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Conserved domains on  [gi|568955929|ref|XP_006530635|]
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chromodomain-helicase-DNA-binding protein 9 isoform X8 [Mus musculus]

Protein Classification

chromo domain-containing DEAD/DEAH box helicase( domain architecture ID 13036620)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
353-574 9.90e-150

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: 462.94  E-value: 9.90e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
352-973 4.47e-147

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: 487.00  E-value: 4.47e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEilLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 427
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:PLN03142  247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKKLA 584
Cdd:PLN03142  316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  585 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKilgefrdtyNPSASD 664
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  665 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 744
Cdd:PLN03142  464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  745 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 824
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  825 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGRGSTFAKASFVASG 903
Cdd:PLN03142  621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  904 NRTDISLDDpnfwQKWAKKAELDIDTISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 973
Cdd:PLN03142  693 TAELYDFDD----EDDKDENKLDFKKIVSDNW--IDPPK-RERKRNYSESeyfKQAMRQGAPAKPKEPRIPRM 758
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
263-321 1.24e-33

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: 124.32  E-value: 1.24e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  263 PDYVEVDRILEVSFCEDKDTGESVIYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 321
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, ...
179-243 7.64e-28

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: 108.19  E-value: 7.64e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  179 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 243
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
BRK smart00592
domain in transcription and CHROMO domain helicases;
2040-2084 5.14e-15

domain in transcription and CHROMO domain helicases;


:

Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 5.14e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 568955929   2040 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2084
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1966-2006 1.70e-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: 69.46  E-value: 1.70e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568955929  1966 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2006
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
PTZ00121 super family cl31754
MAEBL; Provisional
4-259 1.23e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    4 KKPRKRVESESKQEKANRIISEAIARAKERGERNIPRVMSPENFPSASVEGKEEKRGRRMKSKPKDRDNKKPKTYSKLKE 83
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   84 KTKIGKLIITLGKKHKRRNESSDELSDAEQRSQHTFKEQHSQKRRSNRQIKRKKYAED---AEGKQSEEEVKGSLRVKRN 160
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkAEEKKKADELKKAEELKKA 1560
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  161 SAPPPGEQplqlfvENPSEEDAAIVDKI--LACRTVKKEVSPGVMLDIEEFFVKYKNYSYLHCEWATEQQLLKDKRIQQK 238
Cdd:PTZ00121 1561 EEKKKAEE------AKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
                         250       260
                  ....*....|....*....|....
gi 568955929  239 IKRFKLRQAQ---RAHFLADMEEE 259
Cdd:PTZ00121 1635 VEQLKKKEAEekkKAEELKKAEEE 1658
 
Name Accession Description Interval E-value
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
353-574 9.90e-150

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: 462.94  E-value: 9.90e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
352-973 4.47e-147

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 487.00  E-value: 4.47e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEilLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 427
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:PLN03142  247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKKLA 584
Cdd:PLN03142  316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  585 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKilgefrdtyNPSASD 664
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  665 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 744
Cdd:PLN03142  464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  745 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 824
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  825 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGRGSTFAKASFVASG 903
Cdd:PLN03142  621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  904 NRTDISLDDpnfwQKWAKKAELDIDTISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 973
Cdd:PLN03142  693 TAELYDFDD----EDDKDENKLDFKKIVSDNW--IDPPK-RERKRNYSESeyfKQAMRQGAPAKPKEPRIPRM 758
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
352-825 3.26e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 394.59  E-value: 3.26e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEmyfrdsqgriirgayRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKKLAPKE 587
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  588 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNVPNLVNTMMELRKCCNHPYLIKGAEEKILGEfrdtynpsasdfhl 667
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------- 531
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  668 qamiqsAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 747
Cdd:COG0553   532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955929  748 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVLQ 825
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
356-643 3.28e-83

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: 275.33  E-value: 3.28e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   356 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYEILLTGI--RGPFLIIAPLSTIANWEREFRTWT---DINVV 429
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   430 VYHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLM 509
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   510 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKKLAP 585
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   586 KEETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGQTNVPNLVNTMMELRKCCNHPYLI 643
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
675-800 1.22e-55

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  675 GKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 754
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955929  755 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV 800
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, ...
263-321 1.24e-33

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: 124.32  E-value: 1.24e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  263 PDYVEVDRILEVSFCEDKDTGESVIYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 321
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
346-544 3.01e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 3.01e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    346 EYKNGNQLREYQLEGLNWLLFNWynrRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIA-NWEREFRTW- 423
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLg 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    424 --TDINVVVYHGSLISRQMIQQyemyfrdsqgrIIRGayRFQAIITTFEMIL--GGCGELNAIDWRCVIIDEAHRLKNKN 499
Cdd:smart00487   79 psLGLKVVGLYGGDSKREQLRK-----------LESG--KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 568955929    500 --CKLLEGLKLMNLE-HKVLLTGTP---LQNTVEELFSLLHFLEPLRFPSE 544
Cdd:smart00487  146 fgDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
179-243 7.64e-28

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: 108.19  E-value: 7.64e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  179 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 243
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
675-789 3.52e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 101.90  E-value: 3.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   675 GKLVLIDKLLPKMKagGHKVLIFSQMVRCLDilEDYLIHKR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 753
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568955929   754 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 789
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 ...
375-839 2.57e-22

