|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
603-1215 |
2.94e-156 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 515.12 E-value: 2.94e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 603 DLFKVRRERLKgfnryakEFHKRKerlhREKIDKIqREKINLLKINDVEGYLRmvqdaksDRVKQLLKETEKYLQKL-GS 681
Cdd:PLN03142 56 EISKREKARLK-------ELKKQK----KQEIQKI-LEQQNAAIDADMNNKGK-------GRLKYLLQQTEIFAHFAkGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 682 KLKEAKLLTSRFENeadetrTSNATDDEtlienEDESdqakhYLESNEKYYLMAHSIKenINEQPSsLVGGKLREYQMNG 761
Cdd:PLN03142 117 QSASAKKAKGRGRH------ASKLTEEE-----EDEE-----YLKEEEDGLGGSGGTR--LLVQPS-CIKGKMRDYQLAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 762 LRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIVYCGTPDER 841
Cdd:PLN03142 178 LNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEER 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 842 RKLFKEQIVHQKFNVLLTTYEylMNKHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTGTPLQNNLE 921
Cdd:PLN03142 258 AHQREELLVAGKFDVCVTSFE--MAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 922 ELWALLNFLLPNIFNSSEDFSQWFnkpfQSNGESSAEEallseeenllIINRLHQVLRPFVLRRLKHKVENELPEKIERL 1001
Cdd:PLN03142 336 ELWALLNFLLPEIFSSAETFDEWF----QISGENDQQE----------VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1002 IRCEASAYQK-----LLMKRVEdnLGSIGNAKSRAVhNSVMELRNICNHPYLSQLHSEEVNNIIPKHflppIVRLCGKLE 1076
Cdd:PLN03142 402 LKVGMSQMQKqyykaLLQKDLD--VVNAGGERKRLL-NIAMQLRKCCNHPYLFQGAEPGPPYTTGEH----LVENSGKMV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1077 MLDRMLPKLKATDHRVLFFSTMTRLLDVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPFFIFLLSIRAGGVGV 1156
Cdd:PLN03142 475 LLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGI 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 109118318 1157 NLQAADTVILFDTDWNPQVDLQAQARAHRIGQKKDVLVLRFETVNSVEEQVRASAEHKL 1215
Cdd:PLN03142 555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKL 613
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
751-987 |
7.32e-144 |
|
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: 447.59 E-value: 7.32e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 751 GGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIH 830
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 831 KIVYCGTPDERRKLFKeQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLK-HYVSSHRL 909
Cdd:cd17996 81 KIVYKGTPDVRKKLQS-QIRAGKFNVLLTTYEYIIK--DKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNtYYHARYRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109118318 910 LLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGesSAEEALLSEEENLLIINRLHQVLRPFVLRRLK 987
Cdd:cd17996 158 LLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTG--EQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
537-1222 |
9.09e-131 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 428.87 E-value: 9.09e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 537 EFVYNFFKPIATDVEHLKSYKKHKHGRRIKQLEKYEQKMKEERQRRIRERQKEFFGGLEVHKEKLEDLFKVRRERLKGFN 616
Cdd:COG0553 26 LGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 617 RYAKEFHKRKERLHREKIDKIQREKINLLKINDVEGYLRMVQDAKSDRVKQLLKETEKYLQKLGSKLKEAKLLTSRFENE 696
Cdd:COG0553 106 LALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 697 ADETRTSNATDDETLIENEDESDQAKHYLESNEKYYLMAHSIKENINEQPSSLvGGKLREYQMNGLRWLVSLYNNHLNGI 776
Cdd:COG0553 186 LLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 777 LADEMGLGKTVQVISLICYLMETkNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIVYCGTpDERRKLFKEqivHQKFNV 856
Cdd:COG0553 265 LADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT-RERAKGANP---FEDADL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 857 LLTTYEYLmnKHDRPKLSKIHWHYIIIDEGHRIKNAS-------CKLNADlkhyvssHRLLLTGTPLQNNLEELWALLNF 929
Cdd:COG0553 340 VITSYGLL--RRDIELLAAVDWDLVILDEAQHIKNPAtkrakavRALKAR-------HRLALTGTPVENRLEELWSLLDF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 930 LLPNIFNSSEDFSQWFNKPFQSNGESSaeeallseeenlliINRLHQVLRPFVLRRLKHKVENELPEKIERLIRC----- 1004
Cdd:COG0553 411 LNPGLLGSLKAFRERFARPIEKGDEEA--------------LERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVeltpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1005 EASAYQKLLMKRVEDNLGSIGNAKSRAVHNSVMELRNICNHPYLsqlhseevnniipkhFLPPIVRLC---GKLEMLDRM 1081
Cdd:COG0553 477 QRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL---------------LLEEGAELSgrsAKLEALLEL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1082 LPKLKATDHRVLFFSTMTRLLDVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNkSGSPFFIFLLSIRAGGVGVNLQAA 1161
Cdd:COG0553 542 LEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ-EGPEAPVFLISLKAGGEGLNLTAA 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109118318 1162 DTVILFDTDWNPQVDLQAQARAHRIGQKKDVLVLRFETVNSVEEQVRASAEHKLGVANQSI 1222
Cdd:COG0553 621 DHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
757-1048 |
2.82e-103 |
|
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: 333.50 E-value: 2.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 757 YQMNGLRWLVSLYNN-HLNGILADEMGLGKTVQVISLICYLME-TKNDRGPFLVVVPSSVLPGWQSEINFWA--PSIHKI 832
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 833 VYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLmnKHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLT 912
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETL--RKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 913 GTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGESsaeeallseeenlLIINRLHQVLRPFVLRRLKHKVEN 992
Cdd:pfam00176 159 GTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK-------------KGVSRLHKLLKPFLLRRTKKDVEK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109118318 993 ELPEKIERLIRCEASAYQ------KLLMKRV-EDNLGSIGNAKSRAVHNSVMELRNICNHPYL 1048
Cdd:pfam00176 226 SLPPKVEYILFCRLSKLQrklyqtFLLKKDLnAIKTGEGGREIKASLLNILMRLRKICNHPGL 288
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
731-987 |
3.64e-93 |
|
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: 303.12 E-value: 3.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 731 YYLMAHSIKENINEQPSSLVGGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVV 810
Cdd:cd18062 1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 811 PSSVLPGWQSEINFWAPSIHKIVYCGTPDERRKlFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIK 890
Cdd:cd18062 81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRA-FVPQLRSGKFNVLLTTYEYIIK--DKQILAKIRWKYMIVDEGHRMK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 891 NASCKLNADLK-HYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGessaEEALLSEEENLL 969
Cdd:cd18062 158 NHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----EKVDLNEEETIL 233
|
250
....*....|....*...
