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Conserved domains on  [gi|32563629|ref|NP_491994|]
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DNA helicase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
404-1245 1.22e-160

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: 512.42  E-value: 1.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   484 VYMGDVVSRDMIRQyEWFVGGtkkmKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:PLN03142  249 KFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   564 LITGTPLQNSLKELWALLHFIMPE------KFDCWeeFETAHNESNHKGISALHKKLEPFLLRRVKKDVEKSLPPKTEQI 637
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEifssaeTFDEW--FQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   638 LRVDMTAHQKQFYKWILTKNYRELSKGvkGSINGFVNLVMELKKCCNHASLTRQYD----HIYDDaqgrlqQLLKSSGKL 713
Cdd:PLN03142  402 LKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEpgppYTTGE------HLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   714 ILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGSTDFAFLLSTRAGGLG 793
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   794 INLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLVTKGSVEEEIVERAKRKLVLDHLVIQRmdttGKTVLSK 873
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQK 629
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   874 NAtasgsvpfDKQELSAILKFGAVELFKEKEGEEQEPevDIDRILMGAE--TREAEEEVMKENELLSSFKYANFA----I 947
Cdd:PLN03142  630 TV--------NKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGEeaTAELDAKMKKFTEDAIKFKMDDTAelydF 699
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   948 DEEKDIAAATDEWAAII-------PEEDRNRILEE-ERMKELAEMNLAPRQRKQPIPQVVEDDDGDDDEEEDDTGKKKKk 1019
Cdd:PLN03142  700 DDEDDKDENKLDFKKIVsdnwidpPKRERKRNYSEsEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEK- 778
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1020 kavgnftipEIKRFIKSFRKFSM--PLNRLEEIAQDAELEEHSTDEMKKLVE------------SLSEACKKAADEFDSN 1085
Cdd:PLN03142  779 ---------EVRYLMQAHQKGQLkdTIDVAEPEEPGDPLTAEEQEEKEQLLEegfstwsrrdfnAFIRACEKYGRNDIKS 849
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1086 EKNGDAGAAESEKKDIERKFKFHTCDVN-----LKQIERSHAELKPLHEILKSEETKTS-FKPP-ANAKLQKGWDVD--W 1156
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNdydriIKNIERGEARISRKDEIMKAIGKKLDrYKNPwLELKIQYGQNKGklY 929
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1157 SRPDDSALLLGVWKYGYGSWE----AIKMDPTLGLadKIFIKDKTKkpqgKNLQVRVDYLLKLMSKDKVKTTEKKERKRK 1232
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGNWDelkaAFRTSPLFRF--DWFVKSRTP----QELARRCDTLIRLIEKENQEYDERERQARK 1003
                         890
                  ....*....|...
gi 32563629  1233 ADDVPVGPEKKKR 1245
Cdd:PLN03142 1004 EKKLAKNATPSKR 1016
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
194-275 2.92e-38

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, 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 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: 349313  Cd Length: 85  Bit Score: 137.81  E-value: 2.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  194 TETVERVIKWRHGVPGATGSATTCYNIADKGDPND--QIPGDKTEQQFFVKWTGWSHLHNTWESENSLALMNAKGLKKVQ 271
Cdd:cd18666    2 FETIERVLDHRIGRKGATGASTTIYAVEADGDPNAgfDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLE 81

                 ....
gi 32563629  272 NYVK 275
Cdd:cd18666   82 NYKK 85
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
308-363 6.49e-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: 72.99  E-value: 6.49e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32563629  308 EYKKVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMV---APEQIKAYY 363
Cdd:cd18659    1 EYTIVERIIAHREDDEGV------TEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYK 53
DUF4208 super family cl16467
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1298-1367 5.91e-09

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


The actual alignment was detected with superfamily member pfam13907:

Pssm-ID: 464035  Cd Length: 93  Bit Score: 54.57  E-value: 5.91e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629   1298 ECVKLCMPVHKYMKKLKEAQEAKNQADEAK----YLTRLGDSFlenlETLIKKKPKTNIRKWYNYLWIFLCKFT 1367
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKilkkELLKIGDFI----DSLLEETKKEKKEKLRKHLWSFVSKFW 79
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
404-1245 1.22e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 512.42  E-value: 1.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   484 VYMGDVVSRDMIRQyEWFVGGtkkmKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:PLN03142  249 KFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   564 LITGTPLQNSLKELWALLHFIMPE------KFDCWeeFETAHNESNHKGISALHKKLEPFLLRRVKKDVEKSLPPKTEQI 637
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEifssaeTFDEW--FQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   638 LRVDMTAHQKQFYKWILTKNYRELSKGvkGSINGFVNLVMELKKCCNHASLTRQYD----HIYDDaqgrlqQLLKSSGKL 713
Cdd:PLN03142  402 LKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEpgppYTTGE------HLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   714 ILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGSTDFAFLLSTRAGGLG 793
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   794 INLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLVTKGSVEEEIVERAKRKLVLDHLVIQRmdttGKTVLSK 873
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQK 629
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   874 NAtasgsvpfDKQELSAILKFGAVELFKEKEGEEQEPevDIDRILMGAE--TREAEEEVMKENELLSSFKYANFA----I 947
Cdd:PLN03142  630 TV--------NKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGEeaTAELDAKMKKFTEDAIKFKMDDTAelydF 699
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   948 DEEKDIAAATDEWAAII-------PEEDRNRILEE-ERMKELAEMNLAPRQRKQPIPQVVEDDDGDDDEEEDDTGKKKKk 1019
Cdd:PLN03142  700 DDEDDKDENKLDFKKIVsdnwidpPKRERKRNYSEsEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEK- 778
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1020 kavgnftipEIKRFIKSFRKFSM--PLNRLEEIAQDAELEEHSTDEMKKLVE------------SLSEACKKAADEFDSN 1085
Cdd:PLN03142  779 ---------EVRYLMQAHQKGQLkdTIDVAEPEEPGDPLTAEEQEEKEQLLEegfstwsrrdfnAFIRACEKYGRNDIKS 849
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1086 EKNGDAGAAESEKKDIERKFKFHTCDVN-----LKQIERSHAELKPLHEILKSEETKTS-FKPP-ANAKLQKGWDVD--W 1156
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNdydriIKNIERGEARISRKDEIMKAIGKKLDrYKNPwLELKIQYGQNKGklY 929
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1157 SRPDDSALLLGVWKYGYGSWE----AIKMDPTLGLadKIFIKDKTKkpqgKNLQVRVDYLLKLMSKDKVKTTEKKERKRK 1232
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGNWDelkaAFRTSPLFRF--DWFVKSRTP----QELARRCDTLIRLIEKENQEYDERERQARK 1003
                         890
                  ....*....|...
gi 32563629  1233 ADDVPVGPEKKKR 1245
Cdd:PLN03142 1004 EKKLAKNATPSKR 1016
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
404-621 3.01e-147

