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Conserved domains on  [gi|1958762165|ref|XP_038961036|]
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chromodomain-helicase-DNA-binding protein 6 isoform X9 [Rattus norvegicus]

Protein Classification

chromo domain-containing DEAD/DEAH box helicase( domain architecture ID 13036636)

chromo (chromatin organization modifier) domain-containing DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodelers

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
212-433 8.69e-156

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member cd18058:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 222  Bit Score: 480.31  E-value: 8.69e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
211-736 4.35e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.94  E-value: 4.35e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  211 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 286
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 443
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  444 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 523
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  524 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 603
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  604 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 683
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  684 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 736
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
123-181 1.86e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 126.63  E-value: 1.86e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  123 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 181
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
39-104 4.42e-27

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 105.88  E-value: 4.42e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762165   39 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 104
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
212-433 8.69e-156

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: 480.31  E-value: 8.69e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
211-736 4.35e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.94  E-value: 4.35e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  211 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 286
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 443
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  444 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 523
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  524 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 603
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  604 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 683
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  684 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 736
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
106-670 1.47e-128

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 421.56  E-value: 1.47e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  106 QAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPE 185
Cdd:COG0553    131 LLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLE 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  186 VKPVERPASDAWQKLETSREYKNSNR-----LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIH 260
Cdd:COG0553    211 LELLAEAAVDAFRLRRLREALESLPAglkatLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  261 GPFLIIAPLSTITNWEREFRTWT-EMNAIVYHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELK 339
Cdd:COG0553    291 RPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLA 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  340 KIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---E 416
Cdd:COG0553    356 AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdE 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  417 EQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCC 496
Cdd:COG0553    436 EALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQIC 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  497 NHPYLINGaeekilEDFRKAHSSeasdfqlqamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYT 576
Cdd:COG0553    516 SHPALLLE------EGAELSGRS--------------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIE 575
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  577 YERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVY 656
Cdd:COG0553    576 YAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVY 654
                          570
                   ....*....|....
gi 1958762165  657 RLITRNSYEREMFD 670
Cdd:COG0553    655 KLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
215-502 3.61e-86

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: 284.19  E-value: 3.61e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  215 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSIAFLSeiFVRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 286
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 442
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  443 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 502
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
534-659 1.98e-57

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: 195.39  E-value: 1.98e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  534 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 613
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762165  614 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 659
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
123-181 1.86e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 126.63  E-value: 1.86e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  123 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 181
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
205-403 2.31e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 2.31e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   205 EYKNSNRLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTIT-NWEREFRTWT 283
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   284 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVVIDEAHRLKN- 356
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958762165   357 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 403
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
39-104 4.42e-27

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 105.88  E-value: 4.42e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762165   39 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 104
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
534-648 8.25e-26

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: 103.83  E-value: 8.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  534 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 612
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958762165  613 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 648
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
234-682 1.90e-23

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 109.00  E-value: 1.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  234 ILADEMGLGKTIQS---IAFLSEIFVRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 309
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  310 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 386
Cdd:NF038318   122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  387 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 451
Cdd:NF038318   197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  452 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDf 513
Cdd:NF038318   268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVED- 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  514 rkahSSEASDFQL---------QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVR 561
Cdd:NF038318   346 ----EIDESGFEEkqdelytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKR 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  562 CLDILEDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGG 614
Cdd:NF038318   422 TQKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGS 497
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762165  615 LGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKAI 682
Cdd:NF038318   498 EGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAL 574
HELICc smart00490
helicase superfamily c-terminal domain;
564-648 4.76e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 4.76e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   564 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 643
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958762165   644 CHRIG 648
Cdd:smart00490   78 AGRAG 82
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
127-179 3.52e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.51  E-value: 3.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762165  127 EIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 179
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
44-105 4.20e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 45.65  E-value: 4.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165   44 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 105
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
127-178 6.99e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 6.99e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958762165   127 EIDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 178
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
CHROMO smart00298
Chromatin organization modifier domain;
45-107 2.79e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.79e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165    45 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 107
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
212-433 8.69e-156

