|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
19-1011 |
0e+00 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 1699.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 19 PVAPGGTEETPAvEDTTANDAEASPATadaSEDPSGAEGAAAIALAKAEKARLRQLKKQQREEIEKVRLQQNAAIAKDNS 98
Cdd:PLN03142 17 ELEAVARSAGSD-SDDDEVPAEDEDED---EEDDEEAESPAKAEISKREKARLKELKKQKKQEIQKILEQQNAAIDADMN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 99 G---GKWKYLMQQTEVFSHFLAGTKAHNAKKGGRRSKQA----EDAEDHELVEAAEE----YHAVRLTVQPECIKfGKMR 167
Cdd:PLN03142 93 NkgkGRLKYLLQQTEIFAHFAKGDQSASAKKAKGRGRHAskltEEEEDEEYLKEEEDglggSGGTRLLVQPSCIK-GKMR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 168 EYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFH 247
Cdd:PLN03142 172 DYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 248 GNQEARAAQKAQYLDKNNaFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPL 327
Cdd:PLN03142 252 GNPEERAHQREELLVAGK-FDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 328 QNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTEVVQQLHKVLRPFLLRRLKAEVEKNLPPKKEMILKVGMSEMQ 407
Cdd:PLN03142 331 QNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 408 KEYYKRALQKDIQVVNSGGDRSRLLNMVMQLRKCCNHPYLFQGAEPGPPFFTDEHLVENSGKMVLLDKLLKKLKEKGSRV 487
Cdd:PLN03142 411 KQYYKALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 488 LIFSQMTRLLDILEDYLLFRRYKYCRIDGNTDGDTREDMIDSYNAPGSEKFVFLLSTRAGGLGINLTTADTVVIYDSDWN 567
Cdd:PLN03142 491 LIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWN 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 568 PQMDLQAMDRAHRIGQTKEVSVFRFCTDGSVEEKVIEKAYKKLALDALVIQQGRLQEnQKNVNKEELLSMVRFGADKIFD 647
Cdd:PLN03142 571 PQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAE-QKTVNKDELLQMVRYGAEMVFS 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 648 gTTNSTITDEDIDTIIAKGEDETKLLNEKMAGFTDKALKFSMDADASLYEFEDKEAADSKEafegLDVKAVIAQGWIDPP 727
Cdd:PLN03142 650 -SKDSTITDEDIDRIIAKGEEATAELDAKMKKFTEDAIKFKMDDTAELYDFDDEDDKDENK----LDFKKIVSDNWIDPP 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 728 KRERKKNYNESDYYRDVMNQGPrKPAASGPRILKLQNMSDFQFYEVPRITELYNKEVaRKQYEWHREKQLEALQNNAvpq 807
Cdd:PLN03142 725 KRERKRNYSESEYFKQAMRQGA-PAKPKEPRIPRMPQLHDFQFFNVQRLTELYEKEV-RYLMQAHQKGQLKDTIDVA--- 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 808 dlPPEEPTApkPLTDAERDEYEQKLNGGFKDWNRRDFQAFCRAAEKYGRADAEGMASEIEGKTLEEVKEYNAVFWQRYTE 887
Cdd:PLN03142 800 --EPEEPGD--PLTAEEQEEKEQLLEEGFSTWSRRDFNAFIRACEKYGRNDIKSIASEMEGKTEEEVERYAKVFWERYKE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 888 IADYKRILGNIERGEAKLQRQNEMLKNVKRKLEMYKNPWRDLKLVYGsSSKVKSYTEEEDRFLLCSIPEVGFGNWEELKA 967
Cdd:PLN03142 876 LNDYDRIIKNIERGEARISRKDEIMKAIGKKLDRYKNPWLELKIQYG-QNKGKLYNEECDRFMLCMVHKLGYGNWDELKA 954
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 255079182 968 QIRQHWLFRFDWFIKSRTPKELQRRIETLINLVEKEFEEVDKKR 1011
Cdd:PLN03142 955 AFRTSPLFRFDWFVKSRTPQELARRCDTLIRLIEKENQEYDERE 998
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
41-618 |
2.52e-142 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 441.97 E-value: 2.52e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 41 ASPATADASEDPSGAEGAAAIALAKAEKARLRQLKKQQREEIEKVRLQQNAAIAKDNSGGKWKYLMQQTEVFSHFLAGTK 120
Cdd:COG0553 118 LSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 121 AHNAKKGGRRSKQAEDAEDHELVEAAEEYHAVRLTVQPECIKfGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQ 200
Cdd:COG0553 198 EAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLK-ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 201 TISLLGYLSEyRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFHGNQEaRAAQKAQYLDknnaFDVCVTSYEMVIKE 280
Cdd:COG0553 277 ALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPFED----ADLVITSYGLLRRD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 281 KNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGT 360
Cdd:COG0553 351 IELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 361 EGDNTEVVQQLHKVLRPFLLRRLKAEVEKNLPPKKEMILKVGMSEMQKEYYKRALQK-DIQVVNSGGDRSR--LLNMVMQ 437
Cdd:COG0553 431 EKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYlRRELEGAEGIRRRglILAALTR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 438 LRKCCNHPYLFQGaepgppffTDEHLVENSGKMVLLDKLLKKLKEKGSRVLIFSQMTRLLDILEDYLLFRRYKYCRIDGN 517
Cdd:COG0553 511 LRQICSHPALLLE--------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGG 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 518 TDGDTREDMIDSYNApGSEKFVFLLSTRAGGLGINLTTADTVVIYDSDWNPQMDLQAMDRAHRIGQTKEVSVFRFCTDGS 597
Cdd:COG0553 583 TSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
|
570 580
....*....|....*....|.
