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Conserved domains on  [gi|1958747496|ref|XP_038953992|]
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chromodomain-helicase-DNA-binding protein 9 isoform X5 [Rattus norvegicus]

Protein Classification

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; ...
386-607 2.19e-149

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: 462.17  E-value: 2.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
385-1006 5.54e-148

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: 489.70  E-value: 5.54e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEvlLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 460
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  461 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLK 540
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  541 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKRLA 617
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  618 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKiigefrdtyNPSASD 697
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  698 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 777
Cdd:PLN03142   464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  778 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 857
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  858 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGCGSTFAKASFVASG 936
Cdd:PLN03142   621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  937 NRTDISLDDpnfwQKWAKKAELDLDAISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 1006
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, ...
296-354 8.30e-34

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


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 124.71  E-value: 8.30e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  296 PDYVEVDRILEVSFCEDKDTGESVVYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 354
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, ...
212-276 3.24e-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: 109.35  E-value: 3.24e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747496  212 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 276
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
BRK smart00592
domain in transcription and CHROMO domain helicases;
2060-2104 4.47e-15

domain in transcription and CHROMO domain helicases;


:

Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 4.47e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1958747496  2060 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2104
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1986-2026 1.52e-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: 1.52e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958747496 1986 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2026
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
CDC27 super family cl25760
DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It ...
3-202 3.61e-05

DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It carries the essential residues for binding to the Pol1 subunit of polymerase alpha, from residues 293-332, which are characterized by the motif D--G--VT, referred to as the DPIM motif. The first 160 residues of the protein form the minimal domain for binding to the B subunit, Cdc1, of polymerase delta, the final 10 C-terminal residues, 362-372, being the DNA sliding clamp, PCNA, binding motif.


The actual alignment was detected with superfamily member pfam09507:

Pssm-ID: 462819 [Multi-domain]  Cd Length: 427  Bit Score: 48.66  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496    3 SVKRPRGRPPSSKKSDGSGTYSRLQ-NTQVRVMSEKKPRKKAESESKQEKANRIISEAIARAKERGERNIPRVMSPENFP 81
Cdd:pfam09507  200 SVKAPSLKRSPSAKSNIMSAFFKAKpKNKKKKTSASEQKVQEESAEESGKEDVTLEDDSAAEEEEDEQLPTKKDKRRQKR 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   82 SSSVDGKEEKRAQRvksKPKDRDNRKPKACSKLKEKTKIgklIITLGKNHKRRSESSDELSDAEQMPQHTFKEQHSQKRR 161
Cdd:pfam09507  280 GESSDSEESTRESR---KEKRERLKKMMEDDSDDDEMED---VPESPVATEEEETGSPPPLLKKEVEKEEVTESGDGRRR 353
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958747496  162 SNRQVKRKKYAEDAEGRQCEEEVRGS---------LKVKRTSAPPPGEQP 202
Cdd:pfam09507  354 KRRKVMKKKTFKDEEGYMVTEKVYEWesfsededePPVKPKPAVSTPASP 403
 
Name Accession Description Interval E-value
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
386-607 2.19e-149

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: 462.17  E-value: 2.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
385-1006 5.54e-148

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 489.70  E-value: 5.54e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEvlLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 460
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  461 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLK 540
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  541 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKRLA 617
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  618 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKiigefrdtyNPSASD 697
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  698 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 777
Cdd:PLN03142   464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  778 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 857
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  858 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGCGSTFAKASFVASG 936
Cdd:PLN03142   621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  937 NRTDISLDDpnfwQKWAKKAELDLDAISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 1006
Cdd:PLN03142   693 TAELYDFDD----EDDKDENKLDFKKIVSDNW--IDPPK-RERKRNYSESeyfKQAMRQGAPAKPKEPRIPRM 758
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
385-858 1.85e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.06  E-value: 1.85e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEmyfrdsqgriirgayRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:COG0553    321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKRLAPKE 620
Cdd:COG0553    386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  621 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNVPNLVNTMMELRKCCNHPYLIKGAEEKIIGEfrdtynpsasdfhl 700
Cdd:COG0553    466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------- 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  701 qamiqsAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 780
Cdd:COG0553    532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747496  781 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVLQ 858
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-676 1.43e-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: 276.49  E-value: 1.43e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  389 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYEVLLTGI--RGPFLIIAPLSTIANWEREFRTWT---DINVV 462
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 VYHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLM 542
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  543 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKRLAP 618
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  619 KEETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGQTNVPNLVNTMMELRKCCNHPYLI 676
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
708-833 5.72e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.15  E-value: 5.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  708 GKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 787
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958747496  788 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV 833
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, ...
296-354 8.30e-34

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 124.71  E-value: 8.30e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  296 PDYVEVDRILEVSFCEDKDTGESVVYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 354
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
379-577 2.91e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 2.91e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   379 EYKNGNQLREYQLEGLNWLLFNWynrRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIA-NWEREFRTW- 456
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLg 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   457 --TDINVVVYHGSLISRQMIQQyemyfrdsqgrIIRGayRFQAIITTFEMIL--GGCGELNAIEWRCVIIDEAHRLKNKN 532
Cdd:smart00487   79 psLGLKVVGLYGGDSKREQLRK-----------LESG--KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958747496   533 --CKLLEGLKLMNLE-HKVLLTGTP---LQNTVEELFSLLHFLEPLRFPSE 577
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, ...
212-276 3.24e-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: 109.35  E-value: 3.24e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747496  212 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 276
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
708-822 1.74e-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: 103.06  E-value: 1.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  708 GKLVLIDKLLPKMKagGHKVLIFSQMVRCLDilEDYLIHKR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 786
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958747496  787 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 822
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 ...
408-872 3.56e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 108.23  E-value: 3.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  408 ILADEMGLGKTIQSITFLYEVLLTGIRgPFLIIAPLSTIANWEREFRTWTDINVVVyhgslISRQMIQQYemyfRDSQGR 487
Cdd:NF038318    51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  488 IIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKN--KNCKLLEGL-KLMNLEHKVLLTGTPLQNTVEELFS 564
Cdd:NF038318   121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLDLYG 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  565 LLHFLEPLRFPSESTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKRLAPKEETIIEV--ELTNIQKKYY 636
Cdd:NF038318   201 LVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCITVdfELSPDEIELY 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  637 RAI---LEKNFSFlskgagqtNVPN--------------------LVNTMMELRKCCNHPY---LIKGAEEKI--IGEFR 688
Cdd:NF038318   272 VRVnnfLKRDILY--------SIPTsnrtliilvirkllasssfaLAETFEVLKKRLEKLKegtRSANAQEGFdlFWSFV 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  689 DTYNpSASDFHL---------QAMIQSAGKLV--LID-----KLLPKMKAG----------------GHKVLIFSQMVRC 736
Cdd:NF038318   344 EDEI-DESGFEEkqdelytrqKEFIQHEIDEVdaIIDvakriKTNAKVTALktaleiafeyqreegiAQKVVVFTESKRT 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  737 LDILEDYLIHKRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGL 789
Cdd:NF038318   423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSE 498
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  790 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV-TRNSYEREMFDRASLKLGL--------DKA--VLQ 858
Cdd:NF038318   499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLE 578
                          570
                   ....*....|....
gi 1958747496  859 SMSGRDSNVSGIQQ 872
Cdd:NF038318   579 SGTDFEKRVLQIYQ 592
HELICc smart00490
helicase superfamily c-terminal domain;
738-822 5.33e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.11  E-value: 5.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   738 DILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 817
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958747496   818 CHRIG 822
Cdd:smart00490   78 AGRAG 82
BRK smart00592
domain in transcription and CHROMO domain helicases;
2060-2104 4.47e-15