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: 480.31  E-value: 8.69e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
211-736 4.35e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.94  E-value: 4.35e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  211 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 286
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 443
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  444 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 523
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  524 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 603
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  604 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 683
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  684 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 736
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
212-433 3.88e-148

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: 458.64  E-value: 3.88e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVY 290
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYqVEGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 HGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 370
Cdd:cd17995     81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  371 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
212-433 1.31e-128

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: 402.89  E-value: 1.31e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
106-670 1.47e-128

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 421.56  E-value: 1.47e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  106 QAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPE 185
Cdd:COG0553    131 LLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLE 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  186 VKPVERPASDAWQKLETSREYKNSNR-----LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIH 260
Cdd:COG0553    211 LELLAEAAVDAFRLRRLREALESLPAglkatLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  261 GPFLIIAPLSTITNWEREFRTWT-EMNAIVYHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELK 339
Cdd:COG0553    291 RPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLA 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  340 KIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---E 416
Cdd:COG0553    356 AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdE 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  417 EQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCC 496
Cdd:COG0553    436 EALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQIC 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  497 NHPYLINGaeekilEDFRKAHSSeasdfqlqamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYT 576
Cdd:COG0553    516 SHPALLLE------EGAELSGRS--------------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIE 575
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  577 YERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVY 656
Cdd:COG0553    576 YAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVY 654
                          570
                   ....*....|....
gi 1958762165  657 RLITRNSYEREMFD 670
Cdd:COG0553    655 KLVAEGTIEEKILE 668
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
212-433 3.51e-127

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: 398.64  E-value: 3.51e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18059     81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
212-433 9.96e-124

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: 388.98  E-value: 9.96e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 291
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  292 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 371
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  372 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
215-502 3.61e-86

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: 284.19  E-value: 3.61e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  215 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSIAFLSeiFVRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 286
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 442
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  443 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 502
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
212-433 2.79e-83

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 272.69  E-value: 2.79e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMvYRDaQGNPLsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd17993     82 YLGDIKSRDTIREYEF-YFS-QTKKL----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFK 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFlEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd17993    156 TNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
212-397 2.53e-77

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 254.03  E-value: 2.53e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSE-IFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd17919     81 YHGSQRERAQIRAKEKLD------------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEP 397
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
212-435 3.20e-74

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: 247.68  E-value: 3.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 290
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLLY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 HGSQISRQMIQqyemvyRDAQGNPLSGVfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 370
Cdd:cd18009     84 HGTKEERERLR------KKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  371 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-----------DLKTEEQ----VKKLQSILKPMMLRRLK 435
Cdd:cd18009    157 DNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLRRLK 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
212-433 1.09e-71

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: 238.49  E-value: 1.09e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSqisrqmiqqyemvyrdaqgnplsgvfkfHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd17994     81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
209-435 5.40e-70

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: 234.91  E-value: 5.40e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  209 SNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWEREFRTWT-EMN 286
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLkHYKNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  287 AIVYHGSQISRQMIQQYEMVYRdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 366
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPG-----------KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF----GDLKTEEQVKKLQSILKPMMLRRLK 435
Cdd:cd17997    150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
212-433 1.53e-69

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: 234.13  E-value: 1.53e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYRDAQGNPLSGVFK--------FHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 361
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  362 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
212-435 5.88e-68

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: 229.56  E-value: 5.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd17996      4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMeKKKNNGPYLVIVPLSTLSNWVSEFEKWApSVSKIV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd17996     84 YKGTPDVRKKLQSQIRAG------------KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYY 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  370 L-EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG------------DLKTEEQV---KKLQSILKPMMLRR 433
Cdd:cd17996    152 HaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRPFLLRR 231

                   ..
gi 1958762165  434 LK 435
Cdd:cd17996    232 LK 233
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
212-433 1.27e-66

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: 225.71  E-value: 1.27e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYRD--------AQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 361
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFEDnairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  362 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
212-433 1.74e-66

