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Conserved domains on  [gi|282165704|ref|NP_001164100|]
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chromodomain-helicase-DNA-binding protein 8 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
811-1032 2.54e-154

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: 476.47  E-value: 2.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
810-1409 7.48e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.56  E-value: 7.48e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 887
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:PLN03142  249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1044
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1045 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAghtNMPNLLNTMMELRKCCNHPYLINGAEEKiltefreachiiPHDFH 1124
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGG---ERKRLLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1125 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1204
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1205 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1284
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1285 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1363
Cdd:PLN03142  622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282165704 1364 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1409
Cdd:PLN03142  686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
721-779 4.28e-36

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: 131.26  E-value: 4.28e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 282165704  721 PDYVEVDRILDESHSIDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 779
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
638-703 1.57e-29

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: 112.82  E-value: 1.57e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165704  638 EEDAAIVDKVLSMRIVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 703
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
BRK smart00592
domain in transcription and CHROMO domain helicases;
2310-2354 1.22e-14

domain in transcription and CHROMO domain helicases;


:

Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.68  E-value: 1.22e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2310 DLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPRFL 2354
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK smart00592
domain in transcription and CHROMO domain helicases;
2379-2419 4.03e-07

domain in transcription and CHROMO domain helicases;


:

Pssm-ID: 197800  Cd Length: 45  Bit Score: 48.50  E-value: 4.03e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2379 LGMEPVQTANSRNGKKG----HHTETVFNRVLPGPIAPESSKKRA 2419
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEVAPRSA 45
PHA03247 super family cl33720
large tegument protein UL36; Provisional
68-280 6.59e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   68 PPPEETAPTELSKESTAPAPESITLHDYTTQPASQEQPAQPVLQTSTPTSGLLQVSKSQEILSQGNPFMGVSATAVSSSS 147
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  148 AG----------------GQPPQSAPKIVIlKAPPSSSVTGAHVAQIQAQGITSTAQPLVAGTANGGKVT--FTKVLTGT 209
Cdd:PHA03247 2687 AArptvgsltsladppppPPTPEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAG 2765
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165704  210 PLRPGVSI--VSGNTVLAAKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGATGPPLKPAVTlTSTPT 280
Cdd:PHA03247 2766 PPAPAPPAapAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-SAQPT 2837
 
Name Accession Description Interval E-value
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
811-1032 2.54e-154

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: 476.47  E-value: 2.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
810-1409 7.48e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.56  E-value: 7.48e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 887
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:PLN03142  249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1044
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1045 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAghtNMPNLLNTMMELRKCCNHPYLINGAEEKiltefreachiiPHDFH 1124
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGG---ERKRLLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1125 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1204
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1205 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1284
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1285 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1363
Cdd:PLN03142  622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282165704 1364 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1409
Cdd:PLN03142  686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
810-1269 1.66e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 410.00  E-value: 1.66e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEmyckdsrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKQ 1045
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1046 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILtefreachiiphdfhl 1125
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELS---------------- 529
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1126 qamVRSaGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 1205
Cdd:COG0553   530 ---GRS-AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165704 1206 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFD 1269
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
814-1101 1.25e-88

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: 291.12  E-value: 1.25e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   814 YQLEGVNWLLFNWYNRQ-NCILADEMGLGKTIQSIAFLQEVYNVGI--HGPFLVIAPLSTITNWEREFNTWT---EMNTI 887
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   888 VYHGSLASRQMIQQYEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNF-----------LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAP 1043
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1044 KQETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGHTNMPNLLNTMMELRKCCNHPYLI 1101
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1133-1258 3.19e-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: 3.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1133 GKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 1212
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 282165704 1213 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 1258
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
721-779 4.28e-36

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: 131.26  E-value: 4.28e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 282165704  721 PDYVEVDRILDESHSIDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 779
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
638-703 1.57e-29

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: 112.82  E-value: 1.57e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165704  638 EEDAAIVDKVLSMRIVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 703
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc smart00487
DEAD-like helicases superfamily;
804-1002 5.74e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.44  E-value: 5.74e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704    804 EYKNRNQLREYQLEGVNWLLFNWynrQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTIT-NWEREFNTWT 882
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704    883 E---MNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykFDALITTFEMILSDCPE--LREIEWRCVIIDEAHRLKN-- 955
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLRKLESGK-------------TDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 282165704    956 RNCKLLDSLKHMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSQFPSE 1002
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1133-1247 5.98e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 104.21  E-value: 5.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1133 GKLVLIDKLLPKLKagGHKVLIFSQMVRCLDilEDYLIQRR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 1211
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 282165704  1212 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 1247
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
833-1309 3.85e-21

