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Conserved domains on  [gi|1868034362|ref|XP_035304502|]
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chromodomain-helicase-DNA-binding protein 2 isoform X4 [Cricetulus griseus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
366-602 0e+00

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: 547.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  366 RPRFVALKKQPAYLGGENLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLS 445
Cdd:cd18054      1 RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  446 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 525
Cdd:cd18054     81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  526 NDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd18054    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
370-923 1.20e-168

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: 539.39  E-value: 1.20e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  370 VALKKQPAYLGGEnleLRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTS 449
Cdd:PLN03142   157 TRLLVQPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  450 WQREFEIWAPEINVVVYIGDLMSRNTIREYewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 529
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAHQREE-----LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  530 LLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRRVKK 605
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDqqevVQQLHKVLRPFLLRRLKS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  606 DVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGtrGSTSGFLNIVMELKKCCNHCYLIKAPEENERENGQEvl 685
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE-- 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  686 qSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCF 765
Cdd:PLN03142   465 -HLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVF 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  766 LLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRm 845
Cdd:PLN03142   544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ- 622
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  846 dttGRtVLENNSgrsnsnpFNKEELTAILKFGAEDLFkeiEGEESEPQEMDIDEILrlaetRENEVSTSATDELLSQF 923
Cdd:PLN03142   623 ---GR-LAEQKT-------VNKDELLQMVRYGAEMVF---SSKDSTITDEDIDRII-----AKGEEATAELDAKMKKF 681
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
161-245 3.36e-46

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: 160.53  E-value: 3.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  161 NSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSGDFDTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKVKGLKKL 240
Cdd:cd18666      1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                   ....*
gi 1868034362  241 ENFKK 245
Cdd:cd18666     81 ENYKK 85
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1032-1120 1.35e-36

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: 133.63  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1032 GFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCASAMQEYEEQLKENASEGKGPGKRRGPT 1111
Cdd:pfam18375    2 GFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKRIRGPS 81

                   ....*....
gi 1868034362 1112 IKISGVQVN 1120
Cdd:pfam18375   82 FKLGGVSVN 90
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
278-349 2.40e-30

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: 114.32  E-value: 2.40e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  278 QYQIVERVIAVKTSKStlgqtdfpahsrkpAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSR 349
Cdd:cd18661      1 QYQIVERIIAHSPQKS--------------AASGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1373-1455 4.78e-26

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: 103.49  E-value: 4.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1373 ICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYsDQEHIKLWRRNLWIFVSKFTE--FDARKL 1450
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFWPnkVSGKKL 88

                   ....*
gi 1868034362 1451 HKLYK 1455
Cdd:pfam13907   89 KEMYK 93
 
Name Accession Description Interval E-value
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
366-602 0e+00

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: 547.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  366 RPRFVALKKQPAYLGGENLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLS 445
Cdd:cd18054      1 RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  446 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 525
Cdd:cd18054     81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  526 NDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd18054    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
370-923 1.20e-168

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 539.39  E-value: 1.20e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  370 VALKKQPAYLGGEnleLRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTS 449
Cdd:PLN03142   157 TRLLVQPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  450 WQREFEIWAPEINVVVYIGDLMSRNTIREYewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 529
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAHQREE-----LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  530 LLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRRVKK 605
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDqqevVQQLHKVLRPFLLRRLKS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  606 DVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGtrGSTSGFLNIVMELKKCCNHCYLIKAPEENERENGQEvl 685
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE-- 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  686 qSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCF 765
Cdd:PLN03142   465 -HLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVF 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  766 LLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRm 845
Cdd:PLN03142   544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ- 622
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  846 dttGRtVLENNSgrsnsnpFNKEELTAILKFGAEDLFkeiEGEESEPQEMDIDEILrlaetRENEVSTSATDELLSQF 923
Cdd:PLN03142   623 ---GR-LAEQKT-------VNKDELLQMVRYGAEMVF---SSKDSTITDEDIDRII-----AKGEEATAELDAKMKKF 681
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
361-841 1.30e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 413.08  E-value: 1.30e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  361 KALKQRPRFVALKKQPAYLGGEnleLRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLyGPFLI 440
Cdd:COG0553    220 DAFRLRRLREALESLPAGLKAT---LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLI 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  441 VVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEwihsqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDE 520
Cdd:COG0553    296 VAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDE 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  521 AHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLE 596
Cdd:COG0553    367 AQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLR 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  597 PFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKwILTRNYKALAKGTRGSTSGF--LNIVMELKKCCNHCYLIKapE 674
Cdd:COG0553    447 PFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGliLAALTRLRQICSHPALLL--E 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  675 ENERENGQevlqslirsSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDH 754
Cdd:COG0553    524 EGAELSGR---------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDR 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  755 FNADGSEDFcFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIER-AKK 833
Cdd:COG0553    595 FQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELlEEK 673

                   ....*...
gi 1868034362  834 KMVLDHLV 841
Cdd:COG0553    674 RALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-670 2.08e-109

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: 349.67  E-value: 2.08e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  389 YQLEGLNWLAHSWCKS-NSVILADEMGLGKTIQTISFLSYLFHQHQLYG-PFLIVVPLSTLTSWQREFEIWA--PEINVV 464
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGDLMSRNtireyEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRL 544
Cdd:pfam00176   81 VLHGNKRPQE-----RWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  545 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-----GRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQIL 619
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  620 RVEMSALQKQYYK-WILTRNYKALAKGTRGST--SGFLNIVMELKKCCNHCYLI 670
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
692-818 2.28e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.62  E-value: 2.28e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  692 SGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADgSEDFCFLLSTRA 771
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1868034362  772 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLV 818
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
161-245 3.36e-46

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: 160.53  E-value: 3.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  161 NSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSGDFDTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKVKGLKKL 240
Cdd:cd18666      1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                   ....*
gi 1868034362  241 ENFKK 245
Cdd:cd18666     81 ENYKK 85
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1032-1120 1.35e-36

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: 133.63  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1032 GFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCASAMQEYEEQLKENASEGKGPGKRRGPT 1111
Cdd:pfam18375    2 GFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKRIRGPS 81

                   ....*....
gi 1868034362 1112 IKISGVQVN 1120
Cdd:pfam18375   82 FKLGGVSVN 90
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
278-349 2.40e-30

