|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
219-464 |
2.73e-146 |
|
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: 429.58 E-value: 2.73e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPDaGKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18067 1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQ-CKPEIDKAIVVSPSSLVKNWANELG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDaINPFAVDGKaSKEELIQQLRQWAIASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd18067 80 KWLGGR-LQPLAIDGG-SKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSELLTMVN 458
Cdd:cd18067 158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237
|
....*.
gi 1868550494 459 KFIIRR 464
Cdd:cd18067 238 RCIIRR 243
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
133-716 |
5.10e-124 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 388.04 E-value: 5.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 133 RQGAVFVARPLHDPTGEFAIVLYDPTIDDKPTPVEEGKDKKEDEAEKTKLDVPLVHKSLADILGLKKKVEGRPRVPvvid 212
Cdd:COG0553 160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 213 PRLAKVLRPHQVEGVKFLYRCTT-GLvdpkanGCIMADEMGLGKTLQCIALMWTLLRQSPdagkstIQKCVIACPSSLVK 291
Cdd:COG0553 236 AGLKATLRPYQLEGAAWLLFLRRlGL------GGLLADDMGLGKTIQALALLLELKERGL------ARPVLIVAPTSLVG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 292 NWANELVKWLgkDAINPFAVDGKASKEELIQQLRQwaiasgravvRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLK 371
Cdd:COG0553 304 NWQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 372 NDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDadgtdedrkvgdERLS 451
Cdd:COG0553 372 NPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDE------------EALE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 452 ELLTMVNKFIIRRT-NDILsKYLPRKYEHVVFCNLAPFQKDLYNLFIKSpEIQQLLRGKGSQP----LKAINILKKLCNH 526
Cdd:COG0553 440 RLRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSH 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 527 PDLLDlpgdlpgsedcfpddyvpkdargRDRDVKSWYSGKMAVLDRMLARIRqDTNDKIVLISNYTQTLDVFEKLCRARQ 606
Cdd:COG0553 518 PALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERG 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 607 YGSLRLDGTMNVNKRQKLVDKFNDPEGSEfVFLLSSKAGGCGINLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 686
Cdd:COG0553 574 IEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
|
570 580 590
....*....|....*....|....*....|
gi 1868550494 687 VYRFIATGTIEEKIFQRQSHKQSLSSCVVD 716
Cdd:COG0553 653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
219-464 |
1.18e-112 |
|
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: 342.73 E-value: 1.18e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPDaGKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18004 1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPY-GKPTAKKALIVCPSSLVGNWKAEFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDGKASKEELIQQlrqwaiASGRAVVRPVLIVSYETLRLYVGELKNT-PIGLLLCDEGHRLKNDESLT 377
Cdd:cd18004 80 KWLGLRRIKVVTADGNAKDVKASLD------FFSSASTYPVLIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSESKT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 378 FTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSELLTMV 457
Cdd:cd18004 154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233
|
....*..
gi 1868550494 458 NKFIIRR 464
Cdd:cd18004 234 SRFILRR 240
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
222-530 |
1.63e-96 |
|
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: 302.29 E-value: 1.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 222 HQVEGVKFLYRCTTGLVdpkaNGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTIqkcvIACPSSLVKNWANELVKWL 301
Cdd:pfam00176 1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTL----IVVPLSLLHNWMNEFERWV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 302 GKDAINPFAVDGKaskeelIQQLRQWAIASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTFTAL 381
Cdd:pfam00176 73 SPPALRVVVLHGN------KRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 382 NDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGrdadgtdedrkVGDERLSELLTMVNKFI 461
Cdd:pfam00176 147 KSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKPFL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868550494 462 IRRTNDILSKYLPRKYEHVVFCNLAPFQKDLYNLFIKSPEIQQLLRGKG-----SQPLKAINILKKLCNHPDLL 530
Cdd:pfam00176 216 LRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGgreikASLLNILMRLRKICNHPGLI 289
|
|
| Rad54_N |
pfam08658 |
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54. |
28-198 |
1.86e-93 |
|
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
Pssm-ID: 430137 Cd Length: 180 Bit Score: 290.32 E-value: 1.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 28 TPKSLDRLIKPFKCPGSATPTRASEKPARKRRKIDYSGADGDAEDG--DKVYTN-EDRLALATRDVNKYPVFKVKDKDST 104
Cdd:pfam08658 1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdsDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 105 FRQRFSVPLLKKDAAEYNANRPAPLLGMRQGAVFVARPLHDPTGEFAIVLYDPTIDDKPTPVEEGKDKKEDEAEKT---- 180
Cdd:pfam08658 81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKPEEEEEAEEEEEEEEPeeka 160
|
170 180
....*....|....*....|
gi 1868550494 181 --KLDVPLVHKSLADILGLK 198
Cdd:pfam08658 161 rkKLDNPLPHKSLAEILGIK 180
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
219-464 |
3.93e-84 |
|
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: 267.87 E-value: 3.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18066 1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDGKASKEELIQqlrqwaiasgrAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd18066 81 KWLGSERIKVFTVDQDHKVEEFIA-----------SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSELLTMVN 458
Cdd:cd18066 150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTG 229
|
....*.