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 101.68  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  833 ILADEMGLGKTIQSIAFLQEVYNVGIHgPFLVIAPLSTITNWEREFNTWTEMNTIVyhgslASRQMIQQYemycKDSRGR 912
Cdd:NF038318   51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  913 LIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN--RNCKLLDSLkhMDLEH---KVLLTGTPLQNTVEEL 987
Cdd:NF038318  121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSLLDL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  988 FSLLHFLEPSQFPSESEFLK------DFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKQETII---------EVE 1052
Cdd:NF038318  199 YGLVSFIDPRIFGSEKVFSKryikdeDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIE 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1053 LTN-----IQKKYYRAILEKN----FSFLSKGAGHTNMP---------NLLNTMMELRKCCNHPYLIN------------ 1102
Cdd:NF038318  270 LYVrvnnfLKRDILYSIPTSNrtliILVIRKLLASSSFAlaetfevlkKRLEKLKEGTRSANAQEGFDlfwsfvedeide 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1103 -GAEEK-----------ILTEFREACHIIphdfHLQAMVRSAGKLVLIDKLLPK-----LKAG-GHKVLIFSQMVRCLDI 1164
Cdd:NF038318  350 sGFEEKqdelytrqkefIQHEIDEVDAII----DVAKRIKTNAKVTALKTALEIafeyqREEGiAQKVVVFTESKRTQKY 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1165 LEDYLIQRRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGLGIN 1217
Cdd:NF038318  426 IAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSEGLN 501
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1218 LTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKA--VLQSMS 1286
Cdd:NF038318  502 LQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLESGT 581
                         570       580       590
                  ....*....|....*....|....*....|
gi 282165704 1287 GRDGNITGIQQ-------FsKKEIEDLLRK 1309
Cdd:NF038318  582 DFEKRVLQIYQscdttaeF-KKEFDKLEKK 610
HELICc smart00490
helicase superfamily c-terminal domain;
1163-1247 1.33e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 1.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   1163 DILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 1242
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 282165704   1243 CHRIG 1247
Cdd:smart00490   78 AGRAG 82
BRK smart00592
domain in transcription and CHROMO domain helicases;
2310-2354 1.22e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.68  E-value: 1.22e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2310 DLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPRFL 2354
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2309-2352 2.05e-14

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 69.08  E-value: 2.05e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 282165704  2309 VDLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPR 2352
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
725-777 7.66e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 7.66e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704   725 EVDRILDesHSIDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 777
Cdd:pfam00385    2 EVERILD--HRKDKGGKE---EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
644-704 3.52e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 51.83  E-value: 3.52e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165704    644 VDKVLSMRIVKKelpsGQYteaeEFFVKYKNYSYLHCEWATISQLEKDKRihqKLKRFKTK 704
Cdd:smart00298    4 VEKILDHRWKKK----GEL----EYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKK 53
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
643-704 3.34e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 49.11  E-value: 3.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704   643 IVDKVLSMRIVKKELpsgqyteaEEFFVKYKNYSYLHCEWATISQLEKDKRIhqkLKRFKTK 704
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
BRK smart00592
domain in transcription and CHROMO domain helicases;
2379-2419 4.03e-07

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 48.50  E-value: 4.03e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2379 LGMEPVQTANSRNGKKG----HHTETVFNRVLPGPIAPESSKKRA 2419
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEVAPRSA 45
CHROMO smart00298
Chromatin organization modifier domain;
725-777 6.26e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 6.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704    725 EVDRILDesHSIDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEG--KIREFKR 777
Cdd:smart00298    3 EVEKILD--HRWKKKGEL---EYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
68-280 6.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   68 PPPEETAPTELSKESTAPAPESITLHDYTTQPASQEQPAQPVLQTSTPTSGLLQVSKSQEILSQGNPFMGVSATAVSSSS 147
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  148 AG----------------GQPPQSAPKIVIlKAPPSSSVTGAHVAQIQAQGITSTAQPLVAGTANGGKVT--FTKVLTGT 209
Cdd:PHA03247 2687 AArptvgsltsladppppPPTPEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAG 2765
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165704  210 PLRPGVSI--VSGNTVLAAKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGATGPPLKPAVTlTSTPT 280
Cdd:PHA03247 2766 PPAPAPPAapAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-SAQPT 2837
 
Name Accession Description Interval E-value
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
811-1032 2.54e-154

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: 476.47  E-value: 2.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
810-1409 7.48e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 498.56  E-value: 7.48e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 887
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:PLN03142  249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1044
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1045 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAghtNMPNLLNTMMELRKCCNHPYLINGAEEKiltefreachiiPHDFH 1124
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGG---ERKRLLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1125 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1204
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1205 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1284
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1285 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1363
Cdd:PLN03142  622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282165704 1364 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1409
Cdd:PLN03142  686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
811-1032 8.58e-147

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: 455.17  E-value: 8.58e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEMNTIVY 889
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  890 HGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 969
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165704  970 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
811-1032 3.20e-134

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: 419.06  E-value: 3.20e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
811-1032 2.76e-128

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: 402.10  E-value: 2.76e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
811-1032 2.81e-128

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: 402.08  E-value: 2.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 890
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 970
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  971 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
810-1269 1.66e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 410.00  E-value: 1.66e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEmyckdsrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKQ 1045
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1046 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILtefreachiiphdfhl 1125
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELS---------------- 529
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1126 qamVRSaGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 1205
Cdd:COG0553   530 ---GRS-AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165704 1206 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFD 1269
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
814-1101 1.25e-88

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: 291.12  E-value: 1.25e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   814 YQLEGVNWLLFNWYNRQ-NCILADEMGLGKTIQSIAFLQEVYNVGI--HGPFLVIAPLSTITNWEREFNTWT---EMNTI 887
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   888 VYHGSLASRQMIQQYEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNF-----------LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAP 1043
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1044 KQETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGHTNMPNLLNTMMELRKCCNHPYLI 1101
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
810-1032 4.41e-86