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: 114.32  E-value: 2.40e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  278 QYQIVERVIAVKTSKStlgqtdfpahsrkpAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSR 349
Cdd:cd18661      1 QYQIVERIIAHSPQKS--------------AASGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
DEXDc smart00487
DEAD-like helicases superfamily;
384-569 7.20e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.36  E-value: 7.20e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   384 LELRDYQLEGLNWLAHSWcksNSVILADEMGLGKTIQTISFLSYLFHQHQlYGPFLIVVPLSTLT-SWQREFEIWAPE-- 460
Cdd:smart00487    7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAeQWAEELKKLGPSlg 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   461 INVVVYIGDLMSRNTIREYewihsqtKRLKFNALITTYEILLKD--KTVLGSINWAFLGVDEAHRLKND---DSLLYKTL 535
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfgDQLEKLLK 155
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1868034362   536 IDFKSSHRLLITGTP---LQNSLKELWSLLHFIMPEK 569
Cdd:smart00487  156 LLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
693-807 1.17e-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: 108.84  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  693 GKLILLDKLLTRlrERGNRVLIFSQMVRMLDilAEYLTIKH-YPFQRLDGSIKGEIRKQALDHFNadgSEDFCFLLSTRA 771
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1868034362  772 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIG 807
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1373-1455 4.78e-26

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: 103.49  E-value: 4.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1373 ICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYsDQEHIKLWRRNLWIFVSKFTE--FDARKL 1450
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFWPnkVSGKKL 88

                   ....*
gi 1868034362 1451 HKLYK 1455
Cdd:pfam13907   89 KEMYK 93
HELICc smart00490
helicase superfamily c-terminal domain;
723-807 4.66e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 4.66e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   723 DILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADgseDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQAR 802
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1868034362   803 AHRIG 807
Cdd:smart00490   78 AGRAG 82
DpdE NF041062
protein DpdE;
409-612 1.07e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 63.84  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  409 LADEMGLGKTIQTisflSYLFHQHQLYGP---FLIVVPLSTLTSWQRE----FeiwapeinvvvYIGDLMSRnTIReyew 481
Cdd:NF041062   175 LADEVGLGKTIEA----GLVIRQHLLDNPdarVLVLVPDALVRQWRRElrdkF-----------FLDDFPGA-RVR---- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  482 ihsqtkrlkfnalITTYEILLKDKTVLGSInwAFLGVDEAHRL-------KNDDSLLYKTLIDF-KSSHR-LLITGTPLQ 552
Cdd:NF041062   235 -------------VLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALaHAAPRlLLLSATPVL 299
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868034362  553 NSLKELWSLLHFIMPEKFEfWEDFE--EDHGKGREN---GYQSLHKVLEPFLLRRVKKDVEKSLP 612
Cdd:NF041062   300 GNEETFLALLHLLDPDLYP-LDDLEafRERLEEREElgrLVLGLDPDNPNFLLRQALDELRALFP 363
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
281-349 2.33e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.51  E-value: 2.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  281 IVERVIAVKTSKSTLGqtdfpahsrkpapsnepEYLCKWMGLPYSECSWEDEALIgKKFQNCIDSFHSR 349
Cdd:pfam00385    2 EVERILDHRKDKGGKE-----------------EYLVKWKGYPYDENTWEPEENL-SKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
202-248 8.24e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 50.29  E-value: 8.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1868034362   202 REEGETQYLIKWKSWSYIHSTWESEESLQQqkvkGLKKLENFKKKED 248
Cdd:smart00298   13 KKKGELEYLVKWKGYSYSEDTWEPEENLLN----CSKKLDNYKKKER 55
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
202-246 6.01e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 47.57  E-value: 6.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1868034362  202 REEGETQYLIKWKSWSYIHSTWESEESLQQQKvkglKKLENFKKK 246
Cdd:pfam00385   12 DKGGKEEYLVKWKGYPYDENTWEPEENLSKCP----ELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
282-351 9.19e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 47.21  E-value: 9.19e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   282 VERVIAVKTSKStlgqtdfpahsrkpapsNEPEYLCKWMGLPYSECSWEDEALIgKKFQNCIDSFHSRNN 351
Cdd:smart00298    4 VEKILDHRWKKK-----------------GELEYLVKWKGYSYSEDTWEPEENL-LNCSKKLDNYKKKER 55
 
Name Accession Description Interval E-value
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
366-602 0e+00

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: 547.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  366 RPRFVALKKQPAYLGGENLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLS 445
Cdd:cd18054      1 RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  446 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 525
Cdd:cd18054     81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  526 NDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd18054    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
370-923 1.20e-168

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 539.39  E-value: 1.20e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  370 VALKKQPAYLGGEnleLRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTS 449
Cdd:PLN03142   157 TRLLVQPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGN 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  450 WQREFEIWAPEINVVVYIGDLMSRNTIREYewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 529
Cdd:PLN03142   234 WMNEIRRFCPVLRAVKFHGNPEERAHQREE-----LLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  530 LLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLEPFLLRRVKK 605
Cdd:PLN03142   309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDqqevVQQLHKVLRPFLLRRLKS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  606 DVEKSLPAKVEQILRVEMSALQKQYYKWILTRNYKALAKGtrGSTSGFLNIVMELKKCCNHCYLIKAPEENERENGQEvl 685
Cdd:PLN03142   389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE-- 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  686 qSLIRSSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEDFCF 765
Cdd:PLN03142   465 -HLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVF 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  766 LLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKMVLDHLVIQRm 845
Cdd:PLN03142   544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ- 622
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  846 dttGRtVLENNSgrsnsnpFNKEELTAILKFGAEDLFkeiEGEESEPQEMDIDEILrlaetRENEVSTSATDELLSQF 923
Cdd:PLN03142   623 ---GR-LAEQKT-------VNKDELLQMVRYGAEMVF---SSKDSTITDEDIDRII-----AKGEEATAELDAKMKKF 681
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
385-602 1.71e-152

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: 465.29  E-value: 1.71e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  385 ELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVV 464
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRL 544
Cdd:cd17993     81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  545 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd17993    161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
367-602 8.66e-136

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: 420.61  E-value: 8.66e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  367 PRFVALKKQPAYLGG-ENLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLS 445
Cdd:cd18053      1 PRFVALKKQPSYIGGhEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  446 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 525
Cdd:cd18053     81 TLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  526 NDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd18053    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRR 237
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
361-841 1.30e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 413.08  E-value: 1.30e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  361 KALKQRPRFVALKKQPAYLGGEnleLRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLyGPFLI 440
Cdd:COG0553    220 DAFRLRRLREALESLPAGLKAT---LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLI 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  441 VVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEwihsqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDE 520
Cdd:COG0553    296 VAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDE 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  521 AHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG----YQSLHKVLE 596
Cdd:COG0553    367 AQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLR 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  597 PFLLRRVKKDVEKSLPAKVEQILRVEMSALQKQYYKwILTRNYKALAKGTRGSTSGF--LNIVMELKKCCNHCYLIKapE 674
Cdd:COG0553    447 PFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGliLAALTRLRQICSHPALLL--E 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  675 ENERENGQevlqslirsSGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDH 754
Cdd:COG0553    524 EGAELSGR---------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDR 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  755 FNADGSEDFcFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGTVEEEIIER-AKK 833
Cdd:COG0553    595 FQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELlEEK 673