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: 225.33  E-value: 1.74e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYRDAQGNPLSGVF--------KFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 361
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  362 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
212-433 1.03e-65

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: 223.34  E-value: 1.03e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18054     21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd18054    101 YIGDLMSRNTIREYEWIH------SQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 433
Cdd:cd18054    175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
212-433 4.79e-59

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 203.05  E-value: 4.79e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQyemvyrDAQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd18006     81 YMGDKEKRLDLQQ------DIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETA--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 433
Cdd:cd18006    150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
212-435 5.82e-59

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: 203.18  E-value: 5.82e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 290
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVLVI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 HGSQISRQMIQQYEmvyrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 370
Cdd:cd18012     85 HGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  371 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLK 435
Cdd:cd18012    150 DHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
534-659 1.98e-57

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: 195.39  E-value: 1.98e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  534 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 613
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762165  614 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 659
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
212-433 1.55e-56

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: 196.42  E-value: 1.55e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFV-RGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIV 289
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACeKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMvyrdaqgNPLSgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd18003     81 YYGSAKERKLKRQGWM-------KPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 433
Cdd:cd18003    150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
212-433 5.78e-56

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 195.27  E-value: 5.78e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18053     21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQTWApQMNAVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 369
Cdd:cd18053    101 YLGDINSRNMIRTHEWMH------PQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFK 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762165  370 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 433
Cdd:cd18053    175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
212-433 5.97e-53

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: 186.17  E-value: 5.97e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfNWYNRK-NCILADEMGLGKTIQSIAFLSEIFVR-GIHGPFLIIAPLSTITNWEREF-RTWTEMNAI 288
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  289 VYHGSQISRQMIQQY----EMVYRDAqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEG 364
Cdd:cd18002     80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  365 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-DLKT---------EEQVKKLQSILKPMMLRR 433
Cdd:cd18002    151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
212-400 1.19e-52

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: 183.74  E-value: 1.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 290
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 HGSQISRqmiqqyemvyRDAQGNPLSGVFKFHVVITTFEMILADCPE---LKKIHWSCVVIDEAHRLKNRNCKLLEGLKL 367
Cdd:cd17998     81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958762165  368 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQF 400
Cdd:cd17998    151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
212-433 5.63e-52

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: 184.12  E-value: 5.63e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLlFNWY-NRKNCILADEMGLGKTIQSIAFLSEI----------------FVRGIH-----GPFLIIAPL 269
Cdd:cd18005      1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprFKKKPPassakKPVLIVAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  270 STITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEmvyrdaQGnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVID 349
Cdd:cd18005     80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AG-------RLEVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  350 EAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---------------LK 414
Cdd:cd18005    147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                          250
                   ....*....|....*....
gi 1958762165  415 TEEQVKKLQSILKPMMLRR 433
Cdd:cd18005    227 GRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
199-446 5.27e-49

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: 175.62  E-value: 5.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  199 KLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWER 277
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  278 EFRTWT-EMNAIVYHGSQisrqmiQQYEMVYRDAQgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN 356
Cdd:cd18064     83 EFKRWVpTLRAVCLIGDK------DQRAAFVRDVL---LPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  357 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18064    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 231
                          250
                   ....*....|...
gi 1958762165  434 LKDDVEKNLAPKQ 446
Cdd:cd18064    232 IKADVEKSLPPKK 244
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
198-435 1.85e-48

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: 174.08  E-value: 1.85e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  198 QKLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWE 276
Cdd:cd18062     10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRINGPFLIIVPLSTLSNWV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  277 REFRTWT-EMNAIVYHGSQISRQMIQqyemvyrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLK 355
Cdd:cd18062     90 YEFDKWApSVVKVSYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  356 NRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKK 421
Cdd:cd18062    158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRR 237
                          250
                   ....*....|....
gi 1958762165  422 LQSILKPMMLRRLK 435
Cdd:cd18062    238 LHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
212-435 3.26e-47