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: 280.78  E-value: 4.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 887
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYEMYcKDSRGRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:cd17993    81 VYLGDIKSRDTIREYEFY-FSQTKKL-----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282165704  968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFgDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd17993   155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEH-DEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
811-996 1.26e-75

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: 249.41  E-value: 1.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLlKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:cd17919    81 YHGSQRERAQIRAKEKLDK------------FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         170       180
                  ....*....|....*....|....*...
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEP 996
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
810-1034 1.01e-72

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: 243.45  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18009     3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEMYCKDSRGrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:cd18009    83 YHGTKEERERLRKKIMKREGTLQ-------DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLK--DFGDLK---------TEEQ----VQKLQAILKPMMLRRL 1033
Cdd:cd18009   156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESwfDFSSLSdnaadisnlSEEReqniVHMLHAILKPFLLRRL 235

                  .
gi 282165704 1034 K 1034
Cdd:cd18009   236 K 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
810-1034 1.25e-69

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: 234.19  E-value: 1.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 887
Cdd:cd17996     3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKkKNNGPYLVIVPLSTLSNWVSEFEKWApSVSKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:cd17996    83 VYKGTPDVRKKLQSQIRAGK------------FNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTY 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  968 -DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF------------LKDFGDLKTEEQV---QKLQAILKPMMLR 1031
Cdd:cd17996   151 yHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFeqwfntpfantgEQVKIELNEEETLliiRRLHKVLRPFLLR 230

                  ...
gi 282165704 1032 RLK 1034
Cdd:cd17996   231 RLK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
811-1032 1.39e-68

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


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 229.63  E-value: 1.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSlasrqmiqqyemyckdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:cd17994    81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd17994   133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
790-1032 3.29e-67

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: 227.58  E-value: 3.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  790 RPQASAWKKlELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPL 868
Cdd:cd18054     1 RPRFVALKK-QPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHqLYGPFLLVVPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  869 STITNWEREFNTWT-EMNTIVYHGSLASRQMIQQYEMYCKDSRgRLipgayKFDALITTFEMILSDCPELREIEWRCVII 947
Cdd:cd18054    80 STLTSWQREFEIWApEINVVVYIGDLMSRNTIREYEWIHSQTK-RL-----KFNALITTYEILLKDKTVLGSINWAFLGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  948 DEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKP 1027
Cdd:cd18054   154 DEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEP 232

                  ....*
gi 282165704 1028 MMLRR 1032
Cdd:cd18054   233 FLLRR 237
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
810-1034 1.02e-65

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: 222.58  E-value: 1.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 887
Cdd:cd17997     3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYkNINGPHLIIVPKSTLDNWMREFKRWCpSLRVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIqqyemyckdSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 967
Cdd:cd17997    83 VLIGDKEERADI---------IRDVLLPG--KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLF 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165704  968 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF----GDLKTEEQVQKLQAILKPMMLRRLK 1034
Cdd:cd17997   152 NSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
811-1032 1.35e-63

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: 217.19  E-value: 1.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEMYCKDSRGRLIPGAYK--------FDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 960
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  961 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
808-1034 5.15e-63

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: 214.74  E-value: 5.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  808 RNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNT 886
Cdd:cd18012     2 KATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  887 IVYHGSLASRQMIQQYEmyckdsrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 966
Cdd:cd18012    82 LVIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  967 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLK 1034
Cdd:cd18012   147 LKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
811-1032 2.60e-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: 213.39  E-value: 2.60e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEMYCKDS--RG-----RLIPGA-YKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 960
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDNaiRGgkkasRMKKEAsVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  961 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
811-1032 4.88e-62

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: 212.62  E-value: 4.88e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQYEMYCKDSRGRLIPGAY--------KFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 960
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704  961 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
811-1032 2.67e-57

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: 198.43  E-value: 2.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQyEMYcKDSRgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:cd18006    81 YMGDKEKRLDLQQ-DIK-STNR---------FHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSES--EFLKDFGDLKTE-EQVQKLQAILKPMMLRR 1032
Cdd:cd18006   150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAYSETDDEsETVEELHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1133-1258 3.19e-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: 3.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1133 GKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 1212
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 282165704 1213 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 1258
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
811-1032 1.90e-55

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: 193.34  E-value: 1.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 888
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLaCEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQMIQQyEMYCKDSrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 968
Cdd:cd18003    81 YYGSAKERKLKRQ-GWMKPNS----------FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165704  969 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT----------EEQVQKLQAILKPMMLRR 1032
Cdd:cd18003   150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
810-1032 1.53e-54

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


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 191.42  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 887
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYE-MYCKDSRgrlipgaYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 966
Cdd:cd18053   100 VYLGDINSRNMIRTHEwMHPQTKR-------LKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLID 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165704  967 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKPMMLRR 1032
Cdd:cd18053   173 FKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
811-999 1.92e-53

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 186.05  E-value: 1.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 889
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  890 HGSLASRqmiqqyemycKDSRGRLIPGAYKFDALITTFEMILSDCPE---LREIEWRCVIIDEAHRLKNRNCKLLDSLKH 966
Cdd:cd17998    81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                         170       180       190
                  ....*....|....*....|....*....|...
gi 282165704  967 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQF 999
Cdd:cd17998   151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
811-1032 3.87e-52