                   ....*...
gi 1868034362  834 KMVLDHLV 841
Cdd:COG0553    674 RALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-670 2.08e-109

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: 349.67  E-value: 2.08e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  389 YQLEGLNWLAHSWCKS-NSVILADEMGLGKTIQTISFLSYLFHQHQLYG-PFLIVVPLSTLTSWQREFEIWA--PEINVV 464
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGDLMSRNtireyEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRL 544
Cdd:pfam00176   81 VLHGNKRPQE-----RWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  545 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-----GRENGYQSLHKVLEPFLLRRVKKDVEKSLPAKVEQIL 619
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  620 RVEMSALQKQYYK-WILTRNYKALAKGTRGST--SGFLNIVMELKKCCNHCYLI 670
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
386-602 1.04e-89

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: 291.07  E-value: 1.04e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPeINVVV 465
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQTKRL------KFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd17995     80 YHGSGESRQIIQQYEMYFKDAQGRkkkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-YQSLHKVLEPFLLRR 602
Cdd:cd17995    160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEqVEKLQALLKPYMLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
386-567 7.79e-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: 260.96  E-value: 7.79e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWihsqtkRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLL 545
Cdd:cd17919     81 YHGSQRERAQIRAKEK------LDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                          170       180
                   ....*....|....*....|..
gi 1868034362  546 ITGTPLQNSLKELWSLLHFIMP 567
Cdd:cd17919    155 LTGTPLQNNLEELWALLDFLDP 176
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
385-604 1.04e-79

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 262.26  E-value: 1.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  385 ELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVV 464
Cdd:cd17997      3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGDLMSRNTIreyewIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRL 544
Cdd:cd17997     83 VLIGDKEERADI-----IRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRL 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868034362  545 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-----DHGKGRENGYQSLHKVLEPFLLRRVK 604
Cdd:cd17997    158 LLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEwfnvnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
386-604 2.97e-74

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 247.30  E-value: 2.97e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLR-ERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQTKRlKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLL 545
Cdd:cd18009     83 YHGTKEERERLRKKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868034362  546 ITGTPLQNSLKELWSLLHFIMPE------KFEFW----------EDFEEDHGKGRENGYQSLHKVLEPFLLRRVK 604
Cdd:cd18009    162 LTGTPLQNNLSELWSLLNFLLPDvfddlsSFESWfdfsslsdnaADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
383-604 6.61e-74

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: 246.13  E-value: 6.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  383 NLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEIN 462
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  463 VVVYIGDLMSRNTIreyewiHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLID-FKSS 541
Cdd:cd17996     81 KIVYKGTPDVRKKL------QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHAR 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  542 HRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE------DHGKGRENGY----------QSLHKVLEPFLLRRVK 604
Cdd:cd17996    155 YRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQwfntpfANTGEQVKIElneeetlliiRRLHKVLRPFLLRRLK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
386-602 6.41e-72

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 238.88  E-value: 6.41e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDlmsrntireyewihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLL 545
Cdd:cd17994     81 YVGD----------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  546 ITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-GRENGYQSLHKVLEPFLLRR 602
Cdd:cd17994    139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADiSKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
386-602 2.61e-70

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: 235.02  E-value: 2.61e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLL 545
Cdd:cd18006     81 YMGDKEKRLDLQQ-----DIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  546 ITGTPLQNSLKELWSLLHFIMPEKF--EFWEDF---EEDHGKGRENgYQSLHKVLEPFLLRR 602
Cdd:cd18006    156 LTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFikaYSETDDESET-VEELHLLLQPFLLRR 216
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
386-602 6.83e-68

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: 228.39  E-value: 6.83e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREyEWihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLL 545
Cdd:cd18003     81 YYGSAKERKLKRQ-GW----MKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  546 ITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-------KGRENGYQS----LHKVLEPFLLRR 602
Cdd:cd18003    156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpltamsEGSQEENEElvrrLHKVLRPFLLRR 223
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
386-602 2.09e-65

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: 221.81  E-value: 2.09e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQT--------------KRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 531
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNavkggkkafkmkreAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  532 YKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-GRENGYQSLHKVLEPFLLRR 602
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
386-602 1.12e-63

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: 216.85  E-value: 1.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEW------IHSQTK--------RLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 531
Cdd:cd18057     81 YTGDKESRSVIRENEFsfednaIRSGKKvfrmkkeaQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  532 YKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-GRENGYQSLHKVLEPFLLRR 602
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
386-602 2.32e-62

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: 213.00  E-value: 2.32e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIH-----------SQTKR---LKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 531
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFednairggkkaSRMKKeasVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  532 YKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-GRENGYQSLHKVLEPFLLRR 602
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADiAKEDQIKKLHDMLGPHMLRR 232
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
386-602 3.46e-62

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: 212.36  E-value: 3.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYeW--IHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHR 543
Cdd:cd18002     81 YWGNPKDRKVLRKF-WdrKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  544 LLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQS-----------LHKVLEPFLLRR 602
Cdd:cd18002    160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENktglnehqlkrLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
385-614 1.91e-60

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: 207.98  E-value: 1.91e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  385 ELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVV 464
Cdd:cd18064     15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGD-----LMSRNTIREYEWihsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd18064     95 CLIGDkdqraAFVRDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLLRRVKKDVEKSLPAK 614
Cdd:cd18064    165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdtNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
386-602 2.02e-60

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: 206.82  E-value: 2.02e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQhQLYGPFLIVVPLSTLTSWQREFEIWApEINVVV 465
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLM-GIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQTK------RLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd18058     79 YHGSQISRQMIQQYEMYYRDEQgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 602
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKtEEQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
386-602 8.87e-60

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: 205.29  E-value: 8.87e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQhQLYGPFLIVVPLSTLTSWQREFEIWApEINVVV 465
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQTK-RL-----KFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd18060     79 YHGSLASRQMIQQYEMYCKDSRgRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 602
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKPMMLRR 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
692-818 2.28e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.62  E-value: 2.28e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  692 SGKLILLDKLLTRLRERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADgSEDFCFLLSTRA 771
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1868034362  772 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLV 818
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
370-604 6.74e-57

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: 197.16  E-value: 6.74e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  370 VALKKQPAYLGGENLelRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTS 449
Cdd:cd18065      2 VRFEESPSYVKGGTL--RDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  450 WQREFEIWAPEINVVVYIGDLMSRNTireyeWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDS 529
Cdd:cd18065     80 WMNEFKRWVPSLRAVCLIGDKDARAA-----FIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKS 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  530 LLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE----DHGKGRENGYQSLHKVLEPFLLRRVK 604
Cdd:cd18065    155 KLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
386-570 7.83e-57