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: 446.80  E-value: 3.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 VYMGDVVSRDMIRQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:cd17993   81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629  564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd17993  161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
386-855 1.24e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 409.61  E-value: 1.24e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  386 EKFESMPDFLKTDgesthkLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLST 465
Cdd:COG0553  229 EALESLPAGLKAT------LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSL 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  466 MAAWQKEFAQWAPEMNLVVYMGdvvSRDMIRQYEWFVGGtkkmkiNAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKN 545
Cdd:COG0553  302 VGNWQRELAKFAPGLRVLVLDG---TRERAKGANPFEDA------DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKN 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  546 DESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKG----ISALHKKLEPFLLRR 621
Cdd:COG0553  373 PATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLRPFLLRR 452
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  622 VKKDVEKSLPPKTEQILRVDMTAHQKQFYKwILTKNYRELSKGVKGSINGFVNL--VMELKKCCNHASLtrqydhiYDDA 699
Cdd:COG0553  453 TKEDVLKDLPEKTEETLYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGLILaaLTRLRQICSHPAL-------LLEE 524
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  700 QGRLQQllkSSGKLILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGST 779
Cdd:COG0553  525 GAELSG---RSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEA 601
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563629  780 DFaFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLVTKGSVEEEIVERAKRKLVL 855
Cdd:COG0553  602 PV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
408-688 4.73e-94

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: 305.38  E-value: 4.73e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    408 YQLEGLNWMVYAWCK-GNSSILADEMGLGKTIQSISLLASLFHRYDLAG-PYLVVVPLSTMAAWQKEFAQWA--PEMNLV 483
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    484 VYMGDvvSRDmirQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:pfam00176   81 VLHGN--KRP---QERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAH-----NESNHKGISALHKKLEPFLLRRVKKDVEKSLPPKTEQIL 638
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFdrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 32563629    639 RVDMTAHQKQFYK-WILTKNYRELSKGVKGS--INGFVNLVMELKKCCNHASL 688
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGReiKASLLNILMRLRKICNHPGL 288
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
194-275 2.92e-38

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, 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 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: 349313  Cd Length: 85  Bit Score: 137.81  E-value: 2.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  194 TETVERVIKWRHGVPGATGSATTCYNIADKGDPND--QIPGDKTEQQFFVKWTGWSHLHNTWESENSLALMNAKGLKKVQ 271
Cdd:cd18666    2 FETIERVLDHRIGRKGATGASTTIYAVEADGDPNAgfDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLE 81

                 ....
gi 32563629  272 NYVK 275
Cdd:cd18666   82 NYKK 85
DEXDc smart00487
DEAD-like helicases superfamily;
404-588 7.89e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.50  E-value: 7.89e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629     404 KLRDYQLEGLNWMVYAWckgNSSILADEMGLGKTIQSISLLASLFHRYDlAGPYLVVVPL-STMAAWQKEFAQWAPEMNL 482
Cdd:smart00487    8 PLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTrELAEQWAEELKKLGPSLGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629     483 --VVYMGDVVSRDMIRQYewfvggtKKMKINAILTTYEILLKD--KAFLSSIDWAALLVDEAHRLKND--ESLLYKSLTQ 556
Cdd:smart00487   84 kvVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 32563629     557 FRFN-HKLLITGTP---LQNSLKELWALLHFIMPEK 588
Cdd:smart00487  157 LPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
308-363 6.49e-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: 72.99  E-value: 6.49e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32563629  308 EYKKVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMV---APEQIKAYY 363
Cdd:cd18659    1 EYTIVERIIAHREDDEGV------TEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYK 53
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
310-365 4.55e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 4.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629    310 KKVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMVA--PEQIKAYYHR 365
Cdd:pfam00385    1 YEVERILDHRKDKGGK------EEYLVKWKGYPYDENTWEPEENLSkcPELIEEFKDR 52
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1298-1367 5.91e-09

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 54.57  E-value: 5.91e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629   1298 ECVKLCMPVHKYMKKLKEAQEAKNQADEAK----YLTRLGDSFlenlETLIKKKPKTNIRKWYNYLWIFLCKFT 1367
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKilkkELLKIGDFI----DSLLEETKKEKKEKLRKHLWSFVSKFW 79
CHROMO smart00298
Chromatin organization modifier domain;
311-365 3.64e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 51.06  E-value: 3.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 32563629     311 KVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMV--APEQIKAYYHR 365
Cdd:smart00298    3 EVEKILDHRWKKKGE------LEYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYKKK 53
CHROMO smart00298
Chromatin organization modifier domain;
231-278 3.51e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.36  E-value: 3.51e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 32563629     231 PGDKTEQQFFVKWTGWSHLHNTWESENSLalmnAKGLKKVQNYVKKQK 278
Cdd:smart00298   12 WKKKGELEYLVKWKGYSYSEDTWEPEENL----LNCSKKLDNYKKKER 55
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
233-276 4.33e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.18  E-value: 4.33e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 32563629    233 DKTEQQFFVKWTGWSHLHNTWESENSLalmnAKGLKKVQNYVKK 276
Cdd:pfam00385   13 KGGKEEYLVKWKGYPYDENTWEPEENL----SKCPELIEEFKDR 52
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
404-1245 1.22e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 512.42  E-value: 1.22e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   484 VYMGDVVSRDMIRQyEWFVGGtkkmKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:PLN03142  249 KFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   564 LITGTPLQNSLKELWALLHFIMPE------KFDCWeeFETAHNESNHKGISALHKKLEPFLLRRVKKDVEKSLPPKTEQI 637
Cdd:PLN03142  324 LITGTPLQNNLHELWALLNFLLPEifssaeTFDEW--FQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   638 LRVDMTAHQKQFYKWILTKNYRELSKGvkGSINGFVNLVMELKKCCNHASLTRQYD----HIYDDaqgrlqQLLKSSGKL 713
Cdd:PLN03142  402 LKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEpgppYTTGE------HLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   714 ILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGSTDFAFLLSTRAGGLG 793
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   794 INLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLVTKGSVEEEIVERAKRKLVLDHLVIQRmdttGKTVLSK 873
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQK 629
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   874 NAtasgsvpfDKQELSAILKFGAVELFKEKEGEEQEPevDIDRILMGAE--TREAEEEVMKENELLSSFKYANFA----I 947
Cdd:PLN03142  630 TV--------NKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGEeaTAELDAKMKKFTEDAIKFKMDDTAelydF 699
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   948 DEEKDIAAATDEWAAII-------PEEDRNRILEE-ERMKELAEMNLAPRQRKQPIPQVVEDDDGDDDEEEDDTGKKKKk 1019
Cdd:PLN03142  700 DDEDDKDENKLDFKKIVsdnwidpPKRERKRNYSEsEYFKQAMRQGAPAKPKEPRIPRMPQLHDFQFFNVQRLTELYEK- 778
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1020 kavgnftipEIKRFIKSFRKFSM--PLNRLEEIAQDAELEEHSTDEMKKLVE------------SLSEACKKAADEFDSN 1085
Cdd:PLN03142  779 ---------EVRYLMQAHQKGQLkdTIDVAEPEEPGDPLTAEEQEEKEQLLEegfstwsrrdfnAFIRACEKYGRNDIKS 849
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1086 EKNGDAGAAESEKKDIERKFKFHTCDVN-----LKQIERSHAELKPLHEILKSEETKTS-FKPP-ANAKLQKGWDVD--W 1156
Cdd:PLN03142  850 IASEMEGKTEEEVERYAKVFWERYKELNdydriIKNIERGEARISRKDEIMKAIGKKLDrYKNPwLELKIQYGQNKGklY 929
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  1157 SRPDDSALLLGVWKYGYGSWE----AIKMDPTLGLadKIFIKDKTKkpqgKNLQVRVDYLLKLMSKDKVKTTEKKERKRK 1232
Cdd:PLN03142  930 NEECDRFMLCMVHKLGYGNWDelkaAFRTSPLFRF--DWFVKSRTP----QELARRCDTLIRLIEKENQEYDERERQARK 1003
                         890
                  ....*....|...
gi 32563629  1233 ADDVPVGPEKKKR 1245
Cdd:PLN03142 1004 EKKLAKNATPSKR 1016
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
404-621 3.01e-147