gi 1868550494 459 KFIIRR 464
Cdd:cd18066 230 LFILRR 235
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
219-715 |
2.75e-65 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 236.24 E-value: 2.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTiqkcVIAcPSSLVKNWANELV 298
Cdd:PLN03142 170 MRDYQLAGLNWLIR----LYENGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHM----VVA-PKSTLGNWMNEIR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLgkDAINPFAVDGKAskEELIQQlRQWAIASGRAvvrPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:PLN03142 240 RFC--PVLRAVKFHGNP--EERAHQ-REELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELpilrgrdadGTDEDRKvgdERLSELLTMVN 458
Cdd:PLN03142 312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQLHKVLR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 459 KFIIRRTNDILSKYLPRKYEHVVFCNLAPFQKDLYNLFIKSpEIQQLLRGKGSQPLkaINI---LKKLCNHPDLLDlpGD 535
Cdd:PLN03142 380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK-DLDVVNAGGERKRL--LNIamqLRKCCNHPYLFQ--GA 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 536 LPGsedcfpddyvPKDARGrDRDVKSwySGKMAVLDRMLARIRQdtNDKIVLI-SNYTQTLDVFEKLCRARQYGSLRLDG 614
Cdd:PLN03142 455 EPG----------PPYTTG-EHLVEN--SGKMVLLDKLLPKLKE--RDSRVLIfSQMTRLLDILEDYLMYRGYQYCRIDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 615 TMNVNKRQKLVDKFNDPEGSEFVFLLSSKAGGCGINLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATG 694
Cdd:PLN03142 520 NTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEY 599
|
490 500
....*....|....*....|.
gi 1868550494 695 TIEEKIFQRQSHKQSLSSCVV 715
Cdd:PLN03142 600 TIEEKVIERAYKKLALDALVI 620
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
219-449 |
3.85e-64 |
|
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: 214.46 E-value: 3.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYR--CTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAgkstiQKCVIACPSSLVKNWANE 296
Cdd:cd18007 1 LKPHQVEGVRFLWSnlVGTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRR-----SRPLVLCPASTLYNWEDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 297 LVKWLGKDAINPFAVDGKASKEELIQQLR---QWAIASGravvrpVLIVSYETLRLYVGELKNTPI-------------- 359
Cdd:cd18007 76 FKKWLPPDLRPLLVLVSLSASKRADARLRkinKWHKEGG------VLLIGYELFRNLASNATTDPRlkqefiaalldpgp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 360 GLLLCDEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGT 439
Cdd:cd18007 150 DLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDST 229
|
250
....*....|
gi 1868550494 440 DEDRKVGDER 449
Cdd:cd18007 230 EEDVRLMLKR 239
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
219-464 |
3.04e-57 |
|
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: 196.06 E-value: 3.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCttgLVDPKanGCIMADEMGLGKTLQCIALMWTLLRQSPDA--------------GKSTIQKCV-I 283
Cdd:cd18005 1 LRDYQREGVEFMYDL---YKNGR--GGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkpPASSAKKPVlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 284 ACPSSLVKNWANELVKWlgkdaiNPFAV---DGKASKEELIQQLRQwaiasGRAvvrPVLIVSYETLRLYVGELKNTPIG 360
Cdd:cd18005 76 VAPLSVLYNWKDELDTW------GHFEVgvyHGSRKDDELEGRLKA-----GRL---EVVVTTYDTLRRCIDSLNSINWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 361 LLLCDEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTD 440
Cdd:cd18005 142 AVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATA 221
|
250 260
....*....|....*....|....
gi 1868550494 441 EDRKVGDERLSELLTMVNKFIIRR 464
Cdd:cd18005 222 RELRLGRKRKQELAVKLSKFFLRR 245
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
219-416 |
5.41e-57 |
|
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: 192.78 E-value: 5.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTtglvdPKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKstiqkCVIACPSSLVKNWANELV 298
Cdd:cd17919 1 LRPYQLEGLNFLLELY-----ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGP-----VLVVCPLSVLENWEREFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKdaINPFAVDGKASKEELIQQLRQWAIAsgravvrPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd17919 71 KWTPD--LRVVVYHGSQRERAQIRAKEKLDKF-------DVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLS 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYL 416
Cdd:cd17919 142 KALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
563-691 |
2.62e-56 |
|
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: 189.22 E-value: 2.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 563 YSGKMAVLDRMLARIRqDTNDKIVLISNYTQTLDVFEKLCRARQYGSLRLDGTMNVNKRQKLVDKFNDPEgSEFVFLLSS 642
Cdd:cd18793 9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLST 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1868550494 643 KAGGCGINLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFI 691
Cdd:cd18793 87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
219-449 |
1.09e-47 |
|
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: 169.68 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDPK----ANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTIqkcVIACPSSLVKNWA 294
Cdd:cd18068 1 LKPHQVDGVQFMWDCCCESLKKTkkspGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRV---LVVCPLNTVLNWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELVKWL----GKDAINPFAVDGKASKEELIQQLRQWAIASGravvrpVLIVSYETLRLYVGE----------------L 354
Cdd:cd18068 78 NEFEKWQeglkDEEKIEVNELATYKRPQERSYKLQRWQEEGG------VMIIGYDMYRILAQErnvksreklkeifnkaL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 355 KNTPIGLLLCDEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGR 434
Cdd:cd18068 152 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQ 231
|
250
....*....|....*
gi 1868550494 435 DADGTDEDRKVGDER 449
Cdd:cd18068 232 CADSTLVDVRVMKKR 246
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
219-464 |
3.26e-47 |
|
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: 167.93 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYrcttGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRqspdagKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18001 1 LYPHQREGVAWLW----SLHDGGKGG-ILADDMGLGKTVQICAFLSGMFD------SGLIKSVLVVMPTSLIPHWVKEFA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWlgKDAINPFAVDGkASKEELIQQLRqwAIASGRAVvrpvLIVSYETLRLYVGELKNTPIG-----LLLCDEGHRLKND 373
Cdd:cd18001 70 KW--TPGLRVKVFHG-TSKKERERNLE--RIQRGGGV----LLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 374 ESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFA-NPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSE 452
Cdd:cd18001 141 KTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAEN 220
|
250
....*....|..