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: 170.63  E-value: 3.26e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFV-RGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 289
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 YHGS-QISRQMIQQYEmvyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLM 368
Cdd:cd18063    104 YKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  369 ALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRRL 434
Cdd:cd18063    171 YVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRRL 250

                   .
gi 1958762165  435 K 435
Cdd:cd18063    251 K 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
199-435 2.42e-46

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: 167.50  E-value: 2.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  199 KLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWER 277
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  278 EFRTWT-EMNAIVYHGSQISRQMIQQYEMvyrdaqgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN 356
Cdd:cd18065     83 EFKRWVpSLRAVCLIGDKDARAAFIRDVM---------MPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  357 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                   ..
gi 1958762165  434 LK 435
Cdd:cd18065    232 IK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
212-433 9.91e-43

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: 157.45  E-value: 9.91e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFnwynrKNCILADEMGLGKTIQSIA--------FLSEIFVRGIHGPF----------LIIAPLSTIT 273
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALAlilatrpqDPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  274 NWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPE------------- 337
Cdd:cd18008     76 QWKDEIEKHTKpgsLKVYVYHGSK----------------RIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  338 ---LKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLK 414
Cdd:cd18008    140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                          250       260
                   ....*....|....*....|..
gi 1958762165  415 TE---EQVKKLQSILKPMMLRR 433
Cdd:cd18008    220 SKndrKALERLQALLKPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
212-433 1.67e-41

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: 153.30  E-value: 1.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 290
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 HGSQisrqmiqqyemvyRDAQGNPLSGVFK-FHVVITTFEMILADCPEL-----KKIHWSCVVIDEAHRLKNRNCKLLEG 364
Cdd:cd18001     81 HGTS-------------KKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  365 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ-FPSETAFLEEFGDLKTEEQVKK---------------LQSILKP 428
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDatqgekalgsevaenLRQIIKP 227

                   ....*
gi 1958762165  429 MMLRR 433
Cdd:cd18001    228 YFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
212-433 4.56e-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: 140.56  E-value: 4.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSIAFL-SEIFVR-----GIHGPFLIIAPLSTITNWEREFRTWTE 284
Cdd:cd17999      1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILaSDHHKRansfnSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  285 ---MNAIVYHGSQISRQMIQQyemvyrdaQGNplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 361
Cdd:cd17999     80 nafLKPLAYVGPPQERRRLRE--------QGE------KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  362 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-------DLK-----TEEQVKKLQSILK-- 427
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                   ....*..
gi 1958762165  428 -PMMLRR 433
Cdd:cd17999    226 lPFLLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
212-433 1.29e-36

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: 139.73  E-value: 1.29e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSIAFLSeIFVRgiHGPF--------LIIAPLSTITNWERE 278
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  279 FRTWTemnaivyhGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHwSC--VVIDEAHRLKN 356
Cdd:cd18004     78 FDKWL--------GLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  357 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF-------------------LEEFGDLKTEE 417
Cdd:cd18004    149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseeDKELGAERSQE 228
                          250
                   ....*....|....*.
gi 1958762165  418 qvkkLQSILKPMMLRR 433
Cdd:cd18004    229 ----LSELTSRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
212-397 6.08e-36

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: 135.91  E-value: 6.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfnWYNRKNC--ILADEMGLGKTIQSIAFLseifvRGIH------GPFLIIAPLSTITNWEREFRTW- 282
Cdd:cd18000      1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFL-----AALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  283 TEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPlSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLL 362
Cdd:cd18000     74 PPFRVVVLHSSGSGTGSEEKLGSIERKSQLIR-KVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEIT 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958762165  363 EGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEP 397
Cdd:cd18000    153 LACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
123-181 1.86e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 126.63  E-value: 1.86e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  123 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 181
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
205-403 2.31e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 2.31e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   205 EYKNSNRLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTIT-NWEREFRTWT 283
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   284 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVVIDEAHRLKN- 356
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958762165   357 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 403
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
212-410 7.87e-31