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: 105.15  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  375 ILADEMGLGKTIQSITFLYEILLTGIRgPFLIIAPLSTIANWEREFRTWTDINVVVyhgslISRQMIQQYemyfRDSQGR 454
Cdd:NF038318   51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  455 IIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKN--KNCKLLEGL-KLMNLEHKVLLTGTPLQNTVEELFS 531
Cdd:NF038318  121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLDLYG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  532 LLHFLEPLRFPSESTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKKLAPKEETIIEV--ELTNIQKKYY 603
Cdd:NF038318  201 LVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCITVdfELSPDEIELY 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  604 RAI---LEKNFSFlskgagqtNVPN--------------------LVNTMMELRKCCNHPY---LIKGAEEKI--LGEFR 655
Cdd:NF038318  272 VRVnnfLKRDILY--------SIPTsnrtliilvirkllasssfaLAETFEVLKKRLEKLKegtRSANAQEGFdlFWSFV 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  656 DTYNpSASDFHL---------QAMIQSAGKLV--LID-----KLLPKMKAG----------------GHKVLIFSQMVRC 703
Cdd:NF038318  344 EDEI-DESGFEEkqdelytrqKEFIQHEIDEVdaIIDvakriKTNAKVTALktaleiafeyqreegiAQKVVVFTESKRT 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  704 LDILEDYLIHKRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGL 756
Cdd:NF038318  423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSE 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  757 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV-TRNSYEREMFDRASLKLGL--------DKA--VLQ 825
Cdd:NF038318  499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLE 578
                         570
                  ....*....|....
gi 568955929  826 SMSGRDSNVSGIQQ 839
Cdd:NF038318  579 SGTDFEKRVLQIYQ 592
HELICc smart00490
helicase superfamily c-terminal domain;
705-789 8.12e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.73  E-value: 8.12e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    705 DILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 784
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 568955929    785 CHRIG 789
Cdd:smart00490   78 AGRAG 82
BRK smart00592
domain in transcription and CHROMO domain helicases;
2040-2084 5.14e-15

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 5.14e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 568955929   2040 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2084
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1966-2006 1.70e-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: 69.46  E-value: 1.70e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568955929  1966 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2006
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
BRK smart00592
domain in transcription and CHROMO domain helicases;
1966-2013 2.42e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 2.42e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568955929   1966 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYvedlgAFIPR 2013
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEY-----EVAPR 43
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2039-2082 2.79e-13

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: 65.99  E-value: 2.79e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568955929  2039 LTGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPE 2082
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
267-319 1.50e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 52.58  E-value: 1.50e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568955929   267 EVDRILEVSFCEDKDTgesviYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 319
Cdd:pfam00385    2 EVERILDHRKDKGGKE-----EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
185-247 1.82e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 52.60  E-value: 1.82e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929    185 VDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRiqqKIKRFKLRQA 247
Cdd:smart00298    4 VEKILDHRWKKKGE--------LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
184-243 1.15e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 50.27  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   184 IVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRIqqkIKRFK 243
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFK 50
CHROMO smart00298
Chromatin organization modifier domain;
267-322 1.21e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 41.82  E-value: 1.21e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955929    267 EVDRILEVSFcedkdTGESVIYYLVKWCSLPYEDSTWELKEDVDLA--KIEEFEQLQA 322
Cdd:smart00298    3 EVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKKKER 55
PTZ00121 PTZ00121
MAEBL; Provisional
4-259 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    4 KKPRKRVESESKQEKANRIISEAIARAKERGERNIPRVMSPENFPSASVEGKEEKRGRRMKSKPKDRDNKKPKTYSKLKE 83
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   84 KTKIGKLIITLGKKHKRRNESSDELSDAEQRSQHTFKEQHSQKRRSNRQIKRKKYAED---AEGKQSEEEVKGSLRVKRN 160
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkAEEKKKADELKKAEELKKA 1560
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  161 SAPPPGEQplqlfvENPSEEDAAIVDKI--LACRTVKKEVSPGVMLDIEEFFVKYKNYSYLHCEWATEQQLLKDKRIQQK 238
Cdd:PTZ00121 1561 EEKKKAEE------AKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
                         250       260
                  ....*....|....*....|....
gi 568955929  239 IKRFKLRQAQ---RAHFLADMEEE 259
Cdd:PTZ00121 1635 VEQLKKKEAEekkKAEELKKAEEE 1658
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
3-183 3.19e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    3 EKKPRKRVESESKQEKANRIISEAIARAKER--GERNIPR-VMSPENFPSASVEGKEEKRGRRMKSKPKDRDNKKPKTYS 79
Cdd:NF033838  258 QDKPKRRAKRGVLGEPATPDKKENDAKSSDSsvGEETLPSpSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYK 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   80 KLK-------EKTKIGKLIITLGKKHKRRNESSDELSDAEQRSqhtfkEQHSQKRRSNRQIKRKKYAEDAEGKQSEEE-V 151
Cdd:NF033838  338 TLEleiaesdVKVKEAELELVKEEAKEPRNEEKIKQAKAKVES-----KKAEATRLEKIKTDRKKAEEEAKRKAAEEDkV 412
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568955929  152 KGSLRVKRNSAPPPGEQPLQLFVENPSEEDAA 183
Cdd:NF033838  413 KEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKA 444
 
Name Accession Description Interval E-value
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
353-574 9.90e-150

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: 462.94  E-value: 9.90e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
352-973 4.47e-147

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 487.00  E-value: 4.47e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEilLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 427
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:PLN03142  247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKKLA 584
Cdd:PLN03142  316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  585 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKilgefrdtyNPSASD 664
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  665 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 744
Cdd:PLN03142  464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  745 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 824
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  825 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGRGSTFAKASFVASG 903
Cdd:PLN03142  621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  904 NRTDISLDDpnfwQKWAKKAELDIDTISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 973
Cdd:PLN03142  693 TAELYDFDD----EDDKDENKLDFKKIVSDNW--IDPPK-RERKRNYSESeyfKQAMRQGAPAKPKEPRIPRM 758
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
353-574 9.93e-144

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: 445.92  E-value: 9.93e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWTDINVVVY 431
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  432 HGSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 511
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  512 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
353-574 8.34e-137

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: 426.38  E-value: 8.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
353-574 2.49e-131

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: 410.58  E-value: 2.49e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
353-574 2.60e-130

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: 407.52  E-value: 2.60e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 432
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 512
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  513 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
352-825 3.26e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 394.59  E-value: 3.26e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEmyfrdsqgriirgayRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:COG0553   321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKKLAPKE 587
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  588 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNVPNLVNTMMELRKCCNHPYLIKGAEEKILGEfrdtynpsasdfhl 667
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------- 531
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  668 qamiqsAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 747
Cdd:COG0553   532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955929  748 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVLQ 825
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
356-643 3.28e-83

