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Conserved domains on  [gi|1958762180|ref|XP_038961042|]
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chromodomain-helicase-DNA-binding protein 6 isoform X18 [Rattus norvegicus]

Protein Classification

chromo domain-containing DEAD/DEAH box helicase( domain architecture ID 13312865)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
460-681 5.25e-158

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


The actual alignment was detected with superfamily member cd18058:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 222  Bit Score: 473.76  E-value: 5.25e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
459-984 5.63e-150

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: 481.99  E-value: 5.63e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  459 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 534
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 691
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  692 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 771
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  772 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 851
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  852 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 931
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  932 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 984
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
371-429 1.14e-33

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


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.55  E-value: 1.14e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  371 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 429
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, ...
287-352 3.54e-25

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: 99.72  E-value: 3.54e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  287 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 352
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
100-372 1.43e-08

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 59.70  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGE----QEGTKASKDREPKP-------KRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEK 168
Cdd:PTZ00449   548 KPGEtkegEVGKKPGPAKEHKPskiptlsKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRP 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  169 RSctdcgpRTKPKKASKDQGPTPVERKkkgkrknettvESLELDQSLPNPslQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:PTZ00449   628 ES------PKSPKRPPPPQRPSSPERP-----------EGPKIIKSPKPP--KSPKPPFDPKFKEKFYDDYLDAAAKSKE 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  249 DLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKilasktvqevhPGEP----PFDLELFYVKYRNF 324
Cdd:PTZ00449   689 TKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEP-----------IGDPdaeqPDDIEFFTPPEEER 757
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  325 SYLHCKWAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 372
Cdd:PTZ00449   758 TFFHETPADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
460-681 5.25e-158

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: 473.76  E-value: 5.25e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
459-984 5.63e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 481.99  E-value: 5.63e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  459 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 534
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 691
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  692 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 771
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  772 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 851
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  852 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 931
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  932 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 984
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
354-918 1.36e-128

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 413.47  E-value: 1.36e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  354 QAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPE 433
Cdd:COG0553    131 LLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLE 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  434 VKPVERPASDAWQKLETSREYKNSNR-----LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIH 508
Cdd:COG0553    211 LELLAEAAVDAFRLRRLREALESLPAglkatLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  509 GPFLIIAPLSTITNWEREFRTWT-EMNAIVYHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELK 587
Cdd:COG0553    291 RPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLA 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  588 KIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---E 664
Cdd:COG0553    356 AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdE 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  665 EQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCC 744
Cdd:COG0553    436 EALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQIC 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  745 NHPYLINGaeekilEDFRKAHSSeasdfqlqamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYT 824
Cdd:COG0553    516 SHPALLLE------EGAELSGRS--------------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIE 575
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  825 YERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVY 904
Cdd:COG0553    576 YAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVY 654
                          570
                   ....*....|....
gi 1958762180  905 RLITRNSYEREMFD 918
Cdd:COG0553    655 KLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
463-750 1.16e-84

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: 278.41  E-value: 1.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  463 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSIAFLSeiFVRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 534
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 690
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  691 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 750
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
782-907 2.49e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.23  E-value: 2.49e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  782 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 861
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762180  862 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 907
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, ...
371-429 1.14e-33

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.55  E-value: 1.14e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  371 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 429
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
453-651 3.08e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.22  E-value: 3.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   453 EYKNSNRLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTIT-NWEREFRTWT 531
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   532 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVVIDEAHRLKN- 604
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180   605 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 651
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
782-896 1.26e-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: 102.67  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  782 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 860
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958762180  861 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 896
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
287-352 3.54e-25

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: 99.72  E-value: 3.54e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  287 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 352
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
HELICc smart00490
helicase superfamily c-terminal domain;
812-896 2.64e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 2.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   812 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 891
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958762180   892 CHRIG 896
Cdd:smart00490   78 AGRAG 82
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
482-930 5.05e-21