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: 122.79  E-value: 7.87e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGmnwLLFNWYN----------RKNCILADEMGLGKTIQSIAFLSEI---FVRGIHgpFLIIAPLSTITNWERE 278
Cdd:cd18007      1 LKPHQVEG---VRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYlaaAPRRSR--PLVLCPASTLYNWEDE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  279 FRTWTEMNAIVYHGsqisrqmiqqyeMVYRDAQGNP---LSGVFKFH----VVITTFEM--ILADCPELKK------IHW 343
Cdd:cd18007     76 FKKWLPPDLRPLLV------------LVSLSASKRAdarLRKINKWHkeggVLLIGYELfrNLASNATTDPrlkqefIAA 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  344 SC------VVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 410
Cdd:cd18007    144 LLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
212-406 3.35e-28

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 115.33  E-value: 3.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGmnwLLFNWY--------NRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGP------FLIIAPLSTITNWER 277
Cdd:cd18066      1 LRPHQREG---IEFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  278 EFRTWtemnaivyhgsqISRQMIQQYeMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNR 357
Cdd:cd18066     78 EFQKW------------LGSERIKVF-TVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958762165  358 NCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF 406
Cdd:cd18066    145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
212-433 7.55e-28

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: 113.45  E-value: 7.55e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfnwynRKN--CILADEMGLGKTIQSIAFLSeiFVRGiHGPFLIIAPLSTITNWEREFRTW----TEM 285
Cdd:cd18010      1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  286 NAIVYHGSQISRQMiqqyemvyRDAQgnplsgvfkfhVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRN---CKLL 362
Cdd:cd18010     73 DIQVIVKSKDGLRD--------GDAK-----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAA 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  363 EGLkLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE---------FGDLKTEEQVKKLQSIL-KPMMLR 432
Cdd:cd18010    134 LPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycaakqggfGWDYSGSSNLEELHLLLlATIMIR 212

                   .
gi 1958762165  433 R 433
Cdd:cd18010    213 R 213
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
39-104 4.42e-27

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 105.88  E-value: 4.42e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762165   39 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 104
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
234-433 5.67e-26

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: 108.71  E-value: 5.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  234 ILADEMGLGKTIQSIAFLseifvrgIHGPFLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyRDA 310
Cdd:cd18071     52 ILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGE-------------RNR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  311 QGNPLSgvfKFHVVITTFEMI------LADCPeLKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNS 384
Cdd:cd18071    112 DPKLLS---KYDIVLTTYNTLasdfgaKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762165  385 VEELFSLLNFLEPSQFPSETAFLEEFG---DLKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18071    188 PKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
534-648 8.25e-26

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: 103.83  E-value: 8.25e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  534 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 612
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958762165  613 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 648
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
230-433 1.40e-25

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 106.60  E-value: 1.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  230 RKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQyemvYRD 309
Cdd:cd18011     17 PVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-----LDRETAAQ----LRR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  310 AQGNPLSgvfKFHVVITTFEMI-----LADcpELKKIHWSCVVIDEAHRLKNRNCKLLEGL-KLMAL-----EHKVLLTG 378
Cdd:cd18011     88 LIGNPFE---EFPIVIVSLDLLkrseeRRG--LLLSEEWDLVVVDEAHKLRNSGGGKETKRyKLGRLlakraRHVLLLTA 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762165  379 TPLQNSVEELFSLLNFLEPSQFpsetAFLEEFGDLKTEEQVkklqsiLKPMMLRR 433
Cdd:cd18011    163 TPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
212-433 1.42e-23

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: 102.16  E-value: 1.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSIAFLSEIFVRGIHGPFLI-----IAPLSTITNWEREFRT 281
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  282 WTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGvfkfHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 361
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVST----PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  362 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---------GD------LKTEEQVKKLQSIL 426
Cdd:cd18067    157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                   ....*..
gi 1958762165  427 KPMMLRR 433
Cdd:cd18067    237 NRCIIRR 243
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
234-682 1.90e-23