gi 255079182 598 VEEKVIEKAYKKLALDALVIQ 618
Cdd:COG0553 662 IEEKILELLEEKRALAESVLG 682
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
163-384 |
2.14e-133 |
|
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: 401.31 E-value: 2.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 163 FGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIR 242
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHGNQEARAAQKAQYLdKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLI 322
Cdd:cd17997 81 VVVLIGDKEERADIIRDVL-LPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255079182 323 TGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGT-EGDNTEVVQQLHKVLRPFLLRRLK 384
Cdd:cd17997 160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNcDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
169-448 |
3.58e-119 |
|
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: 367.01 E-value: 3.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 169 YQLAGLNWMIRLF-DHGINGILADEMGLGKTLQTISLLGYLSEYRGITG-PHMVVVPKSTLGNWMNEFKRWC--PMIRPF 244
Cdd:pfam00176 1 YQIEGVNWMLSLEnNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 245 KFHGNQEARAAQKaQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITG 324
Cdd:pfam00176 81 VLHGNKRPQERWK-NDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 325 TPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTG-TEGDNTEVVQQLHKVLRPFLLRRLKAEVEKNLPPKKEMILKVGM 403
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPiERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 255079182 404 SEMQKEYYKRALQ-KDIQVVNSG----GDRSRLLNMVMQLRKCCNHPYLF 448
Cdd:pfam00176 240 SKLQRKLYQTFLLkKDLNAIKTGeggrEIKASLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
153-395 |
3.34e-104 |
|
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: 325.85 E-value: 3.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 153 RLTVQPECIKFGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMN 232
Cdd:cd18064 3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 233 EFKRWCPMIRPFKFHGNQEARAAQKAQYLDKNNaFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMR 312
Cdd:cd18064 83 EFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGE-WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 313 MFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTEVVQQLHKVLRPFLLRRLKAEVEKNLP 392
Cdd:cd18064 162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLP 241
|
...
gi 255079182 393 PKK 395
Cdd:cd18064 242 PKK 244
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
152-384 |
4.43e-99 |
|
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: 311.57 E-value: 4.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 152 VRLTVQPECIKFGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWM 231
Cdd:cd18065 2 VRFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 232 NEFKRWCPMIRPFKFHGNQEARAAQKAQYLdKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVM 311
Cdd:cd18065 82 NEFKRWVPSLRAVCLIGDKDARAAFIRDVM-MPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255079182 312 RMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTEVVQQLHKVLRPFLLRRLK 384
Cdd:cd18065 161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
164-384 |
1.06e-97 |
|
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: 308.16 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 164 GKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEyRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRP 243
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 244 FKFHGNQEAR---AAQKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRL 320
Cdd:cd18009 81 LLYHGTKEERerlRKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255079182 321 LITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTE------------VVQQLHKVLRPFLLRRLK 384
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAAdisnlseereqnIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
164-384 |
1.07e-94 |
|
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: 300.05 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 164 GKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRP 243
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 244 FKFHGNQEARAAQKAQYldKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVM-RMFACNNRLLI 322
Cdd:cd17996 82 IVYKGTPDVRKKLQSQI--RAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYRLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255079182 323 TGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWF-----GTGTEGD---NTE----VVQQLHKVLRPFLLRRLK 384
Cdd:cd17996 160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFntpfaNTGEQVKielNEEetllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
166-382 |
7.99e-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: 286.56 E-value: 7.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAAqKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGT 325
Cdd:cd18003 81 YYGSAKERKL-KRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255079182 326 PLQNNLHELWALLNFLLPEVFGDAGQFEEWFG-------TGTEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18003 160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
166-346 |
1.55e-89 |
|
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: 284.07 E-value: 1.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAAQKAQylDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGT 325
Cdd:cd17919 81 YHGSQRERAQIRAK--EKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGT 158
|
170 180
....*....|....*....|.
gi 255079182 326 PLQNNLHELWALLNFLLPEVF 346
Cdd:cd17919 159 PLQNNLEELWALLDFLDPPFL 179
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
166-382 |
2.36e-81 |
|
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: 263.73 E-value: 2.36e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMiRPFK 245
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDM-NVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARA-AQKAQYLDKNNA---------FDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFA 315
Cdd:cd17995 80 YHGSGESRQiIQQYEMYFKDAQgrkkkgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255079182 316 CNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevVQQLHKVLRPFLLRR 382
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQ---VEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
165-382 |
1.40e-73 |
|
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: 242.26 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 165 KMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPF 244
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 245 KFHGNQEARAA--QKAQYLDKNN--AFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRL 320
Cdd:cd17993 81 VYLGDIKSRDTirEYEFYFSQTKklKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255079182 321 LITGTPLQNNLHELWALLNFLLPevfgdaGQFEEW--FGTGTEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd17993 161 LITGTPLQNSLKELWALLHFLMP------GKFDIWeeFEEEHDEEQEKGIADLHKELEPFILRR 218
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
166-382 |
7.85e-73 |
|
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350760 [Multi-domain] Cd Length: 229 Bit Score: 240.48 E-value: 7.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAA------QKAQYLdKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNR 319
Cdd:cd18002 81 YWGNPKDRKVlrkfwdRKNLYT-RDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 320 LLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTE-------GDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18002 160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshaenktGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
150-384 |
8.09e-70 |
|
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: 233.01 E-value: 8.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 150 HAV--RLTVQPECIKFGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTL 227
Cdd:cd18062 6 HAVteKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 228 GNWMNEFKRWCPMIRPFKFHGNQEARAAQKAQYldKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRL 307
Cdd:cd18062 86 SNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQL--RSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 308 SKVMRM-FACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFG-----TGTEGDNTE-----VVQQLHKVLR 376
Cdd:cd18062 164 TQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamTGEKVDLNEeetilIIRRLHKVLR 243
|
....*...