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 4.47e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1958747496  2060 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2104
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1986-2026 1.52e-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: 1.52e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958747496 1986 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2026
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
BRK smart00592
domain in transcription and CHROMO domain helicases;
1986-2033 2.11e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 2.11e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1958747496  1986 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYvedlgAFIPR 2033
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEY-----EVAPR 43
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2059-2102 2.55e-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: 2.55e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958747496 2059 LTGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPE 2102
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
300-352 5.42e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.12  E-value: 5.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  300 EVDRILEVSFCEDKdtgesVVYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 352
Cdd:pfam00385    2 EVERILDHRKDKGG-----KEEYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
218-280 1.08e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 53.37  E-value: 1.08e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496   218 VDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRiqqKIKRFKLRQA 280
Cdd:smart00298    4 VEKILDHRWKKKGE--------LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
217-276 7.62e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 50.65  E-value: 7.62e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  217 IVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRIqqkIKRFK 276
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFK 50
DpdE NF041062
protein DpdE;
409-575 2.25e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 49.97  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  409 LADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREfrtwtdinvvvyhgsLISRQMIQQyemyFRDSQGRI 488
Cdd:NF041062   175 LADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDALVRQWRRE---------------LRDKFFLDD----FPGARVRV 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  489 IRgayrfQAIITTFEMILGGCGelnaiewrCVIIDEAHRLKNKNCKLLEGLK-----LMNLEHKV----LLTGTPLQNTV 559
Cdd:NF041062   236 LS-----HEEPERWEPLLDAPD--------LLVVDEAHQLARLAWSGDPPERaryreLAALAHAAprllLLSATPVLGNE 302
                          170
                   ....*....|....*.
gi 1958747496  560 EELFSLLHFLEPLRFP 575
Cdd:NF041062   303 ETFLALLHLLDPDLYP 318
CDC27 pfam09507
DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It ...
3-202 3.61e-05

DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It carries the essential residues for binding to the Pol1 subunit of polymerase alpha, from residues 293-332, which are characterized by the motif D--G--VT, referred to as the DPIM motif. The first 160 residues of the protein form the minimal domain for binding to the B subunit, Cdc1, of polymerase delta, the final 10 C-terminal residues, 362-372, being the DNA sliding clamp, PCNA, binding motif.


Pssm-ID: 462819 [Multi-domain]  Cd Length: 427  Bit Score: 48.66  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496    3 SVKRPRGRPPSSKKSDGSGTYSRLQ-NTQVRVMSEKKPRKKAESESKQEKANRIISEAIARAKERGERNIPRVMSPENFP 81
Cdd:pfam09507  200 SVKAPSLKRSPSAKSNIMSAFFKAKpKNKKKKTSASEQKVQEESAEESGKEDVTLEDDSAAEEEEDEQLPTKKDKRRQKR 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   82 SSSVDGKEEKRAQRvksKPKDRDNRKPKACSKLKEKTKIgklIITLGKNHKRRSESSDELSDAEQMPQHTFKEQHSQKRR 161
Cdd:pfam09507  280 GESSDSEESTRESR---KEKRERLKKMMEDDSDDDEMED---VPESPVATEEEETGSPPPLLKKEVEKEEVTESGDGRRR 353
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958747496  162 SNRQVKRKKYAEDAEGRQCEEEVRGS---------LKVKRTSAPPPGEQP 202
Cdd:pfam09507  354 KRRKVMKKKTFKDEEGYMVTEKVYEWesfsededePPVKPKPAVSTPASP 403
CHROMO smart00298
Chromatin organization modifier domain;
300-355 5.58e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 5.58e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747496   300 EVDRILEVSFcedkdTGESVVYYLVKWCSLPYEDSTWELKEDVDLA--KIEEFEQLQA 355
Cdd:smart00298    3 EVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKKKER 55
PTZ00121 PTZ00121
MAEBL; Provisional
37-292 2.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   37 KKPRKKAESESKQEKANRIISEAIARAKERGERNIPRVMSPENFPSSSVDGKEEKRAQRVKSKPKDRDNRKpkaCSKLKE 116
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---ADEAKK 1477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  117 KTKIGKLIITLGKNHKRRSESSDELSDAEQMPQHTFKEQHSQKRRSNRQVKRKKYAEDAEGRQCEEEVRGSLKVKRTSAP 196
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  197 PPGEQPLQLFVENPSEEDAAIVDKI--LACRTVKKEVSPGVMLDIEEFFVKYKNYSYLHCEWATEQQLLKDKRIQQKIKR 274
Cdd:PTZ00121  1558 KKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                          250       260
                   ....*....|....*....|.
gi 1958747496  275 FKLRQAQ---RAHFLADMEEE 292
Cdd:PTZ00121  1638 LKKKEAEekkKAEELKKAEEE 1658
 
Name Accession Description Interval E-value
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
386-607 2.19e-149

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: 462.17  E-value: 2.19e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
385-1006 5.54e-148

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 489.70  E-value: 5.54e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT---FLYEvlLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 460
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISllgYLHE--YRGITGPHMVVAPKSTLGNWMNEIRRFCPvLR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  461 VVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLK 540
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV-----------AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  541 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKRLA 617
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  618 PKEETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNvpnLVNTMMELRKCCNHPYLIKGAEEKiigefrdtyNPSASD 697
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG---------PPYTTG 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  698 FHLqamIQSAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDR 777
Cdd:PLN03142   464 EHL---VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  778 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVL 857
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  858 QsmSGRdsnvsgIQQLSKKEIEDLLRRGAYGAIMEEEDEGSKFCEEDIDQILLR-RTKTITIESEGCGSTFAKASFVASG 936
Cdd:PLN03142   621 Q--QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDD 692
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  937 NRTDISLDDpnfwQKWAKKAELDLDAISGRNSlvIDTPRiRKQTRPFSAT---KDELAELSEAESEGEEKPKL 1006
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; ...
386-607 3.16e-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: 447.47  E-value: 3.16e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLT-GIRGPFLIIAPLSTIANWEREFRTWTDINVVVY 464
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  465 HGSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNL 544
Cdd:cd17995     81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  545 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
386-607 2.35e-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: 427.92  E-value: 2.35e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
386-607 6.40e-132