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: 275.33  E-value: 3.28e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   356 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYEILLTGI--RGPFLIIAPLSTIANWEREFRTWT---DINVV 429
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   430 VYHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLM 509
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   510 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKKLAP 585
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   586 KEETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGQTNVPNLVNTMMELRKCCNHPYLI 643
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
352-574 4.48e-81

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: 266.53  E-value: 4.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  352 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DINVV 429
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  430 VYHGSLISRQMIQQYEMYFrdSQGRIIRgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLM 509
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYF--SQTKKLK----FNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955929  510 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFmQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd17993   155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
353-540 1.14e-73

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: 243.63  E-value: 1.14e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGkERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEmyfrdsqgriirGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:cd17919    81 YHGSQRERAQIRAKE------------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         170       180       190
                  ....*....|....*....|....*....|...
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEP---LR 540
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDPpflLR 181
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
353-574 1.53e-70

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: 235.41  E-value: 1.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSlisrqmiqqyemyfrdsqgriirgayrfQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:cd17994    81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd17994   133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
350-576 3.03e-69

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: 233.05  E-value: 3.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  350 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINV 428
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  429 VVYHGSLISRQMIQQyEMYFRDSQGRIirgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 508
Cdd:cd18009    81 LLYHGTKEERERLRK-KIMKREGTLQD------FPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  509 MNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-----------DLKTEEQ----VQKLQAILKPMMLR 573
Cdd:cd18009   154 FNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLR 233

                  ...
gi 568955929  574 RLK 576
Cdd:cd18009   234 RLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
350-576 4.60e-66

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: 223.35  E-value: 4.60e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  350 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DIN 427
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLgYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIqqyemyFRDsqgRIIRGayRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:cd17997    81 VVVLIGDKEERADI------IRD---VLLPG--KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF----GDLKTEEQVQKLQAILKPMMLRRLK 576
Cdd:cd17997   150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
353-574 6.80e-66

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: 223.35  E-value: 6.80e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKL 502
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  503 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
350-574 3.52e-65

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 221.80  E-value: 3.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  350 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DIN 427
Cdd:cd18054    18 NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLsYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWApEIN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIQQYEMYFRDSQgRIirgayRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:cd18054    98 VVVYIGDLMSRNTIREYEWIHSQTK-RL-----KFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLI 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQKLQAILKPMMLRR 574
Cdd:cd18054   172 DFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
353-574 3.87e-65

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: 221.48  E-value: 3.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKL 502
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDNAIRGGKKASRmkkeasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  503 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
353-574 3.34e-64

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: 218.78  E-value: 3.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKL 502
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955929  503 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
350-576 1.71e-63

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: 216.47  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  350 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSI---TFLYEIllTGIRGPFLIIAPLSTIANWEREFRTWT-D 425
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  426 INVVVYHGSLISRQMIQQYEMyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEG 505
Cdd:cd17996    79 VSKIVYKGTPDVRKKLQSQIR------------AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  506 LKLM-NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG------------DLKTEEQV---QKLQAILKP 569
Cdd:cd17996   147 LNTYyHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRP 226

                  ....*..
gi 568955929  570 MMLRRLK 576
Cdd:cd17996   227 FLLRRLK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
675-800 1.22e-55

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  675 GKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 754
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955929  755 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV 800
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
351-576 1.98e-54

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: 190.08  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  351 NQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVV 429
Cdd:cd18012     3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  430 VYHGSLISRQMIQQYEMYfrdsqgriirgayrfQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLM 509
Cdd:cd18012    83 VIHGTKRKREKLRALEDY---------------DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955929  510 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLK 576
Cdd:cd18012   148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
353-574 1.88e-53

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: 187.26  E-value: 1.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 430
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:cd18006    81 YMGDKEKRLDLQQD-----------IKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 574
Cdd:cd18006   150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
353-574 1.73e-51

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: 181.78  E-value: 1.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWTD-INVVV 430
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLaHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  431 YHGSLISRQMIQQyEMYFRDSqgriirgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 510
Cdd:cd18003    81 YYGSAKERKLKRQ-GWMKPNS----------FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955929  511 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF----------MQEFGDLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18003   150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpltaMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
350-574 3.09e-51

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: 181.79  E-value: 3.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  350 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 427
Cdd:cd18053    18 GLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPqMN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  428 VVVYHGSLISRQMIQQYEmYFRDSQGRIirgayRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLK 507
Cdd:cd18053    98 AVVYLGDINSRNMIRTHE-WMHPQTKRL-----KFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLI 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  508 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQKLQAILKPMMLRR 574
Cdd:cd18053   172 DFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
353-574 1.68e-50

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: 179.88  E-value: 1.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLlFNWY-NRRNCILADEMGLGKTIQSITFLYEIL-LTGIR--------------------GPFLIIAPL 410
Cdd:cd18005     1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLgKTGTRrdrennrprfkkkppassakKPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  411 STIANWEREFRTWTDINVVVYHGSLISRqmiqqyemyfrDSQGRIIRGAYrfQAIITTFEMILGGCGELNAIDWRCVIID 490
Cdd:cd18005    80 SVLYNWKDELDTWGHFEVGVYHGSRKDD-----------ELEGRLKAGRL--EVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  491 EAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LK 555
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                         250
                  ....*....|....*....
gi 568955929  556 TEEQVQKLQAILKPMMLRR 574
Cdd:cd18005   227 GRKRKQELAVKLSKFFLRR 245
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
353-574 4.72e-49

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: 175.00  E-value: 4.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLfNWYNRR-NCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREF-RTWTDINVV 429
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  430 VYHGSLISRQMIQQY----EMYFRDSQgriirgayrFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEG 505
Cdd:cd18002    80 PYWGNPKDRKVLRKFwdrkNLYTRDAP---------FHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  506 LKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-DLKT---------EEQVQKLQAILKPMMLRR 574
Cdd:cd18002   151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
353-541 4.95e-49