gi 255079182 377 PFLLRRLK 384
Cdd:cd18062 244 PFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
150-384 |
1.39e-69 |
|
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350821 [Multi-domain] Cd Length: 251 Bit Score: 232.65 E-value: 1.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 150 HAV--RLTVQPECIKFGKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTL 227
Cdd:cd18063 6 HAIteRVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 228 GNWMNEFKRWCPMIRPFKFHGNQEARAAQKAQYldKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRL 307
Cdd:cd18063 86 SNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQL--RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 308 SKVMRM-FACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFG-----TGTEGDNTE-----VVQQLHKVLR 376
Cdd:cd18063 164 TQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamTGERVDLNEeetilIIRRLHKVLR 243
|
....*...
gi 255079182 377 PFLLRRLK 384
Cdd:cd18063 244 PFLLRRLK 251
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
164-384 |
1.53e-69 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 230.92 E-value: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 164 GKMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLgyLSEYR-GITGPHMVVVPKSTLGNWMNEFKRWCPMIR 242
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALL--LSRKEeGRKGPSLVVAPTSLIYNWEEEAAKFAPELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHGNQEARAAQKAQyldknNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLI 322
Cdd:cd18012 81 VLVIHGTKRKREKLRAL-----EDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255079182 323 TGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDN-TEVVQQLHKVLRPFLLRRLK 384
Cdd:cd18012 156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdEEALEELKKLISPFILRRLK 218
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
166-382 |
3.82e-67 |
|
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: 224.24 E-value: 3.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAAQKaQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGT 325
Cdd:cd18006 81 YMGDKEKRLDLQ-QDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255079182 326 PLQNNLHELWALLNFLLPEVFG--DAGQFEEWFgtGTEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18006 160 PIQNSLQELYALLSFIEPNVFPkdKLDDFIKAY--SETDDESETVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
166-346 |
2.23e-64 |
|
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: 215.33 E-value: 2.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEyRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAAQKAQYLDKNNAFDVCVTSYEMVI---KEKNALKKFHWRYIIIDEAHRIKNENS-RLSKVMRMFAcNNRLL 321
Cdd:cd17998 80 YYGSQEERKHLRYDILKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSeRYRHLMTINA-NFRLL 158
|
170 180
....*....|....*....|....*
gi 255079182 322 ITGTPLQNNLHELWALLNFLLPEVF 346
Cdd:cd17998 159 LTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
165-382 |
1.05e-62 |
|
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: 212.94 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 165 KMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPF 244
Cdd:cd18054 20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 245 KFHGNQEARAAQK----AQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRL 320
Cdd:cd18054 100 VYIGDLMSRNTIReyewIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255079182 321 LITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDntevVQQLHKVLRPFLLRR 382
Cdd:cd18054 180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRR 237
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
166-382 |
4.31e-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: 191.03 E-value: 4.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLL-----GYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCP- 239
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILasdhhKRANSFNSENLPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 240 -MIRPFKFHGNQEARAAQKAQYLDKNnafdVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNN 318
Cdd:cd17999 81 aFLKPLAYVGPPQERRRLREQGEKHN----VIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255079182 319 RLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFG--------TGTEGDNTE----VVQQLHKVLRPFLLRR 382
Cdd:cd17999 157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrdSKASAKEQEagalALEALHKQVLPFLLRR 232
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
168-382 |
1.11e-54 |
|
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: 189.89 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 168 EYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEyRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFH 247
Cdd:cd18001 3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFD-SGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 248 GnqeARAAQKAQYLDK-NNAFDVCVTSYEMVIKEKNAL-----KKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLL 321
Cdd:cd18001 82 G---TSKKERERNLERiQRGGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255079182 322 ITGTPLQNNLHELWALLNFLLP-EVFGDAGQFEEWFGT----GTEGDNT--------EVVQQLHKVLRPFLLRR 382
Cdd:cd18001 159 LTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENpitrGRDKDATqgekalgsEVAENLRQIIKPYFLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
165-382 |
2.45e-54 |
|
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: 189.11 E-value: 2.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 165 KMREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPF 244
Cdd:cd18053 20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 245 KFHGNQEARAAQKAQYL----DKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRL 320