gi 1868550494 453 LLTMVNKFIIRR 464
Cdd:cd18001 221 LRQIIKPYFLRR 232
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
219-465 |
1.37e-46 |
|
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: 165.43 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYR-CTTGLvdpkanGCIMADEMGLGKTLQCIALMwTLLRQSPDAGKStiqkcVIACPSSLVKNWANEL 297
Cdd:cd18012 5 LRPYQKEGFNWLSFlRHYGL------GGILADDMGLGKTLQTLALL-LSRKEEGRKGPS-----LVVAPTSLIYNWEEEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 298 VKWlgKDAINPFAVDGKASKEELIQQLRQwaiasgravvRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLT 377
Cdd:cd18012 73 AKF--APELKVLVIHGTKRKREKLRALED----------YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 378 FTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDAdgtdedrkvgdERLSELLTMV 457
Cdd:cd18012 141 AKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDE-----------EALEELKKLI 209
|
....*...
gi 1868550494 458 NKFIIRRT 465
Cdd:cd18012 210 SPFILRRL 217
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
219-449 |
4.12e-46 |
|
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: 164.60 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLY----RCTTGLVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPdagkstIQKCVIACPSSLVKNWA 294
Cdd:cd18069 1 LKPHQIGGIRFLYdniiESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTG------AKTVLAIVPVNTLQNWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELVKWL------GKDAINPFAV----DGKASKEELIQQLRQWAIASGravvrpVLIVSYETLRLYVGElkntpiGLLLC 364
Cdd:cd18069 75 SEFNKWLpppealPNVRPRPFKVfilnDEHKTTAARAKVIEDWVKDGG------VLLMGYEMFRLRPGP------DVVIC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 365 DEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRK 444
Cdd:cd18069 143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222
|
....*
gi 1868550494 445 VGDER 449
Cdd:cd18069 223 LMRYR 227
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
219-464 |
2.10e-42 |
|
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: 154.05 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd17999 1 LRPYQQEGINWL----AFLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPSLVVCPPTLVGHWVAEIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDGKASKEELIQQLRQWAiasgravvrPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd17999 76 KYFPNAFLKPLAYVGPPQERRRLREQGEKH---------NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSELLTMVN 458
Cdd:cd17999 147 KAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVL 226
|
....*.
gi 1868550494 459 KFIIRR 464
Cdd:cd17999 227 PFLLRR 232
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
219-464 |
2.26e-35 |
|
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: 133.72 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGlvdpkANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAE-----QHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPF-----LVLCPLSVLDNWKEELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDgKASKEELIQQLRQ---WAiasgravvrpVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDES 375
Cdd:cd18006 71 RFAPDLSVITYMGD-KEKRLDLQQDIKStnrFH----------VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 376 LTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLG--TKNEFRKRFelpilrgrdadgtdEDRKVGDERLSEL 453
Cdd:cd18006 140 LLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAY--------------SETDDESETVEEL 205
|
250
....*....|.
gi 1868550494 454 LTMVNKFIIRR 464
Cdd:cd18006 206 HLLLQPFLLRR 216
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
218-464 |
4.42e-34 |
|
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: 130.58 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 218 VLRPHQVEGVKFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMwTLLRQSPDAGKstiqkCVIACPSSLVKNWANEL 297
Cdd:cd18009 3 VMRPYQLEGMEWLRM----LWENGING-ILADEMGLGKTIQTIALL-AHLRERGVWGP-----FLVIAPLSTLPNWVNEF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 298 VKWLgkDAINPFAVDG-KASKEELIQQLRQwaiASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESL 376
Cdd:cd18009 72 ARFT--PSVPVLLYHGtKEERERLRKKIMK---REGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 377 TFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTDEDRKVGDERLSELLTM 456
Cdd:cd18009 147 LIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAI 226
|
....*...
gi 1868550494 457 VNKFIIRR 464
Cdd:cd18009 227 LKPFLLRR 234
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
219-464 |
1.51e-32 |
|
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: 125.55 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd17993 2 LRDYQLTGLNWLAHSWC-----KGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPF-----LVVVPLSTMPAWQREFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLgkDAINPFAVDGKASKEELIQQLrQWAIASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd17993 72 KWA--PDMNVIVYLGDIKSRDTIREY-EFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNylgtKNEFRKRFElpilrgrdaDGTDEDRKVGDERLSELLtmvN 458
Cdd:cd17993 149 EALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPG----KFDIWEEFE---------EEHDEEQEKGIADLHKEL---E 212
|
....*.
gi 1868550494 459 KFIIRR 464
Cdd:cd17993 213 PFILRR 218
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
219-464 |
2.26e-32 |
|
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: 125.86 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYrcttglvdpkANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTIQKCV------------IACP 286
Cdd:cd18008 1 LLPYQKQGLAWML----------PRGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSdpkklylskttlIVVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 287 SSLVKNWANELVKWLGKDAINPFAVDGkASKEELIQQLRQWAIasgravvrpvLIVSYETLR--------LYVGELKNTP 358
Cdd:cd18008 71 LSLLSQWKDEIEKHTKPGSLKVYVYHG-SKRIKSIEELSDYDI----------VITTYGTLAsefpknkkGGGRDSKEKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 359 IGLLLC--------DEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI 430
Cdd:cd18008 140 ASPLHRirwyrvilDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
|
250 260 270
....*....|....*....|....*....|....