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 195.30  E-value: 7.83e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEwihsQTKRLKFNALITTYEILL---KDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSH 542
Cdd:cd17998     80 YYGSQEERKHLRYDI----LKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANF 155
                          170       180
                   ....*....|....*....|....*...
gi 1868034362  543 RLLITGTPLQNSLKELWSLLHFIMPEKF 570
Cdd:cd17998    156 RLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
386-602 1.97e-56

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: 195.64  E-value: 1.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLsYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWApEINVVV 465
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYEWIHSQTK------RLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd18059     79 YHGSQASRRTIQLYEMYFKDPQgrvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 602
Cdd:cd18059    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKtEEQVQKLQAILKPMMLRR 222
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
385-604 5.05e-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: 191.24  E-value: 5.05e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  385 ELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLyGPFLIVVPLSTLTSWQREFEIWAPEINVV 464
Cdd:cd18012      4 TLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRK-GPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  465 VYIGDLMSRNTIREYEwihsqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRL 544
Cdd:cd18012     83 VIHGTKRKREKLRALE---------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRL 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  545 LITGTPLQNSLKELWSLLHFIMP------EKF-EFWEDFEEDHgkGRENGYQSLHKVLEPFLLRRVK 604
Cdd:cd18012    154 ALTGTPIENHLGELWSIFDFLNPgllgsyKRFkKRFAKPIEKD--GDEEALEELKKLISPFILRRLK 218
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
386-602 9.63e-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: 9.63e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLsYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWApEINVVV 465
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGDLMSRNTIREYE-WIHSQTKRL-----KFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 539
Cdd:cd18061     79 YHGSLISRQMIQQYEmYFRDSQGRIirgayRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  540 SSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 602
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
383-604 1.05e-52

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: 186.02  E-value: 1.05e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  383 NLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEIN 462
Cdd:cd18062     21 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  463 VVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSS 541
Cdd:cd18062    101 KVSYKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAP 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  542 HRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFE-----------EDHGKGRENGY---QSLHKVLEPFLLRRVK 604
Cdd:cd18062    175 RRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgEKVDLNEEETIliiRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
372-604 2.21e-52

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: 184.88  E-value: 2.21e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  372 LKKQPAYLggENLELRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQ 451
Cdd:cd18063     12 VEKQSSLL--INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  452 REFEIWAPEINVVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 531
Cdd:cd18063     90 YEFDKWAPSVVKISYKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  532 YKTL-IDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFE-----------EDHGKGRENGY---QSLHKVLE 596
Cdd:cd18063    164 TQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgERVDLNEEETIliiRRLHKVLR 243

                   ....*...
gi 1868034362  597 PFLLRRVK 604
Cdd:cd18063    244 PFLLRRLK 251
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
161-245 3.36e-46

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: 160.53  E-value: 3.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  161 NSETIEKVLDSRLGKKGATGASTTVYAVEANGDPSGDFDTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKVKGLKKL 240
Cdd:cd18666      1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                   ....*
gi 1868034362  241 ENFKK 245
Cdd:cd18666     81 ENYKK 85
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
386-567 4.97e-46

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: 164.42  E-value: 4.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 Y---IGDLMSRNTIREYEWIHSQTKRLKFNA--LITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKS 540
Cdd:cd18000     81 LhssGSGTGSEEKLGSIERKSQLIRKVVGDGgiLITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                          170       180
                   ....*....|....*....|....*..
gi 1868034362  541 SHRLLITGTPLQNSLKELWSLLHFIMP 567
Cdd:cd18000    161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
386-602 2.50e-45

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: 164.08  E-value: 2.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQhQLYGPFLIVVPLSTLTSWQREFEIWAPEINVVV 465
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDS-GLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  466 YIGdlmSRNTIREY--EWIHSqtkrlKFNALITTYEILLKDKTVLGSIN-----WAFLGVDEAHRLKNDDSLLYKTLIDF 538
Cdd:cd18001     80 FHG---TSKKERERnlERIQR-----GGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  539 KSSHRLLITGTPLQNSLKELWSLLHFIMP-----EKFEFWEDFEEDHGKGRENG------------YQSLHKVLEPFLLR 601
Cdd:cd18001    152 PAKNRIILTGTPIQNNLKELWALFDFACNgsllgTRKTFKMEFENPITRGRDKDatqgekalgsevAENLRQIIKPYFLR 231

                   .
gi 1868034362  602 R 602
Cdd:cd18001    232 R 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
386-602 2.61e-43

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: 158.70  E-value: 2.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQ--------------------HQLYGPFLIVVPLS 445
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppaSSAKKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  446 TLTSWQREFEIWApEINVVVYIG-----DLMSRNTIREYEwihsqtkrlkfnALITTYEILLKDKTVLGSINWAFLGVDE 520
Cdd:cd18005     81 VLYNWKDELDTWG-HFEVGVYHGsrkddELEGRLKAGRLE------------VVVTTYDTLRRCIDSLNSINWSAVIADE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  521 AHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF-----------------EEDHGKG 583
Cdd:cd18005    148 AHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFkkhfsepikrgqrhtatARELRLG 227
                          250
                   ....*....|....*....
gi 1868034362  584 RENGyQSLHKVLEPFLLRR 602
Cdd:cd18005    228 RKRK-QELAVKLSKFFLRR 245
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
386-602 3.37e-42

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 154.82  E-value: 3.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLA-------HSwcksnsvILADEMGLGKTIQTISFLSYLFHQHQLYG-----PFLIVVPlSTLTS-WQR 452
Cdd:cd17999      1 LRPYQQEGINWLAflnkynlHG-------ILCDDMGLGKTLQTLCILASDHHKRANSFnsenlPSLVVCP-PTLVGhWVA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  453 EFEIWAPE--INVVVYIGDLMSRNTIREyewihsqtKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSL 530
Cdd:cd17999     73 EIKKYFPNafLKPLAYVGPPQERRRLRE--------QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  531 LYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMP-----EKfEFWEDF---------EEDHGKGRENGYQS---LHK 593
Cdd:cd17999    145 LSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPgylgtEK-QFQRRFlkpilasrdSKASAKEQEAGALAleaLHK 223

                   ....*....
gi 1868034362  594 VLEPFLLRR 602
Cdd:cd17999    224 QVLPFLLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
386-602 3.85e-38

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: 143.58  E-value: 3.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLahswcKSNSVILADEMGLGKTIQTIS---------------FLSYLFHQHQLY--GPFLIVVPLSTLT 448
Cdd:cd18008      1 LLPYQKQGLAWM-----LPRGGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYlsKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  449 SWQREFE--IWAPEINVVVYIGdlmSRNTIREYEWihsqtkrLKFNALITTYEILLKD----------------KTVLGS 510
Cdd:cd18008     76 QWKDEIEkhTKPGSLKVYVYHG---SKRIKSIEEL-------SDYDIVITTYGTLASEfpknkkgggrdskekeASPLHR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  511 INWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEED----HGKGREN 586
Cdd:cd18008    146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDiskpFSKNDRK 225
                          250
                   ....*....|....*.
gi 1868034362  587 GYQSLHKVLEPFLLRR 602
Cdd:cd18008    226 ALERLQALLKPILLRR 241
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1032-1120 1.35e-36