gi 109118318 970 IINRLHQVLRPFVLRRLK 987
Cdd:cd18062 234 IIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
731-987 |
1.58e-92 |
|
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: 301.21 E-value: 1.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 731 YYLMAHSIKENINEQPSSLVGGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVV 810
Cdd:cd18063 1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 811 PSSVLPGWQSEINFWAPSIHKIVYCGTPDERRKLFKeQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIK 890
Cdd:cd18063 81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVP-QLRSGKFNVLLTTYEYIIK--DKHILAKIRWKYMIVDEGHRMK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 891 NASCKLNADLK-HYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGessaEEALLSEEENLL 969
Cdd:cd18063 158 NHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----ERVDLNEEETIL 233
|
250
....*....|....*...
gi 109118318 970 IINRLHQVLRPFVLRRLK 987
Cdd:cd18063 234 IIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
751-987 |
3.76e-92 |
|
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: 299.30 E-value: 3.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 751 GGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDrGPFLVVVPSSVLPGWQSEINFWAPSIH 830
Cdd:cd18009 1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 831 KIVYCGTPDER----RKLFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSS 906
Cdd:cd18009 80 VLLYHGTKEERerlrKKIMKREGTLQDFPVVVTSYEIAMR--DRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 907 HRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGESSAEEALLSEEENllIINRLHQVLRPFVLRRL 986
Cdd:cd18009 158 NRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQN--IVHMLHAILKPFLLRRL 235
|
.
gi 109118318 987 K 987
Cdd:cd18009 236 K 236
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
751-987 |
6.11e-92 |
|
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: 298.08 E-value: 6.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 751 GGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIH 830
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 831 KIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNKHDrpKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLL 910
Cdd:cd17997 81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKT--VLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109118318 911 LTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNkpfqsngessaeeALLSEEENLLIINRLHQVLRPFVLRRLK 987
Cdd:cd17997 159 LTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-------------VNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
753-985 |
2.50e-77 |
|
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: 256.13 E-value: 2.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 753 KLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKI 832
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 833 VYCGTPDERR-----KLFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSH 907
Cdd:cd17993 81 VYLGDIKSRDtireyEFYFSQTKKLKFNVLLTTYEIILK--DKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109118318 908 RLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKpFQSNGessaeeallseeenlliINRLHQVLRPFVLRR 985
Cdd:cd17993 159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDE-EQEKG-----------------IADLHKELEPFILRR 218
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
754-932 |
3.35e-77 |
|
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: 254.41 E-value: 3.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHqKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTG 913
Cdd:cd17919 81 YHGSQRERAQIRAKEKLD-KFDVVLTTYETLRR--DKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTG 157
|
170
....*....|....*....
gi 109118318 914 TPLQNNLEELWALLNFLLP 932
Cdd:cd17919 158 TPLQNNLEELWALLDFLDP 176
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
754-985 |
3.83e-76 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350753 [Multi-domain] Cd Length: 223 Bit Score: 252.94 E-value: 3.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPsIHKIV 833
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQ-----------KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd17995 80 YHGSGESRQIIQQYEMYFKdaqgrkkkgvyKFDVLITTYEMVIA--DAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKpFQSNGEssaeeallseeenlliINRLHQVLRPFV 982
Cdd:cd17995 158 LTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGD-LKTAEQ----------------VEKLQALLKPYM 220
|
...
gi 109118318 983 LRR 985
Cdd:cd17995 221 LRR 223
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
754-985 |
6.13e-76 |
|
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: 252.27 E-value: 6.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMnkHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTG 913
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVV--QDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109118318 914 TPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPfqsngesSAEEALLSEEENLLIINRLHQVLRPFVLRR 985
Cdd:cd18003 159 TPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-------LTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
744-997 |
3.36e-72 |
|
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: 242.65 E-value: 3.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 744 EQPSSLVGGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEIN 823
Cdd:cd18064 6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 824 FWAPSIHKIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHY 903
Cdd:cd18064 86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIK--EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 904 VSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNkpfqsngessaeeaLLSEEENLLIINRLHQVLRPFVL 983
Cdd:cd18064 164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD--------------TNNCLGDQKLVERLHMVLRPFLL 229
|
250
....*....|....
gi 109118318 984 RRLKHKVENELPEK 997
Cdd:cd18064 230 RRIKADVEKSLPPK 243
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
744-987 |
2.09e-70 |
|
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: 236.84 E-value: 2.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 744 EQPSSLVGGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEIN 823
Cdd:cd18065 6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 824 FWAPSIHKIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHY 903
Cdd:cd18065 86 RWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIK--EKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 904 VSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNkpfqsngessaeeaLLSEEENLLIINRLHQVLRPFVL 983
Cdd:cd18065 164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD--------------TKNCLGDQKLVERLHAVLKPFLL 229
|
....