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: 446.80  E-value: 3.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 VYMGDVVSRDMIRQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:cd17993   81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629  564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd17993  161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
386-855 1.24e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 409.61  E-value: 1.24e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  386 EKFESMPDFLKTDgesthkLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLST 465
Cdd:COG0553  229 EALESLPAGLKAT------LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSL 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  466 MAAWQKEFAQWAPEMNLVVYMGdvvSRDMIRQYEWFVGGtkkmkiNAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKN 545
Cdd:COG0553  302 VGNWQRELAKFAPGLRVLVLDG---TRERAKGANPFEDA------DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKN 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  546 DESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKG----ISALHKKLEPFLLRR 621
Cdd:COG0553  373 PATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLRPFLLRR 452
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  622 VKKDVEKSLPPKTEQILRVDMTAHQKQFYKwILTKNYRELSKGVKGSINGFVNL--VMELKKCCNHASLtrqydhiYDDA 699
Cdd:COG0553  453 TKEDVLKDLPEKTEETLYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGLILaaLTRLRQICSHPAL-------LLEE 524
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  700 QGRLQQllkSSGKLILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGST 779
Cdd:COG0553  525 GAELSG---RSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEA 601
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563629  780 DFaFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLVTKGSVEEEIVERAKRKLVL 855
Cdd:COG0553  602 PV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
382-621 2.97e-123

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: 383.59  E-value: 2.97e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  382 RPKFEKFESMPDFLktdGESTHKLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVV 461
Cdd:cd18054    1 RPRFVALKKQPSYI---GGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  462 PLSTMAAWQKEFAQWAPEMNLVVYMGDVVSRDMIRQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAH 541
Cdd:cd18054   78 PLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  542 RLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18054  158 RLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
383-621 1.12e-102

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: 327.01  E-value: 1.12e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  383 PKFEKFESMPDFLktDGESTHKLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVP 462
Cdd:cd18053    1 PRFVALKKQPSYI--GGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  463 LSTMAAWQKEFAQWAPEMNLVVYMGDVVSRDMIRQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHR 542
Cdd:cd18053   79 LSTLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32563629  543 LKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18053  159 LKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRR 237
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
408-688 4.73e-94

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: 305.38  E-value: 4.73e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    408 YQLEGLNWMVYAWCK-GNSSILADEMGLGKTIQSISLLASLFHRYDLAG-PYLVVVPLSTMAAWQKEFAQWA--PEMNLV 483
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    484 VYMGDvvSRDmirQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:pfam00176   81 VLHGN--KRP---QERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAH-----NESNHKGISALHKKLEPFLLRRVKKDVEKSLPPKTEQIL 638
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFdrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 32563629    639 RVDMTAHQKQFYK-WILTKNYRELSKGVKGS--INGFVNLVMELKKCCNHASL 688
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGReiKASLLNILMRLRKICNHPGL 288
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
405-621 2.23e-87

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: 283.76  E-value: 2.23e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPeMNLVV 484
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFV----GGTKK--MKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFR 558
Cdd:cd17995   80 YHGSGESRQIIQQYEMYFkdaqGRKKKgvYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629  559 FNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNE-SNHKGISALHKKLEPFLLRR 621
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDlKTAEQVEKLQALLKPYMLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
405-586 2.15e-80

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: 262.12  E-value: 2.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFvggtkkMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLL 564
Cdd:cd17919   81 YHGSQRERAQIRAKEKL------DKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                        170       180
                 ....*....|....*....|..
gi 32563629  565 ITGTPLQNSLKELWALLHFIMP 586
Cdd:cd17919  155 LTGTPLQNNLEELWALLDFLDP 176
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
404-623 9.59e-72

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: 239.15  E-value: 9.59e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:cd17997    3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 VYMGDVVSRDMIRQyEWFVGGtkkmKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:cd17997   83 VLIGDKEERADIIR-DVLLPG----KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563629  564 LITGTPLQNSLKELWALLHFIMP------EKFDCWEEFETAHNEsNHKGISALHKKLEPFLLRRVK 623
Cdd:cd17997  158 LLTGTPLQNNLHELWALLNFLLPdvftssEDFDEWFNVNNCDDD-NQEVVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
404-623 7.39e-71

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: 237.28  E-value: 7.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:cd18009    3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 VYMGDVVSRDMIRQYEWFVGGTKkMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:cd18009   82 LYHGTKEERERLRKKIMKREGTL-QDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563629  564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFE-------------TAHNESNHKG---ISALHKKLEPFLLRRVK 623
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFEswfdfsslsdnaaDISNLSEEREqniVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
404-623 9.88e-71

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: 236.88  E-value: 9.88e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  404 KLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLV 483
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 VYMGDVVSRDMIRQYEwfvggtKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSL-TQFRFNHK 562
Cdd:cd17996   83 VYKGTPDVRKKLQSQI------RAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHARYR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563629  563 LLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHN----------------ESNHKGISALHKKLEPFLLRRVK 623
Cdd:cd17996  157 LLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkielneEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
405-621 1.38e-68

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: 228.86  E-value: 1.38e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVsrdmirqyewfvggtkkmkinaILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLL 564
Cdd:cd17994   81 YVGDHV----------------------LLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629  565 ITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNE-SNHKGISALHKKLEPFLLRR 621
Cdd:cd17994  139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADiSKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
405-621 8.79e-65

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: 218.85  E-value: 8.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSR-DMIRQYEWFvggtkkMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKL 563
Cdd:cd18006   81 YMGDKEKRlDLQQDIKST------NRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  564 LITGTPLQNSLKELWALLHFIMPEKF--DCWEEFETAHNE--SNHKGISALHKKLEPFLLRR 621
Cdd:cd18006  155 LLTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSEtdDESETVEELHLLLQPFLLRR 216
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
405-621 1.38e-61

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: 210.64  E-value: 1.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEW------FVGGTKKMKINA--------ILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLL 550
Cdd:cd18055   81 YTGDKDSRAIIRENEFsfddnaVKGGKKAFKMKReaqvkfhvLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  551 YKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF-ETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
387-633 1.72e-61

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 210.68  E-value: 1.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  387 KFESMPDFLKTDgesthKLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTM 466
Cdd:cd18064    3 RFEDSPSYVKWG-----KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  467 AAWQKEFAQWAPEMNLVVYMGD-----VVSRDMIRQYEWfvggtkkmkiNAILTTYEILLKDKAFLSSIDWAALLVDEAH 541
Cdd:cd18064   78 HNWMAEFKRWVPTLRAVCLIGDkdqraAFVRDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  542 RLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESN----HKGISALHKKLEPF 617
Cdd:cd18064  148 RIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNclgdQKLVERLHMVLRPF 227
                        250
                 ....*....|....*.
gi 32563629  618 LLRRVKKDVEKSLPPK 633
Cdd:cd18064  228 LLRRIKADVEKSLPPK 243
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
405-621 5.05e-61

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: 208.36  E-value: 5.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQyEWFvggtKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLL 564
Cdd:cd18003   81 YYGSAKERKLKRQ-GWM----KPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629  565 ITGTPLQNSLKELWALLHFIMPEKFDCWEEF-------ETAHNES----NHKGISALHKKLEPFLLRR 621
Cdd:cd18003  156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpLTAMSEGsqeeNEELVRRLHKVLRPFLLRR 223
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
405-621 6.32e-60