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: 412.50  E-value: 6.40e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18059     81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
386-607 1.88e-131

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: 410.98  E-value: 1.88e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVYH 465
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 545
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  546 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
385-858 1.85e-120

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 398.06  E-value: 1.85e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEmyfrdsqgriirgayRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:COG0553    321 LDGTRERAKGANPFE---------------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKRLAPKE 620
Cdd:COG0553    386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  621 ETIIEVELTNIQKKYYRAILEKNFSFLSKGAGQTNVPNLVNTMMELRKCCNHPYLIKGAEEKIIGEfrdtynpsasdfhl 700
Cdd:COG0553    466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------- 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  701 qamiqsAGKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVF 780
Cdd:COG0553    532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVF 604
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747496  781 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLVTRNSYEREMFDRASLKLGLDKAVLQ 858
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
389-676 1.43e-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: 276.49  E-value: 1.43e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  389 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYEVLLTGI--RGPFLIIAPLSTIANWEREFRTWT---DINVV 462
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 VYHGSLISRQMIQQYEMYFRDsqgriirgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLM 542
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  543 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKRLAP 618
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  619 KEETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGQTNVPNLVNTMMELRKCCNHPYLI 676
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
385-607 6.39e-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: 266.14  E-value: 6.39e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLT-GIRGPFLIIAPLSTIANWEREFRTWT-DINVV 462
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 VYHGSLISRQMIQQYEMYFrdSQGRIIRgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLM 542
Cdd:cd17993     81 VYLGDIKSRDTIREYEFYF--SQTKKLK----FNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  543 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFmQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd17993    155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
386-573 4.62e-74

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: 244.78  E-value: 4.62e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGkERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEmyfrdsqgriirGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:cd17919     81 YHGSQRERAQIRAKE------------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEP---LR 573
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; ...
386-607 2.58e-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: 234.64  E-value: 2.58e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSlisrqmiqqyemyfrdsqgriirgayrfQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:cd17994     81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
383-609 1.80e-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: 233.82  E-value: 1.80e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  383 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINV 461
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  462 VVYHGSLISRQMIQQyEMYFRDSQGRIirgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKL 541
Cdd:cd18009     81 LLYHGTKEERERLRK-KIMKREGTLQD------FPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  542 MNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-----------DLKTEEQ----VQKLQAILKPMMLR 606
Cdd:cd18009    154 FNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLR 233

                   ...
gi 1958747496  607 RLK 609
Cdd:cd18009    234 RLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
383-609 1.02e-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: 225.28  E-value: 1.02e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  383 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DIN 460
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLgYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  461 VVVYHGSLISRQMIqqyemyFRDsqgRIIRGayRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLK 540
Cdd:cd17997     81 VVVLIGDKEERADI------IRD---VLLPG--KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  541 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF----GDLKTEEQVQKLQAILKPMMLRRLK 609
Cdd:cd17997    150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
386-607 5.22e-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: 223.73  E-value: 5.22e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKL 535
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  536 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
386-607 4.14e-65

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: 221.09  E-value: 4.14e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKL 535
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  536 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
357-607 6.84e-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: 220.65  E-value: 6.84e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  357 RPDTRQLDRPPSNIWKKidqsreyknGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRG 435
Cdd:cd18054      1 RPRFVALKKQPSYIGGE---------NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLsYLFHQHQLYG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  436 PFLIIAPLSTIANWEREFRTWT-DINVVVYHGSLISRQMIQQYEMYFRDSQgRIirgayRFQAIITTFEMILGGCGELNA 514
Cdd:cd18054     72 PFLLVVPLSTLTSWQREFEIWApEINVVVYIGDLMSRNTIREYEWIHSQTK-RL-----KFNALITTYEILLKDKTVLGS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  515 IEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQ 594
Cdd:cd18054    146 INWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQ 224
                          250
                   ....*....|...
gi 1958747496  595 KLQAILKPMMLRR 607
Cdd:cd18054    225 SLHKVLEPFLLRR 237
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
386-607 8.95e-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: 220.32  E-value: 8.95e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTG-IRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKL 535
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFEDNAIRGGKKASRmkkeasvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958747496  536 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
383-609 5.01e-64

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: 218.01  E-value: 5.01e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  383 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSI---TFLYEVllTGIRGPFLIIAPLSTIANWEREFRTWT-D 458
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  459 INVVVYHGSLISRQMIQQYEMyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEG 538
Cdd:cd17996     79 VSKIVYKGTPDVRKKLQSQIR------------AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQT 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  539 LKLM-NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG------------DLKTEEQV---QKLQAILKP 602
Cdd:cd17996    147 LNTYyHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRP 226

                   ....*..
gi 1958747496  603 MMLRRLK 609
Cdd:cd17996    227 FLLRRLK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
708-833 5.72e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 191.15  E-value: 5.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  708 GKLVLIDKLLPKMKAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 787
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958747496  788 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV 833
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
384-609 4.01e-55

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 192.01  E-value: 4.01e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  384 NQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVV 462
Cdd:cd18012      3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 VYHGSLISRQMIQQYEMYfrdsqgriirgayrfQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLM 542
Cdd:cd18012     83 VIHGTKRKREKLRALEDY---------------DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958747496  543 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLK 609
Cdd:cd18012    148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
386-607 6.87e-54

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: 188.42  E-value: 6.87e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVV 463
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLwYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:cd18006     81 YMGDKEKRLDLQQD-----------IKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 607
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 ...
386-607 4.09e-52

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: 183.71  E-value: 4.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREFRTWTD-INVVV 463
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLaHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  464 YHGSLISRQMIQQyEMYFRDSqgriirgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMN 543
Cdd:cd18003     81 YYGSAKERKLKRQ-GWMKPNS----------FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958747496  544 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF----------MQEFGDLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18003    150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpltaMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
383-607 2.33e-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: 182.17  E-value: 2.33e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  383 GNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREFRTWTD-IN 460
Cdd:cd18053     18 GLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPqMN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  461 VVVYHGSLISRQMIQQYEmYFRDSQGRIirgayRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLK 540
Cdd:cd18053     98 AVVYLGDINSRNMIRTHE-WMHPQTKRL-----KFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLI 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747496  541 LMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQKLQAILKPMMLRR 607
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 ...
386-607 3.61e-51

