|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
978-1213 |
1.35e-131 |
|
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: 411.38 E-value: 1.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 978 AGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVS 1057
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1058 CIYYVGTKDQRSKLFSQEVcAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRC-QRRLLL 1136
Cdd:cd17996 81 KIVYKGTPDVRKKLQSQIR-AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHaRYRLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1137 TGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIeddWLETEKKVIVIHRLHQILEPFMLRRRV 1213
Cdd:cd17996 160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKI---ELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
831-1438 |
2.61e-120 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 408.42 E-value: 2.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 831 REFSKRKDDgRNKRMEALKNNDVERyreMLLEQQTNMPGDAAERY-AVLSSFLTQTEDYLHKLGGkiTATKNQQEVEEAA 909
Cdd:PLN03142 55 AEISKREKA-RLKELKKQKKQEIQK---ILEQQNAAIDADMNNKGkGRLKYLLQQTEIFAHFAKG--DQSASAKKAKGRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 910 NAAAVaarlqgLSEEEvrAAATCAREEvvirnrftemnapkenssvNKYYTLAHAVNEVVvrQPSMLQaGTLRDYQLVGL 989
Cdd:PLN03142 129 RHASK------LTEEE--EDEEYLKEE-------------------EDGLGGSGGTRLLV--QPSCIK-GKMRDYQLAGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 990 QWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIYYVGTKDQRS 1069
Cdd:PLN03142 179 NWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1070 KLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELW 1149
Cdd:PLN03142 259 HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1150 SLLNLLLPDVFDNRKAFHDWfaqpFQKEGPAHNIEddwletekkviVIHRLHQILEPFMLRRRVEDVEGSLPAKVSVVLR 1229
Cdd:PLN03142 339 ALLNFLLPEIFSSAETFDEW----FQISGENDQQE-----------VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1230 CRMSAIQSavyDWIKAtgTLRVDPDDEKLRAQKnpiyqakiyRTLNNRCMELRKACNHPLL------NYPYFNDfskDFL 1303
Cdd:PLN03142 404 VGMSQMQK---QYYKA--LLQKDLDVVNAGGER---------KRLLNIAMQLRKCCNHPYLfqgaepGPPYTTG---EHL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1304 VRSCGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDCFIFLLS 1383
Cdd:PLN03142 467 VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLS 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571243 1384 IRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYM-------EAVVEK 1438
Cdd:PLN03142 547 TRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFcteytieEKVIER 608
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
722-1490 |
9.10e-106 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 355.30 E-value: 9.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 722 RPDLVLRLQIEEKKLRLSDLQSRVREEVDRQQQEIMSMPDRPYRKFVRLCERQRLEMNRQVLANQKAVREKQLKTIFQWR 801
Cdd:COG0553 3 LLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 802 KKLLEAHWAIRDARTARNRGVAKYHEKMLREFSKRKDDGRNKRMEALKNNDVERYREMLLEQQTNMPGDAAERYAVLSSF 881
Cdd:COG0553 83 LLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 882 LTQTEDYLHKLGGKITATKNQQEVEEAANAAAVAARLQGLSEEEVRAAATCAREEVVIRNRFTEMNAPKENssvnkyytl 961
Cdd:COG0553 163 LLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 962 ahavnevvvrQPSMLQAgTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAV 1041
Cdd:COG0553 234 ----------LPAGLKA-TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1042 LVNWKSELHTWLPSVSCIYYVGTKDqRSKLFSQevcAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVL 1121
Cdd:COG0553 302 VGNWQRELAKFAPGLRVLVLDGTRE-RAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1122 ARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAhnieddwletekkviVIHRLH 1201
Cdd:COG0553 378 AKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEE---------------ALERLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1202 QILEPFMLRRRVEDVEGSLPAKVSVVLRCRMSAIQSAVYDWIKAtgtlRVDpddEKLRAQKNPIYQAKIYRTLnnrcMEL 1281
Cdd:COG0553 443 RLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLE----YLR---RELEGAEGIRRRGLILAAL----TRL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1282 RKACNHPLLnypyFNDFSKDFLVRScGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLE 1361
Cdd:COG0553 512 RQICSHPAL----LLEEGAELSGRS-AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1362 DRESAIVDFNDpDTDCFIFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYMeaVVEklss 1441
Cdd:COG0553 587 ERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKL--VAE---- 659
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42571243 1442 hqkedelrsggsvdleddmagkdryiGSIEGLIrNNIQQYKIDMADEVI 1490
Cdd:COG0553 660 --------------------------GTIEEKI-LELLEEKRALAESVL 681
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
984-1288 |
7.21e-81 |
|
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: 268.78 E-value: 7.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 984 YQLVGLQWMLSLYNN-KLNGILADEMGLGKTVQVMALIAYLMEFKGNYG-PHLIIVPNAVLVNWKSELHTWL--PSVSCI 1059
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGT 1139
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1140 PLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahnieddwleTEKKViviHRLHQILEPFMLRRRVEDVEGS 1219
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGV---SRLHKLLKPFLLRRTKKDVEKS 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1220 LPAKVSVVLRCRMSAIQSAVY-DWIkatgtlrvdpDDEKLRAQKNPIYQAKIYRTLNNRCMELRKACNHP 1288
Cdd:pfam00176 227 LPPKVEYILFCRLSKLQRKLYqTFL----------LKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1307-1432 |
1.33e-52 |
|
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: 181.14 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1307 CGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDtDCFIFLLSIRA 1386
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLSTKA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42571243 1387 AGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYM 1432
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
980-1172 |
7.36e-32 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 124.53 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 980 TLRDYQLVGLQWMLSLYNNklnGILADEMGLGKTVQVMALIAYLMeFKGNYGPHLIIVPNAVLV-NWKSELHTWLPS--- 1055
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAeQWAEELKKLGPSlgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1056 VSCIYYVGT--KDQRSKLFSQevcamKFNVLVTTYEFI--MYDRSKLSKVDWKYIIIDEAQRMKD--RESVLARDLDR-Y 1128
Cdd:smart00487 84 KVVGLYGGDskREQLRKLESG-----KTDILVTTPGRLldLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLlP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42571243 1129 RCQRRLLLTGTPLQNdlKELWSLLNLLLPDVFDNRKAFHDWFAQ 1172
Cdd:smart00487 159 KNVQLLLLSATPPEE--IENLLELFLNDPVFIDVGFTPLEPIEQ 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1308-1422 |
1.39e-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: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1308 GKLWILDRILikLQRTGHRVLLFSTMTKLLDilEEYLQWRRLV-YRRIDGTTSLEDRESAIVDFNDPDTDcfiFLLSIRA 1386
Cdd:pfam00271 1 EKLEALLELL--KKERGGKVLIFSQTKKTLE--AELLLEKEGIkVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 42571243 1387 AGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIG 1422
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1338-1422 |
1.05e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 88.04 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1338 DILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDcfiFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVAR 1417
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 42571243 1418 AHRIG 1422
Cdd:smart00490 78 AGRAG 82
|
|
| BROMO |
smart00297 |
bromo domain; |
1900-2004 |
4.76e-14 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 70.00 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1900 IQKRCKIVISKLQRRIDKEGQQIV-PMLTNLWKRIQNGYAAGGVNNLLELREIDHRVERLEYAGVMELASDVQLMLRGAM 1978
Cdd:smart00297 1 DPKLQKKLQELLKAVLDKLDSHPLsWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80
|
90 100
....*....|....*....|....*.