gi 109118318 984 RRLK 987
Cdd:cd18065 230 RRIK 233
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
754-985 |
1.97e-67 |
|
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: 228.16 E-value: 1.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDER---RKLFKEQIVHQK---FNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSH 907
Cdd:cd18002 81 YWGNPKDRkvlRKFWDRKNLYTRdapFHVVITSYQLVVQ--DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109118318 908 RLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGESSAEEALLSeeenlliINRLHQVLRPFVLRR 985
Cdd:cd18002 159 RLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-------LKRLHMILKPFMLRR 229
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
752-987 |
2.83e-67 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 227.45 E-value: 2.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 752 GKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMEtKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHK 831
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 832 IVYCGTPDERRKLfkEQIvhQKFNVLLTTYEYLmnKHDRPKLSKIHWHYIIIDEGHRIKNAS-------CKLNADlkhyv 904
Cdd:cd18012 82 LVIHGTKRKREKL--RAL--EDYDLVITSYGLL--RRDIELLKEVKFHYLVLDEAQNIKNPQtktakavKALKAD----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 905 ssHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGESSAeeallseeenlliINRLHQVLRPFVLR 984
Cdd:cd18012 151 --HRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA-------------LEELKKLISPFILR 215
|
...
gi 109118318 985 RLK 987
Cdd:cd18012 216 RLK 218
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
742-985 |
3.95e-63 |
|
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: 216.41 E-value: 3.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 742 INEQPSsLVGGK---LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGW 818
Cdd:cd18054 7 LKKQPS-YIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 819 QSEINFWAPSIHKIVYCGTPDERRKLFKEQIVHQ-----KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNAS 893
Cdd:cd18054 86 QREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSqtkrlKFNALITTYEILLK--DKTVLGSINWAFLGVDEAHRLKNDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 894 CKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPfQSNGESSaeeallseeenlliinr 973
Cdd:cd18054 164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKG-RENGYQS----------------- 225
|
250
....*....|..
gi 109118318 974 LHQVLRPFVLRR 985
Cdd:cd18054 226 LHKVLEPFLLRR 237
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
754-985 |
1.45e-59 |
|
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: 205.36 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTG 913
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLK--DASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109118318 914 TPLQNNLEELWALLNFLLPNIF--NSSEDFSQWFNKpfqsngessaeeallsEEENLLIINRLHQVLRPFVLRR 985
Cdd:cd18006 159 TPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSE----------------TDDESETVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
754-935 |
3.18e-57 |
|
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: 197.22 E-value: 3.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETkNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEI-GIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLfKEQIVHQ--KFNVLLTTYEYLM-NKHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLL 910
Cdd:cd17998 80 YYGSQEERKHL-RYDILKGleDFDVIVTTYNLATsNPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
|
170 180
....*....|....*....|....*
gi 109118318 911 LTGTPLQNNLEELWALLNFLLPNIF 935
Cdd:cd17998 159 LTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1065-1197 |
2.68e-55 |
|
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: 189.61 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1065 LPPIVR--LCGKLEMLDRMLPKLKATDHRVLFFSTMTRLLDVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPF 1142
Cdd:cd18793 1 LPPKIEevVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 109118318 1143 fIFLLSIRAGGVGVNLQAADTVILFDTDWNPQVDLQAQARAHRIGQKKDVLVLRF 1197
Cdd:cd18793 81 -VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
742-985 |
1.44e-54 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350811 [Multi-domain] Cd Length: 237 Bit Score: 191.80 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 742 INEQPSSLVGGK---LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGW 818
Cdd:cd18053 6 LKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 819 QSEINFWAPSIHKIVYCGTPDERRKLFKEQIVHQ-----KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNAS 893
Cdd:cd18053 86 QREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPqtkrlKFNILLTTYEILLK--DKSFLGGLNWAFIGVDEAHRLKNDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 894 CKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNgessaeeallseeenlliINR 973
Cdd:cd18053 164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG------------------YAS 225
|
250
....*....|..
gi 109118318 974 LHQVLRPFVLRR 985
Cdd:cd18053 226 LHKELEPFLLRR 237
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
754-985 |
1.31e-53 |
|
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: 187.26 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTpderrklfkeqivhqkfNVLLTTYEylMNKHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTG 913
Cdd:cd17994 81 YVGD-----------------HVLLTSYE--LISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109118318 914 TPLQNNLEELWALLNFLLPNIFNSSEDFSQWF---NKPFQsngessaeeallseeenlliINRLHQVLRPFVLRR 985
Cdd:cd17994 142 TPLQNNLEELFHLLNFLTPERFNNLQGFLEEFadiSKEDQ--------------------IKKLHDLLGPHMLRR 196
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
754-985 |
4.58e-52 |
|
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: 184.11 E-value: 4.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKN-DRGpfLVVVPSSVLPGWQSEINFWAPSIHKI 832
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLiKSV--LVVMPTSLIPHWVKEFAKWTPGLRVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 833 VYCGT-PDERRKLFKEqiVHQKFNVLLTTYEYLMN--------KHDRPKlskihWHYIIIDEGHRIKNASCKLNADLKHY 903
Cdd:cd18001 79 VFHGTsKKERERNLER--IQRGGGVLLTTYGMVLSnteqlsadDHDEFK-----WDYVILDEGHKIKNSKTKSAKSLREI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 904 VSSHRLLLTGTPLQNNLEELWALLNFLLP-NIFNSSEDFSQWFNKPFQSngESSAEEALLSEEENLLIINRLHQVLRPFV 982
Cdd:cd18001 152 PAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITR--GRDKDATQGEKALGSEVAENLRQIIKPYF 229
|
...