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: 173.34  E-value: 4.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVVY 431
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  432 HGSLISRqmiqqyemyfRDSQGRIIRGAYRFQAIITTFEMILGgcgelNAIDWR--------CVIIDEAHRLKNKNCKLL 503
Cdd:cd17998    81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATS-----NPDDRSffkrlklnYVVYDEGHMLKNMTSERY 145
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568955929  504 EGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRF 541
Cdd:cd17998   146 RHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
337-576 1.58e-45

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: 165.60  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  337 IWKKIEQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIAN 415
Cdd:cd18062     8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRINGPFLIIVPLSTLSN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  416 WEREFRTWTDINV-VVYHGSLISRQMIQQyemyfrdsqgrIIRGAyRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHR 494
Cdd:cd18062    88 WVYEFDKWAPSVVkVSYKGSPAARRAFVP-----------QLRSG-KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  495 LKNKNCKLLEGLKLMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---V 560
Cdd:cd18062   156 MKNHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliI 235
                         250
                  ....*....|....*.
gi 568955929  561 QKLQAILKPMMLRRLK 576
Cdd:cd18062   236 RRLHKVLRPFLLRRLK 251
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
340-587 2.26e-45

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: 164.84  E-value: 2.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  340 KIEQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWER 418
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  419 EFRTWTDINVVVyhgSLISRQmiQQYEMYFRDSqgrIIRGAYrfQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNK 498
Cdd:cd18064    83 EFKRWVPTLRAV---CLIGDK--DQRAAFVRDV---LLPGEW--DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  499 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRRL 575
Cdd:cd18064   153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRI 232
                         250
                  ....*....|..
gi 568955929  576 KEDVEKKLAPKE 587
Cdd:cd18064   233 KADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
337-576 2.14e-43

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: 159.46  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  337 IWKKIEQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIAN 415
Cdd:cd18063     8 ITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRLNGPYLIIVPLSTLSN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  416 WEREFRTWT-DINVVVYHGS-LISRQMIQQYEmyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAH 493
Cdd:cd18063    88 WTYEFDKWApSVVKISYKGTpAMRRSLVPQLR-------------SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  494 RLKNKNCKLLEGLKLMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ--- 559
Cdd:cd18063   155 RMKNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETili 234
                         250
                  ....*....|....*..
gi 568955929  560 VQKLQAILKPMMLRRLK 576
Cdd:cd18063   235 IRRLHKVLRPFLLRRLK 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
353-574 9.73e-43

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


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 157.45  E-value: 9.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFnwynrRNCILADEMGLGKTIQSITFLYEILLTGIRGPF------------------LIIAPLSTIA 414
Cdd:cd18008     1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALALILATRPQDPKIPEeleenssdpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  415 NWEREFRTWTD---INVVVYHGSlisrqmiqqyemyfrdSQGRIIRGAYRFQAIITTFEMI----------------LGG 475
Cdd:cd18008    76 QWKDEIEKHTKpgsLKVYVYHGS----------------KRIKSIEELSDYDIVITTYGTLasefpknkkgggrdskEKE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  476 CGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLK 555
Cdd:cd18008   140 ASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                         250       260
                  ....*....|....*....|..
gi 568955929  556 TE---EQVQKLQAILKPMMLRR 574
Cdd:cd18008   220 SKndrKALERLQALLKPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
353-574 2.13e-42

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: 155.99  E-value: 2.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVVY 431
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTpGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  432 HGSLISRQmiqqyemyfRDSQGRIIRGayrFQAIITTFEMILGGCGELNAID-----WRCVIIDEAHRLKNKNCKLLEGL 506
Cdd:cd18001    81 HGTSKKER---------ERNLERIQRG---GGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  507 KLMNLEHKVLLTGTPLQNTVEELFSLLHFLEP-LRFPSESTFMQEF------GDLKTEEQVQK---------LQAILKPM 570
Cdd:cd18001   149 REIPAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFenpitrGRDKDATQGEKalgsevaenLRQIIKPY 228

                  ....
gi 568955929  571 MLRR 574
Cdd:cd18001   229 FLRR 232
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
340-576 6.08e-42

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: 154.79  E-value: 6.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  340 KIEQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWER 418
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  419 EFRTWT-DINVVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKN 497
Cdd:cd18065    83 EFKRWVpSLRAVCLIGDKDARAAFIRDVMM-----------PGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  498 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18065   152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                  ..
gi 568955929  575 LK 576
Cdd:cd18065   232 IK 233
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
353-574 1.56e-37

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: 142.42  E-value: 1.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLL-----FNWYNRRNCILADEMGLGKTIQSITFLYeILLTgiRGPF--------LIIAPLSTIANWERE 419
Cdd:cd18004     1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  420 FRTW---TDINVVVYHGSLISRQMIQQYEMYFRdsqgriirgayRFQAIITTFEMILGGCGELN-AIDWRCVIIDEAHRL 495
Cdd:cd18004    78 FDKWlglRRIKVVTADGNAKDVKASLDFFSSAS-----------TYPVLIISYETLRRHAEKLSkKISIDLLICDEGHRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  496 KNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD--LK------TEEQV------- 560
Cdd:cd18004   147 KNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpiLRsrdpdaSEEDKelgaers 226
                         250
                  ....*....|....
gi 568955929  561 QKLQAILKPMMLRR 574
Cdd:cd18004   227 QELSELTSRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
353-538 8.66e-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: 138.23  E-value: 8.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLfnWYNRRNC--ILADEMGLGKTIQSITFLYEILLTGI-RGPFLIIAPLSTIANWEREFRTW-TDINV 428
Cdd:cd18000     1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWwPPFRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  429 VVYHGSLISRQMIQQYEMYFRDSQgRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 508
Cdd:cd18000    79 VVLHSSGSGTGSEEKLGSIERKSQ-LIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQ 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 568955929  509 MNLEHKVLLTGTPLQNTVEELFSLLHFLEP 538
Cdd:cd18000   158 LRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
263-321 1.24e-33

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: 124.32  E-value: 1.24e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  263 PDYVEVDRILEVSFCEDKDTGESVIYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 321
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
353-574 6.60e-33