gi 42571243 1979 QFYGFSHEVRSEAKKVHNLFFDLLKM 2004
Cdd:smart00297 81 TYNGPDSEVYKDAKKLEKFFEKKLRE 106
|
|
| QLQ |
smart00951 |
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ... |
462-497 |
1.72e-10 |
|
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: 57.54 E-value: 1.72e-10
10 20 30
....*....|....*....|....*....|....*.
gi 42571243 462 SGFTKQQLHVLKAQILAFRRLKKGEGSLPPELLQAI 497
Cdd:smart00951 1 SPFTPAQLELLRAQILAYKYLLARNQPVPPELLQAI 36
|
|
| QLQ |
pfam08880 |
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ... |
464-497 |
1.84e-07 |
|
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.
Pssm-ID: 462622 Cd Length: 35 Bit Score: 48.87 E-value: 1.84e-07
10 20 30
....*....|....*....|....*....|....
gi 42571243 464 FTKQQLHVLKAQILAFRRLKKGEGsLPPELLQAI 497
Cdd:pfam08880 2 FTPAQLQELRAQILAYKYLSRNQP-VPPELQQAI 34
|
|
| Bromodomain |
cd04369 |
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ... |
1900-2002 |
6.07e-06 |
|
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.
Pssm-ID: 99922 [Multi-domain] Cd Length: 99 Bit Score: 46.60 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1900 IQKRCKIVISKLQRRIDKEGQQIVPMLTnlwKRIQNGYAAGgVNNLLELREIDHRVERLEYAGVMELASDVQLMLRGAMQ 1979
Cdd:cd04369 1 LKKKLRSLLDALKKLKRDLSEPFLEPVD---PKEAPDYYEV-IKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKT 76
|
90 100
....*....|....*....|...
gi 42571243 1980 FYGFSHEVRSEAKKVHNLFFDLL 2002
Cdd:cd04369 77 YNGPGSPIYKDAKKLEKLFEKLL 99
|
|
| COG4646 |
COG4646 |
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]; |
965-1127 |
1.88e-03 |
|
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
Pssm-ID: 443684 [Multi-domain] Cd Length: 1711 Bit Score: 43.70 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 965 VNEVVVRQ--------PSMLQAGTLRDYQLVGLqWMLsLYNNklNGILADEMGLGKTVqVMALIAylMEFK--GNYGPHL 1034
Cdd:COG4646 865 FNSIVPREydgshlkfPGDSRKISLRPHQKNAV-ARI-LYGG--NTLLAHEVGAGKTF-TMVAAA--MELRrlGLANKPM 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1035 IIVPNAVLVNW-KSELHTWLPSVSCIYyvgTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQR 1113
Cdd:COG4646 938 IVVPNHLLEQDaPSKLNLYAAANILIA---TKTDFEKGTRLVFCADIATGDYDAVIIGHIQFEKIPASGERQEEILEEQI 1014
|
170
....*....|....
gi 42571243 1114 MKDRESVLARDLDR 1127
Cdd:COG4646 1015 AEILKAIKELKAVV 1028
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
978-1213 |
1.35e-131 |
|
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: 411.38 E-value: 1.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 978 AGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVS 1057
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1058 CIYYVGTKDQRSKLFSQEVcAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRC-QRRLLL 1136
Cdd:cd17996 81 KIVYKGTPDVRKKLQSQIR-AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHaRYRLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1137 TGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIeddWLETEKKVIVIHRLHQILEPFMLRRRV 1213
Cdd:cd17996 160 TGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKI---ELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
831-1438 |
2.61e-120 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 408.42 E-value: 2.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 831 REFSKRKDDgRNKRMEALKNNDVERyreMLLEQQTNMPGDAAERY-AVLSSFLTQTEDYLHKLGGkiTATKNQQEVEEAA 909
Cdd:PLN03142 55 AEISKREKA-RLKELKKQKKQEIQK---ILEQQNAAIDADMNNKGkGRLKYLLQQTEIFAHFAKG--DQSASAKKAKGRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 910 NAAAVaarlqgLSEEEvrAAATCAREEvvirnrftemnapkenssvNKYYTLAHAVNEVVvrQPSMLQaGTLRDYQLVGL 989
Cdd:PLN03142 129 RHASK------LTEEE--EDEEYLKEE-------------------EDGLGGSGGTRLLV--QPSCIK-GKMRDYQLAGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 990 QWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIYYVGTKDQRS 1069
Cdd:PLN03142 179 NWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1070 KLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELW 1149
Cdd:PLN03142 259 HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1150 SLLNLLLPDVFDNRKAFHDWfaqpFQKEGPAHNIEddwletekkviVIHRLHQILEPFMLRRRVEDVEGSLPAKVSVVLR 1229
Cdd:PLN03142 339 ALLNFLLPEIFSSAETFDEW----FQISGENDQQE-----------VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1230 CRMSAIQSavyDWIKAtgTLRVDPDDEKLRAQKnpiyqakiyRTLNNRCMELRKACNHPLL------NYPYFNDfskDFL 1303
Cdd:PLN03142 404 VGMSQMQK---QYYKA--LLQKDLDVVNAGGER---------KRLLNIAMQLRKCCNHPYLfqgaepGPPYTTG---EHL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1304 VRSCGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDCFIFLLS 1383
Cdd:PLN03142 467 VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLS 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571243 1384 IRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYM-------EAVVEK 1438
Cdd:PLN03142 547 TRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFcteytieEKVIER 608
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
722-1490 |
9.10e-106 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 355.30 E-value: 9.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 722 RPDLVLRLQIEEKKLRLSDLQSRVREEVDRQQQEIMSMPDRPYRKFVRLCERQRLEMNRQVLANQKAVREKQLKTIFQWR 801
Cdd:COG0553 3 LLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 802 KKLLEAHWAIRDARTARNRGVAKYHEKMLREFSKRKDDGRNKRMEALKNNDVERYREMLLEQQTNMPGDAAERYAVLSSF 881
Cdd:COG0553 83 LLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 882 LTQTEDYLHKLGGKITATKNQQEVEEAANAAAVAARLQGLSEEEVRAAATCAREEVVIRNRFTEMNAPKENssvnkyytl 961
Cdd:COG0553 163 LLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 962 ahavnevvvrQPSMLQAgTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAV 1041
Cdd:COG0553 234 ----------LPAGLKA-TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1042 LVNWKSELHTWLPSVSCIYYVGTKDqRSKLFSQevcAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVL 1121
Cdd:COG0553 302 VGNWQRELAKFAPGLRVLVLDGTRE-RAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1122 ARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAhnieddwletekkviVIHRLH 1201
Cdd:COG0553 378 AKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEE---------------ALERLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1202 QILEPFMLRRRVEDVEGSLPAKVSVVLRCRMSAIQSAVYDWIKAtgtlRVDpddEKLRAQKNPIYQAKIYRTLnnrcMEL 1281
Cdd:COG0553 443 RLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLE----YLR---RELEGAEGIRRRGLILAAL----TRL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1282 RKACNHPLLnypyFNDFSKDFLVRScGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLE 1361
Cdd:COG0553 512 RQICSHPAL----LLEEGAELSGRS-AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1362 DRESAIVDFNDpDTDCFIFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYMeaVVEklss 1441