gi 109118318 983 LRR 985
Cdd:cd18001 230 LRR 232
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
754-985 |
9.04e-52 |
|
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: 183.32 E-value: 9.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLI----CYLMETKNDRG-PFLVVVPSSVLPGWQSEINFWAPS 828
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILasdhHKRANSFNSENlPSLVVCPPTLVGHWVAEIKKYFPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 829 IHK--IVYCGTPDERRKLFKEQIVHqkfNVLLTTYEYLMNKHDrpKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSS 906
Cdd:cd17999 81 AFLkpLAYVGPPQERRRLREQGEKH---NVIVASYDVLRNDIE--VLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKAN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 907 HRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNgeSSAEEALLSEEENLLIINRLH-QVLrPFVLRR 985
Cdd:cd17999 156 HRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILAS--RDSKASAKEQEAGALALEALHkQVL-PFLLRR 232
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
754-932 |
3.18e-50 |
|
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350758 [Multi-domain] Cd Length: 193 Bit Score: 177.52 E-value: 3.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 Y----CGTPDERRKLFKEQ------IVHQKFNVLLTTYEYLMNKHDrpKLSKIHWHYIIIDEGHRIKNASCKLNADLKHY 903
Cdd:cd18000 81 LhssgSGTGSEEKLGSIERksqlirKVVGDGGILITTYEGFRKHKD--LLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
|
170 180
....*....|....*....|....*....
gi 109118318 904 VSSHRLLLTGTPLQNNLEELWALLNFLLP 932
Cdd:cd18000 159 RTPHRLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
754-985 |
4.48e-49 |
|
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: 175.23 E-value: 4.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLIcYLMETKNDRGPFLVVVPSSVLPGWQSEINFWApSIHKIV 833
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFL-SEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQ-----------KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd18058 79 YHGSQISRQMIQQYEMYYRdeqgnplsgifKFQVVITTFEMILA--DCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFnkpfqsnGESSAEEAllseeenlliINRLHQVLRPFV 982
Cdd:cd18058 157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF-------GDLKTEEQ----------VKKLQSILKPMM 219
|
...
gi 109118318 983 LRR 985
Cdd:cd18058 220 LRR 222
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
754-985 |
5.15e-46 |
|
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: 166.77 E-value: 5.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYlMETKNDRGPFLVVVPSSVLPGWQSEINFWApSIHKIV 833
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQE-VYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQ-----------KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd18060 79 YHGSLASRQMIQQYEMYCKdsrgrlipgayKFDALITTFEMILS--DCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFnkpfqsnGESSAEEAllseeenlliINRLHQVLRPFV 982
Cdd:cd18060 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF-------GDLKTEEQ----------VQKLQAILKPMM 219
|
...
gi 109118318 983 LRR 985
Cdd:cd18060 220 LRR 222
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
754-985 |
9.92e-46 |
|
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: 166.31 E-value: 9.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVslynnHLNGILADEMGLGKTVQVISLIC----------YLMETKNDR-------GPFLVVVPSSVLP 816
Cdd:cd18008 1 LLPYQKQGLAWML-----PRGGILADEMGLGKTIQALALILatrpqdpkipEELEENSSDpkklylsKTTLIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 817 GWQSEIN--FWAPSIHKIVYCGtpDERRKLFKEQivhQKFNVLLTTYEYLMN---KHDRPK-----------LSKIHWHY 880
Cdd:cd18008 76 QWKDEIEkhTKPGSLKVYVYHG--SKRIKSIEEL---SDYDIVITTYGTLASefpKNKKGGgrdskekeaspLHRIRWYR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 881 IIIDEGHRIKNAS-------CKLNAdlkhyvsSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNG 953
Cdd:cd18008 151 VILDEAHNIKNRStktsravCALKA-------ERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKND 223
|
250 260 270
....*....|....*....|....*....|..
gi 109118318 954 ESSaeeallseeenlliINRLHQVLRPFVLRR 985
Cdd:cd18008 224 RKA--------------LERLQALLKPILLRR 241
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
754-985 |
1.41e-45 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 165.20 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLIcYLMETKNDRGPFLVVVPSSVLPGWQSEINFWApSIHKIV 833
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQ-----------KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd18059 79 YHGSQASRRTIQLYEMYFKdpqgrvikgsyKFHAIITTFEMILT--DCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFnkpfqsnGESSAEEAllseeenlliINRLHQVLRPFV 982
Cdd:cd18059 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF-------GDLKTEEQ----------VQKLQAILKPMM 219
|
...
gi 109118318 983 LRR 985
Cdd:cd18059 220 LRR 222
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
754-985 |
4.50e-45 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350813 [Multi-domain] Cd Length: 232 Bit Score: 164.41 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDER------------------RKLFKEQIVHQ-KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASC 894
Cdd:cd18055 81 YTGDKDSRaiirenefsfddnavkggKKAFKMKREAQvKFHVLLTSYELVTI--DQAALGSIRWACLVVDEAHRLKNNQS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 895 KLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGessaeeallseeenlliINRL 974
Cdd:cd18055 159 KFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ-----------------IKKL 221
|
250
....*....|.
gi 109118318 975 HQVLRPFVLRR 985
Cdd:cd18055 222 HDLLGPHMLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
754-985 |
5.67e-45 |
|
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: 164.47 E-value: 5.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDR--------------------GPFLVVVPSS 813
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 814 VLPGWQSEINFWApsiHKIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNKHDRpkLSKIHWHYIIIDEGHRIKNAS 893
Cdd:cd18005 81 VLYNWKDELDTWG---HFEVGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDS--LNSINWSAVIADEAHRIKNPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 894 CKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPF---QSNGESSAEEALLSEeenllI 970
Cdd:cd18005 156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgQRHTATARELRLGRK-----R 230
|
250
....*....|....*
gi 109118318 971 INRLHQVLRPFVLRR 985
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
754-985 |
1.18e-42 |
|
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: 157.15 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDER------------------RKLFKEQIVHQ-KFNVLLTTYEYLMNkhDRPKLSKIHWHYIIIDEGHRIKNASC 894
Cdd:cd18057 81 YTGDKESRsvirenefsfednairsgKKVFRMKKEAQiKFHVLLTSYELITI--DQAILGSIEWACLVVDEAHRLKNNQS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 895 KLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGessaeeallseeenlliINRL 974
Cdd:cd18057 159 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ-----------------IKKL 221
|
250
....*....|.