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 184.50  E-value: 3.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLlFNWY-NRQNCILADEMGLGKTIQSIAFLQEVY-----------------------NVGihGPFLVIA 866
Cdd:cd18005     1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfkkkppasSAK--KPVLIVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  867 PLSTITNWEREFNTWTEMNTIVYHGSLASRQMIqqyemyckdsrGRLIPGAYkfDALITTFEMILSDCPELREIEWRCVI 946
Cdd:cd18005    78 PLSVLYNWKDELDTWGHFEVGVYHGSRKDDELE-----------GRLKAGRL--EVVVTTYDTLRRCIDSLNSINWSAVI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  947 IDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD--------------- 1011
Cdd:cd18005   145 ADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarel 224
                         250       260
                  ....*....|....*....|.
gi 282165704 1012 LKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18005   225 RLGRKRKQELAVKLSKFFLRR 245
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
811-1032 9.45e-52

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: 182.70  E-value: 9.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfNWYNRQ-NCILADEMGLGKTIQSIAF---LQEVYNvgIHGPFLVIAPLSTITNWEREFNTWT-EMN 885
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVlahLAEEHN--IWGPFLVIAPASTLHNWQQEISRFVpQFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  886 TIVYHGSLASRQMIQQY----EMYCKDSrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLL 961
Cdd:cd18002    78 VLPYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRW 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  962 DSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-DLKT---------EEQVQKLQAILKPMMLR 1031
Cdd:cd18002   149 KTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLR 228

                  .
gi 282165704 1032 R 1032
Cdd:cd18002   229 R 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
798-1045 2.09e-49

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


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 176.78  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  798 KLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWER 876
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYrNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  877 EFNTWTEmntivyhgSLASRQMIQQYEMYCKDSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 956
Cdd:cd18064    83 EFKRWVP--------TLRAVCLIGDKDQRAAFVRDVLLPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  957 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRRL 1033
Cdd:cd18064   153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRI 232
                         250
                  ....*....|..
gi 282165704 1034 KEDVEKNLAPKQ 1045
Cdd:cd18064   233 KADVEKSLPPKK 244
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
810-1034 7.42e-47

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: 169.84  E-value: 7.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  810 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTI 887
Cdd:cd18062    23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrINGPFLIIVPLSTLSNWVYEFDKWApSVVKV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQyemyckdsrgrlIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-H 966
Cdd:cd18062   103 SYKGSPAARRAFVP------------QLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  967 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRRL 1033
Cdd:cd18062   171 YVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRRL 250

                  .
gi 282165704 1034 K 1034
Cdd:cd18062   251 K 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
811-1032 4.87e-46

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 166.69  E-value: 4.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFnwynrqnC--ILADEMGLGKTIQSIA--------FLQEVYNVGIHGPF----------LVIAPLST 870
Cdd:cd18008     1 LLPYQKQGLAWMLP-------RggILADEMGLGKTIQALAlilatrpqDPKIPEELEENSSDpkklylskttLIVVPLSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  871 ITNWEREFNTWTE---MNTIVYHGSlasrqmiqqyemyckdSRGRLIPGAYKFDALITTFEMILSDCPE----------- 936
Cdd:cd18008    74 LSQWKDEIEKHTKpgsLKVYVYHGS----------------KRIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdske 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  937 -----LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 1011
Cdd:cd18008   138 keaspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISK 217
                         250       260
                  ....*....|....*....|....
gi 282165704 1012 LKTE---EQVQKLQAILKPMMLRR 1032
Cdd:cd18008   218 PFSKndrKALERLQALLKPILLRR 241
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
811-1034 5.75e-46

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: 167.16  E-value: 5.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 888
Cdd:cd18063    24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASRQmiqqyemyckdsrgRLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 965
Cdd:cd18063   104 YKGTPAMRR--------------SLVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  966 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 1032
Cdd:cd18063   170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 249

                  ..
gi 282165704 1033 LK 1034
Cdd:cd18063   250 LK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
798-1034 1.20e-44

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: 162.49  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  798 KLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWER 876
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYrNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  877 EFNTWTEmntivyhgSLASRQMIQQYEMYCKDSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 956
Cdd:cd18065    83 EFKRWVP--------SLRAVCLIGDKDARAAFIRDVMMPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  957 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRRL 1033
Cdd:cd18065   153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRRI 232

                  .
gi 282165704 1034 K 1034
Cdd:cd18065   233 K 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
811-1032 2.37e-43

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 158.69  E-value: 2.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIVY 889
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  890 HG-SLASRQMIQqyeMYCKDSRGrlipgaykfdALITTFEMILSDCPEL-----REIEWRCVIIDEAHRLKNRNCKLLDS 963
Cdd:cd18001    81 HGtSKKERERNL---ERIQRGGG----------VLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  964 LKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQ-FPSESEFLKDF------GDLKTEEQVQK---------LQAILKP 1027
Cdd:cd18001   148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFenpitrGRDKDATQGEKalgsevaenLRQIIKP 227

                  ....*
gi 282165704 1028 MMLRR 1032
Cdd:cd18001   228 YFLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
811-1032 1.68e-39