Cdd:COG0553 587 ERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKL--VAE---- 659
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42571243 1442 hqkedelrsggsvdleddmagkdryiGSIEGLIrNNIQQYKIDMADEVI 1490
Cdd:COG0553 660 --------------------------GTIEEKI-LELLEEKRALAESVL 681
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
984-1288 |
7.21e-81 |
|
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: 268.78 E-value: 7.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 984 YQLVGLQWMLSLYNN-KLNGILADEMGLGKTVQVMALIAYLMEFKGNYG-PHLIIVPNAVLVNWKSELHTWL--PSVSCI 1059
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGT 1139
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1140 PLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahnieddwleTEKKViviHRLHQILEPFMLRRRVEDVEGS 1219
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGV---SRLHKLLKPFLLRRTKKDVEKS 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1220 LPAKVSVVLRCRMSAIQSAVY-DWIkatgtlrvdpDDEKLRAQKNPIYQAKIYRTLNNRCMELRKACNHP 1288
Cdd:pfam00176 227 LPPKVEYILFCRLSKLQRKLYqTFL----------LKKDLNAIKTGEGGREIKASLLNILMRLRKICNHP 286
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
979-1211 |
1.72e-79 |
|
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: 261.87 E-value: 1.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 979 GTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSC 1058
Cdd:cd17997 2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1059 IYYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTG 1138
Cdd:cd17997 82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571243 1139 TPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpaHNIEDDWLEtekkviVIHRLHQILEPFMLRR 1211
Cdd:cd17997 162 TPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV--------NNCDDDNQE------VVQRLHKVLRPFLLRR 220
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
979-1211 |
2.38e-75 |
|
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: 250.77 E-value: 2.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 979 GTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSC 1058
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1059 IYYVGTKDQRSKL----FSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRL 1134
Cdd:cd18009 81 LLYHGTKEERERLrkkiMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1135 LLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEddwLETEKKVIVIHRLHQILEPFMLRR 1211
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISN---LSEEREQNIVHMLHAILKPFLLRR 234
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
958-1211 |
4.40e-74 |
|
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: 247.67 E-value: 4.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 958 YYTLAHAVNEVVVRQPSMLQAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIV 1037
Cdd:cd18063 1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1038 PNAVLVNWKSELHTWLPSVSCIYYVGTKDQRSKLFSQeVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDR 1117
Cdd:cd18063 81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1118 ESVLARDLD-RYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahniEDDWLETEKKVIV 1196
Cdd:cd18063 160 HCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG-----ERVDLNEEETILI 234
|
250
....*....|....*
gi 42571243 1197 IHRLHQILEPFMLRR 1211
Cdd:cd18063 235 IRRLHKVLRPFLLRR 249
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
958-1211 |
6.44e-72 |
|
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: 241.49 E-value: 6.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 958 YYTLAHAVNEVVVRQPSMLQAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIV 1037
Cdd:cd18062 1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1038 PNAVLVNWKSELHTWLPSVSCIYYVGTKDQRsKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDR 1117
Cdd:cd18062 81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1118 ESVLARDLD-RYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahniEDDWLETEKKVIV 1196
Cdd:cd18062 160 HCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG-----EKVDLNEEETILI 234
|
250
....*....|....*
gi 42571243 1197 IHRLHQILEPFMLRR 1211
Cdd:cd18062 235 IRRLHKVLRPFLLRR 249
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
981-1211 |
1.02e-71 |
|
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: 239.56 E-value: 1.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKL---FSQEVCamkFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLT 1137
Cdd:cd18003 81 YYGSAKERKLKrqgWMKPNS---FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1138 GTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQP---FQKEGPAHNIEddwletekkviVIHRLHQILEPFMLRR 1211
Cdd:cd18003 158 GTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltaMSEGSQEENEE-----------LVRRLHKVLRPFLLRR 223
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
981-1147 |
1.29e-68 |
|
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: 228.99 E-value: 1.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVCaMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTP 1140
Cdd:cd17919 81 YHGSQRERAQIRAKEKL-DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
....*..
gi 42571243 1141 LQNDLKE 1147
Cdd:cd17919 160 LQNNLEE 166
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
980-1211 |
2.08e-66 |
|
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: 224.16 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 980 TLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCI 1059
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YYVGTKDQRS-----KLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRL 1134
Cdd:cd17993 81 VYLGDIKSRDtireyEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1135 LLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDwfaqpfqkegpAHNieddwLETEKKvivIHRLHQILEPFMLRR 1211
Cdd:cd17993 161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE-----------EHD-----EEQEKG---IADLHKELEPFILRR 218
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
973-1223 |
1.57e-61 |
|
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: 211.45 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 973 PSMLQAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTW 1052
Cdd:cd18064 8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1053 LPSVSCIYYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQR 1132
Cdd:cd18064 88 VPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1133 RLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieDDWLETEKkviVIHRLHQILEPFMLRRR 1212
Cdd:cd18064 168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT------------NNCLGDQK---LVERLHMVLRPFLLRRI 232
|
250
....*....|.