gi 109118318 975 HQVLRPFVLRR 985
Cdd:cd18057 222 HDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
754-985 |
5.07e-42 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350814 [Multi-domain] Cd Length: 232 Bit Score: 155.61 E-value: 5.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIV 833
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDER---------------------RKLFKEQIVhqKFNVLLTTYEYLmnKHDRPKLSKIHWHYIIIDEGHRIKNA 892
Cdd:cd18056 81 YVGDKDSRaiirenefsfednairggkkaSRMKKEASV--KFHVLLTSYELI--TIDMAILGSIDWACLIVDEAHRLKNN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 893 SCKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGessaeeallseeenlliIN 972
Cdd:cd18056 157 QSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ-----------------IK 219
|
250
....*....|...
gi 109118318 973 RLHQVLRPFVLRR 985
Cdd:cd18056 220 KLHDMLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
754-985 |
2.70e-41 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350819 [Multi-domain] Cd Length: 222 Bit Score: 152.85 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETkNDRGPFLVVVPSSVLPGWQSEINFWApSIHKIV 833
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 834 YCGTPDERRKLFKEQIVHQ-----------KFNVLLTTYEYLMNKHdrPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd18061 79 YHGSLISRQMIQQYEMYFRdsqgriirgayRFQAIITTFEMILGGC--PELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFnkpfqsnGESSAEEAllseeenlliINRLHQVLRPFV 982
Cdd:cd18061 157 MNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF-------GDLKTEEQ----------VQKLQAILKPMM 219
|
...
gi 109118318 983 LRR 985
Cdd:cd18061 220 LRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
754-950 |
4.20e-37 |
|
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: 141.65 E-value: 4.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVS--LYNNHLNG---ILADEMGLGKTVQVISLICYLMETKNDRGP----FLVVVPSSVLPGWQSEINF 824
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 825 WAPS--IHKIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNkHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKH 902
Cdd:cd18004 81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRR-HAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 109118318 903 YVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQ 950
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIL 207
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
754-948 |
1.24e-36 |
|
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: 140.12 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLR--W--LVSLYNNHLNG---ILADEMGLGKTVQVISLI-CYLMETKNDRGPfLVVVPSSVLPGWQSEINFW 825
Cdd:cd18007 1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 826 APSIHKIVYCGTPDERRKLFKEQIV-----HQKFNVLLTTYEYLMN----KHDRPKLSKIHWHY--------IIIDEGHR 888
Cdd:cd18007 80 LPPDLRPLLVLVSLSASKRADARLRkinkwHKEGGVLLIGYELFRNlasnATTDPRLKQEFIAAlldpgpdlLVLDEGHR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 889 IKNASCKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKP 948
Cdd:cd18007 160 LKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKP 219
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
753-944 |
1.64e-31 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 124.14 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 753 KLREYQMNGLRWLvslYNNHLNGILADEMGLGKT-VQVISLICYLMetKNDRGPFLVVVPSSVL-PGWQSEINFWAPSIH 830
Cdd:smart00487 8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTlAALLPALEALK--RGKGGRVLVLVPTRELaEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 831 KIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNKHDRPKLSKIHWHYIIIDEGHRIKNAS--CKLNADLKH-YVSSH 907
Cdd:smart00487 83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLlPKNVQ 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 109118318 908 RLLLTGTPLQNNLEELWALLN--FLLPNIFNSSEDFSQW 944
Cdd:smart00487 163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
754-948 |
1.15e-28 |
|
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350824 [Multi-domain] Cd Length: 235 Bit Score: 117.25 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSL-----YNNHLNGILADEMGLGKTVQVISLICYLMETKNDRG-PF----LVVVPSSVLPGWQSEIN 823
Cdd:cd18066 1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkPVikraLIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 824 FWAPSIHKIVYCGTPDERRKLFKEQIVhqkFNVLLTTYEYLMNKHDrpKLSKIHWHYIIIDEGHRIKNASCKLNADLKHY 903
Cdd:cd18066 81 KWLGSERIKVFTVDQDHKVEEFIASPL---YSVLIISYEMLLRSLD--QISKLNFDLVICDEGHRLKNTSIKTTTALTSL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109118318 904 VSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKP 948
Cdd:cd18066 156 SCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEP 200
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
754-953 |
1.61e-28 |
|
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: 116.45 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLvslYNNHLNG------------ILADEMGLGKTVQVISLICYLMETKNDRgPFLVVVPSSVLPGWQSE 821
Cdd:cd18069 1 LKPHQIGGIRFL---YDNIIESlerykgssgfgcILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 822 INFWAPSihkivYCGTPDERRKLFKEQIVH-----------------QKFNVLLTTYEYLMNKhDRPKLskihwhyIIID 884
Cdd:cd18069 77 FNKWLPP-----PEALPNVRPRPFKVFILNdehkttaarakviedwvKDGGVLLMGYEMFRLR-PGPDV-------VICD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109118318 885 EGHRIKNASCKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQsNG 953
Cdd:cd18069 144 EGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL-NG 211
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
754-985 |
4.32e-26 |
|
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350830 [Multi-domain] Cd Length: 241 Bit Score: 109.88 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLYN-NHLNGILADEMGLGKTVQVISLICYLMETKN-----------------DRGPF-----LVVV 810
Cdd:cd18072 1 LLLHQKQALAWLLWRERqKPRGGILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 811 PSSVLPGWQSEINFWAPS--IHKIVYCGTPDERR-KLFKEqivhqkFNVLLTTYEYLMNKHDRPK-------LSKIHWHY 880
Cdd:cd18072 81 PASLVHQWKNEVESRVASnkLRVCLYHGPNRERIgEVLRD------YDIVITTYSLVAKEIPTYKeesrsspLFRIAWAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 881 IIIDEGHRIKN-------ASCKLNAdlkHYvsshRLLLTGTPLQNNLEELWALLNFLLPNIFnssEDFSQWfnKPFQSNG 953
Cdd:cd18072 155 IILDEAHNIKNpkvqasiAVCKLRA---HA----RWALTGTPIQNNLLDMYSLLKFLRCSPF---DDLKVW--KKQVDNK 222
|
250 260 270
....*....|....*....|....*....|..