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: 205.68  E-value: 6.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEW------FVGGTK--------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLL 550
Cdd:cd18057   81 YTGDKESRSVIRENEFsfednaIRSGKKvfrmkkeaQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  551 YKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF-ETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
405-621 1.14e-59

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: 204.91  E-value: 1.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEW------FVGGTK--------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLL 550
Cdd:cd18056   81 YVGDKDSRAIIRENEFsfednaIRGGKKasrmkkeaSVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  551 YKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF-ETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFlEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
405-621 3.12e-59

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: 203.51  E-value: 3.12e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYeWfvgGTKKMK-----INAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRF 559
Cdd:cd18002   81 YWGNPKDRKVLRKF-W---DRKNLYtrdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHC 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563629  560 NHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFE-------TAHNES----NHKGISALHKKLEPFLLRR 621
Cdd:cd18002  157 RNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNewfskdiESHAENktglNEHQLKRLHMILKPFMLRR 229
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
405-621 1.16e-58

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: 201.82  E-value: 1.16e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHrYDLAGPYLVVVPLSTMAAWQKEFAQWApEMNLVV 484
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFVGGTK------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFR 558
Cdd:cd18060   79 YHGSLASRQMIQQYEMYCKDSRgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629  559 FNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNE-SNHKGISALHKKLEPFLLRR 621
Cdd:cd18060  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDlKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
405-621 5.09e-57

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: 196.80  E-value: 5.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLSTMAAWQKEFAQWApEMNLVV 484
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLM-GIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFVGGTK------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFR 558
Cdd:cd18058   79 YHGSQISRQMIQQYEMYYRDEQgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563629  559 FNHKLLITGTPLQNSLKELWALLHFIMPEKFDC----WEEFETAHNESNHKGISALhkkLEPFLLRR 621
Cdd:cd18058  159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSettfLEEFGDLKTEEQVKKLQSI---LKPMMLRR 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
710-836 5.46e-56

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.38  E-value: 5.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  710 SGKLILLDKLLCRLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPGStDFAFLLSTRA 789
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 32563629  790 GGLGINLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTKTVNIYRLV 836
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
403-623 2.37e-55

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: 192.01  E-value: 2.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  403 HKLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASlFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNL 482
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  483 VVYMGDVVSRDMIRQYEwfvggtkkmKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHK 562
Cdd:cd18012   82 LVIHGTKRKREKLRALE---------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32563629  563 LLITGTPLQNSLKELWALLHFIMPEKFDCWEEF--------ETAHNESNhkgISALHKKLEPFLLRRVK 623
Cdd:cd18012  153 LALTGTPIENHLGELWSIFDFLNPGLLGSYKRFkkrfakpiEKDGDEEA---LEELKKLISPFILRRLK 218
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
387-623 3.51e-55

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: 192.15  E-value: 3.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  387 KFESMPDFLKTDgesthKLRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTM 466
Cdd:cd18065    3 RFEESPSYVKGG-----TLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  467 AAWQKEFAQWAPEMNLVVYMGD-----VVSRDMIRQYEWfvggtkkmkiNAILTTYEILLKDKAFLSSIDWAALLVDEAH 541
Cdd:cd18065   78 HNWMNEFKRWVPSLRAVCLIGDkdaraAFIRDVMMPGEW----------DVCVTSYEMVIKEKSVFKKFNWRYLVIDEAH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  542 RLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESN----HKGISALHKKLEPF 617
Cdd:cd18065  148 RIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNclgdQKLVERLHAVLKPF 227

                 ....*.
gi 32563629  618 LLRRVK 623
Cdd:cd18065  228 LLRRIK 233
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
405-621 8.15e-55

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: 190.60  E-value: 8.15e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFhRYDLAGPYLVVVPLSTMAAWQKEFAQWApEMNLVV 484
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEIL-LTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFVGGTK------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFR 558
Cdd:cd18061   79 YHGSLISRQMIQQYEMYFRDSQgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629  559 FNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNE-SNHKGISALHKKLEPFLLRR 621
Cdd:cd18061  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDlKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
405-589 2.00e-53

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: 185.28  E-value: 2.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDlAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWfvggTKKMKINAILTTYEILL---KDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNH 561
Cdd:cd17998   80 YYGSQEERKHLRYDIL----KGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANF 155
                        170       180
                 ....*....|....*....|....*...
gi 32563629  562 KLLITGTPLQNSLKELWALLHFIMPEKF 589
Cdd:cd17998  156 RLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
405-621 4.74e-52

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: 182.54  E-value: 4.74e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLSTMAAWQKEFAQWApEMNLVV 484
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLK-GIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMIRQYEWFVGGTK------KMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFR 558
Cdd:cd18059   79 YHGSQASRRTIQLYEMYFKDPQgrvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629  559 FNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNE-SNHKGISALHKKLEPFLLRR 621
Cdd:cd18059  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDlKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
405-623 1.37e-50

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: 179.49  E-value: 1.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18063   24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGD-VVSRDMIRQYewfvggtKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSL-TQFRFNHK 562
Cdd:cd18063  104 YKGTpAMRRSLVPQL-------RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563629  563 LLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHN--------------ESNHKGISALHKKLEPFLLRRVK 623
Cdd:cd18063  177 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervdlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
405-623 2.22e-49

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: 176.00  E-value: 2.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGDVVSRDMirqyewFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSL-TQFRFNHKL 563
Cdd:cd18062  104 YKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRL 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629  564 LITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHN--------------ESNHKGISALHKKLEPFLLRRVK 623
Cdd:cd18062  178 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvdlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
405-621 2.38e-45

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: 163.68  E-value: 2.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHR----YDLAG-PYLVVVPLSTMAAWQKEFAQWAPE 479
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKransFNSENlPSLVVCPPTLVGHWVAEIKKYFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  480 --MNLVVYMGDVVSRDMIRQyewfvggtKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQF 557
Cdd:cd17999   81 afLKPLAYVGPPQERRRLRE--------QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  558 RFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF----------------ETAHNESNHKGISALHKKLEPFLLRR 621
Cdd:cd17999  153 KANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFqrrflkpilasrdskaSAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
405-586 5.47e-45

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: 161.34  E-value: 5.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YM---GDVVSRDMIRQYEWFVGGTKKMKINA--ILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRF 559
Cdd:cd18000   81 LHssgSGTGSEEKLGSIERKSQLIRKVVGDGgiLITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                        170       180
                 ....*....|....*....|....*..
gi 32563629  560 NHKLLITGTPLQNSLKELWALLHFIMP 586
Cdd:cd18000  161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
405-621 1.89e-43

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: 158.30  E-value: 1.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVV 484
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDS-GLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  485 YMGdVVSRDMIRQYEWFvggtkKMKINAILTTYEILLKDKAFLSSID-----WAALLVDEAHRLKNDESLLYKSLTQFRF 559
Cdd:cd18001   80 FHG-TSKKERERNLERI-----QRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  560 NHKLLITGTPLQNSLKELWALLHFIMP-------EKFDcwEEFET----AHNESNHKGISA--------LHKKLEPFLLR 620
Cdd:cd18001  154 KNRIILTGTPIQNNLKELWALFDFACNgsllgtrKTFK--MEFENpitrGRDKDATQGEKAlgsevaenLRQIIKPYFLR 231

                 .
gi 32563629  621 R 621
Cdd:cd18001  232 R 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
405-621 1.32e-42