Cdd:cd18053 100 VYLGDINSRNMIRTHEWmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255079182 321 LITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTevvqQLHKVLRPFLLRR 382
Cdd:cd18053 180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYA----SLHKELEPFLLRR 237
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
461-593 |
1.53e-53 |
|
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: 182.68 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 461 EHLVenSGKMVLLDKLLKKLKEKGSRVLIFSQMTRLLDILEDYLLFRRYKYCRIDGNTDGDTREDMIDSYNAPGSEkFVF 540
Cdd:cd18793 6 EEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVF 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 255079182 541 LLSTRAGGLGINLTTADTVVIYDSDWNPQMDLQAMDRAHRIGQTKEVSVFRFC 593
Cdd:cd18793 83 LLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
168-343 |
8.52e-51 |
|
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: 177.52 E-value: 8.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 168 EYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFH 247
Cdd:cd18000 3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 248 --------GNQEARAAQKAQYLDK-NNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNN 318
Cdd:cd18000 83 ssgsgtgsEEKLGSIERKSQLIRKvVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
|
170 180
....*....|....*....|....*
gi 255079182 319 RLLITGTPLQNNLHELWALLNFLLP 343
Cdd:cd18000 163 RLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
166-382 |
1.18e-50 |
|
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: 178.31 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISllgYLSE--YRGITGPHMVVVPKSTLGNWMNEFKRWCPMiRP 243
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIT---FLSEifLMGIRGPFLIIAPLSTITNWEREFRTWTEM-NA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 244 FKFHGNQEARAA----------QKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRM 313
Cdd:cd18058 77 IVYHGSQISRQMiqqyemyyrdEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255079182 314 FACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGtgtEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18058 157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG---DLKTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
166-382 |
7.40e-50 |
|
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: 174.94 E-value: 7.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQearaaqkaqyldknnafdVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGT 325
Cdd:cd17994 81 YVGDH------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255079182 326 PLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevVQQLHKVLRPFLLRR 382
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 196
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
167-382 |
2.36e-49 |
|
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: 175.17 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 167 REYQLAGLNWMIRlfdHGinGILADEMGLGKTLQTISL-LGYLSEYRGITGPHM----------------VVVPKSTLGN 229
Cdd:cd18008 2 LPYQKQGLAWMLP---RG--GILADEMGLGKTIQALALiLATRPQDPKIPEELEenssdpkklylskttlIVVPLSLLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 230 WMNEFKR--WCPMIRPFKFHGNQEARAAQKAQyldknnAFDVCVTSYEMV----------------IKEKNALKKFHWRY 291
Cdd:cd18008 77 WKDEIEKhtKPGSLKVYVYHGSKRIKSIEELS------DYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 292 IIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNTEVVQQL 371
Cdd:cd18008 151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERL 230
|
250
....*....|.
gi 255079182 372 HKVLRPFLLRR 382
Cdd:cd18008 231 QALLKPILLRR 241
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
166-382 |
4.71e-48 |
|
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: 170.62 E-value: 4.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYrGITGPHMVVVPKSTLGNWMNEFKRWCPMiRPFK 245
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAA----------QKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFA 315
Cdd:cd18060 79 YHGSLASRQMiqqyemyckdSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255079182 316 CNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGtgtEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---DLKTEEQVQKLQAILKPMMLRR 222
|
|
| SLIDE |
pfam09111 |
SLIDE; The SLIDE domain adopts a secondary structure comprising a main core of three ... |
893-1004 |
5.59e-48 |
|
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: 166.16 E-value: 5.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 893 RILGNIERGEAKLQRQNEMLKNVKRKLEMYKNPWRDLKLVYGSSSKVKSYTEEEDRFLLCSIPEVGFGN---WEELKAQI 969
Cdd:pfam09111 2 KYIKQIERGEKKIEKLKEQQELLRRKISQYKNPLQELKINYPPNNKGKTYTEEEDRFLLCMLYKYGYGNedlYEKIKQEI 81
|
90 100 110
....*....|....*....|....*....|....*
gi 255079182 970 RQHWLFRFDWFIKSRTPKELQRRIETLINLVEKEF 1004
Cdd:pfam09111 82 RESPLFRFDWFFKSRTPQELQRRCNTLLKLIEKEF 116
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
166-382 |
3.65e-46 |
|
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: 166.02 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLG------------YLSEYRGITGPH--------MVVVPKS 225
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrENNRPRFKKKPPassakkpvLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 226 TLGNWMNEFKRWcPMIRPFKFHGNQEARAAQKAQyldKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENS 305
Cdd:cd18005 81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGRL---KAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 306 RLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFG---------TGTEGD---NTEVVQQLHK 373
Cdd:cd18005 157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSepikrgqrhTATARElrlGRKRKQELAV 236
|
....*....