gi 109118318 954 ESSAEeallseeenlliiNRLHQVLRPFVLRR 985
Cdd:cd18072 223 SRKGG-------------ERLNILTKSLLLRR 241
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1073-1187 |
2.42e-25 |
|
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: 103.06 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1073 GKLEMLDRMLPKLKatDHRVLFFSTMTRLLDvMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPFfifLLSIRAG 1152
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDVA 74
|
90 100 110
....*....|....*....|....*....|....*
gi 109118318 1153 GVGVNLQAADTVILFDTDWNPQVDLQAQARAHRIG 1187
Cdd:pfam00271 75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
775-948 |
3.06e-25 |
|
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: 107.17 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 775 GILADEMGLGKTVQVISLICYlmetkndrGPFLVVVPSSVLPGWQSEINFWAPSIHKIVYCGTPDERRKLFKEQivhQKF 854
Cdd:cd18071 51 GILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLL---SKY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 855 NVLLTTYEYLM----NKHDRPkLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFL 930
Cdd:cd18071 120 DIVLTTYNTLAsdfgAKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFL 198
|
170
....*....|....*...
gi 109118318 931 LPNIFNSSEDFSQWFNKP 948
Cdd:cd18071 199 HLKPFSNPEYWRRLIQRP 216
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
754-945 |
3.40e-24 |
|
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: 104.73 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLynnhlNGILADEMGLGKTVQVISLI----------------------CYLMETKNDR---GPFLV 808
Cdd:cd18070 1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaadddsdemvcCPDCLVAETPvssKATLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 809 VVPSSVLPGWQSEINFWAPSiHKIVYCGTPDERRKLFKEQIVHQ--KFNVLLTTYEYLMN------------------KH 868
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPS-SLKVLTYQGVKKDGALASPAPEIlaEYDIVVTTYDVLRTelhyaeanrsnrrrrrqkRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 869 DRPK--LSKIHWHYIIIDEGHRIKNASCKLnADLKHYVS-SHRLLLTGTPLQNNLEELWALLNFLLPNIFnSSEDFSQWF 945
Cdd:cd18070 155 EAPPspLVLVEWWRVCLDEAQMVESSTSKA-AEMARRLPrVNRWCVSGTPIQRGLDDLFGLLSFLGVEPF-CDSDWWARV 232
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
776-943 |
6.09e-24 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 102.37 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 776 ILADEMGLGKTVQVISLICYLMeTKNDRGPFLVVVPSSVLPGWQSEIN--FWAPSIhkIVYCGTPDERRKLFKEQIVHqk 853
Cdd:cd18011 21 LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQdkFGLPFL--ILDRETAAQLRRLIGNPFEE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 854 FNVLLTTYEYLM-NKHDRPKLSKIHWHYIIIDEGHRIKNASC-------KLNADLKHyVSSHRLLLTGTPLQNNLEELWA 925
Cdd:cd18011 96 FPIVIVSLDLLKrSEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAK-RARHVLLLTATPHNGKEEDFRA 174
|
170
....*....|....*...
gi 109118318 926 LLNFLLPNIFNSSEDFSQ 943
Cdd:cd18011 175 LLSLLDPGRFAVLGRFLR 192
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
754-941 |
1.30e-23 |
|
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: 101.51 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSLynnhlNG--ILADEMGLGKTVQVISLICYLmetKNDrGPFLVVVPSSVLPGWQSEINFWAPSIhk 831
Cdd:cd18010 1 LLPFQREGVCFALRR-----GGrvLIADEMGLGKTVQAIAIAAYY---REE-WPLLIVCPSSLRLTWADEIERWLPSL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 832 ivycgTPDERRKLF--KEQIVHQKFNVLLTTYEyLMNKHDRpKLSKIHWHYIIIDEGHRIKN-------ASCKLnadLKH 902
Cdd:cd18010 70 -----PPDDIQVIVksKDGLRDGDAKVVIVSYD-LLRRLEK-QLLARKFKVVICDESHYLKNskakrtkAALPL---LKR 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 109118318 903 yvSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDF 941
Cdd:cd18010 140 --AKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
754-948 |
1.11e-22 |
|
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: 99.85 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWL----VSLYNNHLNG-ILADEMGLGKTVQVISLICYLMETKNDRGPFL----VVVPSSVLPGWQSEINF 824
Cdd:cd18067 1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 825 WapsIHKIVYCGTPDERRKLFKEQIVHQKFN---------VLLTTYEYLMNKHDrpKLSKIHWHYIIIDEGHRIKNASCK 895
Cdd:cd18067 81 W---LGGRLQPLAIDGGSKKEIDRKLVQWASqqgrrvstpVLIISYETFRLHVE--VLQKGEVGLVICDEGHRLKNSDNQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 109118318 896 LNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKP 948
Cdd:cd18067 156 TYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELP 208
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1103-1187 |
3.20e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 87.27 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1103 DVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPFfifLLSIRAGGVGVNLQAADTVILFDTDWNPQVDLQAQAR 1182
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV---LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 109118318 1183 AHRIG 1187
Cdd:smart00490 78 AGRAG 82
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
775-953 |
4.55e-20 |
|
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: 92.64 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 775 GILADEMGLGKTVQVISLI-CYLMETK-NDRGPFLVVVPSSVLPGWQSEINFWAP--------SIHKIVYCGTPDERRkl 844