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: 156.39  E-value: 1.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMvYAWCKGNSS-ILADEMGLGKTIQSISLLASLFH-------RYDL-------------AGPYLVVVPL 463
Cdd:cd18005    1 LRDYQREGVEFM-YDLYKNGRGgILGDDMGLGKTVQVIAFLAAVLGktgtrrdRENNrprfkkkppassaKKPVLIVAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  464 STMAAWQKEFAQWApEMNLVVYMGDvvSRDMIRQyewfvGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRL 543
Cdd:cd18005   80 SVLYNWKDELDTWG-HFEVGVYHGS--RKDDELE-----GRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  544 KNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFETAHNESNHKGISA-------------- 609
Cdd:cd18005  152 KNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHtatarelrlgrkrk 231
                        250
                 ....*....|....
gi 32563629  610 --LHKKLEPFLLRR 621
Cdd:cd18005  232 qeLAVKLSKFFLRR 245
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
405-621 1.98e-39

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: 147.05  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVyawCKGnsSILADEMGLGKTIQSISLLASlfHRYDLAGPY-------------------LVVVPLST 465
Cdd:cd18008    1 LLPYQKQGLAWML---PRG--GILADEMGLGKTIQALALILA--TRPQDPKIPeeleenssdpkklylskttLIVVPLSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  466 MAAWQKEFAQ--WAPEMNLVVYMGDVVSRDmirqyewfvgGTKKMKINAILTTYEILLKD----------------KAFL 527
Cdd:cd18008   74 LSQWKDEIEKhtKPGSLKVYVYHGSKRIKS----------IEELSDYDIVITTYGTLASEfpknkkgggrdskekeASPL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  528 SSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFD---CWEEFETA-HNESN 603
Cdd:cd18008  144 HRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGdypWFNSDISKpFSKND 223
                        250
                 ....*....|....*...
gi 32563629  604 HKGISALHKKLEPFLLRR 621
Cdd:cd18008  224 RKALERLQALLKPILLRR 241
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
194-275 2.92e-38

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, 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 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: 349313  Cd Length: 85  Bit Score: 137.81  E-value: 2.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  194 TETVERVIKWRHGVPGATGSATTCYNIADKGDPND--QIPGDKTEQQFFVKWTGWSHLHNTWESENSLALMNAKGLKKVQ 271
Cdd:cd18666    2 FETIERVLDHRIGRKGATGASTTIYAVEADGDPNAgfDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLE 81

                 ....
gi 32563629  272 NYVK 275
Cdd:cd18666   82 NYKK 85
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
405-597 9.79e-34

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: 130.49  E-value: 9.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLN--WMVYAWCKGNSS-----ILADEMGLGKTIQSISLLASLFHRYDLAGPYLVVVPLSTMAAWQKEFAQWA 477
Cdd:cd18007    1 LKPHQVEGVRflWSNLVGTDVGSDegggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  478 PEMNLVVYMGDVVSR--------DMIRQyeWFVGGtkkmkiNAILTTYEILLK--------DKAFLSSIDWAA-----LL 536
Cdd:cd18007   81 PPDLRPLLVLVSLSAskradarlRKINK--WHKEG------GVLLIGYELFRNlasnattdPRLKQEFIAALLdpgpdLL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  537 V-DEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEFET 597
Cdd:cd18007  153 VlDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKK 214
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
405-586 1.47e-32

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: 127.40  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMvyaW-C-------KGNSSILADEMGLGKTIQSISLLASLFHRYDLAGP----YLVVVPLSTMAAWQKE 472
Cdd:cd18004    1 LRPHQREGVQFL---YdCltgrrgyGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  473 FAQWAPEMNLVVYMGDVVSRD-MIRQYEWFVGGTKKMkinaILTTYEILLKDKAFLSSIDWAALLV-DEAHRLKNDESLL 550
Cdd:cd18004   78 FDKWLGLRRIKVVTADGNAKDvKASLDFFSSASTYPV----LIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKT 153
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 32563629  551 YKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMP 586
Cdd:cd18004  154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNP 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
711-825 1.42e-27

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 108.07  E-value: 1.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    711 GKLILLDKLLCrlKDKGHRVLIFSQMVMMLDIlQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPgstDFAFLLSTRAG 790
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 32563629    791 GLGINLATADTVIIFDSDWNPQNDLQAMSRAHRIG 825
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
404-588 7.89e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.50  E-value: 7.89e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629     404 KLRDYQLEGLNWMVYAWckgNSSILADEMGLGKTIQSISLLASLFHRYDlAGPYLVVVPL-STMAAWQKEFAQWAPEMNL 482
Cdd:smart00487    8 PLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTrELAEQWAEELKKLGPSLGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629     483 --VVYMGDVVSRDMIRQYewfvggtKKMKINAILTTYEILLKD--KAFLSSIDWAALLVDEAHRLKND--ESLLYKSLTQ 556
Cdd:smart00487   84 kvVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 32563629     557 FRFN-HKLLITGTP---LQNSLKELWALLHFIMPEK 588
Cdd:smart00487  157 LPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
422-621 2.71e-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: 109.10  E-value: 2.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  422 KGNSSILADEMGLGKTIQSISLLaslfhrydLAGPYLVVVPLSTMAAWQKEFAQWAPEMNLVVYM--GDVVSRDMirqye 499
Cdd:cd18071   47 LVRGGILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTyhGGERNRDP----- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  500 wfvggTKKMKINAILTTYEILL-----KDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSL 574
Cdd:cd18071  114 -----KLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSP 188
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 32563629  575 KELWALLHFIMPEKFDCWEEFETA----HNESNHKGISALHKKLEPFLLRR 621
Cdd:cd18071  189 KDLGSLLSFLHLKPFSNPEYWRRLiqrpLTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
405-586 7.49e-25

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 104.93  E-value: 7.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNW-----MVYAWCKGNSSILADEMGLGKTIQSISLLASLFHRydlaGPY---------LVVVPLSTMAAWQ 470
Cdd:cd18066    1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQ----GPYggkpvikraLIVTPGSLVKNWK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  471 KEFAQWAPEMNLVVYmgdVVSRDmiRQYEWFVggtKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLL 550
Cdd:cd18066   77 KEFQKWLGSERIKVF---TVDQD--HKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT 148
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 32563629  551 YKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMP 586
Cdd:cd18066  149 TTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
405-595 1.15e-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: 101.78  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMvYAWCKG------NSSILADEMGLGKTIQSISLLASLFHRYDLAGPYL----VVVPLSTMAAWQKEFA 474
Cdd:cd18067    1 LRPHQREGVKFL-YRCVTGrrirgsHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  475 QW-APEMNLVVYMGDVVSRDMIRQYEWFVGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKS 553
Cdd:cd18067   80 KWlGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 32563629  554 LTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF 595
Cdd:cd18067  160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEF 201
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
405-595 8.38e-22