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: 128.62  E-value: 6.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLF-NWYNRRNcILADEMGLGKTIQSITFLY------EILLTGIRGPFLIIAPLSTIANWEREFRTWTD 425
Cdd:cd17999     1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILAsdhhkrANSFNSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  426 ---INVVVYHGSLISRQMIQQYemyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKL 502
Cdd:cd17999    80 nafLKPLAYVGPPQERRRLREQ--------------GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  503 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-------DLK-----TEEQVQKLQAILK-- 568
Cdd:cd17999   146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                  ....*..
gi 568955929  569 -PMMLRR 574
Cdd:cd17999   226 lPFLLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
353-551 1.92e-32

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: 127.41  E-value: 1.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNwllFNWYN----------RRNCILADEMGLGKTIQSITFLYEILLTGIRGP-FLIIAPLSTIANWEREFR 421
Cdd:cd18007     1 LKPHQVEGVR---FLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSrPLVLCPASTLYNWEDEFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  422 TWT------DINVVVYHGSLISRQ---MIQQ-----------YEMyFRDSQGRIIRGAYRFQAIITtfEMILGGCGelna 481
Cdd:cd18007    78 KWLppdlrpLLVLVSLSASKRADArlrKINKwhkeggvlligYEL-FRNLASNATTDPRLKQEFIA--ALLDPGPD---- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  482 idwrCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 551
Cdd:cd18007   151 ----LLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
346-544 3.01e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 3.01e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    346 EYKNGNQLREYQLEGLNWLLFNWynrRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIA-NWEREFRTW- 423
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLg 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    424 --TDINVVVYHGSLISRQMIQQyemyfrdsqgrIIRGayRFQAIITTFEMIL--GGCGELNAIDWRCVIIDEAHRLKNKN 499
Cdd:smart00487   79 psLGLKVVGLYGGDSKREQLRK-----------LESG--KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 568955929    500 --CKLLEGLKLMNLE-HKVLLTGTP---LQNTVEELFSLLHFLEPLRFPSE 544
Cdd:smart00487  146 fgDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
353-551 3.14e-28

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 115.33  E-value: 3.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLnwlLFNWY--------NRRNCILADEMGLGKTIQSITFLYEILLTGIRGP------FLIIAPLSTIANWER 418
Cdd:cd18066     1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  419 EFRTWtdinvvvyhgslISRQMIQQYEMYfRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNK 498
Cdd:cd18066    78 EFQKW------------LGSERIKVFTVD-QDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955929  499 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 551
Cdd:cd18066   145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
179-243 7.64e-28

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: 108.19  E-value: 7.64e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955929  179 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 243
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
353-574 1.04e-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: 113.07  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLfnwynRRN--CILADEMGLGKTIQSITFLY----EilltgirGPFLIIAPLSTIANWEREFRTW--- 423
Cdd:cd18010     1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAAyyreE-------WPLLIVCPSSLRLTWADEIERWlps 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  424 ---TDINVVVyHGSlisrqmiqqyeMYFRDSQGRIirgayrfqaIITTFEMILGGCGELNAIDWRCVIIDEAHRLKN--- 497
Cdd:cd18010    69 lppDDIQVIV-KSK-----------DGLRDGDAKV---------VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNska 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  498 KNCKLLEGLkLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF--------MQEFG-DLKTEEQVQKLQAIL- 567
Cdd:cd18010   128 KRTKAALPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakQGGFGwDYSGSSNLEELHLLLl 206

                  ....*..
gi 568955929  568 KPMMLRR 574
Cdd:cd18010   207 ATIMIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
353-574 1.51e-25

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: 107.56  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRRN-----CILADEMGLGKTIQSITFLYEILLTGIRGPFLI-----IAPLSTIANWEREFRT 422
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  423 WTDINVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAyrfqAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKNKNCKL 502
Cdd:cd18067    81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  503 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LKTEEQVQKLQAIL 567
Cdd:cd18067   157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpilkgrdadasekerQLGEEKLQELISIV 236

                  ....*..
gi 568955929  568 KPMMLRR 574
Cdd:cd18067   237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
675-789 3.52e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 101.90  E-value: 3.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   675 GKLVLIDKLLPKMKagGHKVLIFSQMVRCLDilEDYLIHKR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 753
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568955929   754 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 789
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
375-574 3.03e-23

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: 101.01  E-value: 3.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  375 ILADEMGLGKTIQSITFlyeILLTgirgPFLIIAPLSTIANWEREFRTWTD---INVVVYHGSlisrqmiqqyemyfrdS 451
Cdd:cd18071    52 ILADDMGLGKTLTTISL---ILAN----FTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGG----------------E 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  452 QGRIIRGAYRFQAIITTFEMILG-----GCGELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTV 526
Cdd:cd18071   109 RNRDPKLLSKYDIVLTTYNTLASdfgakGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSP 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955929  527 EELFSLLHFLEPLRFPSESTFMQEFG---DLKTEEQVQKLQAILKPMMLRR 574
Cdd:cd18071   189 KDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
353-574 1.32e-22

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: 98.13  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFNWYNRrnCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVyh 432
Cdd:cd18011     1 PLPHQIDAVLRALRKPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  433 gslISRQMIQQyemyfrdSQGRIIRGAYRFQAIITTFEMILGG---CGELNAIDWRCVIIDEAHRLKNKNCKLLEGL-KL 508
Cdd:cd18011    77 ---LDRETAAQ-------LRRLIGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRyKL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955929  509 MNL-----EHKVLLTGTPLQNTVEELFSLLHFLEPLRFpsesTFMQEFGDLKTEEQVqklqaiLKPMMLRR 574
Cdd:cd18011   147 GRLlakraRHVLLLTATPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
375-839 2.57e-22