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 100.14  E-value: 5.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  482 ILADEMGLGKTIQS---IAFLSEIFVRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQYemvyRDA 558
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKK 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  559 QGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVEE 635
Cdd:NF038318   118 WNKRLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLD 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  636 LFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------EV 700
Cdd:NF038318   198 LYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEI 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  701 ELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDfr 762
Cdd:NF038318   269 ELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVED-- 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  763 kahSSEASDFQL---------QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRC 810
Cdd:NF038318   346 ---EIDESGFEEkqdelytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRT 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  811 LDILEDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGL 863
Cdd:NF038318   423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSE 498
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762180  864 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKAI 930
Cdd:NF038318   499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAL 574
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
100-372 1.43e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 59.70  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGE----QEGTKASKDREPKP-------KRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEK 168
Cdd:PTZ00449   548 KPGEtkegEVGKKPGPAKEHKPskiptlsKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRP 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  169 RSctdcgpRTKPKKASKDQGPTPVERKkkgkrknettvESLELDQSLPNPslQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:PTZ00449   628 ES------PKSPKRPPPPQRPSSPERP-----------EGPKIIKSPKPP--KSPKPPFDPKFKEKFYDDYLDAAAKSKE 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  249 DLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKilasktvqevhPGEP----PFDLELFYVKYRNF 324
Cdd:PTZ00449   689 TKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEP-----------IGDPdaeqPDDIEFFTPPEEER 757
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  325 SYLHCKWAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 372
Cdd:PTZ00449   758 TFFHETPADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
375-427 2.50e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 51.42  E-value: 2.50e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762180  375 EIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 427
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
292-353 2.01e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 43.33  E-value: 2.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  292 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 353
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CDC27 pfam09507
DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It ...
21-259 1.51e-04

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: 45.97  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   21 SPMSDASVNFDYKSPSPfDCSPDQGENIEEAANHCLPQKDFYTTEEEADTL-FSRKLMSHNGMEDNGGRGTGVKKKRKKK 99
Cdd:pfam09507  122 GPIVNPNVKRRSGLGIP-PPPPPASPPLETTAPGKTPPVGKPSAAPETSPAkSEKKKKSAAKSQDASKETTPEKAEKAPS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGEQEGTKASKDREPKPK-RKREPKEPKEPRRAKEPKRAKEPKEAKQKDgvkkPRKPREASGT-KEGKEKRSCTDCGPR 177
Cdd:pfam09507  201 VKAPSLKRSPSAKSNIMSAfFKAKPKNKKKKTSASEQKVQEESAEESGKE----DVTLEDDSAAeEEEDEQLPTKKDKRR 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  178 TKPKKASKDQGPTPVERKKKGKR---------KNETTVESLELDQSL-------PNPSLQSPEEPSESADSQ--KRRSGR 239
Cdd:pfam09507  277 QKRGESSDSEESTRESRKEKRERlkkmmeddsDDDEMEDVPESPVATeeeetgsPPPLLKKEVEKEEVTESGdgRRRKRR 356
                          250       260
                   ....*....|....*....|
gi 1958762180  240 QVKRRKynedldfKVVDDDG 259
Cdd:pfam09507  357 KVMKKK-------TFKDEEG 369
CHROMO smart00298
Chromatin organization modifier domain;
375-426 3.92e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 39.50  E-value: 3.92e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958762180   375 EIDRILEVAHTKDAETgeevtHYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 426
Cdd:smart00298    3 EVEKILDHRWKKKGEL-----EYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
115-234 1.01e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.60  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  115 PKPKRKREPKEPKePRRAKEPKRAKePKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPVER 194
Cdd:NF033839   383 PKPEVKPQPEKPK-PEVKPQPEKPK-PEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETP 460
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958762180  195 KKKGKRKNET-------TVESLELDQSLPNPSLQSPEEPSE-SADSQK 234
Cdd:NF033839   461 KPEVKPQPEKpkpevkpQPEKPKPDNSKPQADDKKPSTPNNlSKDKQP 508
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
124-245 2.70e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.31  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  124 KEPKEPRRAKEPKRAKEPKEAKQKDGVK-------KPRKPREASGTKEGKEKRSCT---DCGPRTKPKKASKDQGPTPVE 193
Cdd:NF033838   195 EEAKEPRDEEKIKQAKAKVESKKAEATRlekiktdREKAEEEAKRRADAKLKEAVEknvATSEQDKPKRRAKRGVLGEPA 274
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  194 RKKKgKRKNETTVESLELDQSLPNPSLqSPEEPSESADSQKRRSGRQVKRRK 245
Cdd:NF033838   275 TPDK-KENDAKSSDSSVGEETLPSPSL-KPEKKVAEAEKKVEEAKKKAKDQK 324
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
115-242 2.70e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.06  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  115 PKPKRKREPKEPKE--PRRAKEPKRAKEPKEAKQKDGVK-KPRKPREASGTKEGKEKRSCtdcgpRTKPKKASKDQGPTP 191
Cdd:NF033839   328 PKPEVKPQPEKPKPevKPQLETPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPETPKPEV-----KPQPEKPKPEVKPQP 402
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  192 VERKKKGKRKNETTVESLELDQSLPNPSLQ-SPEEPSESADSQKRRSGRQVK 242
Cdd:NF033839   403 EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPEKPKPEVK 454
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
100-242 4.51e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPG--EQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPR-KPREASGTKEGKEKRSCTDCGP 176
Cdd:NF033839   286 EPGnkKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEvKPQLETPKPEVKPQPEKPKPEV 365
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762180  177 RTKPKKASKDQGPTPVERKKKGKRKNETTVESLELDQSLPNPSLQ-SPEEPSESADSQKRRSGRQVK 242
Cdd:NF033839   366 KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPEKPKPEVK 432
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
591-657 8.87e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 40.59  E-value: 8.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  591 WSCVVIDEAHRL------KNRNCKLLEGLKlMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE 657
Cdd:PRK04914   273 WDLLVVDEAHHLvwseeaPSREYQVVEQLA-EVIPGVLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFVEE 344
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
116-248 9.44e-03