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 95.35  E-value: 8.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNwmvYAWCKGNSSILADEMGLGKTIQSISLLASLFHRYdlagPYLVVVPLSTMAAWQKEFAQWAPEM---N 481
Cdd:cd18010    1 LLPFQREGVC---FALRRGGRVLIADEMGLGKTVQAIAIAAYYREEW----PLLIVCPSSLRLTWADEIERWLPSLppdD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  482 LVVYMGdvvSRDMIRqyewfvGGTKKMKInailTTYEILLKDKAFLSSIDWAALLVDEAHRLKNDESLLYKSLTQF--RF 559
Cdd:cd18010   74 IQVIVK---SKDGLR------DGDAKVVI----VSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRA 140
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 32563629  560 NHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF 595
Cdd:cd18010  141 KRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
HELICc smart00490
helicase superfamily c-terminal domain;
741-825 4.98e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 4.98e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629     741 DILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNAPgstDFAFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAMSR 820
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 32563629     821 AHRIG 825
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
405-595 4.30e-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: 91.49  E-value: 4.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYAWCK---------GNSSILADEMGLGKTIQSISLLASLFHRYDLAG--PYLVVVPLSTMAAWQKEF 473
Cdd:cd18068    1 LKPHQVDGVQFMWDCCCEslkktkkspGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  474 AQWAPEMN----LVVYMGDVVSRDMIRQY---EWFVGGTkKMKINAILttYEILLKDKAFLSSI----DWAALLV----- 537
Cdd:cd18068   81 EKWQEGLKdeekIEVNELATYKRPQERSYklqRWQEEGG-VMIIGYDM--YRILAQERNVKSREklkeIFNKALVdpgpd 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563629  538 ----DEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF 595
Cdd:cd18068  158 fvvcDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEF 219
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1024-1113 4.76e-19

CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays an important role in regulating nucleosome assembly and mobilization. CHD1 consists of double chromodomain, SNF2-related ATPase domain, and a C-terminal DNA-binding domain. The DNA-binding domain contains SANT (Swi3, Ada2, N-CoR, TFIIIB) and SLIDE (SANT-like ISWI) domains in its C-terminal region. SANT domains are structurally related to Myb-like domains are common motifs found in chromatin interacting proteins. Deletion of individual SANT or SLIDE domains in CDH1 does not significantly affect nucleosome binding, but combined deletion of both domains severely compromise binding, suggesting that the SANT-SLIDE motif recognizes DNA/nucleosomes as a single cooperative unit. SANT sequences of Chd1 proteins are the most distantly relation group of sequences relation to other SANT/Myb sequences, and are more diverse than other SANT proteins. The SANT and SLIDE regions are well conserved in both Chd1 and ISWI (imitation switch) remodelling enzymes. This domain comprises the SANT region and the helical linker region 1 (HL1).


Pssm-ID: 465731  Cd Length: 90  Bit Score: 83.17  E-value: 4.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629   1024 NFTIPEIKRFIKSFRKFSMPLNRLEEIAQDAELEEHSTDEMKKLVESLSEACKKAADEFDsnEKNGDAGAAESEKKDIER 1103
Cdd:pfam18375    2 GFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYT--EKEDENPGADGGKKRIRG 79
                           90
                   ....*....|.
gi 32563629   1104 -KFKFHTCDVN 1113
Cdd:pfam18375   80 pSFKLGGVSVN 90
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
405-595 2.70e-18

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: 85.64  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMV---------YAWCKGNSSILADEMGLGKTIQSISLLASLFhRYDLAGPYLVVVPLSTMAAWQKEFAQ 475
Cdd:cd18069    1 LKPHQIGGIRFLYdniieslerYKGSSGFGCILAHSMGLGKTLQVISFLDVLL-RHTGAKTVLAIVPVNTLQNWLSEFNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  476 WAPEMnlvvymgDVVSRDMIRQYEWFVGG----TKKMKINAI----------LTTYEIL-LKDKAFLssidwaaLLVDEA 540
Cdd:cd18069   80 WLPPP-------EALPNVRPRPFKVFILNdehkTTAARAKVIedwvkdggvlLMGYEMFrLRPGPDV-------VICDEG 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 32563629  541 HRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDCWEEF 595
Cdd:cd18069  146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEF 200
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
427-621 3.54e-18

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: 84.65  E-value: 3.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  427 ILADEMGLGKTIQSIsLLASLFHRYDLAGPYLVVVPLSTMAAWQKE----FAQWAPemnlvvymgdVVSRDMIRQYEWFV 502
Cdd:cd18011   21 LLADEVGLGKTIEAG-LIIKELLLRGDAKRVLILCPASLVEQWQDElqdkFGLPFL----------ILDRETAAQLRRLI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  503 GGTKKMkINAILTTYEiLLKDK----AFLSSIDWAALLVDEAHRLKNDESLLYKSLTQF------RFNHKLLITGTPLQN 572
Cdd:cd18011   90 GNPFEE-FPIVIVSLD-LLKRSeerrGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRARHVLLLTATPHNG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 32563629  573 SLKELWALLHFIMPEKFDCWEEFEtahnesnhkGISALHKKLEPFLLRR 621
Cdd:cd18011  168 KEEDFRALLSLLDPGRFAVLGRFL---------RLDGLREVLAKVLLRR 207
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
405-621 1.68e-16

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: 80.60  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVyaW---CKGNSSILADEMGLGKTIQSISL-LASLFHR----------------------YDLAGPyL 458
Cdd:cd18072    1 LLLHQKQALAWLL--WrerQKPRGGILADDMGLGKTLTMIALiLAQKNTQnrkeeekekalteweskkdstlVPSAGT-L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  459 VVVPLSTMAAWQKEFAQWAPEMNLVVYMGDVVSRDMIrqyewfvgGTKKMKINAILTTYEILLKD---------KAFLSS 529
Cdd:cd18072   78 VVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERI--------GEVLRDYDIVITTYSLVAKEiptykeesrSSPLFR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  530 IDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFD---CWEEFETAHNESNHKG 606
Cdd:cd18072  150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDdlkVWKKQVDNKSRKGGER 229
                        250
                 ....*....|....*
gi 32563629  607 ISALHKKLepfLLRR 621
Cdd:cd18072  230 LNILTKSL---LLRR 241
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
308-363 6.49e-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: 72.99  E-value: 6.49e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32563629  308 EYKKVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMV---APEQIKAYY 363
Cdd:cd18659    1 EYTIVERIIAHREDDEGV------TEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYK 53
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
405-620 2.99e-15

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: 77.38  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVyaWCKGnssILADEMGLGKTIQSISLLASlfHR-----YDLA----------------------GPY 457
Cdd:cd18070    1 LLPYQRRAVNWML--VPGG---ILADEMGLGKTVEVLALILL--HPrpdndLDAAdddsdemvccpdclvaetpvssKAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  458 LVVVPLSTMAAWQKEFAQWAPEmNLVVYMGDVVSRDMirqyeWFVGGTKKMKINA--ILTTYEILLKDKAF--------- 526
Cdd:cd18070   74 LIVCPSAILAQWLDEINRHVPS-SLKVLTYQGVKKDG-----ALASPAPEILAEYdiVVTTYDVLRTELHYaeanrsnrr 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  527 -------------LSSIDWAALLVDEAHRLKNDESLLYKSLTQFRFNHKLLITGTPLQNSLKELWALLHFIMPEKFDC-- 591
Cdd:cd18070  148 rrrqkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDsd 227
                        250       260
                 ....*....|....*....|....*....
gi 32563629  592 WEEFETAHNESNHKGISALHKKLEPFLLR 620
Cdd:cd18070  228 WWARVLIRPQGRNKAREPLAALLKELLWR 256
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
195-275 1.61e-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: 69.70  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  195 ETVERVIKWRHGVPGATGSAttcyniaDKGDPNDQIPgdktEQQFFVKWTGWSHLHNTWESENSlaLMNAKGLKKVQNYV 274
Cdd:cd18660    3 DKIEKILDHRPKGPVEEASL-------DLTDPDEPWD----EREFLVKWKGKSYLHCTWVTEET--LEQLRGKKKLKNYI 69