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: 148.20  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSIAFL-----QEVYNVGIHGPFLVIAPLSTITNWEREFNT 880
Cdd:cd18004     1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVwtllkQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  881 WT-EMNTIVYhgSLASRQMIQQYEMYCKDSRGRlipgaykFDALITTFEMILSDCPELREIEwRC--VIIDEAHRLKNRN 957
Cdd:cd18004    81 WLgLRRIKVV--TADGNAKDVKASLDFFSSAST-------YPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKNSE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  958 CKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD--LK------TEEQV-------QKLQ 1022
Cdd:cd18004   151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpiLRsrdpdaSEEDKelgaersQELS 230
                         250
                  ....*....|
gi 282165704 1023 AILKPMMLRR 1032
Cdd:cd18004   231 ELTSRFILRR 240
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
811-1032 7.49e-39

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: 145.96  E-value: 7.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLF-NWYNRQNcILADEMGLGKTIQSIAFL-------QEVYNVgIHGPFLVIAPLSTITNWEREFNTWT 882
Cdd:cd17999     1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILasdhhkrANSFNS-ENLPSLVVCPPTLVGHWVAEIKKYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  883 E---MNTIVYHGSLASRQmiqqyemyckdsrgRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCK 959
Cdd:cd17999    79 PnafLKPLAYVGPPQERR--------------RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  960 LLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLK-----TEEQVQKLQAILK- 1026
Cdd:cd17999   145 LSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKq 224

                  ....*...
gi 282165704 1027 --PMMLRR 1032
Cdd:cd17999   225 vlPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
811-996 2.33e-37

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: 140.15  E-value: 2.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfnWYNRQNC--ILADEMGLGKTIQSIAFLQevynvGIH------GPFLVIAPLSTITNWEREFNTW- 881
Cdd:cd18000     1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFLA-----ALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  882 TEMNTIVYHGSLASrqMIQQYEMYCKDSRGRLIPGAYK-FDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 960
Cdd:cd18000    74 PPFRVVVLHSSGSG--TGSEEKLGSIERKSQLIRKVVGdGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 282165704  961 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 996
Cdd:cd18000   152 TLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
721-779 4.28e-36

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: 131.26  E-value: 4.28e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 282165704  721 PDYVEVDRILDESHSIDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 779
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
811-1009 1.35e-31

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 125.10  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVN--W--LLFNWYNRQN---CILADEMGLGKTIQSIAFLQeVYNvgIHGP----FLVIAPLSTITNWEREFN 879
Cdd:cd18007     1 LKPHQVEGVRflWsnLVGTDVGSDEgggCILAHTMGLGKTLQVITFLH-TYL--AAAPrrsrPLVLCPASTLYNWEDEFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  880 TWTEMNTIVYHGSLASRQ---------MIQQ-----------YEMY-----CKDSRGRLIPGAYKFDALITtfemilsdc 934
Cdd:cd18007    78 KWLPPDLRPLLVLVSLSAskradarlrKINKwhkeggvlligYELFrnlasNATTDPRLKQEFIAALLDPG--------- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282165704  935 PELreiewrcVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1009
Cdd:cd18007   149 PDL-------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
638-703 1.57e-29

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: 112.82  E-value: 1.57e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165704  638 EEDAAIVDKVLSMRIVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 703
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc smart00487
DEAD-like helicases superfamily;
804-1002 5.74e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.44  E-value: 5.74e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704    804 EYKNRNQLREYQLEGVNWLLFNWynrQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTIT-NWEREFNTWT 882
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704    883 E---MNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykFDALITTFEMILSDCPE--LREIEWRCVIIDEAHRLKN-- 955
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLRKLESGK-------------TDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 282165704    956 RNCKLLDSLKHMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSQFPSE 1002
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
811-1009 4.48e-28

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 114.94  E-value: 4.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVnwlLFNWY--------NRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGP------FLVIAPLSTITNWER 876
Cdd:cd18066     1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  877 EFNTWTemntivyhgslaSRQMIQQYEMYcKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 956
Cdd:cd18066    78 EFQKWL------------GSERIKVFTVD-QDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 282165704  957 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1009
Cdd:cd18066   145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
811-1032 1.63e-27

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: 112.68  E-value: 1.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfnwynRQN--CILADEMGLGKTIQSIAFLQEVYNvgiHGPFLVIAPLSTITNWEREFNTW------T 882
Cdd:cd18010     1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAAYYRE---EWPLLIVCPSSLRLTWADEIERWlpslppD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  883 EMNTIVyhgslasrqmiqqyemyckDSRGRLIPGAYKFdaLITTFEMILSDCPELREIEWRCVIIDEAHRLKNRN----- 957
Cdd:cd18010    73 DIQVIV-------------------KSKDGLRDGDAKV--VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrtk 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  958 --CKLLDSLKhmdleHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF---------LKDFGDLKTEEQVQKLQAIL- 1025
Cdd:cd18010   132 aaLPLLKRAK-----RVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakqGGFGWDYSGSSNLEELHLLLl 206

                  ....*..
gi 282165704 1026 KPMMLRR 1032
Cdd:cd18010   207 ATIMIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
811-1032 5.33e-26

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: 109.10  E-value: 5.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGP-----FLVIAPLSTITNWEREFNT 880
Cdd:cd18067     1 LRPHQREGVKFLYrcvtgRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKpeidkAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  881 WTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 960
Cdd:cd18067    81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  961 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---------GD------LKTEEQVQKLQAIL 1025
Cdd:cd18067   157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                  ....*..
gi 282165704 1026 KPMMLRR 1032
Cdd:cd18067   237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1133-1247 5.98e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 104.21  E-value: 5.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1133 GKLVLIDKLLPKLKagGHKVLIFSQMVRCLDilEDYLIQRR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 1211
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 282165704  1212 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 1247
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
826-1032 5.23e-24