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: 181.81  E-value: 3.61e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLlFNWY-NRRNCILADEMGLGKTIQSITFLYEVL-LTGIR--------------------GPFLIIAPL 443
Cdd:cd18005      1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLgKTGTRrdrennrprfkkkppassakKPVLIVAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  444 STIANWEREFRTWTDINVVVYHGSLISRqmiqqyemyfrDSQGRIIRGAYrfQAIITTFEMILGGCGELNAIEWRCVIID 523
Cdd:cd18005     80 SVLYNWKDELDTWGHFEVGVYHGSRKDD-----------ELEGRLKAGRL--EVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  524 EAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LK 588
Cdd:cd18005    147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                          250
                   ....*....|....*....
gi 1958747496  589 TEEQVQKLQAILKPMMLRR 607
Cdd:cd18005    227 GRKRKQELAVKLSKFFLRR 245
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
386-607 2.47e-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: 175.77  E-value: 2.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLfNWYNRR-NCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREF-RTWTDINVV 462
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLaHLAEEHNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 VYHGSLISRQMIQQY----EMYFRDSQgriirgayrFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEG 538
Cdd:cd18002     80 PYWGNPKDRKVLRKFwdrkNLYTRDAP---------FHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  539 LKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-DLKT---------EEQVQKLQAILKPMMLRR 607
Cdd:cd18002    151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
386-574 6.47e-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: 172.95  E-value: 6.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVVY 464
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  465 HGSLISRqmiqqyemyfRDSQGRIIRGAYRFQAIITTFEMILGGCGE---LNAIEWRCVIIDEAHRLKNKNCKLLEGLKL 541
Cdd:cd17998     81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958747496  542 MNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRF 574
Cdd:cd17998    151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
370-609 4.93e-46

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: 167.14  E-value: 4.93e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  370 IWKKIDQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIAN 448
Cdd:cd18062      8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRINGPFLIIVPLSTLSN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  449 WEREFRTWTDINV-VVYHGSLISRQMIQQyemyfrdsqgrIIRGAyRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHR 527
Cdd:cd18062     88 WVYEFDKWAPSVVkVSYKGSPAARRAFVP-----------QLRSG-KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  528 LKNKNCKLLEGLKLMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---V 593
Cdd:cd18062    156 MKNHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliI 235
                          250
                   ....*....|....*.
gi 1958747496  594 QKLQAILKPMMLRRLK 609
Cdd:cd18062    236 RRLHKVLRPFLLRRLK 251
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
373-620 5.74e-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: 163.68  E-value: 5.74e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  373 KIDQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWER 451
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  452 EFRTWTDINVVVyhgSLISRQmiQQYEMYFRDSqgrIIRGAYrfQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNK 531
Cdd:cd18064     83 EFKRWVPTLRAV---CLIGDK--DQRAAFVRDV---LLPGEW--DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  532 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRRL 608
Cdd:cd18064    153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRI 232
                          250
                   ....*....|..
gi 1958747496  609 KEDVEKRLAPKE 620
Cdd:cd18064    233 KADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
376-609 1.48e-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: 160.23  E-value: 1.48e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  376 QSREYKNGNqLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWEREFR 454
Cdd:cd18063     15 QSSLLINGT-LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  455 TWT-DINVVVYHGS-LISRQMIQQYEmyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKN 532
Cdd:cd18063     94 KWApSVVKISYKGTpAMRRSLVPQLR-------------SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  533 CKLLEGLKLMNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQA 598
Cdd:cd18063    161 CKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHK 240
                          250
                   ....*....|.
gi 1958747496  599 ILKPMMLRRLK 609
Cdd:cd18063    241 VLRPFLLRRLK 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
386-607 2.88e-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: 158.99  E-value: 2.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFnwynrRNCILADEMGLGKTIQSI----------------TFLYEVLLTGIR--GPFLIIAPLSTIA 447
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALalilatrpqdpkipeeLEENSSDPKKLYlsKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  448 NWEREFRTWTD---INVVVYHGSlisrqmiqqyemyfrdSQGRIIRGAYRFQAIITTFEMI----------------LGG 508
Cdd:cd18008     76 QWKDEIEKHTKpgsLKVYVYHGS----------------KRIKSIEELSDYDIVITTYGTLasefpknkkgggrdskEKE 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  509 CGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLK 588
Cdd:cd18008    140 ASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                          250       260
                   ....*....|....*....|..
gi 1958747496  589 TE---EQVQKLQAILKPMMLRR 607
Cdd:cd18008    220 SKndrKALERLQALLKPILLRR 241
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
373-609 9.26e-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: 154.41  E-value: 9.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  373 KIDQSREYKNGNQLREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEVLLTGIRGPFLIIAPLSTIANWER 451
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  452 EFRTWT-DINVVVYHGSLISRQMIQQYEMYfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKN 530
Cdd:cd18065     83 EFKRWVpSLRAVCLIGDKDARAAFIRDVMM-----------PGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  531 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---LKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                   ..
gi 1958747496  608 LK 609
Cdd:cd18065    232 IK 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
386-607 1.56e-41

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 153.68  E-value: 1.56e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWT-DINVVVY 464
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTpGLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  465 HGSLISRQmiqqyemyfRDSQGRIIRGayrFQAIITTFEMILGGCGELNAIE-----WRCVIIDEAHRLKNKNCKLLEGL 539
Cdd:cd18001     81 HGTSKKER---------ERNLERIQRG---GGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  540 KLMNLEHKVLLTGTPLQNTVEELFSLLHFLEP-LRFPSESTFMQEF------GDLKTEEQVQK---------LQAILKPM 603
Cdd:cd18001    149 REIPAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFenpitrGRDKDATQGEKalgsevaenLRQIIKPY 228

                   ....
gi 1958747496  604 MLRR 607
Cdd:cd18001    229 FLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
386-607 6.35e-38

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: 143.20  E-value: 6.35e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLL-----FNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGP-----FLIIAPLSTIANWEREFRT 455
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  456 W---TDINVVVYHGSLISRQMIQQYEMYFRdsqgriirgayRFQAIITTFEMILGGCGELNAIEwRC--VIIDEAHRLKN 530
Cdd:cd18004     81 WlglRRIKVVTADGNAKDVKASLDFFSSAS-----------TYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  531 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD--LK------TEEQV-------QK 595
Cdd:cd18004    149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpiLRsrdpdaSEEDKelgaersQE 228
                          250
                   ....*....|..
gi 1958747496  596 LQAILKPMMLRR 607
Cdd:cd18004    229 LSELTSRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
386-571 2.22e-36