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 40.15  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  116 KPKRKREPKE---PKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPV 192
Cdd:NF040676   214 KPKEEVKVQEevkPKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKA 293
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  193 ER--KKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:NF040676   294 QEiaKAKEEEKAQEIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEA 351
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
460-681 5.25e-158

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: 473.76  E-value: 5.25e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
459-984 5.63e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 481.99  E-value: 5.63e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  459 RLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---AFLSEIfvRGIHGPFLIIAPLSTITNWEREFRTWTEM-N 534
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllGYLHEY--RGITGPHMVVAPKSTLGNWMNEIRRFCPVlR 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:PLN03142   247 AVKFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLA 691
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  692 PKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEEKiledfrkahsseASD 771
Cdd:PLN03142   396 PKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPY 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  772 FQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDR 851
Cdd:PLN03142   461 TTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  852 FVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAIL 931
Cdd:PLN03142   541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  932 QDinrkgstNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 984
Cdd:PLN03142   621 QQ-------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
460-681 8.80e-150

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: 452.09  E-value: 8.80e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVY 538
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYqVEGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 HGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 618
Cdd:cd17995     81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  619 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
460-681 1.83e-129

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: 398.27  E-value: 1.83e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
354-918 1.36e-128

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 413.47  E-value: 1.36e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  354 QAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPE 433
Cdd:COG0553    131 LLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLE 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  434 VKPVERPASDAWQKLETSREYKNSNR-----LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIH 508
Cdd:COG0553    211 LELLAEAAVDAFRLRRLREALESLPAglkatLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  509 GPFLIIAPLSTITNWEREFRTWT-EMNAIVYHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELK 587
Cdd:COG0553    291 RPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLA 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  588 KIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---E 664
Cdd:COG0553    356 AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdE 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  665 EQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCC 744
Cdd:COG0553    436 EALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQIC 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  745 NHPYLINGaeekilEDFRKAHSSeasdfqlqamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYT 824
Cdd:COG0553    516 SHPALLLE------EGAELSGRS--------------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIE 575
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  825 YERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVY 904
Cdd:COG0553    576 YAYLHGGTSAEERDELVDRF-QEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVY 654
                          570
                   ....*....|....
gi 1958762180  905 RLITRNSYEREMFD 918
Cdd:COG0553    655 KLVAEGTIEEKILE 668
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
460-681 1.05e-127

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: 393.63  E-value: 1.05e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18059     81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
460-681 4.47e-124

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: 383.97  E-value: 4.47e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 539
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  540 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALE 619
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  620 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
463-750 1.16e-84

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: 278.41  E-value: 1.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  463 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSIAFLSeiFVRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 534
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 690
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  691 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 750
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
460-681 2.01e-82

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: 269.23  E-value: 2.01e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMvYRDaQGNPLsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd17993     82 YLGDIKSRDTIREYEF-YFS-QTKKL----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFK 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFlEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd17993    156 TNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
460-645 3.02e-77

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: 252.87  E-value: 3.02e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSE-IFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd17919     81 YHGSQRERAQIRAKEKLD------------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEP 645
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
460-683 5.54e-74

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


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 246.14  E-value: 5.54e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 538
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLLY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 HGSQISRQMIQqyemvyRDAQGNPLSGVfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 618
Cdd:cd18009     84 HGTKEERERLR------KKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  619 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-----------DLKTEEQ----VKKLQSILKPMMLRRLK 683
Cdd:cd18009    157 DNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLRRLK 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
460-681 2.07e-71