gi 42571243 1213 VEDVEGSLPAK 1223
Cdd:cd18064 233 KADVEKSLPPK 243
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
981-1211 |
1.97e-61 |
|
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: 210.18 E-value: 1.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPsVSCIY 1060
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVCAM-----------KFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd17995 80 YHGSGESRQIIQQYEMYFKdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieddwLETEKKViviHRLHQILEPFML 1209
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGD---------------LKTAEQV---EKLQALLKPYML 221
|
..
gi 42571243 1210 RR 1211
Cdd:cd17995 222 RR 223
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
973-1211 |
1.17e-60 |
|
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: 208.33 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 973 PSMLQAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTW 1052
Cdd:cd18065 8 PSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1053 LPSVSCIYYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQR 1132
Cdd:cd18065 88 VPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571243 1133 RLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieDDWLETEKkviVIHRLHQILEPFMLRR 1211
Cdd:cd18065 168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT------------KNCLGDQK---LVERLHAVLKPFLLRR 231
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
981-1211 |
1.51e-56 |
|
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: 196.57 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRS---KLFSQEVCAMK---FNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRL 1134
Cdd:cd18002 81 YWGNPKDRKvlrKFWDRKNLYTRdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1135 LLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAqpfqKEGPAHNIEDDWLETEKkvivIHRLHQILEPFMLRR 1211
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFS----KDIESHAENKTGLNEHQ----LKRLHMILKPFMLRR 229
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
981-1211 |
1.52e-56 |
|
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: 195.73 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTP 1140
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571243 1141 LQNDLKELWSLLNLLLPDVFDNRKAfhDWFAQPFQkegpahnieddwlETEKKVIVIHRLHQILEPFMLRR 1211
Cdd:cd18006 161 IQNSLQELYALLSFIEPNVFPKDKL--DDFIKAYS-------------ETDDESETVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
981-1147 |
5.80e-54 |
|
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: 187.21 E-value: 5.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVC-AMKFNVLVTTYEFIM---YDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLL 1136
Cdd:cd17998 80 YYGSQEERKHLRYDILKgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
|
170
....*....|.
gi 42571243 1137 TGTPLQNDLKE 1147
Cdd:cd17998 160 TGTPLQNNLLE 170
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1307-1432 |
1.33e-52 |
|
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: 181.14 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1307 CGKLWILDRILIKLQRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDtDCFIFLLSIRA 1386
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLSTKA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42571243 1387 AGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYM 1432
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
971-1211 |
6.60e-52 |
|
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: 183.28 E-value: 6.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 971 RQPSML--QAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSE 1048
Cdd:cd18054 9 KQPSYIggENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1049 LHTWLPSVSCIYYVGTKDQRSKL-----FSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLAR 1123
Cdd:cd18054 89 FEIWAPEINVVVYIGDLMSRNTIreyewIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1124 DLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDwfaqpfqKEGPAHniEDDWletekkviviHRLHQI 1203
Cdd:cd18054 169 TLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGR--ENGY----------QSLHKV 229
|
....*...
gi 42571243 1204 LEPFMLRR 1211
Cdd:cd18054 230 LEPFLLRR 237
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
979-1212 |
2.64e-51 |
|
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: 180.84 E-value: 2.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 979 GTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSC 1058
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1059 IYYVGTKDQRSKLFSQEvcamKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTG 1138
Cdd:cd18012 82 LVIHGTKRKREKLRALE----DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571243 1139 TPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEddwletekkvivihRLHQILEPFMLRRR 1212
Cdd:cd18012 158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALE--------------ELKKLISPFILRRL 217
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
981-1211 |
3.30e-45 |
|
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: 162.61 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTkdqrsklfsqevcamkfNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTP 1140
Cdd:cd17994 81 YVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571243 1141 LQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahnieddwletekkvivIHRLHQILEPFMLRR 1211
Cdd:cd17994 144 LQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQ------------------IKKLHDLLGPHMLRR 196
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
981-1211 |
4.49e-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: 164.09 E-value: 4.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGN--------------------YGPHLIIVPNA 1040
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTrrdrennrprfkkkppassaKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1041 VLVNWKSELHTWLP-SVSCIYYVGTKDQRSklfsQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRES 1119
Cdd:cd18005 81 VLYNWKDELDTWGHfEVGVYHGSRKDDELE----GRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1120 VLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFqKEGPAHNIEDDWLETEKKVIVihR 1199
Cdd:cd18005 157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPI-KRGQRHTATARELRLGRKRKQ--E 233
|
250
....*....|..
gi 42571243 1200 LHQILEPFMLRR 1211
Cdd:cd18005 234 LAVKLSKFFLRR 245
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
971-1211 |
9.63e-45 |
|
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: 162.91 E-value: 9.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 971 RQPSML---QAGTLRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKS 1047
Cdd:cd18053 8 KQPSYIgghEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1048 ELHTWLPSVSCIYYVGTKDQRSKLFSQE-----VCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLA 1122
Cdd:cd18053 88 EIQTWAPQMNAVVYLGDINSRNMIRTHEwmhpqTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1123 RDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDvfdnrkAFHDWfaQPFQKEgpaHNIEDDWLETEkkvivihrLHQ 1202
Cdd:cd18053 168 KTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFSSW--EDFEEE---HGKGREYGYAS--------LHK 228
|
....*....
gi 42571243 1203 ILEPFMLRR 1211
Cdd:cd18053 229 ELEPFLLRR 237
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
981-1211 |
1.23e-41 |
|
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: 153.27 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMeFKGNYGPHLIIVPNAVLVNWKSELHTWlPSVSCIY 1060
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTW-TEMNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVC-----------AMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd18058 79 YHGSQISRQMIQQYEMYyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieddwLETEKKViviHRLHQILEPFML 1209
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD---------------LKTEEQV---KKLQSILKPMML 220
|
..
gi 42571243 1210 RR 1211
Cdd:cd18058 221 RR 222
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
981-1147 |
3.18e-40 |
|
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: 148.24 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLP------ 1054
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1055 ------SVSCIYYVGTKDQRSKLFSQEVcaMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRY 1128
Cdd:cd18000 81 lhssgsGTGSEEKLGSIERKSQLIRKVV--GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
|
170
....*....|....*....
gi 42571243 1129 RCQRRLLLTGTPLQNDLKE 1147
Cdd:cd18000 159 RTPHRLILSGTPIQNNLKE 177
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
981-1211 |
3.55e-40 |
|
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: 149.75 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLynnklNGILADEMGLGKTVQVMALIA---------------YLMEFKGNYGPH--LIIVPNAVLV 1043
Cdd:cd18008 1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALILatrpqdpkipeeleeNSSDPKKLYLSKttLIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1044 NWKSEL--HTWLPSVS-CIYYvgtKDQRSKLFSQevcAMKFNVLVTTY-----EF-----------IMYDRSKLSKVDWK 1104
Cdd:cd18008 76 QWKDEIekHTKPGSLKvYVYH---GSKRIKSIEE---LSDYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1105 YIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAhnie 1184
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK---- 225
|
250 260
....*....|....*....|....*..