gi 255079182 374 VLRPFLLRR 382
Cdd:cd18005 237 KLSKFFLRR 245
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
166-382 |
1.19e-45 |
|
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: 163.66 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLgYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMiRPFK 245
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTEL-NVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAAQKA----------QYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFA 315
Cdd:cd18059 79 YHGSQASRRTIQLyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255079182 316 CNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGtgtEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG---DLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
169-382 |
2.15e-45 |
|
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: 163.26 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 169 YQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFHG 248
Cdd:cd18055 4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 249 NQEARAA-QKAQYLDKNNA-----------------FDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKV 310
Cdd:cd18055 84 DKDSRAIiRENEFSFDDNAvkggkkafkmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255079182 311 MRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevVQQLHKVLRPFLLRR 382
Cdd:cd18055 164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
166-382 |
5.51e-44 |
|
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: 159.46 E-value: 5.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARAA-QKAQYLDKNNA-----------------FDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRL 307
Cdd:cd18057 81 YTGDKESRSViRENEFSFEDNAirsgkkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255079182 308 SKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevVQQLHKVLRPFLLRR 382
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRR 232
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
166-382 |
3.34e-43 |
|
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: 157.45 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWM----IRLFDHGING-ILADEMGLGKTLQTISLLGYLSEYRGITGPH----MVVVPKSTLGNWMNEFKR 236
Cdd:cd18004 1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 237 WCP--MIRPFKFHGNQEARAAQKAQYLdKNNAFDVCVTSYEMV---IKEKNALKKFHwrYIIIDEAHRIKNENSRLSKVM 311
Cdd:cd18004 81 WLGlrRIKVVTADGNAKDVKASLDFFS-SASTYPVLIISYETLrrhAEKLSKKISID--LLICDEGHRLKNSESKTTKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 312 RMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGT----GTEGDNTE--------VVQQLHKVLRPFL 379
Cdd:cd18004 158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrSRDPDASEedkelgaeRSQELSELTSRFI 237
|
...
gi 255079182 380 LRR 382
Cdd:cd18004 238 LRR 240
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
166-382 |
2.44e-42 |
|
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: 154.84 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPMIRPFK 245
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARA----------------AQKAQYLDKNNA--FDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRL 307
Cdd:cd18056 81 YVGDKDSRAiirenefsfednairgGKKASRMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255079182 308 SKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevVQQLHKVLRPFLLRR 382
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ---IKKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
166-382 |
1.70e-41 |
|
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: 151.70 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLFDHGINGILADEMGLGKTLQTISLLgYLSEYRGITGPHMVVVPKSTLGNWMNEFKRWCPmIRPFK 245
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWTD-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 246 FHGNQEARA--AQKAQYLDKNNA--------FDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFA 315
Cdd:cd18061 79 YHGSLISRQmiQQYEMYFRDSQGriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255079182 316 CNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGtgtEGDNTEVVQQLHKVLRPFLLRR 382
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG---DLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
188-367 |
1.03e-38 |
|
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: 144.36 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 188 ILADEMGLGKTLQTISLL-GYLSEYRGITGPhMVVVPKSTLGNWMNEFKRWCP-MIRPFkfHGNQEARAAQKA-QYLDKN 264
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKWLPpDLRPL--LVLVSLSASKRAdARLRKI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 265 NAF----DVCVTSYEM---VIKEKNALKKFHWRY-----------IIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTP 326
Cdd:cd18007 107 NKWhkegGVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255079182 327 LQNNLHELWALLNFLLPEVFGDAGQFEEWF----GTGTEGDNTEV 367
Cdd:cd18007 187 LQNNLKEYWTMVDFARPKYLGTLKEFKKKFvkpiEAGQCVDSTEE 231
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
162-344 |
8.05e-31 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 120.29 E-value: 8.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 162 KFGKMREYQLAGLNWMIRLFDhgiNGILADEMGLGKTLQ-TISLLGYLseYRGITGPHMVVVP-KSTLGNWMNEFKRWCP 239
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAaLLPALEAL--KRGKGGRVLVLVPtRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 240 --MIRPFKFHGNQEARAAQKAQyldKNNAFDVCVTSYEMVIK--EKNALKKFHWRYIIIDEAHRIKNENSR---LSKVMR 312
Cdd:smart00487 80 slGLKVVGLYGGDSKREQLRKL---ESGKTDILVTTPGRLLDllENDKLSLSNVDLVILDEAHRLLDGGFGdqlEKLLKL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 255079182 313 MFACNNRLLITGTP---LQNNLHELWALLNFLLPE 344
Cdd:smart00487 157 LPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVG 191
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
169-382 |
2.10e-29 |
|
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: 116.54 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 169 YQLAGLNWMIRlfdHGINGILADEMGLGKTLQTISLLGYLSEYrgitGPHMVVVPKSTLGNWMNEFKRWCPMIRPFKFH- 247
Cdd:cd18010 4 FQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLPPDDIQv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 248 --GNQEARAAQKAQyldknnafdVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMR--MFACNNRLLIT 323
Cdd:cd18010 77 ivKSKDGLRDGDAK---------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALplLKRAKRVILLS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255079182 324 GTPLQNNLHELWALLNFLLPEVFGD---------AGQFEEWFGTGTEGDNTEvvqQLHKVLRP-FLLRR 382
Cdd:cd18010 148 GTPALSRPIELFTQLDALDPKLFGRfhdfgrrycAAKQGGFGWDYSGSSNLE---ELHLLLLAtIMIRR 213
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
166-382 |
3.51e-29 |
|
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: 117.19 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIRLF----DHGING-ILADEMGLGKTLQTISLLGYLSEYRGITGPH----MVVVPKSTLGNWMNEFKR 236
Cdd:cd18067 1 LRPHQREGVKFLYRCVtgrrIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEidkaIVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 237 WC-PMIRPFKFHGNQEA----RAAQKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVM 311
Cdd:cd18067 81 WLgGRLQPLAIDGGSKKeidrKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 312 RMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWF---------GTGTEGDNT---EVVQQLHKVLRPFL 379
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADASEKERQlgeEKLQELISIVNRCI 240
|
...