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: 103.32  E-value: 5.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  826 WYN-----RQNC--------ILADEMGLGKTIQSIAFLqevynvgIHGPFLVIAPLSTITNWEREFNTWTE---MNTIVY 889
Cdd:cd18071    32 FLNtitnfSQKKrpelvrggILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  890 HGSlasrqmiqqyemyckdSRGRLIPGAYKFDALITTFEMILSD-----CPELREIEWRCVIIDEAHRLKNRNCKLLDSL 964
Cdd:cd18071   105 HGG----------------ERNRDPKLLSKYDIVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAV 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165704  965 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---DLKTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18071   169 LNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
811-1032 6.50e-23

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: 98.90  E-value: 6.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLFNWYNRqnCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREfntwtemntivyh 890
Cdd:cd18011     1 PLPHQIDAVLRALRKPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDE------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  891 gsLASRQMIQQYEMYcKDSRGRLIPGAYK----FDALITTFEMILSDcPELRE----IEWRCVIIDEAHRLKNRNC---- 958
Cdd:cd18011    66 --LQDKFGLPFLILD-RETAAQLRRLIGNpfeeFPIVIVSLDLLKRS-EERRGlllsEEWDLVVVDEAHKLRNSGGgket 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165704  959 ---KLLDSLKHMDlEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpsesEFLKDFGDLKTEEQVqklqaiLKPMMLRR 1032
Cdd:cd18011   142 kryKLGRLLAKRA-RHVLLLTATPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
833-1309 3.85e-21

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 101.68  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  833 ILADEMGLGKTIQSIAFLQEVYNVGIHgPFLVIAPLSTITNWEREFNTWTEMNTIVyhgslASRQMIQQYemycKDSRGR 912
Cdd:NF038318   51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  913 LIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN--RNCKLLDSLkhMDLEH---KVLLTGTPLQNTVEEL 987
Cdd:NF038318  121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSLLDL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  988 FSLLHFLEPSQFPSESEFLK------DFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKQETII---------EVE 1052
Cdd:NF038318  199 YGLVSFIDPRIFGSEKVFSKryikdeDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIE 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1053 LTN-----IQKKYYRAILEKN----FSFLSKGAGHTNMP---------NLLNTMMELRKCCNHPYLIN------------ 1102
Cdd:NF038318  270 LYVrvnnfLKRDILYSIPTSNrtliILVIRKLLASSSFAlaetfevlkKRLEKLKEGTRSANAQEGFDlfwsfvedeide 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1103 -GAEEK-----------ILTEFREACHIIphdfHLQAMVRSAGKLVLIDKLLPK-----LKAG-GHKVLIFSQMVRCLDI 1164
Cdd:NF038318  350 sGFEEKqdelytrqkefIQHEIDEVDAII----DVAKRIKTNAKVTALKTALEIafeyqREEGiAQKVVVFTESKRTQKY 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1165 LEDYLIQRRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGLGIN 1217
Cdd:NF038318  426 IAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSEGLN 501
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704 1218 LTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKA--VLQSMS 1286
Cdd:NF038318  502 LQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLESGT 581
                         570       580       590
                  ....*....|....*....|....*....|
gi 282165704 1287 GRDGNITGIQQ-------FsKKEIEDLLRK 1309
Cdd:NF038318  582 DFEKRVLQIYQscdttaeF-KKEFDKLEKK 610
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
811-1032 6.82e-21

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: 94.08  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfnWYNRQNC---ILADEMGLGKTIQSIAF-----------------------LQEVYNVGIHGPFLV 864
Cdd:cd18072     1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekalteweSKKDSTLVPSAGTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  865 IAPLSTITNWEREFNTWTEMNTI---VYHGslASRqmiqqyemyckDSRGRLIPgayKFDALITTFEMILSDCPELRE-- 939
Cdd:cd18072    79 VCPASLVHQWKNEVESRVASNKLrvcLYHG--PNR-----------ERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  940 -------IEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLKDFGDL 1012
Cdd:cd18072   143 rssplfrIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVDN 221
                         250       260
                  ....*....|....*....|
gi 282165704 1013 KTEEQVQKLQAILKPMMLRR 1032
Cdd:cd18072   222 KSRKGGERLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
1163-1247 1.33e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 1.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   1163 DILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 1242
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 282165704   1243 CHRIG 1247
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
832-1009 1.79e-20

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 93.03  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  832 CILADEMGLGKTIQSIAFLQEVY-NVGIHG--PFLVIAPLSTITNWEREFNTW------------TEMNTI--------- 887
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVLlCEKLENfsRVLVVCPLNTVLNWLNEFEKWqeglkdeekievNELATYkrpqersyk 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  888 VYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKfdaLITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLDSLKH 966
Cdd:cd18068   111 LQRWQEEGGVMIIGYDMYRILAQERNVKSREK---LKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNS 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 282165704  967 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1009
Cdd:cd18068   181 IRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
832-1009 8.58e-20