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 109.00  E-value: 1.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  234 ILADEMGLGKTIQS---IAFLSEIFVRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 309
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  310 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 386
Cdd:NF038318   122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  387 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 451
Cdd:NF038318   197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  452 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDf 513
Cdd:NF038318   268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVED- 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  514 rkahSSEASDFQL---------QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVR 561
Cdd:NF038318   346 ----EIDESGFEEkqdelytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKR 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  562 CLDILEDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGG 614
Cdd:NF038318   422 TQKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGS 497
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762165  615 LGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKAI 682
Cdd:NF038318   498 EGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAL 574
HELICc smart00490
helicase superfamily c-terminal domain;
564-648 4.76e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 4.76e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165   564 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 643
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958762165   644 CHRIG 648
Cdd:smart00490   78 AGRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
212-433 1.10e-20

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: 93.70  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfnWYNRKNC---ILADEMGLGKTIQSIAF------------------LSEIFVRGIHGPF-----LI 265
Cdd:cd18072      1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  266 IAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemvyRDAQGNPLSgvfKFHVVITTFEMILADCPELKK-- 340
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASNKLrvcLYHGPN-------------RERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  341 -------IHWSCVVIDEAHRLKNRNCKLLEGL-KLMALEHKVLlTGTPLQNSVEELFSLLNFLEPSQFpSETAFLEEFGD 412
Cdd:cd18072    143 rssplfrIAWARIILDEAHNIKNPKVQASIAVcKLRAHARWAL-TGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVD 220
                          250       260
                   ....*....|....*....|.
gi 1958762165  413 LKTEEQVKKLQSILKPMMLRR 433
Cdd:cd18072    221 NKSRKGGERLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
233-410 1.96e-20

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 93.03  E-value: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  233 CILADEMGLGKTIQSIAFLSEIFVRGIHGPF---LIIAPLSTITNWEREFRTWTEMNA---------------------I 288
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLKdeekievnelatykrpqersyK 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  289 VYHGSQISRQMIQQYEMvYRD-AQGNPLSGVFKFHvviTTFEMILAD-CPELkkihwscVVIDEAHRLKNRNCKLLEGLK 366
Cdd:cd18068    111 LQRWQEEGGVMIIGYDM-YRIlAQERNVKSREKLK---EIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMN 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958762165  367 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 410
Cdd:cd18068    180 SIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
233-410 5.19e-19

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: 88.33  E-value: 5.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  233 CILADEMGLGKTIQSIAFLsEIFVRGIHGP-FLIIAPLSTITNWEREFRTWteMNAIVYHGSQISRQM---IQQYEMVYR 308
Cdd:cd18069     31 CILAHSMGLGKTLQVISFL-DVLLRHTGAKtVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  309 DAQGNPLSG-VFKFHVVITTFEMI-LADCPELkkihwscVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 386
Cdd:cd18069    108 AARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                          170       180
                   ....*....|....*....|....
gi 1958762165  387 ELFSLLNFLEPSQFPSETAFLEEF 410
Cdd:cd18069    181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
124-179 1.62e-16

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 75.30  E-value: 1.62e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762165  124 DYIEIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV---DPAKVKEFES 179
Cdd:cd18659      1 EYTIVERI--IAHREDDEGVTE---YLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
212-399 2.55e-15

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: 77.39  E-value: 2.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfnwYNRKNCILADeMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAIVY 290
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  291 H---GSQisRQMIqqyemvyRDAQGNPlsgvfkfHVVITTFEMiLADCPELKKIHW--SCVVIDEAHRLKNRNCKllEGL 365
Cdd:cd18013     77 SvavGTE--RQRS-------KAANTPA-------DLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK--RFK 137
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958762165  366 KLMALEHKV----LLTGTPLQNSVEELFSLLNFLEPSQ 399
Cdd:cd18013    138 ALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLDQGE 175
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
41-104 3.58e-14

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 69.31  E-value: 3.58e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762165   41 DANIIEKILASKTVQEVHPG-------EPPFDLELFYVKYRNFSYLHCKWATMEELEKDpRIAQKIKRFRN 104
Cdd:cd18660      1 DEDKIEKILDHRPKGPVEEAsldltdpDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYIK 70
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
212-400 4.61e-12