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: 236.95  E-value: 2.07e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSqisrqmiqqyemvyrdaqgnplsgvfkfHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd17994     81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
457-683 1.23e-68

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: 230.29  E-value: 1.23e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  457 SNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWEREFRTWT-EMN 534
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLkHYKNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  535 AIVYHGSQISRQMIQQYEMVYRdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLK 614
Cdd:cd17997     81 VVVLIGDKEERADIIRDVLLPG-----------KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  615 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF----GDLKTEEQVKKLQSILKPMMLRRLK 683
Cdd:cd17997    150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
460-681 2.42e-68

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: 229.90  E-value: 2.42e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYRDAQGNPLSGVFK--------FHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 609
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  610 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
460-683 3.66e-67

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: 226.48  E-value: 3.66e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd17996      4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMeKKKNNGPYLVIVPLSTLSNWVSEFEKWApSVSKIV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd17996     84 YKGTPDVRKKLQSQIRAG------------KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYY 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  618 L-EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG------------DLKTEEQV---KKLQSILKPMMLRR 681
Cdd:cd17996    152 HaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRPFLLRR 231

                   ..
gi 1958762180  682 LK 683
Cdd:cd17996    232 LK 233
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
460-681 5.38e-66

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: 223.34  E-value: 5.38e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18054     21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd18054    101 YIGDLMSRNTIREYEWIH------SQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 681
Cdd:cd18054    175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
460-681 6.28e-66

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: 223.02  E-value: 6.28e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYRD--------AQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 609
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFEDnairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  610 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
460-681 1.62e-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: 221.48  E-value: 1.62e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYRDAQGNPLSGVF--------KFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 609
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  610 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
460-681 1.67e-58

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: 200.74  E-value: 1.67e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQyemvyrDAQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd18006     81 YMGDKEKRLDLQQ------DIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETA--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 681
Cdd:cd18006    150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
460-683 2.77e-58

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: 200.10  E-value: 2.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 538
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVLVI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 HGSQISRQMIQQYEmvyrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMAL 618
Cdd:cd18012     85 HGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  619 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLK 683
Cdd:cd18012    150 DHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
782-907 2.49e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.23  E-value: 2.49e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  782 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 861
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762180  862 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 907
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
460-681 3.97e-56

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: 194.49  E-value: 3.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFV-RGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIV 537
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACeKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMvyrdaqgNPLSgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd18003     81 YYGSAKERKLKRQGWM-------KPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 681
Cdd:cd18003    150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
460-681 1.05e-55

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: 193.73  E-value: 1.05e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18053     21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQTWApQMNAVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMA 617
Cdd:cd18053    101 YLGDINSRNMIRTHEWMH------PQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFK 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  618 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 681
Cdd:cd18053    175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
460-648 7.19e-53

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 183.74  E-value: 7.19e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 538
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 HGSQISRqmiqqyemvyRDAQGNPLSGVFKFHVVITTFEMILADCPE---LKKIHWSCVVIDEAHRLKNRNCKLLEGLKL 615
Cdd:cd17998     81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958762180  616 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQF 648
Cdd:cd17998    151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
460-681 1.88e-52

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 183.86  E-value: 1.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfNWYNRK-NCILADEMGLGKTIQSIAFLSEIFVR-GIHGPFLIIAPLSTITNWEREF-RTWTEMNAI 536
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  537 VYHGSQISRQMIQQY----EMVYRDAqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEG 612
Cdd:cd18002     80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  613 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-DLKT---------EEQVKKLQSILKPMMLRR 681
Cdd:cd18002    151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
460-681 1.37e-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: 182.19  E-value: 1.37e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLlFNWY-NRKNCILADEMGLGKTIQSIAFLSEI----------------FVRGIH-----GPFLIIAPL 517
Cdd:cd18005      1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprFKKKPPassakKPVLIVAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  518 STITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEmvyrdaQGnplsgvfKFHVVITTFEMILADCPELKKIHWSCVVID 597
Cdd:cd18005     80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AG-------RLEVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  598 EAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---------------LK 662
Cdd:cd18005    147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                          250
                   ....*....|....*....
gi 1958762180  663 TEEQVKKLQSILKPMMLRR 681
Cdd:cd18005    227 GRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
447-694 4.53e-48

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: 172.16  E-value: 4.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  447 KLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWER 525
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  526 EFRTWT-EMNAIVYHGSQisrqmiQQYEMVYRDAQgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN 604
Cdd:cd18064     83 EFKRWVpTLRAVCLIGDK------DQRAAFVRDVL---LPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  605 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18064    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 231
                          250
                   ....*....|...
gi 1958762180  682 LKDDVEKNLAPKQ 694
Cdd:cd18064    232 IKADVEKSLPPKK 244
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
446-683 7.47e-48