                 .
gi 32563629  275 K 275
Cdd:cd18660   70 K 70
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
308-365 4.94e-13

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: 65.01  E-value: 4.94e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563629  308 EYKKVERVVAHQTSRdraADGSMATEYLIKWSGLPYSDCTWEDEKMVA---PEQIKAYYHR 365
Cdd:cd18661    1 QYQIVERIIAHSPQK---SAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHSR 58
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
308-365 3.44e-11

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: 59.98  E-value: 3.44e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563629  308 EYKKVERVVAHQtsRDRAADGSMATEYLIKWSGLPYSDCTWEDEKMV---APEQIKAYYHR 365
Cdd:cd18664    1 EFHVVERIIASQ--RASLEDGTSQLQYLVKWRRLNYDECTWEDATLIaklAPEQVDHFQNR 59
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
310-365 4.55e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 4.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629    310 KKVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMVA--PEQIKAYYHR 365
Cdd:pfam00385    1 YEVERILDHRKDKGGK------EEYLVKWKGYPYDENTWEPEENLSkcPELIEEFKDR 52
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
234-275 3.77e-10

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 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: 349312  Cd Length: 65  Bit Score: 57.01  E-value: 3.77e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 32563629  234 KTEQQFFVKWTGWSHLHNTWESENSLAlmNAKGLKKVQNYVK 275
Cdd:cd18665   26 KENYEFLIKWTDESHLHNTWETYESLK--QVRGLKKVDNYIK 65
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
405-584 4.08e-10

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: 61.21  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVYawcKGNSSILADeMGLGKTIQSISLLASLFHRyDLAGPYLVVVPLsTMAA--WQKEFAQWapemnl 482
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLD-DFTRRVLVIAPL-RVARstWPDEVEKW------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  483 vvymgdvvsrDMIRQYEWFVG-GTKKMKINAI-------LTTYEILLK-DKAFLSSIDWAALLVDEAHRLKNDESLLYKS 553
Cdd:cd18013   69 ----------NHLRNLTVSVAvGTERQRSKAAntpadlyVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKA 138
                        170       180       190
                 ....*....|....*....|....*....|...
gi 32563629  554 LTQFRFNHKLLI--TGTPLQNSLKELWALLHFI 584
Cdd:cd18013  139 LRKVRPVIKRLIglTGTPSPNGLMDLWAQIALL 171
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
309-365 3.22e-09

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: 54.22  E-value: 3.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32563629  309 YKKVERVVAHQTSRDrAADGSMATEYLIKWSGLPYSDCTWEDEKMVAPEQIKAYYHR 365
Cdd:cd18663    3 YVEVDRILDVSVSTD-PNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKL 58
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
348-983 4.20e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 60.81  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  348 WEDEKMVAPEQIKAYYHRIENLKSPNKNSNVLRKRPKFEKFESMPDFLKTDGE---STHKLRDYQLEGLNWMVYAWCKGN 424
Cdd:COG1061   21 LDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEasgTSFELRPYQQEALEALLAALERGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  425 SSILAdEM--GLGKTIqsisLLASLFHRYDLAGPYLVVVP-LSTMAAWQKEFAQWAPEmnlvvymgdvvsrdmirqyEWF 501
Cdd:COG1061  101 GRGLV-VAptGTGKTV----LALALAAELLRGKRVLVLVPrRELLEQWAEELRRFLGD-------------------PLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  502 VGGTKKMKINAILTTYEILLKDKAFLSSIDWAALLV-DEAHRLkndESLLY-KSLTQFRFNHKLLITGTPlqnslkelwa 579
Cdd:COG1061  157 GGGKKDSDAPITVATYQSLARRAHLDELGDRFGLVIiDEAHHA---GAPSYrRILEAFPAAYRLGLTATP---------- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  580 llhFIMPEKFDCWEEFE-TAHNESNHKGISALHkkLEPFLLRRVkkdvekslppkteqilRVDMTAHQKQfykwiltknY 658
Cdd:COG1061  224 ---FRSDGREILLFLFDgIVYEYSLKEAIEDGY--LAPPEYYGI----------------RVDLTDERAE---------Y 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  659 RELSKgvkgsingfvnlvmelkkccnhaSLTRQYDHIYDDAQGRLQQLLKSSGklilldkllcrlkdKGHRVLIFSQMVM 738
Cdd:COG1061  274 DALSE-----------------------RLREALAADAERKDKILRELLREHP--------------DDRKTLVFCSSVD 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  739 MLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNApgsTDFAFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAM 818
Cdd:COG1061  317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRL 393
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  819 SRAHRIGQTK-TVNIYRLVTKGSVEEEIVERAKRKLVLDHlvIQRMDTTGKTVLSKNATASGSVPFDKQELSAILKFGAV 897
Cdd:COG1061  394 GRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYR--VEFLDEEESEELALLIAVKPALEVKGELEEELLEELEL 471
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  898 ELFKEKEGEEQEPEVDIDRILMGAETREAEEEVMKENELLSSFKYANFAIDEEKDIAAATDEWAAIIPEEDRNRILEEER 977
Cdd:COG1061  472 LEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEEL 551

                 ....*.
gi 32563629  978 MKELAE 983
Cdd:COG1061  552 AALLLK 557
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1298-1367 5.91e-09

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 54.57  E-value: 5.91e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32563629   1298 ECVKLCMPVHKYMKKLKEAQEAKNQADEAK----YLTRLGDSFlenlETLIKKKPKTNIRKWYNYLWIFLCKFT 1367
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKilkkELLKIGDFI----DSLLEETKKEKKEKLRKHLWSFVSKFW 79
ResIII pfam04851
Type III restriction enzyme, res subunit;
403-569 2.32e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.99  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    403 HKLRDYQLEGLNWMVYAWCKGNSSILAdEM--GLGKTIQSISLLASLFHRYDlAGPYLVVVP-LSTMAAWQKEFAQWAPE 479
Cdd:pfam04851    2 LELRPYQIEAIENLLESIKNGQKRGLI-VMatGSGKTLTAAKLIARLFKKGP-IKKVLFLVPrKDLLEQALEEFKKFLPN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    480 MNLVvyMGDVVSRDMIRQYewfvgGTKKMKINAILTTYEILLKDKAFLSSIDWAALLVDEAHRLkNDESllYKSLTQFrF 559
Cdd:pfam04851   80 YVEI--GEIISGDKKDESV-----DDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRS-GASS--YRNILEY-F 148
                          170
                   ....*....|..
gi 32563629    560 NHKLLI--TGTP 569
Cdd:pfam04851  149 KPAFLLglTATP 160
CHROMO smart00298
Chromatin organization modifier domain;
311-365 3.64e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 51.06  E-value: 3.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 32563629     311 KVERVVAHQTSRDRAadgsmaTEYLIKWSGLPYSDCTWEDEKMV--APEQIKAYYHR 365
Cdd:smart00298    3 EVEKILDHRWKKKGE------LEYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYKKK 53
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
308-364 4.96e-08

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: 50.73  E-value: 4.96e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  308 EYKKVERVVAHQTSRDraadGSmaTEYLIKWSGLPYSDCTWEDEKMVAPE---QIKAYYH 364
Cdd:cd18662    2 EWLQIHRIINHRVDKD----GN--TWYLVKWRDLPYDQSTWESEDDDIPDyekHIQEYWD 55
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
405-569 2.13e-07