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 137.07  E-value: 2.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLfnWYNRRNC--ILADEMGLGKTIQSITFLYEVLLTGI-RGPFLIIAPLSTIANWEREFRTW-TDINV 461
Cdd:cd18000      1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFLAALHHSKLgLGPSLIVCPATVLKQWVKEFHRWwPPFRV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  462 VVYHGSLISRQMIQQYEMYFRDSQgRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKL 541
Cdd:cd18000     79 VVLHSSGSGTGSEEKLGSIERKSQ-LIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQ 157
                          170       180       190
                   ....*....|....*....|....*....|
gi 1958747496  542 MNLEHKVLLTGTPLQNTVEELFSLLHFLEP 571
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, ...
296-354 8.30e-34

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 124.71  E-value: 8.30e-34
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  296 PDYVEVDRILEVSFCEDKDTGESVVYYLVKWCSLPYEDSTWELKEDVDLAKIEEFEQLQ 354
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
386-607 4.79e-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: 129.01  E-value: 4.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLF-NWYNRRNcILADEMGLGKTIQSITFLY------EVLLTGIRGPFLIIAPLSTIANWEREFRTWTD 458
Cdd:cd17999      1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILAsdhhkrANSFNSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  459 ---INVVVYHGSLISRQMIQQYemyfrdsqgriirgAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKL 535
Cdd:cd17999     80 nafLKPLAYVGPPQERRRLREQ--------------GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  536 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-------DLK-----TEEQVQKLQAILK-- 601
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                   ....*..
gi 1958747496  602 -PMMLRR 607
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 ...
386-584 1.17e-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: 128.18  E-value: 1.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNwllFNWYN----------RRNCILADEMGLGKTIQSITFLYEVLLTGIRGP-FLIIAPLSTIANWEREFR 454
Cdd:cd18007      1 LKPHQVEGVR---FLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSrPLVLCPASTLYNWEDEFK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  455 TWT------DINVVVYHGSLISRQ---MIQQ-----------YEMyFRDSQGRIIRGAYRFQAIITtfEMILGGCGelna 514
Cdd:cd18007     78 KWLppdlrpLLVLVSLSASKRADArlrKINKwhkeggvlligYEL-FRNLASNATTDPRLKQEFIA--ALLDPGPD---- 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  515 iewrCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 584
Cdd:cd18007    151 ----LLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
379-577 2.91e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.99  E-value: 2.91e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   379 EYKNGNQLREYQLEGLNWLLFNWynrRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIA-NWEREFRTW- 456
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLg 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   457 --TDINVVVYHGSLISRQMIQQyemyfrdsqgrIIRGayRFQAIITTFEMIL--GGCGELNAIEWRCVIIDEAHRLKNKN 532
Cdd:smart00487   79 psLGLKVVGLYGGDSKREQLRK-----------LESG--KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGG 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1958747496   533 --CKLLEGLKLMNLE-HKVLLTGTP---LQNTVEELFSLLHFLEPLRFPSE 577
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, ...
212-276 3.24e-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: 109.35  E-value: 3.24e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747496  212 EEDAAIVDKILACRTVKKEVSPGV-MLDIEEFFVKYKNYSYLHCEWATEQQLLK-DKRIQQKIKRFK 276
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGAeEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFK 67
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
386-584 3.51e-28

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 114.94  E-value: 3.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLnwlLFNWY--------NRRNCILADEMGLGKTIQSITFLYEVLLTGIRGP------FLIIAPLSTIANWER 451
Cdd:cd18066      1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  452 EFRTWtdinvvvyhgslISRQMIQQYEMYfRDSQGRIIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNK 531
Cdd:cd18066     78 EFQKW------------LGSERIKVFTVD-QDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  532 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 584
Cdd:cd18066    145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
386-607 2.28e-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: 111.91  E-value: 2.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLfnwynRRN--CILADEMGLGKTIQSITFLY----EvlltgirGPFLIIAPLSTIANWEREFRTW--- 456
Cdd:cd18010      1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAAyyreE-------WPLLIVCPSSLRLTWADEIERWlps 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  457 ---TDINVVVyHGSlisrqmiqqyeMYFRDSQGRIirgayrfqaIITTFEMILGGCGELNAIEWRCVIIDEAHRLKN--- 530
Cdd:cd18010     69 lppDDIQVIV-KSK-----------DGLRDGDAKV---------VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNska 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  531 KNCKLLEGLkLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF--------MQEFG-DLKTEEQVQKLQAIL- 600
Cdd:cd18010    128 KRTKAALPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakQGGFGwDYSGSSNLEELHLLLl 206

                   ....*..
gi 1958747496  601 KPMMLRR 607
Cdd:cd18010    207 ATIMIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
386-607 5.78e-26

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 109.10  E-value: 5.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRRN-----CILADEMGLGKTIQSITFLYEVLLTGIRGPFLI-----IAPLSTIANWEREFRT 455
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  456 WTDINVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAyrfqAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKNKNCKL 535
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  536 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD---------------LKTEEQVQKLQAIL 600
Cdd:cd18067    157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELpilkgrdadasekerQLGEEKLQELISIV 236

                   ....*..
gi 1958747496  601 KPMMLRR 607
Cdd:cd18067    237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
708-822 1.74e-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: 103.06  E-value: 1.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  708 GKLVLIDKLLPKMKagGHKVLIFSQMVRCLDilEDYLIHKR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 786
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958747496  787 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 822
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
408-607 2.29e-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: 101.39  E-value: 2.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  408 ILADEMGLGKTIQSITFlyeVLLTgirgPFLIIAPLSTIANWEREFRTWTD---INVVVYHGSlisrqmiqqyemyfrdS 484
Cdd:cd18071     52 ILADDMGLGKTLTTISL---ILAN----FTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGG----------------E 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  485 QGRIIRGAYRFQAIITTFEMILG-----GCGELNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTV 559
Cdd:cd18071    109 RNRDPKLLSKYDIVLTTYNTLASdfgakGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSP 188
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958747496  560 EELFSLLHFLEPLRFPSESTFMQEFG---DLKTEEQVQKLQAILKPMMLRR 607
Cdd:cd18071    189 KDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
408-872 3.56e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 108.23  E-value: 3.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  408 ILADEMGLGKTIQSITFLYEVLLTGIRgPFLIIAPLSTIANWEREFRTWTDINVVVyhgslISRQMIQQYemyfRDSQGR 487
Cdd:NF038318    51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  488 IIRGAYRFQAIITTFEMILGGCGELNAIEWRCVIIDEAHRLKN--KNCKLLEGL-KLMNLEHKVLLTGTPLQNTVEELFS 564
Cdd:NF038318   121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLDLYG 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  565 LLHFLEPLRFPSESTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKRLAPKEETIIEV--ELTNIQKKYY 636
Cdd:NF038318   201 LVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCITVdfELSPDEIELY 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  637 RAI---LEKNFSFlskgagqtNVPN--------------------LVNTMMELRKCCNHPY---LIKGAEEKI--IGEFR 688
Cdd:NF038318   272 VRVnnfLKRDILY--------SIPTsnrtliilvirkllasssfaLAETFEVLKKRLEKLKegtRSANAQEGFdlFWSFV 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  689 DTYNpSASDFHL---------QAMIQSAGKLV--LID-----KLLPKMKAG----------------GHKVLIFSQMVRC 736
Cdd:NF038318   344 EDEI-DESGFEEkqdelytrqKEFIQHEIDEVdaIIDvakriKTNAKVTALktaleiafeyqreegiAQKVVVFTESKRT 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  737 LDILEDYLIHKRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGL 789
Cdd:NF038318   423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSE 498
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  790 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAVKVYRLV-TRNSYEREMFDRASLKLGL--------DKA--VLQ 858
Cdd:NF038318   499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAlgLLE 578
                          570
                   ....*....|....
gi 1958747496  859 SMSGRDSNVSGIQQ 872
Cdd:NF038318   579 SGTDFEKRVLQIYQ 592
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
386-607 3.89e-23