gi 255079182 380 LRR 382
Cdd:cd18067 241 IRR 243
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
188-356 |
6.60e-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: 113.02 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 188 ILADEMGLGKTLQTISLLGYLSEyRGITGPH------MVVVPKSTLGNWMNEFKRWCPMIRPFKFHGNQEaraaQKAQYL 261
Cdd:cd18066 28 ILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQD----HKVEEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 262 DKNNAFDVCVTSYEMVIKEKNALKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFL 341
Cdd:cd18066 103 IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFV 182
|
170
....*....|....*
gi 255079182 342 LPEVFGDAGQFEEWF 356
Cdd:cd18066 183 NPGILGSLSTYRKVY 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
484-582 |
1.02e-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: 108.07 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 484 GSRVLIFSQMTRLLDilEDYLLFRR-YKYCRIDGNTDGDTREDMIDSYNapgSEKFVFLLSTRAGGLGINLTTADTVVIY 562
Cdd:pfam00271 15 GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDVAERGLDLPDVDLVINY 89
|
90 100
....*....|....*....|
gi 255079182 563 DSDWNPQMDLQAMDRAHRIG 582
Cdd:pfam00271 90 DLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
183-382 |
2.89e-27 |
|
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: 111.41 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 183 HGinGILADEMGLGKTLQTISLLgylseyrgITGPHMVVVPKSTLGNWMNEFKRwcpMIRP-----FKFHGNQEARAAQK 257
Cdd:cd18071 49 RG--GILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEE---HVKPgqlkvYTYHGGERNRDPKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 258 aqyLDKnnaFDVCVTSYEMVIKEKNA-----LKKFHWRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLH 332
Cdd:cd18071 116 ---LSK---YDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255079182 333 ELWALLNFLLPEVFGDagqfEEWFGTG-----TEGDNTEvVQQLHKVLRPFLLRR 382
Cdd:cd18071 190 DLGSLLSFLHLKPFSN----PEYWRRLiqrplTMGDPTG-LKRLQVLMKQITLRR 239
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
187-382 |
1.17e-26 |
|
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: 109.88 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 187 GILADEMGLGKTLQTISLLGY----------------------LSEYRGITGPHMVVVPKSTLGNWMNEFKRWCP--MIR 242
Cdd:cd18072 23 GILADDMGLGKTLTMIALILAqkntqnrkeeekekalteweskKDSTLVPSAGTLVVCPASLVHQWKNEVESRVAsnKLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHG-NQEARAAQKAQYldknnafDVCVTSYEMVIKE---------KNALKKFHWRYIIIDEAHRIKNENSRLS-KVM 311
Cdd:cd18072 103 VCLYHGpNRERIGEVLRDY-------DIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASiAVC 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255079182 312 RMFACNnRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWFGTGTEGDNtevvQQLHKVLRPFLLRR 382
Cdd:cd18072 176 KLRAHA-RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG----ERLNILTKSLLLRR 241
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
182-356 |
1.86e-25 |
|
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: 105.67 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 182 DHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPhMVVVPKSTLGNWMNEFKRWCP--------MIRPFKFH--GNQE 251
Cdd:cd18069 26 SSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTV-LAIVPVNTLQNWLSEFNKWLPppealpnvRPRPFKVFilNDEH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 252 ARAAQKAQYLDK-NNAFDVCVTSYEMvikeknalkkFHWR----YIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTP 326
Cdd:cd18069 105 KTTAARAKVIEDwVKDGGVLLMGYEM----------FRLRpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYP 174
|
170 180 190
....*....|....*....|....*....|
gi 255079182 327 LQNNLHELWALLNFLLPEVFGDAGQFEEWF 356
Cdd:cd18069 175 LQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 204
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
166-367 |
5.86e-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: 104.97 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWM---------IRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITGPH--MVVVPKSTLGNWMNEF 234
Cdd:cd18068 1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSrvLVVCPLNTVLNWLNEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 235 KRWCPMI-RPFKFHGNQEARAAQKAQYLDKNNAFD----VCVTSYEMV--------IKEKNALKKFHWRY--------II 293
Cdd:cd18068 81 EKWQEGLkDEEKIEVNELATYKRPQERSYKLQRWQeeggVMIIGYDMYrilaqernVKSREKLKEIFNKAlvdpgpdfVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255079182 294 IDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEEWF----GTGTEGDNTEV 367
Cdd:cd18068 161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFvnpiQNGQCADSTLV 238
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
498-582 |
2.33e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.59 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 498 DILEDYLLFRRYKYCRIDGNTDGDTREDMIDSYNapgSEKFVFLLSTRAGGLGINLTTADTVVIYDSDWNPQMDLQAMDR 577
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 255079182 578 AHRIG 582
Cdd:smart00490 78 AGRAG 82
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
169-354 |
1.14e-22 |
|
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: 96.97 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 169 YQLAGLNwmiRLFDHGING-ILADEMGLGKTLQTISLLGYLsEYRGITGPHMVVVPKSTLGNWMNEFKRwcpmirpfKFH 247
Cdd:cd18011 4 HQIDAVL---RALRKPPVRlLLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQD--------KFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 248 GNQE---ARAAQKAQYLDKN--NAFDVCVTSYEMV---IKEKNALKKFHWRYIIIDEAHRIKNEN----SRLSKVMRMFA 315
Cdd:cd18011 72 LPFLildRETAAQLRRLIGNpfEEFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKLGRLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255079182 316 CNNR--LLITGTPLQNNLHELWALLNFLLPEVFGDAGQFEE 354
Cdd:cd18011 152 KRARhvLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
166-381 |
1.03e-17 |
|
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: 83.93 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIrlfDHGinGILADEMGLGKTLQTISLL------------GYLSEYRGITGPHM-------------V 220
Cdd:cd18070 1 LLPYQRRAVNWML---VPG--GILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDClvaetpvsskatlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 221 VVPKSTLGNWMNEFKRWCPM-IRPFKFHGnQEARAAQKAQYLDKNNAFDVCVTSYEMVIKEKNALKKFH----------- 288
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPSsLKVLTYQG-VKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkry 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 289 -----------WRYIIIDEAHRIKNENSRLSKVMRMFACNNRLLITGTPLQNNLHELWALLNFLLPEVFgDAGQFEEWFG 357
Cdd:cd18070 155 eappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPF-CDSDWWARVL 233
|
250 260
....*....|....*....|....