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: 68.52  E-value: 4.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGMNWLLfnwyNRKNcILADEMGLGKTIQSIAFL-----------SEIFVRGIH---------------GPFLI 265
Cdd:cd18070      1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLALIllhprpdndldAADDDSDEMvccpdclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  266 IAPLSTITNWEREFRTWTEMNAIVYHgsqisrqmiqqYEMVYRD--AQGNPLSGVFKFHVVITTFEmILAD--------- 334
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDgaLASPAPEILAEYDIVVTTYD-VLRTelhyaeanr 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  335 ---------------CPeLKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ 399
Cdd:cd18070    144 snrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                   .
gi 1958762165  400 F 400
Cdd:cd18070    223 F 223
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
164-804 1.71e-11

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.67  E-value: 1.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  164 ELEEDVDPAKVKEFESLQILPEVKPVERPASDAWQklETSREYKNSNRLREYQLEGMN-WLLFNWYNRKNCILADEMGLG 242
Cdd:COG1061     35 VEARRLAIKEGTREDGRRLPEEDTERELAEAEALE--AGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTG 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  243 KTIQSIAFLSEIFVRGihgPFLIIAPLSTITN-WEREFRTWTemNAIVYHGSQISRQmiqqyemvyrdaqgnplsgvfkF 321
Cdd:COG1061    113 KTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRFL--GDPLAGGGKKDSD----------------------A 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  322 HVVITTFEmILADCPELKKI--HWSCVVIDEAHRLKNRncKLLEGLKLMALEHKVLLTGTPlqnsveelfsllnflepsq 399
Cdd:COG1061    166 PITVATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP------------------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  400 fpsetafleEFGDLKTEEqVKKLQSILKPMMLRRLKDDveKNLAPKQETIIEVELTNIQKKY--YRAILEKNfsfltkga 477
Cdd:COG1061    224 ---------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYdaLSERLREA-------- 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  478 nqhnmpnlintmmelrkccnhpyLINGAEEK--ILEDFRKAHsseasdfqlqamiqaagklvlidkllpkliAGGHKVLI 555
Cdd:COG1061    284 -----------------------LAADAERKdkILRELLREH------------------------------PDDRKTLV 310
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  556 FSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFckpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQ 635
Cdd:COG1061    311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR 387
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  636 NDLQAQARCHRIGQSK-AVKVYRLITRNS-YEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYG 713
Cdd:COG1061    388 EFIQRLGRGLRPAPGKeDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLE 467
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  714 ALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKES 793
Cdd:COG1061    468 ELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLR 547
                          650
                   ....*....|.
gi 1958762165  794 LVIDRPRVRKQ 804
Cdd:COG1061    548 LEELAALLLKE 558
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
123-168 2.42e-09

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 54.96  E-value: 2.42e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762165  123 PDYIEIDRILEvaHTKDAETGeevTHYLVKWCSLPYEESTWELEED 168
Cdd:cd18662      1 PEWLQIHRIIN--HRVDKDGN---TWYLVKWRDLPYDQSTWESEDD 41
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
127-179 3.52e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.51  E-value: 3.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762165  127 EIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 179
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
231-379 7.00e-09

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 56.64  E-value: 7.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  231 KNCILADEMGLGKTIQ-SIAFLSEIFVRGihGPFLIIAPLSTITN-WEREFRTWTEMNA--IVYHGsqiSRQMIQQYEMV 306
Cdd:cd00046      2 ENVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIrvAVLVG---GSSAEEREKNK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  307 YRDAqgnplsgvfkfHVVITTFEMILADCPELKKIH---WSCVVIDEAHRL----KNRNCKLLEGLKLMALEHK-VLLTG 378
Cdd:cd00046     77 LGDA-----------DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSA 145

                   .
gi 1958762165  379 T 379
Cdd:cd00046    146 T 146
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
212-380 2.13e-06