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLhTVLLCEKlENFSRVLVVCPLNTVLNWLNEFEKWQEglkdeekiEVNELATYKRPQERS-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 845 FKEQIVHQKFNVLLTTYEYLM------NKHDRPKLSKIHWHY--------IIIDEGHRIKNASCKLNADLKHYVSSHRLL 910
Cdd:cd18068 109 YKLQRWQEEGGVMIIGYDMYRilaqerNVKSREKLKEIFNKAlvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 109118318 911 LTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQsNG 953
Cdd:cd18068 189 LTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NG 230
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
752-1284 |
4.03e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 75.45 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 752 GKLREYQMNGL-RWLVSLYNNHLNGILADEMGLGKTVqvisLICYLMETKNDRGPFLVVVPSSVL-PGWQSEINFWapsi 829
Cdd:COG1061 79 FELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRGKRVLVLVPRRELlEQWAEELRRF---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 830 hkivycgTPDERRKLFKEQIvhqKFNVLLTTYEYLMNKHDRPKLSKiHWHYIIIDEGHRIKNASCKLNADlkHYVSSHRL 909
Cdd:COG1061 151 -------LGDPLAGGGKKDS---DAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHHAGAPSYRRILE--AFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 910 LLTGTPL-QNNLEELWALLNFLLPNIfnsseDFSQwfnkpfqsngessaeeallseeenllIINRlhQVLRPFVLRRlkh 988
Cdd:COG1061 218 GLTATPFrSDGREILLFLFDGIVYEY-----SLKE--------------------------AIED--GYLAPPEYYG--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 989 kVENELPEKIERLIRCEASAYQKLLMkrvednlgsignaksravhnsvMELRNIcnhpylsqlhsEEVNNIIPKHflppi 1068
Cdd:COG1061 262 -IRVDLTDERAEYDALSERLREALAA----------------------DAERKD-----------KILRELLREH----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1069 vrlcgklemldrmlpklkATDHRVLFFSTMTRLLDVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPffiFLLS 1148
Cdd:COG1061 303 ------------------PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR---ILVT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1149 IRAGGVGVNLQAADTVILFD-TDWnPQVDLQAQARAHRIGQKKDVLVLrFETVNSVEEQVRASAEHKLGVANQSITagFF 1227
Cdd:COG1061 362 VDVLNEGVDVPRLDVAILLRpTGS-PREFIQRLGRGLRPAPGKEDALV-YDFVGNDVPVLEELAKDLRDLAGYRVE--FL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 109118318 1228 DNNTSAEDRKEYLESLLRESKKEEDAPVLDDDALNDLIARRESEIDIFESIDKQRKE 1284
Cdd:COG1061 438 DEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALE 494
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
754-930 |
4.74e-12 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 68.15 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGLRWLVSlynNHLNGILADeMGLGKTVQVISLICYLMEtKNDRGPFLVVVPSSVLPG-WQSEINFW-APSIHK 831
Cdd:cd18013 1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 832 I-VYCGTPDERRKLFKEQIvhqkfNVLLTTYEylmNKHDRPKLSKIHWHY--IIIDEGHRIKNASCKLNADLKhyvsSHR 908
Cdd:cd18013 76 VsVAVGTERQRSKAANTPA-----DLYVINRE---NLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALR----KVR 143
|
170 180
....*....|....*....|....*...
gi 109118318 909 ------LLLTGTPLQNNLEELWALLNFL 930
Cdd:cd18013 144 pvikrlIGLTGTPSPNGLMDLWAQIALL 171
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
753-915 |
7.56e-12 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 66.16 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 753 KLREYQMNGL-RWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMEtKNDRGPFLVVVPS-SVLPGWQSEINFWAPSIH 830
Cdd:pfam04851 3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPRkDLLEQALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 831 KIvycgtPDERRKLFKEQIVHQKfNVLLTTYEYLMNKHDRPKLSKI--HWHYIIIDEGHRiknasckLNAD-----LKHY 903
Cdd:pfam04851 82 EI-----GEIISGDKKDESVDDN-KIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHR-------SGASsyrniLEYF 148
|
170
....*....|..
gi 109118318 904 VSSHRLLLTGTP 915
Cdd:pfam04851 149 KPAFLLGLTATP 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
754-915 |
1.36e-11 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 65.02 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 754 LREYQMNGL-RWLVSLYNNHlnGILADEMGLGKTVQVISLICYLMETKndrgpFLVVVPSSVL-PGWQSEINFWapsihk 831
Cdd:cd17926 1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKELR-----TLIVVPTDALlDQWKERFEDF------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 832 ivycgTPDERRKLFKEQIVHQK--FNVLLTTYEYLMNKHDRPKLSKIHWHYIIIDEGHRIknASCKLNADLKHYVSSHRL 909
Cdd:cd17926 68 -----LGDSSIGLIGGGKKKDFddANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL--PAKTFSEILKELNAKYRL 140
|
....*.
gi 109118318 910 LLTGTP 915
Cdd:cd17926 141 GLTATP 146
|
|
| SnAC |
pfam14619 |
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ... |
1281-1368 |
7.72e-10 |
|
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.
Pssm-ID: 464219 [Multi-domain] Cd Length: 69 Bit Score: 57.27 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1281 QRKENEMETWntlvhgpgsdsfahiPSIPSRLVTEDDLKLLYetmklndvpmvakeSTVGMKRKDGSMGGLDTHQYGRGK 1360
Cdd:pfam14619 1 ERRREEAEQL---------------PPLPSRLMEESELPEWY--------------LKDDDEEKKEDKEELDEQVYGRGK 51
|
....*...