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: 133.63  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1032 GFTDAEIRRFIKAYKKFGLPLERLECIARDAELVDKSVADLKRLGELIHNSCASAMQEYEEQLKENASEGKGPGKRRGPT 1111
Cdd:pfam18375    2 GFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKRIRGPS 81

                   ....*....
gi 1868034362 1112 IKISGVQVN 1120
Cdd:pfam18375   82 FKLGGVSVN 90
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
386-602 2.08e-34

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: 132.79  E-value: 2.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWL-----AHSWCKSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGP----FLIVVPLSTLTSWQREFEI 456
Cdd:cd18004      1 LRPHQREGVQFLydcltGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  457 WAPEINVVVYIgdlMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGS-INWAFLGVDEAHRLKNDDSLLYKTL 535
Cdd:cd18004     81 WLGLRRIKVVT---ADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  536 IDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKF----EFWEDFEEDHGKGRENGY------------QSLHKVLEPFL 599
Cdd:cd18004    158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILgslaSFRKVFEEPILRSRDPDAseedkelgaersQELSELTSRFI 237

                   ...
gi 1868034362  600 LRR 602
Cdd:cd18004    238 LRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
386-576 4.57e-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: 131.64  E-value: 4.57e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLN--W--LAHSWCKSNS---VILADEMGLGKTIQTISFLsylfHQHQLYGP----FLIVVPLSTLTSWQREF 454
Cdd:cd18007      1 LKPHQVEGVRflWsnLVGTDVGSDEgggCILAHTMGLGKTLQVITFL----HTYLAAAPrrsrPLVLCPASTLYNWEDEF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  455 EIWAPEINVVVYIGDLMSRntireyewIHSQTKRL-KFNA-------LITTYEI---LLKDKTVLGSINWAF-------- 515
Cdd:cd18007     77 KKWLPPDLRPLLVLVSLSA--------SKRADARLrKINKwhkeggvLLIGYELfrnLASNATTDPRLKQEFiaalldpg 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1868034362  516 ---LGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF 576
Cdd:cd18007    149 pdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
278-349 2.40e-30

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: 114.32  E-value: 2.40e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  278 QYQIVERVIAVKTSKStlgqtdfpahsrkpAPSNEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSR 349
Cdd:cd18661      1 QYQIVERIIAHSPQKS--------------AASGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
DEXDc smart00487
DEAD-like helicases superfamily;
384-569 7.20e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.36  E-value: 7.20e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   384 LELRDYQLEGLNWLAHSWcksNSVILADEMGLGKTIQTISFLSYLFHQHQlYGPFLIVVPLSTLT-SWQREFEIWAPE-- 460
Cdd:smart00487    7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAeQWAEELKKLGPSlg 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   461 INVVVYIGDLMSRNTIREYewihsqtKRLKFNALITTYEILLKD--KTVLGSINWAFLGVDEAHRLKND---DSLLYKTL 535
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKL-------ESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfgDQLEKLLK 155
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1868034362   536 IDFKSSHRLLITGTP---LQNSLKELWSLLHFIMPEK 569
Cdd:smart00487  156 LLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
386-602 1.04e-28

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: 116.42  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHswC-------KSNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFL----IVVPLSTLTSWQREF 454
Cdd:cd18067      1 LRPHQREGVKFLYR--CvtgrrirGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  455 EIW-APEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYK 533
Cdd:cd18067     79 GKWlGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  534 TLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPE----KFEFWEDFEEDHGKGR------------ENGYQSLHKVLEP 597
Cdd:cd18067    159 ALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGilgtAAEFKKNFELPILKGRdadasekerqlgEEKLQELISIVNR 238

                   ....*
gi 1868034362  598 FLLRR 602
Cdd:cd18067    239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
386-576 4.82e-28

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 113.45  E-value: 4.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNW-LAHSwcksNSVILADEMGLGKTIQTISFLSYLFHqhqlYGPFLIVVPLSTLTSWQREFEIWAP----- 459
Cdd:cd18010      1 LLPFQREGVCFaLRRG----GRVLIADEMGLGKTVQAIAIAAYYRE----EWPLLIVCPSSLRLTWADEIERWLPslppd 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  460 EINVVVyigdlMSRNTIReyewiHSQTKrlkfnALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF- 538
Cdd:cd18010     73 DIQVIV-----KSKDGLR-----DGDAK-----VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLl 137
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1868034362  539 -KSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF 576
Cdd:cd18010    138 kRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
693-807 1.17e-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: 108.84  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  693 GKLILLDKLLTRlrERGNRVLIFSQMVRMLDilAEYLTIKH-YPFQRLDGSIKGEIRKQALDHFNadgSEDFCFLLSTRA 771
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1868034362  772 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIG 807
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
408-602 1.25e-27

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: 113.33  E-value: 1.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  408 ILADEMGLGKTIQTISFLsylfhqhqLYGPFLIVVPLSTLTSWQREFE--IWAPEINVVVYIGDlmsrntireyEWIHSQ 485
Cdd:cd18071     52 ILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEehVKPGQLKVYTYHGG----------ERNRDP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  486 TKRLKFNALITTYEILL-----KDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWS 560
Cdd:cd18071    114 KLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1868034362  561 LLHFIMPEKF---EFWED-FEEDHGKGRENGYQSLHKVLEPFLLRR 602
Cdd:cd18071    194 LLSFLHLKPFsnpEYWRRlIQRPLTMGDPTGLKRLQVLMKQITLRR 239
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1373-1455 4.78e-26

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: 103.49  E-value: 4.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362 1373 ICKERMRPVKKALKQLDKPDKGLNVQEQLEHTRNCLLKIGDRIAECLKAYsDQEHIKLWRRNLWIFVSKFTE--FDARKL 1450
Cdd:pfam13907   10 ECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFWPnkVSGKKL 88

                   ....*
gi 1868034362 1451 HKLYK 1455
Cdd:pfam13907   89 KEMYK 93
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
386-567 2.79e-24

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: 103.39  E-value: 2.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKSNSV-----ILADEMGLGKTIQTISFLSYLFHQHQlYGP------FLIVVPLSTLTSWQREF 454
Cdd:cd18066      1 LRPHQREGIEFLYECVMGMRVNerfgaILADEMGLGKTLQCISLIWTLLRQGP-YGGkpvikrALIVTPGSLVKNWKKEF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  455 EIWAPEINVVVYIGDlmSRNTIREYewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKT 534
Cdd:cd18066     80 QKWLGSERIKVFTVD--QDHKVEEF------IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTA 151
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1868034362  535 LIDFKSSHRLLITGTPLQNSLKELWSLLHFIMP 567
Cdd:cd18066    152 LTSLSCERRIILTGTPIQNDLQEFFALIDFVNP 184
HELICc smart00490
helicase superfamily c-terminal domain;
723-807 4.66e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 4.66e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   723 DILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADgseDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQAR 802
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1868034362   803 AHRIG 807
Cdd:smart00490   78 AGRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
386-602 4.38e-20