gi 1868550494 431 LRGRDADGtdedrkvgdERLSELLtmvNKFIIRR 464
Cdd:cd18008 220 SKNDRKAL---------ERLQALL---KPILLRR 241
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
219-426 |
2.58e-32 |
|
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: 125.05 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKSTiqkcVIAcPSSLVKNWANELV 298
Cdd:cd17995 1 LRDYQLEGVNWLLFNWY-----NRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFL----VIA-PLSTIPNWQREFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLgkdAINPFAVDGKASKEELIQQ----LRQWAIASGRAVVR-PVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKND 373
Cdd:cd17995 71 TWT---DMNVVVYHGSGESRQIIQQyemyFKDAQGRKKKGVYKfDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1868550494 374 ESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd17995 148 NSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
219-476 |
5.95e-29 |
|
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: 115.54 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd17996 4 LKEYQLKGLQWM----VSLYNNNLNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPY-----LVIVPLSTLSNWVSEFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKdaINPFAVDG-KASKEELIQQLRQWAIAsgravvrpVLIVSYEtlrlYVgeLKNTPI------GLLLCDEGHRLK 371
Cdd:cd17996 74 KWAPS--VSKIVYKGtPDVRKKLQSQIRAGKFN--------VLLTTYE----YI--IKDKPLlskikwKYMIIDEGHRMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 372 NDES-LTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELP--ILRGRDADGTDEDRKVgde 448
Cdd:cd17996 138 NAQSkLTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPfaNTGEQVKIELNEEETL--- 214
|
250 260
....*....|....*....|....*...
gi 1868550494 449 rlselltmvnkFIIRRTNDILSKYLPRK 476
Cdd:cd17996 215 -----------LIIRRLHKVLRPFLLRR 231
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
219-464 |
9.75e-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: 114.61 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFlyrcttGLvdpKANG-CIMADEMGLGKTLQCIALM------WTLLrqspdagkstiqkcvIACPSSLVK 291
Cdd:cd18010 1 LLPFQREGVCF------AL---RRGGrVLIADEMGLGKTVQAIAIAayyreeWPLL---------------IVCPSSLRL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 292 NWANELVKWLGKDAINPFAVdgkaskeeliqqlrqwaIASGRAVVRP----VLIVSYETLRLYVGELKNTPIGLLLCDEG 367
Cdd:cd18010 57 TWADEIERWLPSLPPDDIQV-----------------IVKSKDGLRDgdakVVIVSYDLLRRLEKQLLARKFKVVICDES 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 368 HRLKNDESLTFTALNDLNVQ-KRVI-LSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGTdedrkv 445
Cdd:cd18010 120 HYLKNSKAKRTKAALPLLKRaKRVIlLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYS------ 193
|
250 260
....*....|....*....|
gi 1868550494 446 GDERLSELLTMVNK-FIIRR 464
Cdd:cd18010 194 GSSNLEELHLLLLAtIMIRR 213
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
219-416 |
1.83e-28 |
|
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: 113.19 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRcttgLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18000 1 LFKYQQTGVQWLWE----LHCQRVGG-ILGDEMGLGKTIQIIAFLAALHHSKLGLGPS-----LIVCPATVLKQWVKEFH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGkdainPFAV-------------DGKASKEELIQQLRQWAIASGravvrpVLIVSYETLRLYVGELKNTPIGLLLCD 365
Cdd:cd18000 71 RWWP-----PFRVvvlhssgsgtgseEKLGSIERKSQLIRKVVGDGG------ILITTYEGFRKHKDLLLNHNWQYVILD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1868550494 366 EGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYL 416
Cdd:cd18000 140 EGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
219-465 |
3.70e-28 |
|
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: 113.19 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd17997 4 MRDYQIRGLNWL----ISLFENGING-ILADEMGLGKTLQTISLLGYLKHYKNINGPH-----LIIVPKSTLDNWMREFK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKdainPFAVDGKASKEELIQQLRQwaiasgRAVVRP--VLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESL 376
Cdd:cd17997 74 RWCPS----LRVVVLIGDKEERADIIRD------VLLPGKfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 377 TFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFElpilrgrdadgTDEDRKVGDERLSELLTM 456
Cdd:cd17997 144 LSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-----------VNNCDDDNQEVVQRLHKV 212
|
....*....
gi 1868550494 457 VNKFIIRRT 465
Cdd:cd17997 213 LRPFLLRRI 221
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
219-464 |
1.54e-27 |
|
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: 111.29 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18003 1 LREYQHIGLDWL----ATLYEKNLNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPH-----LIVVPTSVMLNWEMEFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWL-GKDAINPFAvdgkaSKEELIQQLRQWAiasgravvRP----VLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKND 373
Cdd:cd18003 71 RWCpGFKILTYYG-----SAKERKLKRQGWM--------KPnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 374 ESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPiLRGRDADGTDEDRKVgderLSEL 453
Cdd:cd18003 138 KSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSEGSQEENEEL----VRRL 212
|
250
....*....|.