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 99.67  E-value: 3.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFNWYNRrnCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWTDINVVVyh 465
Cdd:cd18011      1 PLPHQIDAVLRALRKPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  466 gslISRQMIQQyemyfrdSQGRIIRGAYRFQAIITTFEMILGG---CGELNAIEWRCVIIDEAHRLKNKNCKLLEGL-KL 541
Cdd:cd18011     77 ---LDRETAAQ-------LRRLIGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRyKL 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958747496  542 MNL-----EHKVLLTGTPLQNTVEELFSLLHFLEPLRFpsesTFMQEFGDLKTEEQVqklqaiLKPMMLRR 607
Cdd:cd18011    147 GRLlakraRHVLLLTATPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
407-584 4.75e-22

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: 97.65  E-value: 4.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  407 CILADEMGLGKTIQSITFLYEVLLTGIRGPF---LIIAPLSTIANWEREFRTWTDIN-----VVVYHGSLISRQ------ 472
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLkdeekIEVNELATYKRPqersyk 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  473 ----------MIQQYEMYFRDSQGRIIRGAYRFQAiitTFEMILGGCGElnaiewRCVIIDEAHRLKNKNCKLLEGLKLM 542
Cdd:cd18068    111 lqrwqeeggvMIIGYDMYRILAQERNVKSREKLKE---IFNKALVDPGP------DFVVCDEGHILKNEASAVSKAMNSI 181
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958747496  543 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 584
Cdd:cd18068    182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
HELICc smart00490
helicase superfamily c-terminal domain;
738-822 5.33e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.11  E-value: 5.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   738 DILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 817
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958747496   818 CHRIG 822
Cdd:smart00490   78 AGRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
386-607 8.30e-18

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: 85.22  E-value: 8.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLfnWYNRRNC---ILADEMGLGKTIQSITFLY--------------EVLLTGI---------RGPFLI 439
Cdd:cd18072      1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALILaqkntqnrkeeekeKALTEWEskkdstlvpSAGTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  440 IAPLSTIANWEREFRTWTD---INVVVYHGSlisrqmiqqyemyFRDSQGRIIRgayRFQAIITTFEMI---LGGCGE-- 511
Cdd:cd18072     79 VCPASLVHQWKNEVESRVAsnkLRVCLYHGP-------------NRERIGEVLR---DYDIVITTYSLVakeIPTYKEes 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  512 ----LNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFgDL 587
Cdd:cd18072    143 rsspLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV-DN 221
                          250       260
                   ....*....|....*....|
gi 1958747496  588 KTEEQVQKLQAILKPMMLRR 607
Cdd:cd18072    222 KSRKGGERLNILTKSLLLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
407-584 4.46e-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: 4.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  407 CILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREFRTWtdinvvVYHGSLISRQMIQQYEMYFRDSQG 486
Cdd:cd18069     31 CILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW------LPPPEALPNVRPRPFKVFILNDEH 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  487 RiirgAYRFQAIITTFEMILGGCGELNAIEWR------CVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVE 560
Cdd:cd18069    105 K----TTAARAKVIEDWVKDGGVLLMGYEMFRlrpgpdVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                          170       180
                   ....*....|....*....|....
gi 1958747496  561 ELFSLLHFLEPLRFPSESTFMQEF 584
Cdd:cd18069    181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
297-352 1.99e-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: 72.22  E-value: 1.99e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  297 DYVEVDRILEVSfcedkDTGESVVYYLVKWCSLPYEDSTWELKEDV---DLAKIEEFEQ 352
Cdd:cd18659      1 EYTIVERIIAHR-----EDDEGVTEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
BRK smart00592
domain in transcription and CHROMO domain helicases;
2060-2104 4.47e-15

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 70.84  E-value: 4.47e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1958747496  2060 TGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPEWG 2104
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
1986-2026 1.52e-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: 1.52e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958747496 1986 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYVED 2026
Cdd:pfam07533    2 TGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 42
BRK smart00592
domain in transcription and CHROMO domain helicases;
1986-2033 2.11e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 2.11e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1958747496  1986 DTESPVPVINLKDGTRLAGDDAPKRKDLDRWLKEHPGYvedlgAFIPR 2033
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEY-----EVAPR 43
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2059-2102 2.55e-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: 2.55e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958747496 2059 LTGEERVQLINRRNARKVGGAFAPPLKDLCRFLKENSEYGVAPE 2102
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
214-276 1.30e-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: 61.99  E-value: 1.30e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958747496  214 DAAIVDKILACRtVKKEVSPGVMLDIE--------EFFVKYKNYSYLHCEWATEQQlLKDKRIQQKIKRFK 276
Cdd:cd18660      1 DEDKIEKILDHR-PKGPVEEASLDLTDpdepwderEFLVKWKGKSYLHCTWVTEET-LEQLRGKKKLKNYI 69
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
386-569 9.60e-11