gi 42571243 1185 ddwletekkviVIHRLHQILEPFMLRR 1211
Cdd:cd18008 226 -----------ALERLQALLKPILLRR 241
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
981-1211 |
9.58e-40 |
|
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: 148.29 E-value: 9.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEV-------------------CAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVL 1121
Cdd:cd18056 81 YVGDKDSRAIIRENEFsfednairggkkasrmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1122 ARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahnieddwletekkvivIHRLH 1201
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ------------------IKKLH 222
|
250
....*....|
gi 42571243 1202 QILEPFMLRR 1211
Cdd:cd18056 223 DMLGPHMLRR 232
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
981-1211 |
1.55e-39 |
|
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: 147.52 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEV-------------------CAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVL 1121
Cdd:cd18057 81 YTGDKESRSVIRENEFsfednairsgkkvfrmkkeAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1122 ARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGpahnieddwletekkvivIHRLH 1201
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ------------------IKKLH 222
|
250
....*....|
gi 42571243 1202 QILEPFMLRR 1211
Cdd:cd18057 223 DLLGPHMLRR 232
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
981-1211 |
3.32e-39 |
|
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: 146.69 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWLPSVSCIY 1060
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKL----FSQEVCAMK---------------FNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVL 1121
Cdd:cd18055 81 YTGDKDSRAIIreneFSFDDNAVKggkkafkmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1122 ARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpFQKEGPahnieddwletekkvivIHRLH 1201
Cdd:cd18055 161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD-ISKEDQ-----------------IKKLH 222
|
250
....*....|
gi 42571243 1202 QILEPFMLRR 1211
Cdd:cd18055 223 DLLGPHMLRR 232
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
981-1211 |
3.57e-38 |
|
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: 143.27 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAVLVNWKSELHTWlPSVSCIY 1060
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTW-TEMNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEV-C----------AMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd18060 79 YHGSLASRQMIQQYEMyCkdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieddwLETEKKViviHRLHQILEPFML 1209
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---------------LKTEEQV---QKLQAILKPMML 220
|
..
gi 42571243 1210 RR 1211
Cdd:cd18060 221 RR 222
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
981-1211 |
4.99e-38 |
|
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: 142.86 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIaYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWlPSVSCIY 1060
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-TELNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVC-----------AMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd18059 79 YHGSQASRRTIQLYEMYfkdpqgrvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieddwLETEKKViviHRLHQILEPFML 1209
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---------------LKTEEQV---QKLQAILKPMML 220
|
..
gi 42571243 1210 RR 1211
Cdd:cd18059 221 RR 222
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
981-1211 |
2.76e-37 |
|
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: 141.33 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIA---YL--MEFKGNYGPHLIIVPNAVLVNWKSELHTWLP- 1054
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhHKraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1055 -SVSCIYYVGTKDQRSKLFSQEVCAmkfNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRR 1133
Cdd:cd17999 81 aFLKPLAYVGPPQERRRLREQGEKH---NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571243 1134 LLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKegpAHNIEDDWLETEKKVIVIHRLHQILEPFMLRR 1211
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILA---SRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
981-1211 |
1.12e-36 |
|
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: 139.43 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIAYLmeFKGNYGPH-LIIVPNAVLVNWKSELHTWLPSVSCI 1059
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGM--FDSGLIKSvLVVMPTSLIPHWVKEFAKWTPGLRVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YYVGT-KDQRSKlfSQEVCAMKFNVLVTTYEFIMYDRSKLSKVD-----WKYIIIDEAQRMKDRESVLARDLDRYRCQRR 1133
Cdd:cd18001 79 VFHGTsKKERER--NLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1134 LLLTGTPLQNDLKELWSllnlllpdVFD---------NRKAFHDWFAQPFQKeGPAHNIEDDwletEKKV--IVIHRLHQ 1202
Cdd:cd18001 157 IILTGTPIQNNLKELWA--------LFDfacngsllgTRKTFKMEFENPITR-GRDKDATQG----EKALgsEVAENLRQ 223
|
....*....
gi 42571243 1203 ILEPFMLRR 1211
Cdd:cd18001 224 IIKPYFLRR 232
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
981-1211 |
3.56e-35 |
|
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: 135.49 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLS--LYNNKLNG---ILADEMGLGKTVQVMALIAYLMEFKGNYGPH----LIIVPNAVLVNWKSELHT 1051
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1052 WLPSVSCIYYvgTKDQRSKLFSQEVCAMK----FNVLVTTYE-FIMYDR--SKLSKVDwkYIIIDEAQRMKDRESVLARD 1124
Cdd:cd18004 81 WLGLRRIKVV--TADGNAKDVKASLDFFSsastYPVLIISYEtLRRHAEklSKKISID--LLICDEGHRLKNSESKTTKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1125 LDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEDDWLETEKKViviHRLHQIL 1204
Cdd:cd18004 157 LNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERS---QELSELT 233
|
....*..
gi 42571243 1205 EPFMLRR 1211
Cdd:cd18004 234 SRFILRR 240
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
981-1211 |
4.26e-35 |
|
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: 134.36 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNGILADEMGLGKTVQVMALIaYLMEFKGNYGPHLIIVPNAVLVNWKSELHTWlPSVSCIY 1060
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTW-TDLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1061 YVGTKDQRSKLFSQEVC-----------AMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd18061 79 YHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQpfqkegpahnieddwLETEKKViviHRLHQILEPFML 1209
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LKTEEQV---QKLQAILKPMML 220
|
..
gi 42571243 1210 RR 1211
Cdd:cd18061 221 RR 222
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
980-1172 |
7.36e-32 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 124.53 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 980 TLRDYQLVGLQWMLSLYNNklnGILADEMGLGKTVQVMALIAYLMeFKGNYGPHLIIVPNAVLV-NWKSELHTWLPS--- 1055
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAeQWAEELKKLGPSlgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1056 VSCIYYVGT--KDQRSKLFSQevcamKFNVLVTTYEFI--MYDRSKLSKVDWKYIIIDEAQRMKD--RESVLARDLDR-Y 1128
Cdd:smart00487 84 KVVGLYGGDskREQLRKLESG-----KTDILVTTPGRLldLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLlP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42571243 1129 RCQRRLLLTGTPLQNdlKELWSLLNLLLPDVFDNRKAFHDWFAQ 1172
Cdd:smart00487 159 KNVQLLLLSATPPEE--IENLLELFLNDPVFIDVGFTPLEPIEQ 200
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
981-1193 |
6.53e-26 |
|
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: 108.53 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWM-----LSLYNNKLNG--ILADEMGLGKTVQVMALI-AYLMEFKGNYGPhLIIVPNAVLVNWKSELHTW 1052
Cdd:cd18007 1 LKPHQVEGVRFLwsnlvGTDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1053 LPSVSCIYYVGTKDQRSKLFSQevCAMKFN-------VLVTTYEF---IMYDRSKLSKVDWKY-----------IIIDEA 1111
Cdd:cd18007 80 LPPDLRPLLVLVSLSASKRADA--RLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlLVLDEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1112 QRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEDDWLETE 1191
Cdd:cd18007 158 HRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLML 237
|
..