gi 1868550494 454 LTMVNKFIIRR 464
Cdd:cd18003 213 HKVLRPFLLRR 223
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
219-427 |
4.44e-26 |
|
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: 106.37 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTIQTIVFLYSLYKEGHSKGPF-----LVSAPLSTIINWEREFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDGkaskeeliqqlrqwaiasgravvrpVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd17994 71 MWAPDFYVVTYVGDH-------------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFF 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFE 427
Cdd:cd17994 126 RILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA 174
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
219-435 |
1.23e-25 |
|
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: 106.24 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYR--CttglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANE 296
Cdd:cd18054 21 LRDYQLEGLNWLAHswC-------KNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPF-----LLVVPLSTLTSWQRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 297 LVKWlgKDAINPFAVDGKASKEELIQQLrQWAIASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESL 376
Cdd:cd18054 89 FEIW--APEINVVVYIGDLMSRNTIREY-EWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1868550494 377 TFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNylgtKNEFRKRFELPILRGRD 435
Cdd:cd18054 166 LYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE----KFEFWEDFEEDHGKGRE 220
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
219-423 |
5.80e-25 |
|
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: 103.52 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrcttglVDPKANGCIMADEMGLGKTLQCIALMWTLLRQSPdagkstIQKCVIACPSSLVKNWANELv 298
Cdd:cd18011 1 PLPHQIDAVLRA-------LRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGD------AKRVLILCPASLVEQWQDEL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 kwLGKDAINPFAVDGKASKEELIQQLRQWAiasgravVRPVLIVSYETLR---LYVGELKNTPIGLLLCDEGHRLKNDES 375
Cdd:cd18011 67 --QDKFGLPFLILDRETAAQLRRLIGNPFE-------EFPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1868550494 376 LTFTALNDL------NVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFR 423
Cdd:cd18011 138 GKETKRYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
219-426 |
6.67e-25 |
|
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: 103.59 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFL----YrcttglvdpKANGCIMADEMGLGKTLQCIAL---MWTLLRQSPdagkstiqkCVIACPSSLVK 291
Cdd:cd18060 1 LREYQLEGVNWLlfnwY---------NRQNCILADEMGLGKTIQSIAFlqeVYNVGIHGP---------FLVIAPLSTIT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 292 NWANELVKWLGKDAInpfAVDGKASKEELIQQLRQWAIAS-GR----AVVRPVLIVSYETLRLYVGELKNTPIGLLLCDE 366
Cdd:cd18060 63 NWEREFNTWTEMNTI---VYHGSLASRQMIQQYEMYCKDSrGRlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 367 GHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18060 140 AHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
219-426 |
7.72e-25 |
|
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: 103.99 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTVQTIVFLYSLYKEGHSKGPY-----LVSAPLSTIINWEREFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDgKASKEELIQQ---LRQWAIASGRAVVR---------PVLIVSYETLRLYVGELKNTPIGLLLCDE 366
Cdd:cd18057 71 MWAPDFYVVTYTGD-KESRSVIRENefsFEDNAIRSGKKVFRmkkeaqikfHVLLTSYELITIDQAILGSIEWACLVVDE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 367 GHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18057 150 AHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
219-414 |
1.60e-24 |
|
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: 101.31 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrcttGLVDPKANGCIMADEMGLGKTLQCIALMwTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd17998 1 LKDYQLIGLNWL-----NLLYQKKLSGILADEMGLGKTIQVIAFL-AYLKEIGIPGPH-----LVVVPSSTLDNWLREFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFavdgKASKEELiQQLRQwaIASGRAVVRPVLIVSYEtlrLYVGE------LKNTPIGLLLCDEGHRLKN 372
Cdd:cd17998 70 RWCPSLKVEPY----YGSQEER-KHLRY--DILKGLEDFDVIVTTYN---LATSNpddrsfFKRLKLNYVVYDEGHMLKN 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1868550494 373 DESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPN 414
Cdd:cd17998 140 MTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
211-410 |
3.35e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.03 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 211 IDPRLAKVLRPHQVEGVKFLYRCTtglvdpkaNGCIMADEMGLGKTLQ-CIALMWTLLRQSPdagkstiQKCVIACP-SS 288
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGL--------RDVILAAPTGSGKTLAaLLPALEALKRGKG-------GRVLVLVPtRE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 289 LVKNWANELVKWLGKDAINPFAVDGKASKEELIQQLRqwaiaSGRAvvrPVLIVSYETLR--LYVGELKNTPIGLLLCDE 366
Cdd:smart00487 66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLE-----SGKT---DILVTTPGRLLdlLENDKLSLSNVDLVILDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1868550494 367 GHRLKND--ESLTFTALNDLNVQKRVI-LSGTP---IQNDLSEYFALLNF 410
Cdd:smart00487 138 AHRLLDGgfGDQLEKLLKLLPKNVQLLlLSATPpeeIENLLELFLNDPVF 187
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
219-464 |
7.37e-24 |
|
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: 100.91 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTVQTAVFLYSLYKEGHSKGPF-----LVSAPLSTIINWEREFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFA--VDGKASKEELIQQLRQWAIASGRAVVR---------PVLIVSYETLRLYVGELKNTPIGLLLCDEG 367
Cdd:cd18056 71 MWAPDMYVVTYVgdKDSRAIIRENEFSFEDNAIRGGKKASRmkkeasvkfHVLLTSYELITIDMAILGSIDWACLIVDEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 368 HRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdADGTDEDrkvgd 447
Cdd:cd18056 151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF---------ADIAKED----- 216
|
250
....*....|....*..
gi 1868550494 448 eRLSELLTMVNKFIIRR 464
Cdd:cd18056 217 -QIKKLHDMLGPHMLRR 232
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
565-680 |
9.73e-24 |
|
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: 96.51 E-value: 9.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 565 GKMAVLDRMLARIRqdtNDKIVLISNYTQTLDvFEKLCRARQYGSLRLDGTMNVNKRQKLVDKFNDpegSEFVFLLSSKA 644
Cdd:pfam00271 1 EKLEALLELLKKER---GGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1868550494 645 GGCGINLIGANRLVLFDPDWNPAADQQALARVWRDG 680
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
219-426 |
4.00e-23 |
|
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: 98.93 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGLVDpkangCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTD-----TILADEMGLGKTIQTIVFLYSLYKEGHTKGPF-----LVSAPLSTIINWEREFQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFA--VDGKASKEELIQQLRQWAIASGRAVVR---------PVLIVSYETLRLYVGELKNTPIGLLLCDEG 367
Cdd:cd18055 71 MWAPDFYVVTYTgdKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1868550494 368 HRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18055 151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
219-426 |
8.95e-23 |
|
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: 97.38 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAgkstiqKCVIACPSSLVKNWANELV 298
Cdd:cd18061 1 LREYQLEGLNWLLFNWY-----NRRNCILADEMGLGKTIQSITFLYEILLTGIRG------PFLIIAPLSTIANWEREFR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWlgkDAINPFAVDGKASKEELIQQLRQWAIASGRAVVR-----PVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKND 373
Cdd:cd18061 70 TW---TDLNVVVYHGSLISRQMIQQYEMYFRDSQGRIIRgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1868550494 374 ESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18061 147 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
219-464 |
2.28e-22 |
|
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: 96.42 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQspdagKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18002 1 LKEYQLKGLNWL----ANLYEQGING-ILADEMGLGKTVQSIAVLAHLAEE-----HNIWGPFLVIAPASTLHNWQQEIS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAvdGKASKEELIQQLRQWAIASGRAVVRPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLTF 378
Cdd:cd18002 71 RFVPQFKVLPYW--GNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 379 TALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDADGtdedrKVGDERLSELLTMVN 458
Cdd:cd18002 149 KTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKT-----GLNEHQLKRLHMILK 223
|
....*.