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: 90.43  E-value: 4.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNW-LAHswcKSNSVILADEMGLGKTIQTISFLSYLFHQHqLYGPFLIVVPLSTLTSWQRE----FEIWAPe 460
Cdd:cd18011      1 PLPHQIDAVLRaLRK---PPVRLLLADEVGLGKTIEAGLIIKELLLRG-DAKRVLILCPASLVEQWQDElqdkFGLPFL- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  461 invvvyigdLMSRNTIREYEWIHSQTKRLkFNALITTYEiLLKDKT----VLGSINWAFLGVDEAHRLKN----DDSLLY 532
Cdd:cd18011     76 ---------ILDRETAAQLRRLIGNPFEE-FPIVIVSLD-LLKRSEerrgLLLSEEWDLVVVDEAHKLRNsgggKETKRY 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1868034362  533 KT---LIDfKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGkgrengyqsLHKVLEPFLLRR 602
Cdd:cd18011    145 KLgrlLAK-RARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRLDG---------LREVLAKVLLRR 207
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
386-567 1.26e-19

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: 90.33  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSWCKS---------NSVILADEMGLGKTIQTISFLSYLFHQHQLYG--PFLIVVPLSTLTSWQREF 454
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  455 EIWapeinvvvyIGDLMSRNTIREYE---WIHSQTKRLKFN-------ALITTYE---ILLKDKTV-------------L 508
Cdd:cd18068     81 EKW---------QEGLKDEEKIEVNElatYKRPQERSYKLQrwqeeggVMIIGYDmyrILAQERNVksreklkeifnkaL 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  509 GSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMP 567
Cdd:cd18068    152 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKP 210
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
408-577 4.54e-19

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 87.95  E-value: 4.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  408 ILADEMGLGKTIQTISFLsYLFHQHQLYGPFLIVVPLSTLTSWQREFEIWAPEinvvvYIGDLMSRNTIREYEWIHSQTK 487
Cdd:cd18069     32 ILAHSMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPP-----PEALPNVRPRPFKVFILNDEHK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  488 RLKFNA-LITTYEillKDKTVL--GSINWAF------LGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKEL 558
Cdd:cd18069    106 TTAARAkVIEDWV---KDGGVLlmGYEMFRLrpgpdvVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEY 182
                          170       180
                   ....*....|....*....|...
gi 1868034362  559 WSLLHFIMPE----KFEFWEDFE 577
Cdd:cd18069    183 WCMVDFVRPDflgtRQEFSNMFE 205
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
161-245 2.91e-17

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: 77.79  E-value: 2.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  161 NSETIEKVLDSRLGKKGATgasttvyaveangDPSGDFDTEREEGETQYLIKWKSWSYIHSTWESEESLQQQkvKGLKKL 240
Cdd:cd18660      1 DEDKIEKILDHRPKGPVEE-------------ASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL--RGKKKL 65

                   ....*
gi 1868034362  241 ENFKK 245
Cdd:cd18660     66 KNYIK 70
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
278-348 1.87e-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: 74.92  E-value: 1.87e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1868034362  278 QYQIVERVIAVKTSKSTlgqtdfpahsrkpapsnEPEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHS 348
Cdd:cd18659      1 EYTIVERIIAHREDDEG-----------------VTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
386-602 1.84e-15

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: 77.91  E-value: 1.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLahSWCKSNSV---ILADEMGLGKTIQTISFLSYLFHQHQL----------------------YGPFLI 440
Cdd:cd18072      1 LLLHQKQALAWL--LWRERQKPrggILADDMGLGKTLTMIALILAQKNTQNRkeeekekalteweskkdstlvpSAGTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  441 VVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYewihsqtkRLKFNALITTYEILLKD---------KTVLGSI 511
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEV--------LRDYDIVITTYSLVAKEiptykeesrSSPLFRI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  512 NWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSL 591
Cdd:cd18072    151 AWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGERL 230
                          250
                   ....*....|.
gi 1868034362  592 HKVLEPFLLRR 602
Cdd:cd18072    231 NILTKSLLLRR 241
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
386-601 1.03e-12