gi 42571243 1192 KK 1193
Cdd:cd18007 238 KR 239
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1308-1422 |
1.39e-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: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1308 GKLWILDRILikLQRTGHRVLLFSTMTKLLDilEEYLQWRRLV-YRRIDGTTSLEDRESAIVDFNDPDTDcfiFLLSIRA 1386
Cdd:pfam00271 1 EKLEALLELL--KKERGGKVLIFSQTKKTLE--AELLLEKEGIkVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 42571243 1387 AGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIG 1422
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
981-1173 |
2.96e-25 |
|
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: 106.47 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQW-----MLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPH------LIIVPNAVLVNWKSEL 1049
Cdd:cd18066 1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1050 HTWLPSVSCIYYVGTKDQRSKLFsqeVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR 1129
Cdd:cd18066 80 QKWLGSERIKVFTVDQDHKVEEF---IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42571243 1130 CQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQP 1173
Cdd:cd18066 157 CERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEP 200
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
981-1211 |
2.03e-22 |
|
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: 97.66 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSlynNKLNGILADEMGLGKTVQVMALIAYLMEfkgnYGPHLIIVPNAVLVNWKSELHTWLPSVS--C 1058
Cdd:cd18010 1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPSLPpdD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1059 IYYVGT-KDQRSKLFSQevcamkfnVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRY--RCQRRLL 1135
Cdd:cd18010 74 IQVIVKsKDGLRDGDAK--------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVIL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1136 LTGTP-------LQNDLKelwsllnLLLPDVFDNRKAFHDWFAQPFQK------EGPAHNIEddwletekkvivihrLHQ 1202
Cdd:cd18010 146 LSGTPalsrpieLFTQLD-------ALDPKLFGRFHDFGRRYCAAKQGgfgwdySGSSNLEE---------------LHL 203
|
250
....*....|
gi 42571243 1203 ILEP-FMLRR 1211
Cdd:cd18010 204 LLLAtIMIRR 213
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1338-1422 |
1.05e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 88.04 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1338 DILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDcfiFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVAR 1417
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77
|
....*
gi 42571243 1418 AHRIG 1422
Cdd:smart00490 78 AGRAG 82
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
981-1175 |
2.34e-20 |
|
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: 92.19 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWM-------LSLYNNK--LNGILADEMGLGKTVQVMALIAYLMEFKGnYGPHLIIVPNAVLVNWKSELHT 1051
Cdd:cd18069 1 LKPHQIGGIRFLydniiesLERYKGSsgFGCILAHSMGLGKTLQVISFLDVLLRHTG-AKTVLAIVPVNTLQNWLSEFNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1052 WLPSVSCIYYVG--------------TKDQRSKLFSQEVcaMKFNVLVTTYEfiMYDRSKLSKVdwkyIIIDEAQRMKDR 1117
Cdd:cd18069 80 WLPPPEALPNVRprpfkvfilndehkTTAARAKVIEDWV--KDGGVLLMGYE--MFRLRPGPDV----VICDEGHRIKNC 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42571243 1118 ESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQ 1175
Cdd:cd18069 152 HASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
981-1211 |
7.71e-20 |
|
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: 90.99 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNG-----ILADEMGLGKTVQVMALIAYLM----EFKGNYGPHLIIVPNAVLVNWKSELHT 1051
Cdd:cd18067 1 LRPHQREGVKFLYRCVTGRRIRgshgcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1052 WL-PSVSCIYYVG-TKDQRSKLFSQEVCAMKFN----VLVTTYEFIMYDRSKLSKVDWKYIIIDEAQRMKDRESVLARDL 1125
Cdd:cd18067 81 WLgGRLQPLAIDGgSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1126 DRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQKEGPAHNIEDDWLETEKKvivIHRLHQILE 1205
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEK---LQELISIVN 237
|
....*.
gi 42571243 1206 PFMLRR 1211
Cdd:cd18067 238 RCIIRR 243
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
981-1173 |
2.85e-18 |
|
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: 86.37 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKL-----------------------------NGILADEMGLGKTVQVMALIAYlmefkgnyG 1031
Cdd:cd18071 1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLILA--------N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1032 PHLIIVPNAVLVNWKSELHTWLPSVSC---IYYVGTKDQRSKLFsqevcaMKFNVLVTTY-----EFIMYDRSKLSKVDW 1103
Cdd:cd18071 73 FTLIVCPLSVLSNWETQFEEHVKPGQLkvyTYHGGERNRDPKLL------SKYDIVLTTYntlasDFGAKGDSPLHTINW 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1104 KYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQP 1173
Cdd:cd18071 147 LRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRP 216
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
981-1145 |
3.71e-18 |
|
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: 86.63 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLynnklNGILADEMGLGKTVQVMALI------------AYLMEFKGNYGPH-------------LI 1035
Cdd:cd18070 1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCCPDclvaetpvsskatLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1036 IVPNAVLVNWKSELHTWLP-SVSCIYYVGtkdQRSKLFSQEVCAMKFN---VLVTTYE-------FIMY----------- 1093
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPsSLKVLTYQG---VKKDGALASPAPEILAeydIVVTTYDvlrtelhYAEAnrsnrrrrrqk 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 42571243 1094 ----DRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDL 1145
Cdd:cd18070 153 ryeaPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGL 208
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
981-1176 |
1.55e-16 |
|
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: 81.47 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLN---------GILADEMGLGKTVQVMALIAYLM--EFKGNYGPHLIIVPNAVLVNWKSEL 1049
Cdd:cd18068 1 LKPHQVDGVQFMWDCCCESLKktkkspgsgCILAHCMGLGKTLQVVTFLHTVLlcEKLENFSRVLVVCPLNTVLNWLNEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1050 HTWLP--------SVSCIYYVGTKDQRS-KLF-SQE---VCAMKFNVlvttYEFIMYDRSKLSKVDWK------------ 1104
Cdd:cd18068 81 EKWQEglkdeekiEVNELATYKRPQERSyKLQrWQEeggVMIIGYDM----YRILAQERNVKSREKLKeifnkalvdpgp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571243 1105 -YIIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNRKAFHDWFAQPFQK 1176
Cdd:cd18068 157 dFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQN 229
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
981-1147 |
1.99e-16 |
|
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: 80.03 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLngILADEMGLGKTVQVMALIAYLMeFKGNYGPHLIIVPNAVLVNWKSELHT--WLPsvsc 1058
Cdd:cd18011 1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELL-LRGDAKRVLILCPASLVEQWQDELQDkfGLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1059 IYYVGTKDQRSKLFSQEVCAMKFNVLVTTYEFIM---YDRSKLSKVDWKYIIIDEAQRM-------KDRESVLARDLDRy 1128
Cdd:cd18011 74 FLILDRETAAQLRRLIGNPFEEFPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLrnsgggkETKRYKLGRLLAK- 152
|
170
....*....|....*....