gi 1868550494 459 KFIIRR 464
Cdd:cd18002 224 PFMLRR 229
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
219-426 |
2.72e-22 |
|
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: 96.25 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLLRqspdagKSTIQKCVIACPSSLVKNWANELV 298
Cdd:cd18059 1 LREYQLEGVNWLLFNWY-----NTRNCILADEMGLGKTIQSITFLYEIYL------KGIHGPFLVIAPLSTIPNWEREFR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWlgkDAINPFAVDGKASKEELIQQLRQWAIASGRAVVRP-----VLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKND 373
Cdd:cd18059 70 TW---TELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGsykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1868550494 374 ESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18059 147 NCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
219-476 |
3.33e-22 |
|
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: 96.66 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18064 16 LRDYQVRGLNWL----ISLYENGING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPH-----MVLVPKSTLHNWMAEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLgkDAINPFAVDGKASKEEliqqlrqwaiASGRAVVRP----VLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDE 374
Cdd:cd18064 86 RWV--PTLRAVCLIGDKDQRA----------AFVRDVLLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 375 SLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdadgtDEDRKVGDERLSELL 454
Cdd:cd18064 154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-------------DTNNCLGDQKLVERL 220
|
250 260
....*....|....*....|...
gi 1868550494 455 TMVNK-FIIRRTNDILSKYLPRK 476
Cdd:cd18064 221 HMVLRpFLLRRIKADVEKSLPPK 243
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
219-426 |
6.89e-22 |
|
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: 95.11 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFL----YrcttglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAgkstiqKCVIACPSSLVKNWA 294
Cdd:cd18058 1 LREYQLEGMNWLlfnwY---------NRKNCILADEMGLGKTIQSITFLSEIFLMGIRG------PFLIIAPLSTITNWE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELVKWlgkDAINPFAVDGKASKEELIQQLR------QWAIASGRAVVRpVLIVSYETLRLYVGELKNTPIGLLLCDEGH 368
Cdd:cd18058 66 REFRTW---TEMNAIVYHGSQISRQMIQQYEmyyrdeQGNPLSGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAH 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1868550494 369 RLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRF 426
Cdd:cd18058 142 RLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
219-424 |
9.33e-22 |
|
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: 95.12 E-value: 9.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTglvdpKANGCIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18053 21 LRDYQLNGLNWLAHSWC-----KGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPF-----LLVVPLSTLTSWQREIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWlgKDAINPFAVDGKASKEELIQQlRQWAIASGRAVVRPVLIVSYETL---RLYVGELKNTPIGLllcDEGHRLKNDES 375
Cdd:cd18053 91 TW--APQMNAVVYLGDINSRNMIRT-HEWMHPQTKRLKFNILLTTYEILlkdKSFLGGLNWAFIGV---DEAHRLKNDDS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1868550494 376 LTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRK 424
Cdd:cd18053 165 LLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE 213
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
219-464 |
9.38e-22 |
|
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: 95.52 E-value: 9.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18063 24 LKHYQLQGLEWM----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNGPY-----LIIVPLSTLSNWTYEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWlgKDAINPFAVDGK-ASKEELIQQLRqwaiaSGRAvvrPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLT 377
Cdd:cd18063 94 KW--APSVVKISYKGTpAMRRSLVPQLR-----SGKF---NVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 378 FTALNDLNVQ-KRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI-LRGRDADGTDEDRKVGDERLSELLt 455
Cdd:cd18063 164 TQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLHKVL- 242
|
....*....
gi 1868550494 456 mvNKFIIRR 464
Cdd:cd18063 243 --RPFLLRR 249
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
218-464 |
1.39e-21 |
|
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: 94.73 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 218 VLRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANEL 297
Cdd:cd18062 23 VLKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPF-----LIIVPLSTLSNWVYEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 298 VKWlGKDAINPFAVDGKASKEELIQQLRqwaiaSGRAvvrPVLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDESLT 377
Cdd:cd18062 93 DKW-APSVVKVSYKGSPAARRAFVPQLR-----SGKF---NVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 378 FTALNDLNVQ-KRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFELPI-LRGRDADGTDEDRKVGDERLSELLt 455
Cdd:cd18062 164 TQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHKVL- 242
|
....*....
gi 1868550494 456 mvNKFIIRR 464
Cdd:cd18062 243 --RPFLLRR 249
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
219-464 |
2.16e-21 |
|
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: 93.93 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrctTGLVDPKANGcIMADEMGLGKTLQCIALMWTLLRQSPDAGKStiqkcVIACPSSLVKNWANELV 298
Cdd:cd18065 16 LRDYQVRGLNWM----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH-----MVLVPKSTLHNWMNEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 299 KWLGKDAINPFAVDgKASKEELIqqlrqwaiasgRAVVRP----VLIVSYETLRLYVGELKNTPIGLLLCDEGHRLKNDE 374
Cdd:cd18065 86 RWVPSLRAVCLIGD-KDARAAFI-----------RDVMMPgewdVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 375 SLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFANPNYLGTKNEFRKRFelpilrgrdadgtDEDRKVGDERLSELL 454
Cdd:cd18065 154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-------------DTKNCLGDQKLVERL 220
|
250
....*....|.