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 70.07  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNWLAHSwcksnSVILADEMGLGKTIQTISFLsyLFHQHQL---------------------------YGPF 438
Cdd:cd18070      1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPDndldaadddsdemvccpdclvaetpvsSKAT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  439 LIVVPLSTLTSWQREFEIWAPE-INVVVYIGdlmsrntIREYEWIHSQT-KRL-KFNALITTYEILLKD----------- 504
Cdd:cd18070     74 LIVCPSAILAQWLDEINRHVPSsLKVLTYQG-------VKKDGALASPApEILaEYDIVVTTYDVLRTElhyaeanrsnr 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  505 -----------KTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSSHRLLITGTPLQNSLKELWSLLHFIMPEKF--E 571
Cdd:cd18070    147 rrrrqkryeapPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFcdS 226
                          250       260       270
                   ....*....|....*....|....*....|
gi 1868034362  572 FWEDFEEDHGKGRENGYQSLHKVLEPFLLR 601
Cdd:cd18070    227 DWWARVLIRPQGRNKAREPLAALLKELLWR 256
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
381-923 1.31e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 72.75  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  381 GENLELRDYQLEGLN-WLAHSWCKSNSVILADEMGLGKTIqtisFLSYLFHQHQLYGPFLIVVPLSTL-TSWQREFEIWA 458
Cdd:COG1061     76 GTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRGKRVLVLVPRRELlEQWAEELRRFL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  459 PEINVvvyigdlmsrntireyewiHSQTKRLKFNALITTYEILLKDKTV--LGSiNWAFLGVDEAHRLKnddSLLYKTLI 536
Cdd:COG1061    152 GDPLA-------------------GGGKKDSDAPITVATYQSLARRAHLdeLGD-RFGLVIIDEAHHAG---APSYRRIL 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  537 D-FKSSHRLLITGTPlqNSLKELWSLLHFIMPEKFEF-WEDFEEDhgkgrengyqslhKVLEPFLLRRVkkdvekslpak 614
Cdd:COG1061    209 EaFPAAYRLGLTATP--FRSDGREILLFLFDGIVYEYsLKEAIED-------------GYLAPPEYYGI----------- 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  615 veqilRVEMSALQKQYYKwILTRNYKALAKGTRgstsgflnivmelkkccnhcylikapeenerengqevlqslirssGK 694
Cdd:COG1061    263 -----RVDLTDERAEYDA-LSERLREALAADAE---------------------------------------------RK 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  695 LILLDKLLTRLRERGnRVLIFSQMVRMLDILAEYLTIKHYPFQRLDGSIKGEIRKQALDHFNADGSEdfcFLLSTRAGGL 774
Cdd:COG1061    292 DKILRELLREHPDDR-KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR---ILVTVDVLNE 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  775 GINLASADTVVIFDSDWNPQNDLQAQARAHRIGQ-KKQVNIYRLVTKGTVEEEIIERAKKKMVLDHlvIQRMDTTGRTVL 853
Cdd:COG1061    368 GVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYR--VEFLDEEESEEL 445
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  854 ENNSGRSNSNPFNKEELTAILKFGAEDLFKEIEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQF 923
Cdd:COG1061    446 ALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELL 515
ResIII pfam04851
Type III restriction enzyme, res subunit;
383-550 5.32e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 62.69  E-value: 5.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  383 NLELRDYQLEGL-NWLAHSWCKSNSVILADEMGLGKTIqTISFLSYLFHQHQLYGPFLIVVP-LSTLTSWQREFEIWAPe 460
Cdd:pfam04851    1 KLELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTL-TAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLP- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  461 iNVVVYIGDLMSRNTIREYewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLkNDDSllYKTLID-FK 539
Cdd:pfam04851   79 -NYVEIGEIISGDKKDESV-----DDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRS-GASS--YRNILEyFK 149
                          170
                   ....*....|.
gi 1868034362  540 SSHRLLITGTP 550
Cdd:pfam04851  150 PAFLLGLTATP 160
DpdE NF041062
protein DpdE;
409-612 1.07e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 63.84  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  409 LADEMGLGKTIQTisflSYLFHQHQLYGP---FLIVVPLSTLTSWQRE----FeiwapeinvvvYIGDLMSRnTIReyew 481
Cdd:NF041062   175 LADEVGLGKTIEA----GLVIRQHLLDNPdarVLVLVPDALVRQWRRElrdkF-----------FLDDFPGA-RVR---- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  482 ihsqtkrlkfnalITTYEILLKDKTVLGSInwAFLGVDEAHRL-------KNDDSLLYKTLIDF-KSSHR-LLITGTPLQ 552
Cdd:NF041062   235 -------------VLSHEEPERWEPLLDAP--DLLVVDEAHQLarlawsgDPPERARYRELAALaHAAPRlLLLSATPVL 299
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1868034362  553 NSLKELWSLLHFIMPEKFEfWEDFE--EDHGKGREN---GYQSLHKVLEPFLLRRVKKDVEKSLP 612
Cdd:NF041062   300 GNEETFLALLHLLDPDLYP-LDDLEafRERLEEREElgrLVLGLDPDNPNFLLRQALDELRALFP 363
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
281-349 2.33e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.51  E-value: 2.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868034362  281 IVERVIAVKTSKSTLGqtdfpahsrkpapsnepEYLCKWMGLPYSECSWEDEALIgKKFQNCIDSFHSR 349
Cdd:pfam00385    2 EVERILDHRKDKGGKE-----------------EYLVKWKGYPYDENTWEPEENL-SKCPELIEEFKDR 52
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
386-565 2.71e-09

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: 59.29  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGLNW-LAHSWCKsnsvILADeMGLGKTIQTISFLSYLFHQhQLYGPFLIVVPLSTLTS-WQREFEIWAPEINV 463
Cdd:cd18013      1 PHPYQKVAINFiIEHPYCG----LFLD-MGLGKTVTTLTALSDLQLD-DFTRRVLVIAPLRVARStWPDEVEKWNHLRNL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  464 VVYIGDlmsrNTIREyewihsQTKRLKFNALITTYEI-LLKDKTVLGSINWAFLGV--DEAHRLKNDDSLLYKTLidfkS 540
Cdd:cd18013     75 TVSVAV----GTERQ------RSKAANTPADLYVINReNLKWLVNKSGDPWPFDMVviDELSSFKSPRSKRFKAL----R 140
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1868034362  541 SHRLLI------TGTPLQNSLKELWSLLHFI 565
Cdd:cd18013    141 KVRPVIkrliglTGTPSPNGLMDLWAQIALL 171
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
191-245 1.82e-08

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: 52.39  E-value: 1.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1868034362  191 NGDPSGDFDTEREEgeTQYLIKWKSWSYIHSTWESEESLQQqkVKGLKKLENFKK 245
Cdd:cd18665     15 EGLEEGELDDPKEN--YEFLIKWTDESHLHNTWETYESLKQ--VRGLKKVDNYIK 65
CHROMO smart00298
Chromatin organization modifier domain;
202-248 8.24e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 50.29  E-value: 8.24e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1868034362   202 REEGETQYLIKWKSWSYIHSTWESEESLQQqkvkGLKKLENFKKKED 248
Cdd:smart00298   13 KKKGELEYLVKWKGYSYSEDTWEPEENLLN----CSKKLDNYKKKER 55
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
695-922 1.40e-07

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.66  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  695 LILLDKLLTRlrERGNRVLIFSQMVRMLDILAEYLTIKHYPFQRL-----DGSIKGEIRKQ---ALDHFNAdgsEDFCFL 766
Cdd:COG1111    341 REILKEQLGT--NPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqasKEGDKGLTQKEqieILERFRA---GEFNVL 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  767 LSTRAGGLGINLASADTVVIFDSDWNPQNDLQaqaRAHRIGQKKQVNIYRLVTKGTVEEEIIERAKKKmvldhlvIQRMD 846
Cdd:COG1111    416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEAYYWSSRRK-------EKKMK 485
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  847 TTGRTV--LENNSGRSNSNPFNKEELTAILKFGAEDLFKEIEGEESEPQEMDIDEILRLAETRENEVSTSATDELLSQ 922
Cdd:COG1111    486 SILKKLkkLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLEL 563
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
202-246 6.01e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 47.57  E-value: 6.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1868034362  202 REEGETQYLIKWKSWSYIHSTWESEESLQQQKvkglKKLENFKKK 246
Cdd:pfam00385   12 DKGGKEEYLVKWKGYPYDENTWEPEENLSKCP----ELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
282-351 9.19e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 47.21  E-value: 9.19e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362   282 VERVIAVKTSKStlgqtdfpahsrkpapsNEPEYLCKWMGLPYSECSWEDEALIgKKFQNCIDSFHSRNN 351
Cdd:smart00298    4 VEKILDHRWKKK-----------------GELEYLVKWKGYSYSEDTWEPEENL-LNCSKKLDNYKKKER 55
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
278-349 1.21e-06