gi 42571243 1129 RCQRRLLLTGTPLQNDLKE 1147
Cdd:cd18011 153 RARHVLLLTATPHNGKEED 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
978-1570 |
2.06e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.99 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 978 AGTLRDYQLVGL-QWMLSLYNNKLNGILADEMGLGKTVqVMALIAYLMEFKGNYgphLIIVPNAVLVN-WKSELHTWLPS 1055
Cdd:COG1061 78 SFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTV-LALALAAELLRGKRV---LVLVPRRELLEqWAEELRRFLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1056 vscIYYVGTKDQRSklfsqevcamkFNVLVTTYE-FIMYDRSKLSKVDWKYIIIDEAQRMkdRESVLARDLDRYRCQRRL 1134
Cdd:COG1061 154 ---PLAGGGKKDSD-----------APITVATYQsLARRAHLDELGDRFGLVIIDEAHHA--GAPSYRRILEAFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1135 LLTGTPLQNDLKELwsllnlllpdvfdnrkaFHDWFaqpfqkEGPAHNIeddwletekkvivihRLHQILEpfmlrrrve 1214
Cdd:COG1061 218 GLTATPFRSDGREI-----------------LLFLF------DGIVYEY---------------SLKEAIE--------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1215 dvEGSLpAKVSVVlrcrmsaiqsavydwikatgTLRVDPDDEKLRaqknpiyqakiyrtlnnrcmelrkacnhpllnYPY 1294
Cdd:COG1061 251 --DGYL-APPEYY--------------------GIRVDLTDERAE--------------------------------YDA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1295 FNDFSKDFLVRSC-GKLWILDRILIKLqRTGHRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDP 1373
Cdd:COG1061 276 LSERLREALAADAeRKDKILRELLREH-PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1374 DTDcfiFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQTREVKVIYMEAV--VEKLSSHQKEDELRSG 1451
Cdd:COG1061 355 ELR---ILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGndVPVLEELAKDLRDLAG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1452 GSVDLEDDMAGKDRYIGSIEGLIRNNIQQYKIDMADEVINAGRFDQRTTHEERRMTLETLLHDEERYQETVHDVPSLHEV 1531
Cdd:COG1061 432 YRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEE 511
|
570 580 590
....*....|....*....|....*....|....*....
gi 42571243 1532 NRMIARSEEEVELFDQMDEEFDWTEEMTNHEQVPKWLRA 1570
Cdd:COG1061 512 KELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEE 550
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
981-1145 |
1.25e-14 |
|
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: 75.08 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSlynNKLNGILADeMGLGKTVQVMALIAYLMeFKGNYGPHLIIVPNAVLVN-WKSELHTWLPSVSCI 1059
Cdd:cd18013 1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YY--VGTKDQRSKLFSQEVcamkfNVLVTTYEFIMY-DRSKLSKVDWKYIIIDEAQRMKDRESVLARDLDRYR--CQRRL 1134
Cdd:cd18013 76 VSvaVGTERQRSKAANTPA-----DLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVRpvIKRLI 150
|
170
....*....|.
gi 42571243 1135 LLTGTPLQNDL 1145
Cdd:cd18013 151 GLTGTPSPNGL 161
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
981-1211 |
3.09e-14 |
|
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: 74.44 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLNG-ILADEMGLGKTVQVMALIAY------------------LMEFKGN----YGPHLIIV 1037
Cdd:cd18072 1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAqkntqnrkeeekekalteWESKKDStlvpSAGTLVVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1038 PNAVLVNWKSELHTWLPSVS---CIYYVGTKDQRSKLFSQevcamkFNVLVTTYEFIMYD---------RSKLSKVDWKY 1105
Cdd:cd18072 81 PASLVHQWKNEVESRVASNKlrvCLYHGPNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1106 IIIDEAQRMKDRESVLARDLDRYRCQRRLLLTGTPLQNDLKELWSLLNLLLPDVFDNrkaFHDWFAQPFQKEGPAHNied 1185
Cdd:cd18072 155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDD---LKVWKKQVDNKSRKGGE--- 228
|
250 260
....*....|....*....|....*.
gi 42571243 1186 dwletekkvivihRLHQILEPFMLRR 1211
Cdd:cd18072 229 -------------RLNILTKSLLLRR 241
|
|
| BROMO |
smart00297 |
bromo domain; |
1900-2004 |
4.76e-14 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 70.00 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1900 IQKRCKIVISKLQRRIDKEGQQIV-PMLTNLWKRIQNGYAAGGVNNLLELREIDHRVERLEYAGVMELASDVQLMLRGAM 1978
Cdd:smart00297 1 DPKLQKKLQELLKAVLDKLDSHPLsWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80
|
90 100
....*....|....*....|....*.
gi 42571243 1979 QFYGFSHEVRSEAKKVHNLFFDLLKM 2004
Cdd:smart00297 81 TYNGPDSEVYKDAKKLEKFFEKKLRE 106
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
981-1140 |
4.67e-13 |
|
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: 68.49 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 981 LRDYQLVGLQWMLSLYNNKLnGILADEMGLGKTVQVMALIAYLMEFKgnygpHLIIVPNAVLVN-WKSELHTWLPSVScI 1059
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRR-GILVLPTGSGKTLTALALIAYLKELR-----TLIVVPTDALLDqWKERFEDFLGDSS-I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1060 YYVGTKDQRSKLfsqevcamKFNVLVTTY---EFIMYDRSKLSKvDWKYIIIDEAQRMKDREsvLARDLDRYRCQRRLLL 1136
Cdd:cd17926 74 GLIGGGKKKDFD--------DANVVVATYqslSNLAEEEKDLFD-QFGLLIVDEAHHLPAKT--FSEILKELNAKYRLGL 142
|
....