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: 49.61  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  212 LREYQLEGM-NWLLFNWYNRKNCILAdeMGLGKTIQSIAFLSEIFVRgihgPFLIIAP-LSTITNWEREFRTWTemnaiv 289
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKEL----RTLIVVPtDALLDQWKERFEDFL------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  290 yHGSQISRQmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPELKKI--HWSCVVIDEAHRLknrNCKLLEGLKL 367
Cdd:cd17926     69 -GDSSIGLI------------GGGKKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILK 132
                          170
                   ....*....|....
gi 1958762165  368 MALEHKVL-LTGTP 380
Cdd:cd17926    133 ELNAKYRLgLTATP 146
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
44-105 4.20e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 45.65  E-value: 4.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762165   44 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 105
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
127-179 8.02e-06

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 44.78  E-value: 8.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762165  127 EIDRILevahtkDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEFES 179
Cdd:cd00024      2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
124-179 2.31e-05

repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349311  Cd Length: 59  Bit Score: 44.19  E-value: 2.31e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762165  124 DYIEIDRILEvahTKDAETGEEVTH--YLVKWCSLPYEESTWELEEDV---DPAKVKEFES 179
Cdd:cd18664      1 EFHVVERIIA---SQRASLEDGTSQlqYLVKWRRLNYDECTWEDATLIaklAPEQVDHFQN 58
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
213-388 2.40e-05

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: 46.85  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  213 REYQLEGMNWLLfnwyNRKNCILADEMGLGKT-IQSIAFLSEIFVRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAI-- 288
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLkv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762165  289 --VYHGSQISRQMiqqyemvyrdaqgNPLSGVfkfHVVITTFEMILADCPE---LKKIhwSCVVIDEAHRL--KNRNCKL 361
Cdd:pfam00270   77 asLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 1958762165  362 LEGLKLMALEHK-VLLTGTPLQNsVEEL 388
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
CHROMO smart00298
Chromatin organization modifier domain;
127-178 6.99e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 6.99e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958762165   127 EIDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 178
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
125-179 8.32e-05

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349308  Cd Length: 58  Bit Score: 42.29  E-value: 8.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762165  125 YIEIDRIleVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD---PAKVKEFES 179
Cdd:cd18661      2 YQIVERI--IAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHS 57
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
601-653 6.49e-04

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 6.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762165  601 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 653
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
127-176 9.61e-04

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 39.19  E-value: 9.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958762165  127 EIDRILevahtkdAETGEE-VTHYLVKWCSLPYEESTWELEEDVDPAKVKE 176
Cdd:cd18966      2 EVERIL-------AERRDDgGKRYLVKWEGYPLEEATWEPEENIGDEELLK 45
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
133-173 1.18e-03

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 39.00  E-value: 1.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958762165  133 EVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK 173
Cdd:cd18974      2 EVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAP 42
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
149-177 1.41e-03

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 38.68  E-value: 1.41e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958762165  149 YLVKWCSLPYEESTWELEEDVDPAK-VKEF 177
Cdd:cd18975     18 YLIQWKGYPLEEASWELEDNIKNPRlIEEF 47
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
147-169 1.61e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349321  Cd Length: 53  Bit Score: 38.61  E-value: 1.61e-03
                           10        20
                   ....*....|....*....|...
gi 1958762165  147 THYLVKWCSLPYEESTWELEEDV 169
Cdd:cd18965     16 LEYLVKWHGLPESENTWEREKDI 38
CHROMO smart00298
Chromatin organization modifier domain;
45-107 2.79e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.79e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165    45 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 107
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
28-90 4.14e-03

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 38.09  E-value: 4.14e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762165   28 FWsstREKEPPEDDAnIIEKILASKTVQEVHPGEPPFDLELFyVKYRNFSYLHCKWATMEELE 90
Cdd:cd18667     10 TW---RWAEPPYPEP-LPEKPDEDPYPPPPRKLQPRPEREFF-VKWHGMSYWHCEWVSELQLE 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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