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


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 90.64  E-value: 8.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  832 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWteMNTIVYHGSLASRQM---IQQYEMYCKD 908
Cdd:cd18069    31 CILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTTA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  909 SRGRLIPG-AYKFDALITTFEMI-LSDCPELreiewrcVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEE 986
Cdd:cd18069   109 ARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIE 181
                         170       180
                  ....*....|....*....|...
gi 282165704  987 LFSLLHFLEPSQFPSESEFLKDF 1009
Cdd:cd18069   182 YWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
722-777 3.26e-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: 74.53  E-value: 3.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 282165704  722 DYVEVDRILDEShsidkDNGEPVIYYLVKWCSLPYEDSTWELKEDV---DEGKIREFKR 777
Cdd:cd18659     1 EYTIVERIIAHR-----EDDEGVTEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
BRK smart00592
domain in transcription and CHROMO domain helicases;
2310-2354 1.22e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.68  E-value: 1.22e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2310 DLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPRFL 2354
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2309-2352 2.05e-14

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 69.08  E-value: 2.05e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 282165704  2309 VDLETRIPVINKVDGTLLVGEDAPRRAELEMWLQGHPEFAVDPR 2352
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
640-702 1.96e-11

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: 61.61  E-value: 1.96e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  640 DAAIVDKVLSMRIVK-KELPSGQYTEAE------EFFVKYKNYSYLHCEWATISQLEKDkRIHQKLKRFK 702
Cdd:cd18660     1 DEDKIEKILDHRPKGpVEEASLDLTDPDepwderEFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYI 69
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
811-998 2.82e-11

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: 65.45  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfnwYNRQNCILADeMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMNTIVY 889
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  890 hgSLAsrqmiqqyemyckDSRGR-LIPGAYK-FDALITTFEMiLSDCPELREIEW--RCVIIDEAHRLKNRNCKLLDSLK 965
Cdd:cd18013    77 --SVA-------------VGTERqRSKAANTpADLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALR 140
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 282165704  966 HMD--LEHKVLLTGTPLQNTVEELFSLLHFLEPSQ 998
Cdd:cd18013   141 KVRpvIKRLIGLTGTPSPNGLMDLWAQIALLDQGE 175
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
811-1031 3.42e-11

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: 66.21  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGVNWLLfnwyNRQNcILADEMGLGKTIQSIAFL--------------------------QEVYNVGIHGPFLV 864
Cdd:cd18070     1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLALIllhprpdndldaadddsdemvccpdcLVAETPVSSKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  865 IAPLSTITNWEREFNTWTEMNTIVYHgslasrqmiqqYEMYCKDsrGRLIPGAYKF----DALITTFEMILSD------- 933
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKD--GALASPAPEIlaeyDIVVTTYDVLRTElhyaean 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  934 ----------------CPeLREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS 997
Cdd:cd18070   143 rsnrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVE 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 282165704  998 QFpSESEFLKDFGDLKTEEQ--VQKLQAILKPMMLR 1031
Cdd:cd18070   222 PF-CDSDWWARVLIRPQGRNkaREPLAALLKELLWR 256
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
725-777 7.66e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 7.66e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704   725 EVDRILDesHSIDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 777
Cdd:pfam00385    2 EVERILD--HRKDKGGKE---EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
721-768 2.85e-09

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 54.96  E-value: 2.85e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 282165704  721 PDYVEVDRILDesHSIDKDNGepvIYYLVKWCSLPYEDSTWElKEDVD 768
Cdd:cd18662     1 PEWLQIHRIIN--HRVDKDGN---TWYLVKWRDLPYDQSTWE-SEDDD 42
CHROMO smart00298
Chromatin organization modifier domain;
644-704 3.52e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 51.83  E-value: 3.52e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165704    644 VDKVLSMRIVKKelpsGQYteaeEFFVKYKNYSYLHCEWATISQLEKDKRihqKLKRFKTK 704
Cdd:smart00298    4 VEKILDHRWKKK----GEL----EYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKK 53
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
643-704 3.34e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 49.11  E-value: 3.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165704   643 IVDKVLSMRIVKKELpsgqyteaEEFFVKYKNYSYLHCEWATISQLEKDKRIhqkLKRFKTK 704
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
BRK smart00592
domain in transcription and CHROMO domain helicases;
2379-2419 4.03e-07

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 48.50  E-value: 4.03e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 282165704   2379 LGMEPVQTANSRNGKKG----HHTETVFNRVLPGPIAPESSKKRA 2419
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEVAPRSA 45
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
725-777 2.83e-06

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 46.32  E-value: 2.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704  725 EVDRILDesHSIDKDngepVIYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 777
Cdd:cd00024     2 EVEKILD--HRVRKG----KLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
811-979 2.97e-05

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: 46.14  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  811 LREYQLEGV-NWLLFNWYNRQNCILAdeMGLGKTIQSIAFLQEVYNvgihGPFLVIAP-LSTITNWEREFNTWTEMNTIV 888
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKE----LRTLIVVPtDALLDQWKERFEDFLGDSSIG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  889 YHGSLASrqmiqqyemycKDSRGRLIpgaykfdaLITTFEMILSDCPELREIEWRC--VIIDEAHRLknrNCKLLDSLKH 966
Cdd:cd17926    75 LIGGGKK-----------KDFDDANV--------VVATYQSLSNLAEEEKDLFDQFglLIVDEAHHL---PAKTFSEILK 132
                         170
                  ....*....|....
gi 282165704  967 MDLEHKVL-LTGTP 979
Cdd:cd17926   133 ELNAKYRLgLTATP 146
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
667-689 3.05e-05