gi 42571243 1137 TGTP 1140
Cdd:cd17926 143 TATP 146
|
|
| QLQ |
smart00951 |
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ... |
462-497 |
1.72e-10 |
|
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: 57.54 E-value: 1.72e-10
10 20 30
....*....|....*....|....*....|....*.
gi 42571243 462 SGFTKQQLHVLKAQILAFRRLKKGEGSLPPELLQAI 497
Cdd:smart00951 1 SPFTPAQLELLRAQILAYKYLLARNQPVPPELLQAI 36
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1001-1139 |
1.43e-08 |
|
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: 55.49 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1001 NGILADEMGLGKTVQVMALIAYLMEFKGnyGPHLIIVPNAVLVN-WKSELHTWL-PSVSCIYYVGTKDqrsklfSQEVCA 1078
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFgPGIRVAVLVGGSS------AEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571243 1079 MKFN---VLVTTYEFI--MYDRSKLSKV-DWKYIIIDEAQRMKDRESVLARDLDRYRCQ-----RRLLLTGT 1139
Cdd:cd00046 75 NKLGdadIIIATPDMLlnLLLREDRLFLkDLKLIIVDEAHALLIDSRGALILDLAVRKAglknaQVILLSAT 146
|
|
| QLQ |
pfam08880 |
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ... |
464-497 |
1.84e-07 |
|
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.
Pssm-ID: 462622 Cd Length: 35 Bit Score: 48.87 E-value: 1.84e-07
10 20 30
....*....|....*....|....*....|....
gi 42571243 464 FTKQQLHVLKAQILAFRRLKKGEGsLPPELLQAI 497
Cdd:pfam08880 2 FTPAQLQELRAQILAYKYLSRNQP-VPPELQQAI 34
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
980-1140 |
3.73e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.90 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 980 TLRDYQLVGLQ-WMLSLYNNKLNGILADEMGLGKTVQVMALIAYLMEfKGNYGPHLIIVPNAVLVN-WKSELHTWLPS-- 1055
Cdd:pfam04851 3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPRKDLLEqALEEFKKFLPNyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1056 VSCIYYVGTKDQRSKLFSQevcamkfnVLVTTYE----FIMYDRSKLSKVDWKYIIIDEAQRmkdresvLARD-----LD 1126
Cdd:pfam04851 82 EIGEIISGDKKDESVDDNK--------IVVTTIQslykALELASLELLPDFFDVIIIDEAHR-------SGASsyrniLE 146
|
170
....*....|....
gi 42571243 1127 RYRCQRRLLLTGTP 1140
Cdd:pfam04851 147 YFKPAFLLGLTATP 160
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1009-1140 |
1.30e-06 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 50.32 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1009 GLGKTVqvMALIAYLMEFKGNY-GPH-LIIVPNAVLVN-----WKSELHTWLPSVSCIYY-VGTKDQRSKLFSQevcamk 1080
Cdd:pfam00270 24 GSGKTL--AFLLPALEALDKLDnGPQaLVLAPTRELAEqiyeeLKKLGKGLGLKVASLLGgDSRKEQLEKLKGP------ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571243 1081 fNVLVTTYEFIMY---DRSKLSKVdwKYIIIDEAQRM--KDRESVLARDLDRYRCQRR-LLLTGTP 1140
Cdd:pfam00270 96 -DILVGTPGRLLDllqERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATL 158
|
|
| Bromodomain |
cd04369 |
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ... |
1900-2002 |
6.07e-06 |
|
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.
Pssm-ID: 99922 [Multi-domain] Cd Length: 99 Bit Score: 46.60 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1900 IQKRCKIVISKLQRRIDKEGQQIVPMLTnlwKRIQNGYAAGgVNNLLELREIDHRVERLEYAGVMELASDVQLMLRGAMQ 1979
Cdd:cd04369 1 LKKKLRSLLDALKKLKRDLSEPFLEPVD---PKEAPDYYEV-IKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKT 76
|
90 100
....*....|....*....|...
gi 42571243 1980 FYGFSHEVRSEAKKVHNLFFDLL 2002
Cdd:cd04369 77 YNGPGSPIYKDAKKLEKLFEKLL 99
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1375-1431 |
1.19e-05 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 45.39 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 42571243 1375 TDCFIFLLSIRAAGRGLNLQTADTVVIYDPDPNPKNEEQAVARAHRIGQtREVKVIY 1431
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVIL 75
|
|
| COG4646 |
COG4646 |
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]; |
965-1127 |
1.88e-03 |
|
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
Pssm-ID: 443684 [Multi-domain] Cd Length: 1711 Bit Score: 43.70 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 965 VNEVVVRQ--------PSMLQAGTLRDYQLVGLqWMLsLYNNklNGILADEMGLGKTVqVMALIAylMEFK--GNYGPHL 1034
Cdd:COG4646 865 FNSIVPREydgshlkfPGDSRKISLRPHQKNAV-ARI-LYGG--NTLLAHEVGAGKTF-TMVAAA--MELRrlGLANKPM 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1035 IIVPNAVLVNW-KSELHTWLPSVSCIYyvgTKDQRSKLFSQEVCAMKFNVLVTTYEFIMYDRSKLSKVDWKYIIIDEAQR 1113
Cdd:COG4646 938 IVVPNHLLEQDaPSKLNLYAAANILIA---TKTDFEKGTRLVFCADIATGDYDAVIIGHIQFEKIPASGERQEEILEEQI 1014
|
170
....*....|....
gi 42571243 1114 MKDRESVLARDLDR 1127
Cdd:COG4646 1015 AEILKAIKELKAVV 1028
|
|
| Bromo_tif1_like |
cd05502 |
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ... |
1960-2008 |
3.06e-03 |
|
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99934 [Multi-domain] Cd Length: 109 Bit Score: 39.20 E-value: 3.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 42571243 1960 YAGVMELASDVQLMLRGAMQFYGFSHEVRSEAKKVHNLFFDLLKMSFPD 2008
Cdd:cd05502 61 YSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELELFFEEQLKEILPD 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
1304-1424 |
7.83e-03 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 38.64 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571243 1304 VRSCGKLWILDRILIKLQRTGhRVLLFSTMTKLLDILEEYLQWRRLVYRRIDGTTSLEDRESAIVDFNDPDTDCFIflls 1383
Cdd:cd18787 8 VEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLV---- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 42571243 1384 irA---AGRGLNLQTADTVVIYDPdpnPKNEEQAVaraHRIGQT 1424
Cdd:cd18787 83 --AtdvAARGLDIPGVDHVINYDL---PRDAEDYV---HRIGRT 118
|
|
| |