gi 255079182 358 TGTEGDNtEVVQQLHKVLRPFLLR 381
Cdd:cd18070 234 IRPQGRN-KAREPLAALLKELLWR 256
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
166-341 |
4.14e-12 |
|
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: 66.60 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNWMIrlfDHGINGILADeMGLGKTLQTISLLGYLSEyRGITGPHMVVVPKSTLGN-WMNEFKRWCPMIRPF 244
Cdd:cd18013 1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 245 KFHGNQEARAAQKAqyLDKNNafDVCVTSYEMV---IKEKNalKKFHWRYIIIDEAHRIKNENS-RLSKVMRMFACNNRL 320
Cdd:cd18013 76 VSVAVGTERQRSKA--ANTPA--DLYVINRENLkwlVNKSG--DPWPFDMVVIDELSSFKSPRSkRFKALRKVRPVIKRL 149
|
170 180
....*....|....*....|..
gi 255079182 321 L-ITGTPLQNNLHELWALLNFL 341
Cdd:cd18013 150 IgLTGTPSPNGLMDLWAQIALL 171
|
|
| HAND |
pfam09110 |
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ... |
739-830 |
7.27e-10 |
|
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: 57.18 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 739 DYYRDVMNQGPRK--PAASGPRILKLQNMSDFQFYEvPRITELYNKEVA--RKQYEW-----------------HREKQL 797
Cdd:pfam09110 4 NYYKDVLGTGGKKstTKPKAPRAPKQINIQDHQFFP-PRLKELQEKEQLyyKKKIGYkvtlddgkeedgeefeeEREAKR 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 255079182 798 EALQ---NNAVpqdlppeeptapkPLTDAERDEYEQ 830
Cdd:pfam09110 83 KLEQeeiDNAE-------------PLTEEEEAEKEE 105
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
164-733 |
3.14e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 60.81 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 164 GKMREYQLAGLN-WMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITgphmVVVPKSTLGN-WMNEFKRWCPMI 241
Cdd:COG1061 79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVL----VLVPRRELLEqWAEELRRFLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 242 RpfkFHGNQearaaqkaqyldKNNAFDVCVTSYEMVIKEKNaLKKF--HWRYIIIDEAHRIKNEnsRLSKVMRMFACNNR 319
Cdd:COG1061 155 L---AGGGK------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 320 LLITGTPL-QNNLHELWALLNFLLPEVfgDAGQFEEwfgtgtegdntevvqqlHKVLRPFLLrrlkaeveknlppkkeMI 398
Cdd:COG1061 217 LGLTATPFrSDGREILLFLFDGIVYEY--SLKEAIE-----------------DGYLAPPEY----------------YG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 399 LKVGMSEMQKEyYKRALQKDIQVVNSGGDRSRLLnmvmqlrkccnhpylfqgaepgppffTDEHLVENSGKMvlldkllk 478
Cdd:COG1061 262 IRVDLTDERAE-YDALSERLREALAADAERKDKI--------------------------LRELLREHPDDR-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 479 klkekgsRVLIFSQMTRLLDILEDYLLFRRYKYCRIDGNTDGDTREDMIDSYNapgSEKFVFLLSTRAGGLGINLTTADT 558
Cdd:COG1061 307 -------KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 559 VVIYDSDWNPQMDLQAMDRAHRIGQTKE-VSVFRFCTDGSVEEKVIEKAYKKLALDALVIQQGRLQENQKNVNKEELLSM 637
Cdd:COG1061 377 AILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 638 VRFGaDKIFDGTTNSTITDEDIDTIIAKGEDETKLLNEKMAGFTDKALKFSMDADASLYEFEDKEAADSKEAFEGLDVKA 717
Cdd:COG1061 457 VKGE-LEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLL 535
|
570
....*....|....*.