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


Pssm-ID: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 44.25  E-value: 3.05e-05
                          10        20
                  ....*....|....*....|...
gi 282165704  667 EFFVKYKNYSYLHCEWATISQLE 689
Cdd:cd18667    45 EFFVKWHGMSYWHCEWVSELQLE 67
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
831-978 3.20e-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: 46.24  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  831 NCILADEMGLGKTIqsIAFLQ-EVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMN--TIVYHGSlasrqmiqqyemyc 906
Cdd:cd00046     3 NVLITAPTGSGKTL--AALLAaLLLLLKKGKKVLVLVPTKALALqTAERLRELFGPGirVAVLVGG-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  907 KDSRGRLIPGAYKFDALITTFEMILSDCPELREI---EWRCVIIDEAHRL----KNRNCKLLDSLKHMDLEHK-VLLTGT 978
Cdd:cd00046    67 SSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSAT 146
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
722-781 3.22e-05

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


Pssm-ID: 349311  Cd Length: 59  Bit Score: 43.80  E-value: 3.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  722 DYVEVDRILDeSHSIDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQSR 781
Cdd:cd18664     1 EFHVVERIIA-SQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
CHROMO smart00298
Chromatin organization modifier domain;
725-777 6.26e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 6.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704    725 EVDRILDesHSIDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEG--KIREFKR 777
Cdd:smart00298    3 EVEKILD--HRWKKKGEL---EYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
725-770 3.77e-04

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


Pssm-ID: 349322  Cd Length: 49  Bit Score: 40.34  E-value: 3.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 282165704  725 EVDRILDEshsiDKDNGEpvIYYLVKWCSLPYEDSTWELKEDVDEG 770
Cdd:cd18966     2 EVERILAE----RRDDGG--KRYLVKWEGYPLEEATWEPEENIGDE 41
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1200-1252 6.81e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 6.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 282165704 1200 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 1252
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1091-1264 1.26e-03

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


Pssm-ID: 402894  Cd Length: 281  Bit Score: 43.47  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1091 LRKCC---NHPYLIngaeekiltefreACHIIPHDFHLQAM----VRSAGKLV----LIDKLLPKLKAGGHKVLIFSQMV 1159
Cdd:pfam11496   54 LENLSlvaTHPYLL-------------VDHYMPKSLLLKDEpeklAYTSGKFLvlndLVNLLIERDRKEPINVAIVARSG 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  1160 RCLDILEDYLIQRRYLYERIDG-RVRGNLRQAAIDRFSKPDSDRFVFL----LCTRAGGLGINlTAADTCIIFDSDWNPQ 1234
Cdd:pfam11496  121 KTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLLsstgQLTNDDSLLEN-YKFDLIIAFDSSVDTS 199
                          170       180       190
                   ....*....|....*....|....*....|
gi 282165704  1235 NDLQAQARCHRIGQSKAVKVYRLITRNSYE 1264
Cdd:pfam11496  200 SPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
723-762 1.41e-03

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: 38.82  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 282165704  723 YVEVDRILDESHSIDKDNGEPviYYLVKWCSLPYEDSTWE 762
Cdd:cd18661     2 YQIVERIIAHSPQKSAASGYP--DYLCKWQGLPYSECTWE 39
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
812-987 2.06e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 41.46  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   812 REYQLEGVNWLLfnwyNRQNCILADEMGLGKT-IQSIAFLQEVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMNTIVY 889
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   890 HGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPE---LREIewRCVIIDEAHRL--KNRNCKLLDSL 964
Cdd:pfam00270   77 ASLLGGDSRKEQLEKLKG------------PDILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDLEEIL 142
                          170       180
                   ....*....|....*....|....
gi 282165704   965 KHMDLEHK-VLLTGTPLQNtVEEL 987
Cdd:pfam00270  143 RRLPKKRQiLLLSATLPRN-LEDL 165
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
725-777 4.49e-03

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


Pssm-ID: 349330  Cd Length: 50  Bit Score: 37.46  E-value: 4.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282165704  725 EVDRILDEShSIDKDNgepviYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 777
Cdd:cd18974     2 EVEEIVDEK-MIDDEL-----HYLVKWKGWPAEYNQWEPEDDMENAPkaIQSYEK 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
68-280 6.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704   68 PPPEETAPTELSKESTAPAPESITLHDYTTQPASQEQPAQPVLQTSTPTSGLLQVSKSQEILSQGNPFMGVSATAVSSSS 147
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165704  148 AG----------------GQPPQSAPKIVIlKAPPSSSVTGAHVAQIQAQGITSTAQPLVAGTANGGKVT--FTKVLTGT 209
Cdd:PHA03247 2687 AArptvgsltsladppppPPTPEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAG 2765
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165704  210 PLRPGVSI--VSGNTVLAAKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGATGPPLKPAVTlTSTPT 280
Cdd:PHA03247 2766 PPAPAPPAapAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-SAQPT 2837
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
737-775 6.97e-03

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


Pssm-ID: 349320  Cd Length: 54  Bit Score: 36.93  E-value: 6.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 282165704  737 DKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGK--IREF 775
Cdd:cd18964    12 SARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAklIEDF 52
 
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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