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 64.67  E-value: 9.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLFnwynrRNCILADEMGLGKTIQSITFL---------YEVLLTGIR-----------------GPFLI 439
Cdd:cd18070      1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALIllhprpdndLDAADDDSDemvccpdclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  440 IAPLSTIANWEREFRTWTDINVVVYHGSLISRQMIQQYEMYFRDSQGRIIRGAY---RFQ-AIITTFEMILGGCGE---- 511
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYdvlRTElHYAEANRSNRRRRRQkrye 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  512 -----LNAIEWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFL 569
Cdd:cd18070    156 appspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFL 218
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
332-916 4.27e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 65.05  E-value: 4.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  332 EDSTWELKEDVDLAKIEEFEQLQASRPDTRQLDRPPSNIWKKIDQSREYKNGN-------QLREYQLEGLN-WLLFNWYN 403
Cdd:COG1061     20 LLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDeasgtsfELRPYQQEALEaLLAALERG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  404 RRNCILADEMGLGKTIQSITFLYEVLLtgiRGPFLIIAPLSTIAN-WEREFRTWTDiNVVVYHGSlisrqmiqqyemyfR 482
Cdd:COG1061    100 GGRGLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRRELLEqWAEELRRFLG-DPLAGGGK--------------K 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  483 DSQGRIIrgayrfqaiITTFEmILGGCGELNAI--EWRCVIIDEAHRLKNKncKLLEGLKLMNLEHKVLLTGTPlqntve 560
Cdd:COG1061    162 DSDAPIT---------VATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP------ 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  561 elfsllhfleplrfpsestfmqEFGDLKTEEqVQKLQAILKPMMLRRLKEDveKRLAPKEETIIEVELTNIQKKYyrail 640
Cdd:COG1061    224 ----------------------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEY----- 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  641 eknfsflskgagqtnvpnlvntmmelrkccnhPYLIKGAEEKIIGefrdtynpsasdfhlqamiQSAGKLVLIDKLLPKM 720
Cdd:COG1061    274 --------------------------------DALSERLREALAA-------------------DAERKDKILRELLREH 302
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  721 kAGGHKVLIFSQMVRCLDILEDYLIHKRYLYERIDGRVRGNLRQAAIDRFSkpdSDRFVFLLCTRAGGLGINLTAADTCI 800
Cdd:COG1061    303 -PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDVAI 378
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  801 IFDSDWNPQNDLQAQARCHRIGQNK-AVKVYRLVTRNSYEREMFDRASLKLGLDKavLQSMSGRDSNVSGIQQLSKKEIE 879
Cdd:COG1061    379 LLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYR--VEFLDEEESEELALLIAVKPALE 456
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1958747496  880 DLLRRGAYGAIMEEEDEGSKFCEEDIDQILLRRTKTI 916
Cdd:COG1061    457 VKGELEEELLEELELLEDALLLVLAELLLLELLALAL 493
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
386-570 8.63e-10

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 61.21  E-value: 8.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  386 LREYQLEGLNWLLfnwYNRRNCILADeMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIAN-WEREFRTW-----TDI 459
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWnhlrnLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  460 NVVVYHGSLISRQMIQQYEMYfrdsqgriirgayrfqaiITTFEMILGGCGELNaIEW--RCVIIDEAHRLKNKNCKllE 537
Cdd:cd18013     77 SVAVGTERQRSKAANTPADLY------------------VINRENLKWLVNKSG-DPWpfDMVVIDELSSFKSPRSK--R 135
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958747496  538 GLKLMNLEHKV----LLTGTPLQNTVEELFSLLHFLE 570
Cdd:cd18013    136 FKALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLD 172
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
300-352 5.42e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 54.12  E-value: 5.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  300 EVDRILEVSFCEDKdtgesVVYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 352
Cdd:pfam00385    2 EVERILDHRKDKGG-----KEEYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
218-280 1.08e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 53.37  E-value: 1.08e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496   218 VDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRiqqKIKRFKLRQA 280
Cdd:smart00298    4 VEKILDHRWKKKGE--------LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
406-553 1.30e-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: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  406 NCILADEMGLGKTIQSITFLYEVLLTGiRGPFLIIAPLSTIAN-WEREFRTW--TDINVVVYHGsliSRQMIQQYEMYFR 482
Cdd:cd00046      3 NVLITAPTGSGKTLAALLAALLLLLKK-GKKVLVLVPTKALALqTAERLRELfgPGIRVAVLVG---GSSAEEREKNKLG 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747496  483 DSqgriirgayrfQAIITTFEMILGGCGELNAI---EWRCVIIDEAHRL----KNKNCKLLEGLKLMNLEHK-VLLTGT 553
Cdd:cd00046     79 DA-----------DIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSAT 146
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
296-350 2.01e-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: 52.27  E-value: 2.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  296 PDYVEVDRILEVSfcEDKDTGesvVYYLVKWCSLPYEDSTWElKEDVDLAKIEEF 350
Cdd:cd18662      1 PEWLQIHRIINHR--VDKDGN---TWYLVKWRDLPYDQSTWE-SEDDDIPDYEKH 49
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
217-276 7.62e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 50.65  E-value: 7.62e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  217 IVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLKDKRIqqkIKRFK 276
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 ...
241-262 4.02e-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: 4.02e-06
                           10        20
                   ....*....|....*....|..
gi 1958747496  241 EFFVKYKNYSYLHCEWATEQQL 262
Cdd:cd18667     45 EFFVKWHGMSYWHCEWVSELQL 66
ResIII pfam04851
Type III restriction enzyme, res subunit;
385-554 4.22e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 4.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  385 QLREYQLEGL-NWLLFNWYNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAP-LSTIANWEREFRTWTDINVV 462
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  463 vyHGSLIS----RQMIQQYEMYF--RDSQGRIIRGAYRfQAIITTFEMIlggcgelnaiewrcvIIDEAHRL-------- 528
Cdd:pfam04851   83 --IGEIISgdkkDESVDDNKIVVttIQSLYKALELASL-ELLPDFFDVI---------------IIDEAHRSgassyrni 144
                          170       180
                   ....*....|....*....|....*...
gi 1958747496  529 --KNKNCKLLEglklmnlehkvlLTGTP 554
Cdd:pfam04851  145 leYFKPAFLLG------------LTATP 160
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
300-352 1.85e-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: 44.00  E-value: 1.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  300 EVDRILevsfceDKDTGESVVYYLVKWCSLPYEDSTWELKEDVDLAK--IEEFEQ 352
Cdd:cd00024      2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
DpdE NF041062
protein DpdE;
409-575 2.25e-05

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 49.97  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  409 LADEMGLGKTIQSITFLYEVLLTGIRGPFLIIAPLSTIANWEREfrtwtdinvvvyhgsLISRQMIQQyemyFRDSQGRI 488
Cdd:NF041062   175 LADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDALVRQWRRE---------------LRDKFFLDD----FPGARVRV 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  489 IRgayrfQAIITTFEMILGGCGelnaiewrCVIIDEAHRLKNKNCKLLEGLK-----LMNLEHKV----LLTGTPLQNTV 559
Cdd:NF041062   236 LS-----HEEPERWEPLLDAPD--------LLVVDEAHQLARLAWSGDPPERaryreLAALAHAAprllLLSATPVLGNE 302
                          170
                   ....*....|....*.
gi 1958747496  560 EELFSLLHFLEPLRFP 575
Cdd:NF041062   303 ETFLALLHLLDPDLYP 318
CDC27 pfam09507
DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It ...
3-202 3.61e-05

DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It carries the essential residues for binding to the Pol1 subunit of polymerase alpha, from residues 293-332, which are characterized by the motif D--G--VT, referred to as the DPIM motif. The first 160 residues of the protein form the minimal domain for binding to the B subunit, Cdc1, of polymerase delta, the final 10 C-terminal residues, 362-372, being the DNA sliding clamp, PCNA, binding motif.