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: 105.15  E-value: 2.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  375 ILADEMGLGKTIQSITFLYEILLTGIRgPFLIIAPLSTIANWEREFRTWTDINVVVyhgslISRQMIQQYemyfRDSQGR 454
Cdd:NF038318   51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  455 IIRGAYRFQAIITTFEMILGGCGELNAIDWRCVIIDEAHRLKN--KNCKLLEGL-KLMNLEHKVLLTGTPLQNTVEELFS 531
Cdd:NF038318  121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLDLYG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  532 LLHFLEPLRFPSESTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKKLAPKEETIIEV--ELTNIQKKYY 603
Cdd:NF038318  201 LVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCITVdfELSPDEIELY 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  604 RAI---LEKNFSFlskgagqtNVPN--------------------LVNTMMELRKCCNHPY---LIKGAEEKI--LGEFR 655
Cdd:NF038318  272 VRVnnfLKRDILY--------SIPTsnrtliilvirkllasssfaLAETFEVLKKRLEKLKegtRSANAQEGFdlFWSFV 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  656 DTYNpSASDFHL---------QAMIQSAGKLV--LID-----KLLPKMKAG----------------GHKVLIFSQMVRC 703
Cdd:NF038318  344 EDEI-DESGFEEkqdelytrqKEFIQHEIDEVdaIIDvakriKTNAKVTALktaleiafeyqreegiAQKVVVFTESKRT 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  704 LDILEDYLIHKRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGL 756
Cdd:NF038318  423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSE 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  757 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV-TRNSYEREMFDRASLKLGL--------DKA--VLQ 825
Cdd:NF038318  499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLE 578
                         570
                  ....*....|....
gi 568955929  826 SMSGRDSNVSGIQQ 839
Cdd:NF038318  579 SGTDFEKRVLQIYQ 592
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
374-551 1.42e-21

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: 96.11  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  374 CILADEMGLGKTIQSITFLYEILLTGIRGPF---LIIAPLSTIANWEREFRTWTDIN-----VVVYHGSLISRQ------ 439
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLkdeekIEVNELATYKRPqersyk 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  440 ----------MIQQYEMYFRDSQGRIIRGAYRFQAiitTFEMILGGCGElnaidwRCVIIDEAHRLKNKNCKLLEGLKLM 509
Cdd:cd18068   111 lqrwqeeggvMIIGYDMYRILAQERNVKSREKLKE---IFNKALVDPGP------DFVVCDEGHILKNEASAVSKAMNSI 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568955929  510 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 551
Cdd:cd18068   182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
HELICc smart00490
helicase superfamily c-terminal domain;
705-789 8.12e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.73  E-value: 8.12e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    705 DILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 784
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 568955929    785 CHRIG 789
Cdd:smart00490   78 AGRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
353-574 1.81e-17

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: 84.07  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLfnWYNRRNC---ILADEMGLGKTIQSITFLY--------------EILLTGI---------RGPFLI 406
Cdd:cd18072     1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALILaqkntqnrkeeekeKALTEWEskkdstlvpSAGTLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  407 IAPLSTIANWEREFRTWTD---INVVVYHGSlisrqmiqqyemyFRDSQGRIIRgayRFQAIITTFEMI---LGGCGE-- 478
Cdd:cd18072    79 VCPASLVHQWKNEVESRVAsnkLRVCLYHGP-------------NRERIGEVLR---DYDIVITTYSLVakeIPTYKEes 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  479 ----LNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFgDL 554
Cdd:cd18072   143 rsspLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV-DN 221
                         250       260
                  ....*....|....*....|
gi 568955929  555 KTEEQVQKLQAILKPMMLRR 574
Cdd:cd18072   222 KSRKGGERLNILTKSLLLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
374-551 4.39e-17

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: 82.56  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  374 CILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWtdinvvVYHGSLISRQMIQQYEMYFRDSQG 453
Cdd:cd18069    31 CILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW------LPPPEALPNVRPRPFKVFILNDEH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  454 RiirgAYRFQAIITTFEMILGGCGELNAIDWR------CVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVE 527
Cdd:cd18069   105 K----TTAARAKVIEDWVKDGGVLLMGYEMFRlrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                         170       180
                  ....*....|....*....|....
gi 568955929  528 ELFSLLHFLEPLRFPSESTFMQEF 551
Cdd:cd18069   181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
264-319 3.80e-15

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: 71.45  E-value: 3.80e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  264 DYVEVDRILEVSfcedkDTGESVIYYLVKWCSLPYEDSTWELKEDV---DLAKIEEFEQ 319
Cdd:cd18659     1 EYTIVERIIAHR-----EDDEGVTEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
BRK smart00592
domain in transcription and CHROMO domain helicases;
2040-2084 5.14e-15

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 5.14e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 568955929   2040 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2084
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1966-2006 1.70e-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: 69.46  E-value: 1.70e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568955929  1966 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2006
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
BRK smart00592
domain in transcription and CHROMO domain helicases;
1966-2013 2.42e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 2.42e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568955929   1966 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYvedlgAFIPR 2013
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEY-----EVAPR 43
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2039-2082 2.79e-13

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: 65.99  E-value: 2.79e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568955929  2039 LTGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPE 2082
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
181-243 1.84e-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: 1.84e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955929  181 DAAIVDKILACRtVKKEVSPGVMLDIE--------EFFVKYKNYSYLHCEWATEQQlLKDKRIQQKIKRFK 243
Cdd:cd18660     1 DEDKIEKILDHR-PKGPVEEASLDLTDpdepwderEFLVKWKGKSYLHCTWVTEET-LEQLRGKKKLKNYI 69
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
353-537 1.16e-10

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 63.52  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLfnwYNRRNCILADeMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIAN-WEREFRTW-----TDI 426
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWnhlrnLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  427 NVVVYHGSLISRQMIQQYEMYfrdsqgriirgayrfqaiITTFEMILGGCGELNA-IDWRCVIIDEAHRLKNKNCKllEG 505
Cdd:cd18013    77 SVAVGTERQRSKAANTPADLY------------------VINRENLKWLVNKSGDpWPFDMVVIDELSSFKSPRSK--RF 136
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568955929  506 LKLMNLEHKV----LLTGTPLQNTVEELFSLLHFLE 537
Cdd:cd18013   137 KALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLD 172
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
353-536 2.52e-10