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: 171.77  E-value: 7.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  446 QKLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIF-VRGIHGPFLIIAPLSTITNWE 524
Cdd:cd18062     10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRINGPFLIIVPLSTLSNWV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  525 REFRTWT-EMNAIVYHGSQISRQMIQqyemvyrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLK 603
Cdd:cd18062     90 YEFDKWApSVVKVSYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  604 NRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKK 669
Cdd:cd18062    158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRR 237
                          250
                   ....*....|....
gi 1958762180  670 LQSILKPMMLRRLK 683
Cdd:cd18062    238 LHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
460-683 8.12e-47

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: 168.70  E-value: 8.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFV-RGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 537
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 YHGS-QISRQMIQQYEmvyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLM 616
Cdd:cd18063    104 YKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  617 ALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRRL 682
Cdd:cd18063    171 YVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRRL 250

                   .
gi 1958762180  683 K 683
Cdd:cd18063    251 K 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
447-683 1.07e-45

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: 164.81  E-value: 1.07e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  447 KLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEI-FVRGIHGPFLIIAPLSTITNWER 525
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  526 EFRTWT-EMNAIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN 604
Cdd:cd18065     83 EFKRWVpSLRAVCLIGDKDARAAFIRDVMMPGE-----------WDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  605 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                   ..
gi 1958762180  682 LK 683
Cdd:cd18065    232 IK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
460-681 1.80e-42

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: 155.91  E-value: 1.80e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFnwynrKNCILADEMGLGKTIQSIA--------FLSEIFVRGIHGPF----------LIIAPLSTIT 521
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALAlilatrpqDPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  522 NWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPE------------- 585
Cdd:cd18008     76 QWKDEIEKHTKpgsLKVYVYHGSK----------------RIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  586 ---LKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLK 662
Cdd:cd18008    140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                          250       260
                   ....*....|....*....|..
gi 1958762180  663 TE---EQVKKLQSILKPMMLRR 681
Cdd:cd18008    220 SKndrKALERLQALLKPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
460-681 1.59e-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: 152.53  E-value: 1.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 538
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 HGSQisrqmiqqyemvyRDAQGNPLSGVFK-FHVVITTFEMILADCPEL-----KKIHWSCVVIDEAHRLKNRNCKLLEG 612
Cdd:cd18001     81 HGTS-------------KKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  613 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ-FPSETAFLEEFGDLKTEEQVKK---------------LQSILKP 676
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDatqgekalgsevaenLRQIIKP 227

                   ....*
gi 1958762180  677 MMLRR 681
Cdd:cd18001    228 YFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
460-681 4.49e-37

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: 139.79  E-value: 4.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSIAFL-SEIFVR-----GIHGPFLIIAPLSTITNWEREFRTWTE 532
Cdd:cd17999      1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILaSDHHKRansfnSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  533 ---MNAIVYHGSQISRQMIQQyemvyrdaQGNplsgvfKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 609
Cdd:cd17999     80 nafLKPLAYVGPPQERRRLRE--------QGE------KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  610 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-------DLK-----TEEQVKKLQSILK-- 675
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                   ....*..
gi 1958762180  676 -PMMLRR 681
Cdd:cd17999    226 lPFLLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
460-681 2.28e-36

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: 138.19  E-value: 2.28e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSIAFLSeIFVRgiHGPF--------LIIAPLSTITNWERE 526
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  527 FRTWTemnaivyhGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHwSC--VVIDEAHRLKN 604
Cdd:cd18004     78 FDKWL--------GLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  605 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF-------------------LEEFGDLKTEE 665
Cdd:cd18004    149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseeDKELGAERSQE 228
                          250
                   ....*....|....*.
gi 1958762180  666 qvkkLQSILKPMMLRR 681
Cdd:cd18004    229 ----LSELTSRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
460-645 3.25e-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: 135.91  E-value: 3.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfnWYNRKNC--ILADEMGLGKTIQSIAFLseifvRGIH------GPFLIIAPLSTITNWEREFRTW- 530
Cdd:cd18000      1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFL-----AALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  531 TEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPlSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLL 610
Cdd:cd18000     74 PPFRVVVLHSSGSGTGSEEKLGSIERKSQLIR-KVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEIT 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958762180  611 EGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEP 645
Cdd:cd18000    153 LACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
371-429 1.14e-33