gi 255079182 718 VIAQGWIDPPKRERKK 733
Cdd:COG1061 536 LELLELLAALLRLEEL 551
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
166-326 |
1.71e-08 |
|
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: 54.23 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 166 MREYQLAGLNwmiRLFDHGIN--GILADEMGLGKTLQTISLLGYLSEYRGItgphmVVVPKSTLGN-WMNEFKRWCPMIR 242
Cdd:cd17926 1 LRPYQEEALE---AWLAHKNNrrGILVLPTGSGKTLTALALIAYLKELRTL-----IVVPTDALLDqWKERFEDFLGDSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHGNqearaaqkaqYLDKNNAFDVCVTSYEMVIKEKNALKKF--HWRYIIIDEAHRIKNENsrLSKVMRMFACNNRL 320
Cdd:cd17926 73 IGLIGGG----------KKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLPAKT--FSEILKELNAKYRL 140
|
....*.
gi 255079182 321 LITGTP 326
Cdd:cd17926 141 GLTATP 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
165-326 |
2.36e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.52 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 165 KMREYQLAGL-NWMIRLFDHGINGILADEMGLGKTLQTISLLGYLSEYRGITgPHMVVVPKSTLGN-WMNEFKRWCPMIR 242
Cdd:pfam04851 3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHGNQEARAAQKAQYldknnafDVCVTSYEMV----IKEKNALKKFHWRYIIIDEAHRIKNENSRlsKVMRMFACNN 318
Cdd:pfam04851 82 EIGEIISGDKKDESVDDN-------KIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYFKPAF 152
|
....*...
gi 255079182 319 RLLITGTP 326
Cdd:pfam04851 153 LLGLTATP 160
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
186-300 |
5.97e-07 |
|
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: 50.09 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 186 NGILADEMGLGKTLQ-TISLLGYLSEYRGITgphMVVVPKSTLGN-WMNEFKRWCPM-IRPFKFHGNQEAraaqKAQYLD 262
Cdd:cd00046 3 NVLITAPTGSGKTLAaLLAALLLLLKKGKKV---LVLVPTKALALqTAERLRELFGPgIRVAVLVGGSSA----EEREKN 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 255079182 263 KNNAFDVCVTSYEMVIKEKNALKKFH---WRYIIIDEAHRI 300
Cdd:cd00046 76 KLGDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAL 116
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
535-593 |
1.06e-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: 47.31 E-value: 1.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 255079182 535 SEKFVFLLSTRAGGLGINLTTADTVVIYDSDWNPQMDLQAMDRAHRIGQtKEVSVFRFC 593
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
|
|
| DpdE |
NF041062 |
protein DpdE; |
189-354 |
1.18e-04 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 46.12 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 189 LADEMGLGKTLQT-ISLLGYLSEYRGITGphMVVVPKSTLGNWMNEFKRwcpmirpfKFHGNQEARAaqkaqyldknnaf 267
Cdd:NF041062 175 LADEVGLGKTIEAgLVIRQHLLDNPDARV--LVLVPDALVRQWRRELRD--------KFFLDDFPGA------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 268 DVCVTSYEMVIKeknaLKKFHWRY--IIIDEAHRI----KNENSRLSKVMRMFA-----CNNRLLITGTPLQNNLHELWA 336
Cdd:NF041062 232 RVRVLSHEEPER----WEPLLDAPdlLVVDEAHQLarlaWSGDPPERARYRELAalahaAPRLLLLSATPVLGNEETFLA 307
|
170 180
....*....|....*....|
gi 255079182 337 LLNFLLPEVFG--DAGQFEE 354
Cdd:NF041062 308 LLHLLDPDLYPldDLEAFRE 327
|
|
| HDA2-3 |
pfam11496 |
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ... |
399-544 |
6.89e-04 |
|
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.
Pssm-ID: 402894 Cd Length: 281 Bit Score: 42.70 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 399 LKVGMSEMQKEYYKRALQ-------KDIQVVNSGGDRSRLLNMVMQLRKCC---NHPYLF----------QGAEPgppff 458
Cdd:pfam11496 8 LPTPMTSYQKELTEQIVSlhysdilKYCETSDSKEDISLIKSMTLCLENLSlvaTHPYLLvdhympksllLKDEP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 459 tdEHLVENSGK------MVLLDKLLKKLKEKgsRVLIFSQMTRLLDILEDYLLFRRYKYCRIDGNTDGDTREDMIDSYNA 532
Cdd:pfam11496 83 --EKLAYTSGKflvlndLVNLLIERDRKEPI--NVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSDSGNK 158
|
170
....*....|..
gi 255079182 533 PGSEKFVFLLST 544
Cdd:pfam11496 159 KIHSTTCHLLSS 170
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
167-299 |
8.20e-03 |
|
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: 38.31 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 167 REYQLAGLNWMIRLFDHGINGILAdEM--GLGKTLQTISLLGYLSEYRgiTGPH-MVVVPKSTLGNW-MNEFKRWCPMIR 242
Cdd:cd18032 2 RYYQQEAIEALEEAREKGQRRALL-VMatGTGKTYTAAFLIKRLLEAN--RKKRiLFLAHREELLEQaERSFKEVLPDGS 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255079182 243 PFKFHGNQearaaqkaqylDKNNAFDVCVTSYEMVIKEKNaLKKF---HWRYIIIDEAHR 299
Cdd:cd18032 79 FGNLKGGK-----------KKPDDARVVFATVQTLNKRKR-LEKFppdYFDLIIIDEAHH 126
|
|
| |