gi 1868550494 455 TMVNK-FIIRR 464
Cdd:cd18065 221 HAVLKpFLLRR 231
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
596-680 |
2.22e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 83.03 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 596 DVFEKLCRARQYGSLRLDGTMNVNKRQKLVDKFNDpegSEFVFLLSSKAGGCGINLIGANRLVLFDPDWNPAADQQALAR 675
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN---GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 1868550494 676 VWRDG 680
Cdd:smart00490 78 AGRAG 82
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
219-412 |
2.48e-18 |
|
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: 85.22 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVK-FLYRcttglVDPKANGCIMADEMGLGKTLQCIAL-----------------MWTLLRQSPDAGKSTIQK 280
Cdd:cd18072 1 LLLHQKQALAwLLWR-----ERQKPRGGILADDMGLGKTLTMIALilaqkntqnrkeeekekALTEWESKKDSTLVPSAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 281 CVIACPSSLVKNWANELVKWLGKDAINPFAVDGkASKEELIQQLRQWAIasgraVVRPVLIVSYEtLRLYVGELKNTPIG 360
Cdd:cd18072 76 TLVVCPASLVHQWKNEVESRVASNKLRVCLYHG-PNRERIGEVLRDYDI-----VITTYSLVAKE-IPTYKEESRSSPLF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1868550494 361 L-----LLCDEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQNDLSEYFALLNFAN 412
Cdd:cd18072 149 RiawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
244-436 |
1.71e-17 |
|
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: 82.52 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 244 GCIMADEMGLGKTLQCIALMWTllrqspdagkstiQKCVIACPSSLVKNWANELVKWLGKDAINPFAVDGKAskeeliqQ 323
Cdd:cd18071 50 GGILADDMGLGKTLTTISLILA-------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGE-------R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 324 LRQWAIASGRAVVrpvlIVSYETLRLYVGELKNTPIGLL-----LCDEGHRLKNDESLTFTALNDLNVQKRVILSGTPIQ 398
Cdd:cd18071 110 NRDPKLLSKYDIV----LTTYNTLASDFGAKGDSPLHTInwlrvVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQ 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1868550494 399 NDLSEYFALLNFANPNYLGTKNEFRKRFELPILRGRDA 436
Cdd:cd18071 186 NSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPT 223
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
219-410 |
4.66e-10 |
|
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: 60.82 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrcttglvdpKANGCIMADEMGLGKTLQCIALMWT-------LLRQSPDAGKSTIQKCV--------- 282
Cdd:cd18070 1 LLPYQRRAVNWM----------LVPGGILADEMGLGKTVEVLALILLhprpdndLDAADDDSDEMVCCPDClvaetpvss 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 283 ----IACPSSLVKNWANEL-------VKWLGKDAINPFAVDGKASKEELIQQlrqwaiasgravvrPVLIVSYETLR--L 349
Cdd:cd18070 71 katlIVCPSAILAQWLDEInrhvpssLKVLTYQGVKKDGALASPAPEILAEY--------------DIVVTTYDVLRteL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 350 YV---------------GELKNTPigLLLCdEGHRLKNDE-----SLTFTALN---DLNVQKRVILSGTPIQNDLSEYFA 406
Cdd:cd18070 137 HYaeanrsnrrrrrqkrYEAPPSP--LVLV-EWWRVCLDEaqmveSSTSKAAEmarRLPRVNRWCVSGTPIQRGLDDLFG 213
|
....
gi 1868550494 407 LLNF 410
Cdd:cd18070 214 LLSF 217
|
|
| DpdE |
NF041062 |
protein DpdE; |
219-678 |
1.03e-09 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 62.30 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKflyrctTGLVDPkangcIM----ADEMGLGKTLQCIALMWTLLRQSPDAgkstiqKCVIACPSSLVKNWA 294
Cdd:NF041062 154 LEPHQVAVVR------RVLQDP-----VQryllADEVGLGKTIEAGLVIRQHLLDNPDA------RVLVLVPDALVRQWR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELvkwLGKDAINPFAvdgkaskeeliqqlrqwaiasgRAVVRpvlIVSYETLRLYvgELKNTPIGLLLCDEGHRL---- 370
Cdd:NF041062 217 REL---RDKFFLDDFP----------------------GARVR---VLSHEEPERW--EPLLDAPDLLVVDEAHQLarla 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 371 ---KNDESLTFTALNDL-NVQKRVI-LSGTPIQNDLSEYFALLNFANP-NY-LGTKNEFRKRFEL-----PILRGRDADG 438
Cdd:NF041062 267 wsgDPPERARYRELAALaHAAPRLLlLSATPVLGNEETFLALLHLLDPdLYpLDDLEAFRERLEEreelgRLVLGLDPDN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 439 TD---------------EDRKVGD--ERLSELLTMVNKFII---------------------------RRTNDILSKYLP 474
Cdd:NF041062 347 PNfllrqaldelralfpEDEELQElaEELLPLLDEFDDEEPeeraravsalrahisetyrlhrrmirnRRSSVLGADYLV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 475 RKYEHVVFCNLAPFQKDLYNLFIKSPEIQQLLRGKGSQPLKAIN------ILKKLCNHPDLLD------LPGDLPGSEDC 542
Cdd:NF041062 427 PGRAGPRVLVWESPAREAADEALEDWREEAALLDAESDPAARAAyaralaWLVARLGGPDDLAallrwrLRGDAASADLA 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 543 FPDDYVpkDARGRDRDVKSWYSGKMAVLDRMLaRIRQDTNDKIVLISNYTQTLD-VFEKLCRARQYGSLRLDGTMNVNKR 621
Cdd:NF041062 507 GERELL--EALIAALEDEAKDADLLAALADWL-LPLLRGSGKAVVFCGDGSLADhLAAALARLGAGSVERHLSGQGADQA 583
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1868550494 622 QKLVDKFNDPEGSeFVfLLSSKAGGCGINLIGANRLVLFDPDWNPAADQQALARVWR 678
Cdd:NF041062 584 ERAVRAFRQDPSA-RV-LVCDRSGEEGLNLQGADRLVHLDLPWSPNRLEQRIGRLDR 638
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
219-484 |
2.58e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 57.34 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTTGlvDPKANGCIMAdeMGLGKTLQCIALMWTLLRqspdagkstIQKCVIACPS-SLVKNWANEL 297
Cdd:COG1061 81 LRPYQQEALEALLAALER--GGGRGLVVAP--TGTGKTVLALALAAELLR---------GKRVLVLVPRrELLEQWAEEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 298 VKWLGkdaiNPFAVDGKASKEeliqqlrqwaiasgravvRPVLIVSYETL--RLYVGELKNTpIGLLLCDEGHRLkndES 375
Cdd:COG1061 148 RRFLG----DPLAGGGKKDSD------------------APITVATYQSLarRAHLDELGDR-FGLVIIDEAHHA---GA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 376 LTFTA-LNDLNVQKRVILSGTPIQNDLSEyFALLNFANPNY-LGTKNEFRKRFeL--PILRGRDADGTDEDRK--VGDER 449
Cdd:COG1061 202 PSYRRiLEAFPAAYRLGLTATPFRSDGRE-ILLFLFDGIVYeYSLKEAIEDGY-LapPEYYGIRVDLTDERAEydALSER 279
|
250 260 270
....*....|....*....|....*....|....*.