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 123.55  E-value: 1.14e-33
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  371 PDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 429
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
453-651 3.08e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.22  E-value: 3.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   453 EYKNSNRLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTIT-NWEREFRTWT 531
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   532 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVVIDEAHRLKN- 604
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180   605 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 651
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
460-658 1.30e-30

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: 121.63  E-value: 1.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGmnwLLFNWYN----------RKNCILADEMGLGKTIQSIAFLSEI---FVRGIHgpFLIIAPLSTITNWERE 526
Cdd:cd18007      1 LKPHQVEG---VRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYlaaAPRRSR--PLVLCPASTLYNWEDE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  527 FRTWTEMNAIVYHGsqisrqmiqqyeMVYRDAQGNP---LSGVFKFH----VVITTFEM--ILADCPELKK------IHW 591
Cdd:cd18007     76 FKKWLPPDLRPLLV------------LVSLSASKRAdarLRKINKWHkeggVLLIGYELfrNLASNATTDPrlkqefIAA 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  592 SC------VVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 658
Cdd:cd18007    144 LLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
460-654 4.98e-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: 113.79  E-value: 4.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGmnwLLFNWY--------NRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGP------FLIIAPLSTITNWER 525
Cdd:cd18066      1 LRPHQREG---IEFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  526 EFRTWtemnaivyhgsqISRQMIQQYeMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNR 605
Cdd:cd18066     78 EFQKW------------LGSERIKVF-TVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958762180  606 NCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF 654
Cdd:cd18066    145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
460-681 7.85e-28

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 112.68  E-value: 7.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfnwynRKN--CILADEMGLGKTIQSIAFLSeiFVRGiHGPFLIIAPLSTITNWEREFRTW----TEM 533
Cdd:cd18010      1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  534 NAIVYHGSQISRQMiqqyemvyRDAQgnplsgvfkfhVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRN---CKLL 610
Cdd:cd18010     73 DIQVIVKSKDGLRD--------GDAK-----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAA 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  611 EGLkLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE---------FGDLKTEEQVKKLQSIL-KPMMLR 680
Cdd:cd18010    134 LPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycaakqggfGWDYSGSSNLEELHLLLlATIMIR 212

                   .
gi 1958762180  681 R 681
Cdd:cd18010    213 R 213
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
482-681 2.61e-26

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 109.10  E-value: 2.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  482 ILADEMGLGKTIQSIAFLseifvrgIHGPFLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyRDA 558
Cdd:cd18071     52 ILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGE-------------RNR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  559 QGNPLSgvfKFHVVITTFEMI------LADCPeLKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNS 632
Cdd:cd18071    112 DPKLLS---KYDIVLTTYNTLasdfgaKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  633 VEELFSLLNFLEPSQFPSETAFLEEFG---DLKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18071    188 PKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
782-896 1.26e-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: 102.67  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  782 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 860
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958762180  861 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 896
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
287-352 3.54e-25

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: 99.72  E-value: 3.54e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  287 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 352
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
478-681 4.28e-25

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: 104.68  E-value: 4.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  478 RKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQyemvYRD 557
Cdd:cd18011     17 PVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-----LDRETAAQ----LRR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  558 AQGNPLSgvfKFHVVITTFEMI-----LADcpELKKIHWSCVVIDEAHRLKNRNCKLLEGL-KLMAL-----EHKVLLTG 626
Cdd:cd18011     88 LIGNPFE---EFPIVIVSLDLLkrseeRRG--LLLSEEWDLVVVDEAHKLRNSGGGKETKRyKLGRLlakraRHVLLLTA 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762180  627 TPLQNSVEELFSLLNFLEPSQFpsetAFLEEFGDLKTEEQVkklqsiLKPMMLRR 681
Cdd:cd18011    163 TPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
460-681 1.54e-23

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


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 101.01  E-value: 1.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSIAFLSEIFVRGIHGPFLI-----IAPLSTITNWEREFRT 529
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  530 WTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGvfkfHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKL 609
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVST----PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  610 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---------GD------LKTEEQVKKLQSIL 674
Cdd:cd18067    157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                   ....*..
gi 1958762180  675 KPMMLRR 681
Cdd:cd18067    237 NRCIIRR 243
HELICc smart00490
helicase superfamily c-terminal domain;
812-896 2.64e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 2.64e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   812 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 891
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1958762180   892 CHRIG 896
Cdd:smart00490   78 AGRAG 82
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
482-930 5.05e-21