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: 51.54  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  405 LRDYQLEGLNWMVyAWCKGNSSILADEMGLGKTIQSISLLASLFhrydlAGPYLVVVP-LSTMAAWQKEFAQWAPemnlv 483
Cdd:cd17926    1 LRPYQEEALEAWL-AHKNNRRGILVLPTGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLG----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  484 vymgdvvsRDMIRQyewfVGGTKKMK---INAILTTYEIL---LKDKAFLSSiDWAALLVDEAHRLknDESLLYKSLTQF 557
Cdd:cd17926   70 --------DSSIGL----IGGGKKKDfddANVVVATYQSLsnlAEEEKDLFD-QFGLLIVDEAHHL--PAKTFSEILKEL 134
                        170
                 ....*....|..
gi 32563629  558 RFNHKLLITGTP 569
Cdd:cd17926  135 NAKYRLGLTATP 146
CHROMO smart00298
Chromatin organization modifier domain;
231-278 3.51e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.36  E-value: 3.51e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 32563629     231 PGDKTEQQFFVKWTGWSHLHNTWESENSLalmnAKGLKKVQNYVKKQK 278
Cdd:smart00298   12 WKKKGELEYLVKWKGYSYSEDTWEPEENL----LNCSKKLDNYKKKER 55
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
642-842 1.46e-06

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 51.56  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    642 MTAHQKQFYKWILTKNYRELSKGV-----KGSINGFVNLVMELKKCC---NHASLTrqYDHIYDDAQGRLQ---QLLKSS 710
Cdd:pfam11496   12 MTSYQKELTEQIVSLHYSDILKYCetsdsKEDISLIKSMTLCLENLSlvaTHPYLL--VDHYMPKSLLLKDepeKLAYTS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629    711 GKLILLDKLLC----RLKDKGHRVLIFSQMVMMLDILQEYLQLRRFPSQRLDG-SMRADLRKQALDHYNAPGSTDFAFLL 785
Cdd:pfam11496   90 GKFLVLNDLVNllieRDRKEPINVAIVARSGKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLLS 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563629    786 STR-----AGGLGINlaTADTVIIFDSDWNPQND-LQAMSRAHRIGQTKTVnIYRLVTKGSVE 842
Cdd:pfam11496  170 STGqltndDSLLENY--KFDLIIAFDSSVDTSSPsVEHLRTQNRRKGNLAP-IIRLVVINSIE 229
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
312-362 2.19e-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: 45.93  E-value: 2.19e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32563629  312 VERVVAHQTSRDRaadgsmaTEYLIKWSGLPYSDCTWEDEKMV--APEQIKAY 362
Cdd:cd00024    3 VEKILDHRVRKGK-------LEYLVKWKGYPPEENTWEPEENLtnAPELIKEY 48
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
233-276 4.33e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.18  E-value: 4.33e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 32563629    233 DKTEQQFFVKWTGWSHLHNTWESENSLalmnAKGLKKVQNYVKK 276
Cdd:pfam00385   13 KGGKEEYLVKWKGYPYDENTWEPEENL----SKCPELIEEFKDR 52
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
400-543 7.65e-05

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 44.98  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  400 ESTHKLRDYQLEGLNWMvYAWCKGNSSILADEMGLGKTIQSISLLAslfhrydLAGPYLVVVPLSTMAA--WQKEFAQWA 477
Cdd:cd18029    4 KPSTQLRPYQEKALSKM-FGNGRARSGVIVLPCGAGKTLVGITAAC-------TIKKSTLVLCTSAVSVeqWRRQFLDWT 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563629  478 PemnlvvymgdvVSRDMIRQyewFVGGTKKMKINA--ILTTYEILLKDKA----------FLSSIDWAALLVDEAHRL 543
Cdd:cd18029   76 T-----------IDDEQIGR---FTSDKKEIFPEAgvTVSTYSMLANTRKrspesekfmeFITEREWGLIILDEVHVV 139
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
781-828 9.22e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 42.31  E-value: 9.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 32563629  781 FAFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAMSRAHRIGQTK 828
Cdd:cd18785   23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
712-827 1.20e-04

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 43.26  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563629  712 KLILLDKLLCRLKDKghRVLIFSQMVMMLDILQEYLQLRRFPSQRLDGSMRADLRKQALDHYNapgSTDFAFLLST---- 787
Cdd:cd18787   14 KLLLLLLLLEKLKPG--KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR---SGKVRVLVATdvaa 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 32563629  788 RagglGINLATADTVIIFDsdwNPQNdlqamSRA--HRIGQT 827
Cdd:cd18787   89 R----GLDIPGVDHVINYD---LPRD-----AEDyvHRIGRT 118
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
312-361 2.75e-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: 39.96  E-value: 2.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 32563629  312 VERVVAhqtsrDRAADGsmATEYLIKWSGLPYSDCTWEDEKMVAPEQIKA 361
Cdd:cd18966    3 VERILA-----ERRDDG--GKRYLVKWEGYPLEEATWEPEENIGDEELLK 45
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
310-352 1.03e-03

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: 38.88  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 32563629  310 KKVERVVAHQTSRDRAADGSMAT---------EYLIKWSGLPYSDCTWEDEK 352
Cdd:cd18660    3 DKIEKILDHRPKGPVEEASLDLTdpdepwderEFLVKWKGKSYLHCTWVTEE 54
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
332-352 1.38e-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: 38.23  E-value: 1.38e-03
                         10        20
                 ....*....|....*....|.
gi 32563629  332 TEYLIKWSGLPYSDCTWEDEK 352
Cdd:cd18965   16 LEYLVKWHGLPESENTWEREK 36
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
233-259 1.82e-03

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: 37.84  E-value: 1.82e-03
                         10        20
                 ....*....|....*....|....*..
gi 32563629  233 DKTEQQFFVKWTGWSHLHNTWESENSL 259
Cdd:cd00024   12 RKGKLEYLVKWKGYPPEENTWEPEENL 38
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
238-256 3.86e-03

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 36.60  E-value: 3.86e-03
                         10
                 ....*....|....*....
gi 32563629  238 QFFVKWTGWSHLHNTWESE 256
Cdd:cd18627   17 EYLVKWKGWSQKYNTWEPE 35
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
238-259 4.33e-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: 349324  Cd Length: 57  Bit Score: 36.94  E-value: 4.33e-03
                         10        20
                 ....*....|....*....|..
gi 32563629  238 QFFVKWTGWSHLHNTWESENSL 259
Cdd:cd18968   24 KYLVKWAGYPDEENTWEPEESF 45
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
238-256 5.17e-03

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 36.67  E-value: 5.17e-03
                         10
                 ....*....|....*....
gi 32563629  238 QFFVKWTGWSHLHNTWESE 256
Cdd:cd18644   20 EYLVKWKGWSNKHNTWEPE 38
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
333-365 5.57e-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: 36.37  E-value: 5.57e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 32563629  333 EYLIKWSGLPYSDCTWEDEKMVAPEQIKAYYHR 365
Cdd:cd18975   17 QYLIQWKGYPLEEASWELEDNIKNPRLIEEFHK 49
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
312-351 7.62e-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: 349320  Cd Length: 54  Bit Score: 36.16  E-value: 7.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 32563629  312 VERVVAHqtsRDRAADGSMATEYLIKWSGLPYSDCTWEDE 351
Cdd:cd18964    3 VERIIGR---RPSARDGPGKFLWLVKWDGYPIEDATWEPP 39
 
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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