gi 109118318 1361 RAREVRSY 1368
Cdd:pfam14619 52 RKRKEVSY 59
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1490-1818 |
1.33e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 57.87 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1490 SSDKRLEAASHPTSSLALTSPDLSGPPGfQSLPASPAPTPIRGRGRGRSRGRGAGRGRRVEGVLHGSNSSITQRTETATS 1569
Cdd:PHA03307 92 LSTLAPASPAREGSPTPPGPSSPDPPPP-TPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1570 LASDA----EATKFALPRSASEIVSRVPKAnEGSTSNPDQVSPVHSATTALRSDKAADKDLDAPPGFDSGSHVQ------ 1639
Cdd:PHA03307 171 QAALPlsspEETARAPSSPPAEPPPSTPPA-AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSEssgcgw 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1640 -----------TLNVLENSSERKAFAVKKRPLIQGVSSQHPGPNKQPLDLPVSTSSTLLGGGPVQNQNAVSSVCDGSKSP 1708
Cdd:PHA03307 250 gpenecplprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1709 SEGRTYTALQGVTTAPSDATLPMSSQPSDATLPmSSQPVGSTVEAQEANvPSLPAALPAKRRVRNLPSRGETPKRQGKRR 1788
Cdd:PHA03307 330 SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP-SSPRKRPRPSRAPSS-PAASAGRPTRRRARAAVAGRARRRDATGRF 407
|
330 340 350
....*....|....*....|....*....|
gi 109118318 1789 GQPLPATDASSARSTGLTPQIEVKVGNLSG 1818
Cdd:PHA03307 408 PAGRPRPSPLDAGAASGAFYARYPLLTPSG 437
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
782-915 |
2.35e-06 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 50.25 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 782 GLGKTVQVISLICYLMEtKNDRGPFLVVVPSSVLpGWQSEINFWAPsihkivycGTPDERRKLFKEQIVHQKFNVLLTTY 861
Cdd:cd18032 30 GTGKTYTAAFLIKRLLE-ANRKKRILFLAHREEL-LEQAERSFKEV--------LPDGSFGNLKGGKKKPDDARVVFATV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 109118318 862 EYLMNKHDRPKLSKIHWHYIIIDEGHRikNASCKLNADLKHYVSSHRLLLTGTP 915
Cdd:cd18032 100 QTLNKRKRLEKFPPDYFDLIIIDEAHH--AIASSYRKILEYFEPAFLLGLTATP 151
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
774-889 |
4.04e-06 |
|
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: 49.32 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 774 NGILADEMGLGKTVQVISLICYLMETKndRGPFLVVVPSSVL-PGWQSEINFWAPSIHKIVYC--GTPDERRKLFKEQiv 850
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALaLQTAERLRELFGPGIRVAVLvgGSSAEEREKNKLG-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 109118318 851 hqKFNVLLTTYEYLMNKHDRPKLSKIH-WHYIIIDEGHRI 889
Cdd:cd00046 79 --DADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHAL 116
|
|
| QLQ |
smart00951 |
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ... |
277-310 |
6.25e-06 |
|
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.
Pssm-ID: 214931 Cd Length: 36 Bit Score: 45.22 E-value: 6.25e-06
10 20 30
....*....|....*....|....*....|....*.
gi 109118318 277 SPFREQQLKQLRAQCLVFLAL--RNGLVPKKLHVEI 310
Cdd:smart00951 1 SPFTPAQLELLRAQILAYKYLlaRNQPVPPELLQAI 36
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
592-729 |
1.14e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 592 GGLEVHKEKLEDLFKVRRERLKGFnRYAKEFHKRKERLHREKIDKIQREKINLlkINDVEGYLRMVQDAKSDRvKQLLKE 671
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLELEKVKL--VNAGSERLRAVKDIKQER-DQLLNE 661
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 109118318 672 TEKYLQKLGSKLKEAKLLTSRFENEADETRTSNATDDETLIENEDESDQAKHYLESNE 729
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1382-1805 |
2.13e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1382 QTESPDSPQGKGEGSERSLAndtsniPVENSSDTLLPTSPTQAITVQPMEPVRPQSHTLKEETQPIKRGRG----RPKRT 1457
Cdd:PHA03247 2594 QSARPRAPVDDRGDPRGPAP------PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvsRPRRA 2667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1458 DKALTPVSLSAVS---RTQATGNAISSAATGLDFVSSDKRLEAASHPTSS-LALTSPDLSGPPGFQSLPASPAPTPIRGR 1533
Cdd:PHA03247 2668 RRLGRAAQASSPPqrpRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSaTPLPPGPAAARQASPALPAAPAPPAVPAG 2747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1534 GRGRSRGRGAGRGRRVEGVLHGS----NSSITQRTETATSLASDAEATKFA-LPRSASEIVSRVPKANEGSTSNPDQVSP 1608
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAppaaPAAGPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPAGP 2827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1609 VHSATTALRSDKAADKDLDAPPGFDSGSHVQTLNVLENSSERKAFAV---KKRPLIQGVSSQHPGPNKQPLDLPvstsst 1685
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpaaPARPPVRRLARPAVSRSTESFALP------ 2901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 1686 llgggpvQNQNAVSSVCDGSKSPSEGRTYTALQGVTTAPSDATLPMSSQPSDATLPMSSQPVGSTVEAQEANVPSLPAAL 1765
Cdd:PHA03247 2902 -------PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 109118318 1766 PAKRRVRNLPSRGETPKRQGKRRGQPLPATdASSARSTGL 1805
Cdd:PHA03247 2975 PRFRVPQPAPSREAPASSTPPLTGHSLSRV-SSWASSLAL 3013
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1143-1195 |
2.86e-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: 41.92 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 109118318 1143 FIFLLSIRAGGVGVNLQAADTVILFDTDWNPQVDLQAQARAHRIGQKKDVLVL 1195
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
3167-3341 |
1.53e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 44.65 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 3167 PSAEPVISEGTELATLPLTEEENADSQLANIEPsssPSVVEKNIEAQDQDQVKTAGCELVSTGCSSEPQVHLPPsaepdg 3246
Cdd:PRK10811 864 VQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITES------ 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109118318 3247 DIHVHLKETEKSEsmvvvgegtafpsslPVTEEGNAESQLADTEPFTSPTVVEKNIKDQEQVETTGCGLVDDSTGCSSEP 3326
Cdd:PRK10811 935 DVAVAQEVAEHAE---------------PVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEP 999
|
170
....*....|....*
gi 109118318 3327 QVQLPPSAEPMEGTH 3341
Cdd:PRK10811 1000 EVAPAQVPEATVEHN 1014
|
|
| |