gi 1868550494 450 LSELLTMVNKFIIRRTNDILSKYlpRKYEHV-VFCN 484
Cdd:COG1061 280 LREALAADAERKDKILRELLREH--PDDRKTlVFCS 313
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
219-406 |
1.57e-07 |
|
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: 52.74 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLyrcttgLVDPKAngCIMADeMGLGKTLQCIALMWTLLRQSPdagkstIQKCVIACPSSLVKN-WANEL 297
Cdd:cd18013 1 PHPYQKVAINFI------IEHPYC--GLFLD-MGLGKTVTTLTALSDLQLDDF------TRRVLVIAPLRVARStWPDEV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 298 VKWLGKDAINPFAVDGKASKeeliqqlRQWAIASGRAvvrpVLIVSYETLRLYVGELKNT-PIGLLLCDEGHRLKNDESL 376
Cdd:cd18013 66 EKWNHLRNLTVSVAVGTERQ-------RSKAANTPAD----LYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSK 134
|
170 180 190
....*....|....*....|....*....|..
gi 1868550494 377 TFTALNDLNVQ-KRVI-LSGTPIQNDLSEYFA 406
Cdd:cd18013 135 RFKALRKVRPViKRLIgLTGTPSPNGLMDLWA 166
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
217-397 |
4.06e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.67 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 217 KVLRPHQVEGVKflyRCTTGLVDPKANGCI-MAdeMGLGKTLQCIALMWTLLRqspdagKSTIQKCVIACPS-SLVKNWA 294
Cdd:pfam04851 2 LELRPYQIEAIE---NLLESIKNGQKRGLIvMA--TGSGKTLTAAKLIARLFK------KGPIKKVLFLVPRkDLLEQAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELVKWLGkdaiNPFAVDGKASKEELIQQLRQWaiasgravvrPVLIVSYETL----RLYVGELKNTPIGLLLCDEGHRL 370
Cdd:pfam04851 71 EEFKKFLP----NYVEIGEIISGDKKDESVDDN----------KIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRS 136
|
170 180
....*....|....*....|....*...
gi 1868550494 371 kNDESltFTALND-LNVQKRVILSGTPI 397
Cdd:pfam04851 137 -GASS--YRNILEyFKPAFLLGLTATPE 161
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
219-396 |
3.10e-05 |
|
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: 44.60 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 219 LRPHQVEGVKFLYRCTT---GLVdpkangcIMAdeMGLGKTLQCIALMWTLLRqspdagkstiQKCVIACPS-SLVKNWA 294
Cdd:cd17926 1 LRPYQEEALEAWLAHKNnrrGIL-------VLP--TGSGKTLTALALIAYLKE----------LRTLIVVPTdALLDQWK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 295 NELVKWLGKDAINPFAVDGKASKEEliqqlrqwaiasgravvRPVLIVSYETLRLYVGELKNTP--IGLLLCDEGHRLkn 372
Cdd:cd17926 62 ERFEDFLGDSSIGLIGGGKKKDFDD-----------------ANVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL-- 122
|
170 180
....*....|....*....|....*
gi 1868550494 373 dESLTFTA-LNDLNVQKRVILSGTP 396
Cdd:cd17926 123 -PAKTFSEiLKELNAKYRLGLTATP 146
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
634-683 |
5.91e-04 |
|
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: 39.22 E-value: 5.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1868550494 634 SEFVFLLSSKAGGCGINLIGANRLVLFDPDWNPAADQQALARVWRDGQKK 683
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
242-395 |
5.96e-04 |
|
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: 40.85 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 242 ANGCIMADEMGLGKTLqcIALMWTLLRQSPDAGKStiqkcVIACP-SSLVKNWANELVKWLGKDaINPFAVDGKASKEEl 320
Cdd:cd00046 1 GENVLITAPTGSGKTL--AALLAALLLLLKKGKKV-----LVLVPtKALALQTAERLRELFGPG-IRVAVLVGGSSAEE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868550494 321 iqqlrQWAIASGRAvvrPVLIVSYETLRLYV---GELKNTPIGLLLCDEGHRLKNDE------SLTFTALNDLNVQkRVI 391
Cdd:cd00046 72 -----REKNKLGDA---DIIIATPDMLLNLLlreDRLFLKDLKLIIVDEAHALLIDSrgalilDLAVRKAGLKNAQ-VIL 142
|
....
gi 1868550494 392 LSGT 395
Cdd:cd00046 143 LSAT 146
|
|
| |