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: 47.27  E-value: 1.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1868034362  278 QYQIVERVIAVKTSKSTLGQTDFpahsrkpapsnepEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFHSR 349
Cdd:cd18664      1 EFHVVERIIASQRASLEDGTSQL-------------QYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
386-550 1.31e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 49.61  E-value: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  386 LRDYQLEGL-NWLAHSWCKSNSVILAdeMGLGKTIQTISFLSYLFHQhqlygPFLIVVP-LSTLTSWQREFEIWAPEINV 463
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKEL-----RTLIVVPtDALLDQWKERFEDFLGDSSI 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  464 -VVYIGDLMSRNTIreyewihsqtkrlkfNALITTYEILLKDKTVLGSI--NWAFLGVDEAHRLkndDSLLYKTLID-FK 539
Cdd:cd17926     74 gLIGGGKKKDFDDA---------------NVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILKeLN 135
                          170
                   ....*....|.
gi 1868034362  540 SSHRLLITGTP 550
Cdd:cd17926    136 AKYRLGLTATP 146
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
201-232 1.67e-06

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: 46.41  E-value: 1.67e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1868034362  201 EREEGETQYLIKWKSWSYIHSTWESEESLQQQ 232
Cdd:cd18659     13 EDDEGVTEYLVKWKGLPYDECTWESEEDISDI 44
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
711-810 7.04e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.39  E-value: 7.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  711 RVLIFSQMVRMLDILAEYLTIkhypfqrldgsikgeirkqaldhfnadgsedfcfLLSTRAGGLGINLASADTVVIFDSD 790
Cdd:cd18785      5 KIIVFTNSIEHAEEIASSLEI----------------------------------LVATNVLGEGIDVPSLDTVIFFDPP 50
                           90       100
                   ....*....|....*....|
gi 1868034362  791 WNPQNDLQAQARAHRIGQKK 810
Cdd:cd18785     51 SSAASYIQRVGRAGRGGKDE 70
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
160-235 2.44e-05

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 43.86  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  160 DNSETIEKVLDSRlgkkgatgasttvyaVEANGDPSGDFDTEREEgetqYLIKWKSWSYIHSTWESEESLQ------QQK 233
Cdd:cd18668      2 EDTMIIEKILASR---------------KKKKEKEEGAEEIEVEE----YLVKYKNFSYLHCEWKTEEELEkgdkriKQK 62

                   ..
gi 1868034362  234 VK 235
Cdd:cd18668     63 IK 64
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
407-549 8.28e-05

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 44.32  E-value: 8.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868034362  407 VILADEMGLGKTIQ-TISFLSYLFHQHqlyGPFLIVVPLSTLT-SWQREFEIWAPEINVVVYIGDLMS-----RNTIREY 479
Cdd:cd00046      4 VLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALAlQTAERLRELFGPGIRVAVLVGGSSaeereKNKLGDA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868034362  480 EWIhsqtkrlkfnalITTYEILLKDKTVLGSI---NWAFLGVDEAHR-LKNDDSLLYKTLID----FKSSHRLLITGT 549
Cdd:cd00046     81 DII------------IATPDMLLNLLLREDRLflkDLKLIIVDEAHAlLIDSRGALILDLAVrkagLKNAQVILLSAT 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
199-231 8.88e-05

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: 41.69  E-value: 8.88e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1868034362  199 DTEREEGETQYLIKWKSWSYIHSTWESEESLQQ 231
Cdd:cd00024      8 DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTN 40
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
305-347 1.99e-04

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: 40.71  E-value: 1.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1868034362  305 RKPAPSNEpEYLCKWMGLPYSECSWEDEALIGKKFQNCIDSFH 347
Cdd:cd18662     13 RVDKDGNT-WYLVKWRDLPYDQSTWESEDDDIPDYEKHIQEYW 54
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
185-247 2.28e-04

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: 40.53  E-value: 2.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1868034362  185 VYAVEANgdpsgdFDTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKVkglkkLENFKKKE 247
Cdd:cd18644      3 VYAAEKI------LKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILDRRL-----IEIFERTN 54
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
199-241 4.85e-04

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: 39.96  E-value: 4.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1868034362  199 DTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKVKGLKKLE 241
Cdd:cd18663     17 DPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
203-228 4.91e-04

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: 39.56  E-value: 4.91e-04
                           10        20
                   ....*....|....*....|....*.
gi 1868034362  203 EEGETQYLIKWKSWSYIHSTWESEES 228
Cdd:cd18662     16 KDGNTWYLVKWRDLPYDQSTWESEDD 41
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
279-333 6.91e-04

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: 39.19  E-value: 6.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868034362  279 YQIVERVIAVKTSKStlgqtdfpahsrkpAPSNEP--EYLCKWMGLPYSECSWEDEA 333
Cdd:cd18663      3 YVEVDRILDVSVSTD--------------PNTGEPvtHYLVKWCSLPYEDSTWELEE 45
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
205-229 1.15e-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: 38.53  E-value: 1.15e-03
                           10        20
                   ....*....|....*....|....*
gi 1868034362  205 GETQYLIKWKSWSYIHSTWESEESL 229
Cdd:cd18627     14 GKVEYLVKWKGWSQKYNTWEPEENI 38
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
204-229 1.73e-03

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component 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: 349294  Cd Length: 53  Bit Score: 38.11  E-value: 1.73e-03
                           10        20
                   ....*....|....*....|....*.
gi 1868034362  204 EGETQYLIKWKSWSYIHSTWESEESL 229
Cdd:cd18647     16 KGKLEYLVKWRGWSSKHNSWEPEENI 41
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
199-229 2.53e-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: 37.71  E-value: 2.53e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1868034362  199 DTEREEGETQYLIKWKSWSYIHSTWESEESL 229
Cdd:cd18968     15 DAESRKKGWKYLVKWAGYPDEENTWEPEESF 45
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
204-229 3.61e-03

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component 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. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 37.39  E-value: 3.61e-03
                           10        20
                   ....*....|....*....|....*.
gi 1868034362  204 EGETQYLIKWKSWSYIHSTWESEESL 229
Cdd:cd18649     17 KGRMEYLVKWKGWSQKYSTWEPEENI 42
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
204-249 5.36e-03

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component 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: 349295  Cd Length: 58  Bit Score: 36.96  E-value: 5.36e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1868034362  204 EGETQYLIKWKSWSYIHSTWESEESLQQQKVkglkkLENFKKKEDE 249
Cdd:cd18648     16 KGRIEYLVKWKGWAIKYSTWEPEENILDSRL-----IAAFEQKERE 56
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
199-241 5.71e-03

chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349329  Cd Length: 50  Bit Score: 36.46  E-value: 5.71e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1868034362  199 DTEREEGETQYLIKWKSWSYIHSTWESEESLQQQKvKGLKKLE 241
Cdd:cd18973      8 DNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQ-KLLKKYY 49
 
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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