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: 63.52  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  353 LREYQLEGLNWLLFnwynrRNCILADEMGLGKTIQSI----------------------TFLYEILLTGIR----GPFLI 406
Cdd:cd18070     1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLalillhprpdndldaadddsdeMVCCPDCLVAETpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  407 IAPLSTIANWEREFRTWTDINVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAY---RFQ-AIITTFEMILGGCGE---- 478
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYdvlRTElHYAEANRSNRRRRRQkrye 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  479 -----LNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFL 536
Cdd:cd18070   156 appspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFL 218
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
299-898 7.60e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 64.28  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  299 EDSTWELKEDVDLAKIEEFEQLQASRPDTRHLDRPPSNIWKKIEQSREYKNGN-------QLREYQLEGLN-WLLFNWYN 370
Cdd:COG1061    20 LLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDeasgtsfELRPYQQEALEaLLAALERG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  371 RRNCILADEMGLGKTIqsiTFLYEILLTGIRGPFLIIAPLSTIAN-WEREFRTWTDiNVVVYHGSlisrqmiqqyemyfR 449
Cdd:COG1061   100 GGRGLVVAPTGTGKTV---LALALAAELLRGKRVLVLVPRRELLEqWAEELRRFLG-DPLAGGGK--------------K 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  450 DSQGRIIrgayrfqaiITTFEmILGGCGELNAI--DWRCVIIDEAHRLKNKncKLLEGLKLMNLEHKVLLTGTPlqntve 527
Cdd:COG1061   162 DSDAPIT---------VATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP------ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  528 elfsllhfleplrfpsestfmqEFGDLKTEEqVQKLQAILKPMMLRRLKEDveKKLAPKEETIIEVELTNIQKKY--YRA 605
Cdd:COG1061   224 ----------------------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYdaLSE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  606 ILEKNfsflskgagqtnvpnlvntmmelrkccnhpyLIKGAEEKILgefrdtynpsasdfhlqamiqsagklvLIDKLLP 685
Cdd:COG1061   279 RLREA-------------------------------LAADAERKDK---------------------------ILRELLR 300
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  686 KMkAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSkpdSDRFVFLLCTRAGGLGINLTAADT 765
Cdd:COG1061   301 EH-PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDV 376
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  766 CIIFDSDWNPQNDLQAQARCHRIGQNK-AVKVYRLVTRNSYEREMFDRASLKLGLDKavLQSMSGRDSNVSGIQQLSKKE 844
Cdd:COG1061   377 AILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYR--VEFLDEEESEELALLIAVKPA 454
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955929  845 IEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLRRTKTITIESEGRGSTFAKAS 898
Cdd:COG1061   455 LEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEE 508
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
373-520 1.29e-08

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 55.87  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  373 NCILADEMGLGKTIQSITFLYEILLTGiRGPFLIIAPLSTIAN-WEREFRTW--TDINVVVYHGSlisRQMIQQYEMYFR 449
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKK-GKKVLVLVPTKALALqTAERLRELfgPGIRVAVLVGG---SSAEEREKNKLG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955929  450 DSQgriirgayrfqAIITTFEMILGGCGELNAI---DWRCVIIDEAHRL----KNKNCKLLEGLKLMNLEHK-VLLTGT 520
Cdd:cd00046    79 DAD-----------IIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSAT 146
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
267-319 1.50e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 52.58  E-value: 1.50e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568955929   267 EVDRILEVSFCEDKDTgesviYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 319
Cdd:pfam00385    2 EVERILDHRKDKGGKE-----EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
185-247 1.82e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 52.60  E-value: 1.82e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929    185 VDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRiqqKIKRFKLRQA 247
Cdd:smart00298    4 VEKILDHRWKKKGE--------LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
263-317 4.16e-08

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 51.50  E-value: 4.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955929  263 PDYVEVDRILEVSfcEDKDTGesvIYYLVKWCSLPYEDSTWElKEDVDLAKIEEF 317
Cdd:cd18662     1 PEWLQIHRIINHR--VDKDGN---TWYLVKWRDLPYDQSTWE-SEDDDIPDYEKH 49
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
184-243 1.15e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 50.27  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   184 IVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRIqqkIKRFK 243
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFK 50
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
208-229 4.32e-06

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: 46.56  E-value: 4.32e-06
                          10        20
                  ....*....|....*....|..
gi 568955929  208 EFFVKYKNYSYLHCEWATEQQL 229
Cdd:cd18667    45 EFFVKWHGMSYWHCEWVSELQL 66
ResIII pfam04851
Type III restriction enzyme, res subunit;
352-521 5.80e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.44  E-value: 5.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   352 QLREYQLEGL-NWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAP-LSTIANWEREFRTWTDINVV 429
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   430 vyHGSLIS----RQMIQQYEMYF--RDSQGRIIRGAYRfQAIITTFEMIlggcgelnaidwrcvIIDEAHRL-------- 495
Cdd:pfam04851   83 --IGEIISgdkkDESVDDNKIVVttIQSLYKALELASL-ELLPDFFDVI---------------IIDEAHRSgassyrni 144
                          170       180
                   ....*....|....*....|....*...
gi 568955929   496 --KNKNCKLLEglklmnlehkvlLTGTP 521
Cdd:pfam04851  145 leYFKPAFLLG------------LTATP 160
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
267-319 2.75e-05

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 43.23  E-value: 2.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955929  267 EVDRILevsfceDKDTGESVIYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 319
Cdd:cd00024     2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
181-243 5.38e-05

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: 42.56  E-value: 5.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955929  181 DAAIVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLkdKRIQQKIKRFK 243
Cdd:cd18659     1 EYTIVERIIAHREDDEGV--------TEYLVKWKGLPYDECTWESEEDIS--DIFQEAIDEYK 53
CHROMO smart00298
Chromatin organization modifier domain;
267-322 1.21e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 41.82  E-value: 1.21e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955929    267 EVDRILEVSFcedkdTGESVIYYLVKWCSLPYEDSTWELKEDVDLA--KIEEFEQLQA 322
Cdd:smart00298    3 EVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKKKER 55
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
633-806 1.50e-04