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 100.14  E-value: 5.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  482 ILADEMGLGKTIQS---IAFLSEIFVRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQYemvyRDA 558
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKK 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  559 QGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVEE 635
Cdd:NF038318   118 WNKRLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLLD 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  636 LFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------EV 700
Cdd:NF038318   198 LYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEI 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  701 ELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDfr 762
Cdd:NF038318   269 ELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVED-- 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  763 kahSSEASDFQL---------QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRC 810
Cdd:NF038318   346 ---EIDESGFEEkqdelytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRT 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  811 LDILEDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGL 863
Cdd:NF038318   423 QKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSE 498
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762180  864 GINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGL--------DKAI 930
Cdd:NF038318   499 GLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELfegvfgasDIAL 574
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
460-681 5.05e-20

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: 91.00  E-value: 5.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfnWYNRKNC---ILADEMGLGKTIQSIAF------------------LSEIFVRGIHGPF-----LI 513
Cdd:cd18072      1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  514 IAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemvyRDAQGNPLSgvfKFHVVITTFEMILADCPELKK-- 588
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASNKLrvcLYHGPN-------------RERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  589 -------IHWSCVVIDEAHRLKNRNCKLLEGL-KLMALEHKVLlTGTPLQNSVEELFSLLNFLEPSQFpSETAFLEEFGD 660
Cdd:cd18072    143 rssplfrIAWARIILDEAHNIKNPKVQASIAVcKLRAHARWAL-TGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVD 220
                          250       260
                   ....*....|....*....|.
gi 1958762180  661 LKTEEQVKKLQSILKPMMLRR 681
Cdd:cd18072    221 NKSRKGGERLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
481-658 8.03e-20

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 90.33  E-value: 8.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  481 CILADEMGLGKTIQSIAFLSEIFVRGIHGPF---LIIAPLSTITNWEREFRTWTEMNA---------------------I 536
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLKdeekievnelatykrpqersyK 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  537 VYHGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHvviTTFEMILAD-CPELkkihwscVVIDEAHRLKNRNCKLLEGLKL 615
Cdd:cd18068    111 LQRWQEEGGVMIIGYDMYRILAQERNVKSREKLK---EIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNS 180
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958762180  616 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 658
Cdd:cd18068    181 IRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
481-658 2.75e-19

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


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 88.33  E-value: 2.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  481 CILADEMGLGKTIQSIAFLsEIFVRGIHGP-FLIIAPLSTITNWEREFRTWteMNAIVYHGSQISRQM---IQQYEMVYR 556
Cdd:cd18069     31 CILAHSMGLGKTLQVISFL-DVLLRHTGAKtVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  557 DAQGNPLSG-VFKFHVVITTFEMI-LADCPELkkihwscVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 634
Cdd:cd18069    108 AARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                          170       180
                   ....*....|....*....|....
gi 1958762180  635 ELFSLLNFLEPSQFPSETAFLEEF 658
Cdd:cd18069    181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
372-427 8.11e-16

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


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 72.61  E-value: 8.11e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958762180  372 DYIEIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV---DPAKVKEFES 427
Cdd:cd18659      1 EYTIVERI--IAHREDDEGVTE---YLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
460-647 5.63e-15

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: 75.46  E-value: 5.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfnwYNRKNCILADeMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAIVY 538
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  539 H---GSQisRQMIqqyemvyRDAQGNPlsgvfkfHVVITTFEMiLADCPELKKIHW--SCVVIDEAHRLKNRNCKllEGL 613
Cdd:cd18013     77 SvavGTE--RQRS-------KAANTPA-------DLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK--RFK 137
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958762180  614 KLMALEHKV----LLTGTPLQNSVEELFSLLNFLEPSQ 647
Cdd:cd18013    138 ALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLDQGE 175
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
289-352 2.24e-13

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: 66.23  E-value: 2.24e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762180  289 DANIIEKILASKTVQEVHPG-------EPPFDLELFYVKYRNFSYLHCKWATMEELEKDpRIAQKIKRFRN 352
Cdd:cd18660      1 DEDKIEKILDHRPKGPVEEAsldltdpDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYIK 70
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
460-648 2.49e-12

