEIKIY 419
Cdd:COG1061 219 LTATPFrSDGREILLFLFDGIVYEY--------SL---------KEAIED--GYLAPPEYYGIRVDLT------DERAEY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 420 LGLSkmqrEWYTKILMKDidvlnsagkmdkmrllnilmqlrkccnhpylfdgaepgppyttdehivsNSGKMVVLDKLLA 499
Cdd:COG1061 274 DALS----ERLREALAAD-------------------------------------------------AERKDKILRELLR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 500 KLKEQGsRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREdkflevellgqrEAIEAFnipNSSKFIFMLSTRA 579
Cdd:COG1061 301 EHPDDR-KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKERE------------EILEAF---RDGELRILVTVDV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 580 GGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQ-KKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQ 658
Cdd:COG1061 365 LNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 659 QSNKMAKEEMLQMIRHGATHVFASKESELTDEDITTLLERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYR 738
Cdd:COG1061 445 LALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLL 524
|
570 580 590
....*....|....*....|....*....|...
gi 529013608 739 EKQKLGMVEWIEPPKRERKANYAVDAYFREALR 771
Cdd:COG1061 525 KLLLLLLLLLLLELLELLAALLRLEELAALLLK 557
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
185-345 |
7.77e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 61.53 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 185 PLRDYQIRGL-NWLISLYENGVNGILADEMGLGKTL---QTIALLGYLKHYRNIpgphMVLVP-KSTLHNWMNEFKRWVP 259
Cdd:pfam04851 3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLtaaKLIARLFKKGPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 260 SLRVIC--FVGDKDARaafirdemMPGEWDVCVTSYEMV----IKEKSVFKKFHWRYLVIDEAHRIKNEKSKlsEIVRDF 333
Cdd:pfam04851 79 NYVEIGeiISGDKKDE--------SVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYF 148
|
170
....*....|..
gi 529013608 334 KSTNRLLLTGTP 345
Cdd:pfam04851 149 KPAFLLGLTATP 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
186-345 |
2.89e-10 |
|
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: 59.63 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGL-NWLISLYENGvnGILADEMGLGKTLQTIALLGYLKhyrniPGPHMVLVP-KSTLHNWMNEFKRWVPSlRV 263
Cdd:cd17926 1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGD-SS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 264 ICFVGdKDARAAFIrdemmpgEWDVCVTSYEMVIK-EKSVFKKFH-WRYLVIDEAHRIKNEksKLSEIVRDFKSTNRLLL 341
Cdd:cd17926 73 IGLIG-GGKKKDFD-------DANVVVATYQSLSNlAEEEKDLFDqFGLLIVDEAHHLPAK--TFSEILKELNAKYRLGL 142
|
....
gi 529013608 342 TGTP 345
Cdd:cd17926 143 TATP 146
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
206-344 |
1.82e-09 |
|
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: 57.41 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 206 NGILADEMGLGKTLQ-TIALLGYLKHYRnipGPHMVLVPKSTL-HNWMNEFKRWV-PSLRVICFVGDKDARAAFIRDEmm 282
Cdd:cd00046 3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLRELFgPGIRVAVLVGGSSAEEREKNKL-- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 283 pGEWDVCVTSYEMVIKEKSVFKKFH---WRYLVIDEAHRI-KNEKS----KLSEIVRDFKSTNRLLLTGT 344
Cdd:cd00046 78 -GDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlIDSRGalilDLAVRKAGLKNAQVILLSAT 146
|
|
| DpdE |
NF041062 |
protein DpdE; |
209-371 |
5.21e-08 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 57.29 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 209 LADEMGLGKTLQTiallGYL-------KHYRNIpgphMVLVPKSTLHNWMNEfkrwvpsLRVICFVGDkdaraafirdem 281
Cdd:NF041062 175 LADEVGLGKTIEA----GLVirqhlldNPDARV----LVLVPDALVRQWRRE-------LRDKFFLDD------------ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 282 MPGEwDVCVTSYEmvikEKSVFKKFHWRY--LVIDEAHRI--------KNEKSKLSEIVRDFKSTNR-LLLTGTPLQNNL 350
Cdd:NF041062 228 FPGA-RVRVLSHE----EPERWEPLLDAPdlLVVDEAHQLarlawsgdPPERARYRELAALAHAAPRlLLLSATPVLGNE 302
|
170 180
....*....|....*....|...