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: 46.17  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   633 LRKCC---NHPYLIKgaeekilgefrDTYNPSASDF-----HLqamIQSAGKLV----LIDKLLPKMKAGGHKVLIFSQM 700
Cdd:pfam11496   54 LENLSlvaTHPYLLV-----------DHYMPKSLLLkdepeKL---AYTSGKFLvlndLVNLLIERDRKEPINVAIVARS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   701 VRCLDILEDYLIHKRYLYERIDG-RVRGNLRQAAIDRFSKPDSDRFVFL----LCTRAGGLGINlTAADTCIIFDSDWNP 775
Cdd:pfam11496  120 GKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLLsstgQLTNDDSLLEN-YKFDLIIAFDSSVDT 198
                          170       180       190
                   ....*....|....*....|....*....|.
gi 568955929   776 QNDLQAQARCHRIGQNKAVKVYRLVTRNSYE 806
Cdd:pfam11496  199 SSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
742-794 9.37e-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: 39.99  E-value: 9.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955929  742 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAV 794
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
PTZ00121 PTZ00121
MAEBL; Provisional
4-259 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    4 KKPRKRVESESKQEKANRIISEAIARAKERGERNIPRVMSPENFPSASVEGKEEKRGRRMKSKPKDRDNKKPKTYSKLKE 83
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   84 KTKIGKLIITLGKKHKRRNESSDELSDAEQRSQHTFKEQHSQKRRSNRQIKRKKYAED---AEGKQSEEEVKGSLRVKRN 160
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkAEEKKKADELKKAEELKKA 1560
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929  161 SAPPPGEQplqlfvENPSEEDAAIVDKI--LACRTVKKEVSPGVMLDIEEFFVKYKNYSYLHCEWATEQQLLKDKRIQQK 238
Cdd:PTZ00121 1561 EEKKKAEE------AKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
                         250       260
                  ....*....|....*....|....
gi 568955929  239 IKRFKLRQAQ---RAHFLADMEEE 259
Cdd:PTZ00121 1635 VEQLKKKEAEekkKAEELKKAEEE 1658
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
207-243 1.31e-03

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


Pssm-ID: 349313  Cd Length: 85  Bit Score: 39.97  E-value: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568955929  207 EEFFVKYKNYSYLHCEWATEQQLLkdkriQQKIKRFK 243
Cdd:cd18666    47 IQYLIKWKGWSHIHNTWESEESLK-----DQNVKGMK 78
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
264-309 1.86e-03

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: 38.41  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568955929  264 DYVEVDRILEVSFCEDKDtGESVIYYLVKWCSLPYEDSTWELKEDV 309
Cdd:cd18664     1 EFHVVERIIASQRASLED-GTSQLQYLVKWRRLNYDECTWEDATLI 45
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
267-310 1.94e-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: 349322  Cd Length: 49  Bit Score: 38.03  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568955929  267 EVDRILevsfCEDKDTGEsvIYYLVKWCSLPYEDSTWELKEDVD 310
Cdd:cd18966     2 EVERIL----AERRDDGG--KRYLVKWEGYPLEEATWEPEENIG 39
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
278-319 2.26e-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: 38.08  E-value: 2.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568955929  278 EDKDTGESVIYYLVKWCSLPYEDSTWELKEDV-DLAK-IEEFEQ 319
Cdd:cd18964    11 PSARDGPGKFLWLVKWDGYPIEDATWEPPENLgEHAKlIEDFEK 54
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
3-183 3.19e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929    3 EKKPRKRVESESKQEKANRIISEAIARAKER--GERNIPR-VMSPENFPSASVEGKEEKRGRRMKSKPKDRDNKKPKTYS 79
Cdd:NF033838  258 QDKPKRRAKRGVLGEPATPDKKENDAKSSDSsvGEETLPSpSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYK 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   80 KLK-------EKTKIGKLIITLGKKHKRRNESSDELSDAEQRSqhtfkEQHSQKRRSNRQIKRKKYAEDAEGKQSEEE-V 151
Cdd:NF033838  338 TLEleiaesdVKVKEAELELVKEEAKEPRNEEKIKQAKAKVES-----KKAEATRLEKIKTDRKKAEEEAKRKAAEEDkV 412
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568955929  152 KGSLRVKRNSAPPPGEQPLQLFVENPSEEDAA 183
Cdd:NF033838  413 KEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKA 444
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
267-317 4.70e-03

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. 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: 349285  Cd Length: 57  Bit Score: 37.29  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955929  267 EVDRILEVSFCEDKDTGESVIYYLVKWCSLPYEDSTWELKEDVD--LAKIEEF 317
Cdd:cd18635     3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSncPEKIKEF 55
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
354-529 5.27e-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: 39.92  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   354 REYQLEGLNWLLfnwyNRRNCILADEMGLGKTIQSITFLYEILLTGIRGP-FLIIAPLSTIAN-WEREFRTW---TDINV 428
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEqIYEELKKLgkgLGLKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955929   429 V-VYHGSLISRQMiqqyemyfrdsqgRIIRGAyrfQAIITTFEMILGGCGELNAI-DWRCVIIDEAHRLKNKN--CKLLE 504
Cdd:pfam00270   77 AsLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQERKLLkNLKLLVLDEAHRLLDMGfgPDLEE 140
                          170       180
                   ....*....|....*....|....*.
gi 568955929   505 GLKLMNLEHK-VLLTGTPLQNtVEEL 529
Cdd:pfam00270  141 ILRRLPKKRQiLLLSATLPRN-LEDL 165
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
264-318 6.28e-03

chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 3 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349278  Cd Length: 51  Bit Score: 36.98  E-value: 6.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955929  264 DYVEVDRILEVSFCEDKDTGEsviyYLVKWcsLPYEDSTWELKEDVDLAKIEEFE 318
Cdd:cd18628     2 EYAVAESVIGKRVGDDGKTIE----YLVKW--TDMSDATWEPQDNVDSTLVLLYQ 50
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
273-314 9.54e-03

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. 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: 349289  Cd Length: 49  Bit Score: 36.34  E-value: 9.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568955929  273 EVSFCEDKDTGESVIYYLVKWCSLPYEDSTWELKEDVDLAKI 314
Cdd:cd18639     2 EVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLKCSRL 43
 
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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