Pssm-ID: 462819 [Multi-domain]  Cd Length: 427  Bit Score: 48.66  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496    3 SVKRPRGRPPSSKKSDGSGTYSRLQ-NTQVRVMSEKKPRKKAESESKQEKANRIISEAIARAKERGERNIPRVMSPENFP 81
Cdd:pfam09507  200 SVKAPSLKRSPSAKSNIMSAFFKAKpKNKKKKTSASEQKVQEESAEESGKEDVTLEDDSAAEEEEDEQLPTKKDKRRQKR 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   82 SSSVDGKEEKRAQRvksKPKDRDNRKPKACSKLKEKTKIgklIITLGKNHKRRSESSDELSDAEQMPQHTFKEQHSQKRR 161
Cdd:pfam09507  280 GESSDSEESTRESR---KEKRERLKKMMEDDSDDDEMED---VPESPVATEEEETGSPPPLLKKEVEKEEVTESGDGRRR 353
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958747496  162 SNRQVKRKKYAEDAEGRQCEEEVRGS---------LKVKRTSAPPPGEQP 202
Cdd:pfam09507  354 KRRKVMKKKTFKDEEGYMVTEKVYEWesfsededePPVKPKPAVSTPASP 403
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
214-276 4.49e-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: 42.95  E-value: 4.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  214 DAAIVDKILACRTVKKEVspgvmldiEEFFVKYKNYSYLHCEWATEQQLLkdKRIQQKIKRFK 276
Cdd:cd18659      1 EYTIVERIIAHREDDEGV--------TEYLVKWKGLPYDECTWESEEDIS--DIFQEAIDEYK 53
CHROMO smart00298
Chromatin organization modifier domain;
300-355 5.58e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 42.59  E-value: 5.58e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747496   300 EVDRILEVSFcedkdTGESVVYYLVKWCSLPYEDSTWELKEDVDLA--KIEEFEQLQA 355
Cdd:smart00298    3 EVEKILDHRW-----KKKGELEYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKKKER 55
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
666-839 1.14e-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: 46.55  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  666 LRKCC---NHPYLIKgaeekiigefrDTYNPSASDF-----HLqamIQSAGKLV----LIDKLLPKMKAGGHKVLIFSQM 733
Cdd:pfam11496   54 LENLSlvaTHPYLLV-----------DHYMPKSLLLkdepeKL---AYTSGKFLvlndLVNLLIERDRKEPINVAIVARS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  734 VRCLDILEDYLIHKRYLYERIDG-RVRGNLRQAAIDRFSKPDSDRFVFL----LCTRAGGLGINlTAADTCIIFDSDWNP 808
Cdd:pfam11496  120 GKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLLsstgQLTNDDSLLEN-YKFDLIIAFDSSVDT 198
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958747496  809 QNDLQAQARCHRIGQNKAVKVYRLVTRNSYE 839
Cdd:pfam11496  199 SSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
PTZ00121 PTZ00121
MAEBL; Provisional
37-292 2.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496   37 KKPRKKAESESKQEKANRIISEAIARAKERGERNIPRVMSPENFPSSSVDGKEEKRAQRVKSKPKDRDNRKpkaCSKLKE 116
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---ADEAKK 1477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  117 KTKIGKLIITLGKNHKRRSESSDELSDAEQMPQHTFKEQHSQKRRSNRQVKRKKYAEDAEGRQCEEEVRGSLKVKRTSAP 196
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  197 PPGEQPLQLFVENPSEEDAAIVDKI--LACRTVKKEVSPGVMLDIEEFFVKYKNYSYLHCEWATEQQLLKDKRIQQKIKR 274
Cdd:PTZ00121  1558 KKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                          250       260
                   ....*....|....*....|.
gi 1958747496  275 FKLRQAQ---RAHFLADMEEE 292
Cdd:PTZ00121  1638 LKKKEAEekkKAEELKKAEEE 1658
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
775-827 9.43e-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: 9.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  775 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQNKAV 827
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
240-276 9.67e-04

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: 40.35  E-value: 9.67e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958747496  240 EEFFVKYKNYSYLHCEWATEQQLLkdkriQQKIKRFK 276
Cdd:cd18666     47 IQYLIKWKGWSHIHNTWESEESLK-----DQNVKGMK 78
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
300-343 1.05e-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: 38.80  E-value: 1.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958747496  300 EVDRILevsfCEDKDTGEsvVYYLVKWCSLPYEDSTWELKEDVD 343
Cdd:cd18966      2 EVERIL----AERRDDGG--KRYLVKWEGYPLEEATWEPEENIG 39
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
297-342 2.21e-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: 2.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958747496  297 DYVEVDRILEVSFCEDKDtGESVVYYLVKWCSLPYEDSTWELKEDV 342
Cdd:cd18664      1 EFHVVERIIASQRASLED-GTSQLQYLVKWRRLNYDECTWEDATLI 45
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
300-350 4.64e-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: 4.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958747496  300 EVDRILEVSFCEDKDTGESVVYYLVKWCSLPYEDSTWELKEDVD--LAKIEEF 350
Cdd:cd18635      3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSncPEKIKEF 55
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
297-351 4.84e-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: 37.36  E-value: 4.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958747496  297 DYVEVDRILEVSFCEDKDTGEsvvyYLVKWcsLPYEDSTWELKEDVDLAKIEEFE 351
Cdd:cd18628      2 EYAVAESVIGKRVGDDGKTIE----YLVKW--TDMSDATWEPQDNVDSTLVLLYQ 50
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
311-352 5.01e-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: 37.31  E-value: 5.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958747496  311 EDKDTGESVVYYLVKWCSLPYEDSTWELKEDV-DLAK-IEEFEQ 352
Cdd:cd18964     11 PSARDGPGKFLWLVKWDGYPIEDATWEPPENLgEHAKlIEDFEK 54
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
387-562 6.34e-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: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  387 REYQLEGLNWLLfnwyNRRNCILADEMGLGKTIQSITFLYEVLLTGIRGP-FLIIAPLSTIAN-WEREFRTW---TDINV 461
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEqIYEELKKLgkgLGLKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747496  462 V-VYHGSLISRQMiqqyemyfrdsqgRIIRGAyrfQAIITTFEMI---LGGCGELNAIewRCVIIDEAHRLKNKN--CKL 535
Cdd:pfam00270   77 AsLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLLDMGfgPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 1958747496  536 LEGLKLMNLEHK-VLLTGTPLQNtVEEL 562
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
306-347 6.73e-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: 36.73  E-value: 6.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958747496  306 EVSFCEDKDTGESVVYYLVKWCSLPYEDSTWELKEDVDLAKI 347
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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