gi 529013608 351 HELWALLNFLLPDVF--NSAEDF 371
Cdd:NF041062 303 ETFLALLHLLDPDLYplDDLEAF 325
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
862-901 |
3.74e-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: 3.74e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 529013608 862 NWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 901
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKNNWEKIAKELPGRTPKQCRER 40
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
860-901 |
1.29e-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: 1.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 529013608 860 FTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEY 901
Cdd:smart00717 1 KGEWTEEEDELLIELVKKYGKNNWEKIAKELPGRTAEQCRER 42
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
494-633 |
3.74e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 50.88 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 494 LDKLLAKLKEQ-----GSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREdkflevellG-----QREAIEAF 563
Cdd:COG1111 337 LSKLREILKEQlgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASKEGDK---------GltqkeQIEILERF 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 564 NipnSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQamdRAHRIGQKKPVRVFRLITDNTVEE 633
Cdd:COG1111 408 R---AGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDE 471
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
214-345 |
4.56e-06 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 48.01 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 214 GLGKTLqtIALLGYLKH-YRNIPGPH-MVLVPKSTL-HNWMNEFKRW--VPSLRVICFVG--DKDARAAFIRDEmmpgew 286
Cdd:pfam00270 24 GSGKTL--AFLLPALEAlDKLDNGPQaLVLAPTRELaEQIYEELKKLgkGLGLKVASLLGgdSRKEQLEKLKGP------ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529013608 287 DVCVTSYEMV---IKEKSVFKKFhwRYLVIDEAHRIKNE--KSKLSEIVRDF-KSTNRLLLTGTP 345
Cdd:pfam00270 96 DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMgfGPDLEEILRRLpKKRQILLLSATL 158
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
568-626 |
7.27e-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: 7.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 529013608 568 SSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQkKPVRVFRLI 626
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 ... |
186-345 |
8.09e-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: 44.09 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 186 LRDYQIRGLNWLISLYENGVNGILAdEM--GLGKTlqTIALLGYLKHYRNIPGPH-MVLVPKSTL-HNWMNEFKRWVPSL 261
Cdd:cd18032 1 PRYYQQEAIEALEEAREKGQRRALL-VMatGTGKT--YTAAFLIKRLLEANRKKRiLFLAHREELlEQAERSFKEVLPDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 262 RVICFVGDKDAraafirdemmPGEWDVCVTSYEMVIKEK--SVFKKFHWRYLVIDEAHRikNEKSKLSEIVRDFKSTNRL 339
Cdd:cd18032 78 SFGNLKGGKKK----------PDDARVVFATVQTLNKRKrlEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLL 145
|
....*.
gi 529013608 340 LLTGTP 345
Cdd:cd18032 146 GLTATP 151
|
|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
209-371 |
8.46e-05 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 46.75 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 209 LADEMGLGKTLQTiallGYLKHYRNIPGPH---MVLVPKSTLHNWMNEFKRWVpSLRVICFvgDKDARAAFIRDEMMPGE 285
Cdd:PRK04914 174 LADEVGLGKTIEA----GMIIHQQLLTGRAervLILVPETLQHQWLVEMLRRF-NLRFSLF--DEERYAEAQHDADNPFE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 286 WDVCV-TSYEMVIKEKSVFKKF---HWRYLVIDEAHRI---KNEKSKLSEIVRDF--KSTNRLLLTGTPLQNNLHELWAL 356
Cdd:PRK04914 247 TEQLViCSLDFLRRNKQRLEQAlaaEWDLLVVDEAHHLvwsEEAPSREYQVVEQLaeVIPGVLLLTATPEQLGQESHFAR 326
|
170
....*....|....*
gi 529013608 357 LNFLLPDVFNSAEDF 371
Cdd:PRK04914 327 LRLLDPDRFHDYEAF 341
|
|
| DBINO |
pfam13892 |
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ... |
87-113 |
1.30e-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: 1.30e-03
10 20
....*....|....*....|....*...
gi 529013608 87 EEKMKADR-AKRFEFLLKQTELFAHFIQ 113
Cdd:pfam13892 101 EELREAKRqQRKLNFLITQTELYSHFMG 128
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
201-323 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529013608 201 YENGVNGILADEMGLGKTLqtIALLGYLKHYRNiPGPHMVLVPKSTLHNW-MNEFKRW-VPSLRVICFVGDKDARAAFIr 278
Cdd:cd18028 14 LLKGENLLISIPTASGKTL--IAEMAMVNTLLE-GGKALYLVPLRALASEkYEEFKKLeEIGLKVGISTGDYDEDDEWL- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 529013608 279 demmpGEWDVCVTSYEmviKEKSVFK-KFHW----RYLVIDEAHRIKNEK 323
Cdd:cd18028 90 -----GDYDIIVATYE---KFDSLLRhSPSWlrdvGVVVVDEIHLISDEE 131
|
|
| |