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 68.52  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGMNWLLfnwyNRKNcILADEMGLGKTIQSIAFL-----------SEIFVRGIH---------------GPFLI 513
Cdd:cd18070      1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLALIllhprpdndldAADDDSDEMvccpdclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  514 IAPLSTITNWEREFRTWTEMNAIVYHgsqisrqmiqqYEMVYRD--AQGNPLSGVFKFHVVITTFEmILAD--------- 582
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDgaLASPAPEILAEYDIVVTTYD-VLRTelhyaeanr 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  583 ---------------CPeLKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ 647
Cdd:cd18070    144 snrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                   .
gi 1958762180  648 F 648
Cdd:cd18070    223 F 223
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
412-1052 2.51e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 64.66  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  412 ELEEDVDPAKVKEFESLQILPEVKPVERPASDAWQklETSREYKNSNRLREYQLEGMN-WLLFNWYNRKNCILADEMGLG 490
Cdd:COG1061     35 VEARRLAIKEGTREDGRRLPEEDTERELAEAEALE--AGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTG 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  491 KTIQSIAFLSEIFVRGihgPFLIIAPLSTITN-WEREFRTWTemNAIVYHGSQISRQmiqqyemvyrdaqgnplsgvfkF 569
Cdd:COG1061    113 KTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRFL--GDPLAGGGKKDSD----------------------A 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  570 HVVITTFEmILADCPELKKI--HWSCVVIDEAHRLKNRncKLLEGLKLMALEHKVLLTGTPlqnsveelfsllnflepsq 647
Cdd:COG1061    166 PITVATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP------------------- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  648 fpsetafleEFGDLKTEEqVKKLQSILKPMMLRRLKDDveKNLAPKQETIIEVELTNIQKKY--YRAILEKNfsfltkga 725
Cdd:COG1061    224 ---------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYdaLSERLREA-------- 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  726 nqhnmpnlintmmelrkccnhpyLINGAEEK--ILEDFRKAHsseasdfqlqamiqaagklvlidkllpkliAGGHKVLI 803
Cdd:COG1061    284 -----------------------LAADAERKdkILRELLREH------------------------------PDDRKTLV 310
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  804 FSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFckpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQ 883
Cdd:COG1061    311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPR 387
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  884 NDLQAQARCHRIGQSK-AVKVYRLITRNS-YEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYG 961
Cdd:COG1061    388 EFIQRLGRGLRPAPGKeDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLE 467
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  962 ALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKES 1041
Cdd:COG1061    468 ELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLR 547
                          650
                   ....*....|.
gi 1958762180 1042 LVIDRPRVRKQ 1052
Cdd:COG1061    548 LEELAALLLKE 558
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
479-627 3.80e-09

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: 56.64  E-value: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  479 KNCILADEMGLGKTIQ-SIAFLSEIFVRGihGPFLIIAPLSTITN-WEREFRTWTEMNA--IVYHGsqiSRQMIQQYEMV 554
Cdd:cd00046      2 ENVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIrvAVLVG---GSSAEEREKNK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  555 YRDAqgnplsgvfkfHVVITTFEMILADCPELKKIH---WSCVVIDEAHRL----KNRNCKLLEGLKLMALEHK-VLLTG 626
Cdd:cd00046     77 LGDA-----------DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSA 145

                   .
gi 1958762180  627 T 627
Cdd:cd00046    146 T 146
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
371-416 6.15e-09

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 53.04  E-value: 6.15e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958762180  371 PDYIEIDRILEvaHTKDAETGeevTHYLVKWCSLPYEESTWELEED 416
Cdd:cd18662      1 PEWLQIHRIIN--HRVDKDGN---TWYLVKWRDLPYDQSTWESEDD 41
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
100-372 1.43e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 59.70  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGE----QEGTKASKDREPKP-------KRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEK 168
Cdd:PTZ00449   548 KPGEtkegEVGKKPGPAKEHKPskiptlsKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRP 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  169 RSctdcgpRTKPKKASKDQGPTPVERKkkgkrknettvESLELDQSLPNPslQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:PTZ00449   628 ES------PKSPKRPPPPQRPSSPERP-----------EGPKIIKSPKPP--KSPKPPFDPKFKEKFYDDYLDAAAKSKE 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  249 DLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKilasktvqevhPGEP----PFDLELFYVKYRNF 324
Cdd:PTZ00449   689 TKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEP-----------IGDPdaeqPDDIEFFTPPEEER 757
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958762180  325 SYLHCKWAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 372
Cdd:PTZ00449   758 TFFHETPADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
375-427 2.50e-08

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 51.42  E-value: 2.50e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762180  375 EIDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 427
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
460-628 1.16e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 49.61  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  460 LREYQLEGM-NWLLFNWYNRKNCILAdeMGLGKTIQSIAFLSEIFVRgihgPFLIIAP-LSTITNWEREFRTWTemnaiv 537
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKEL----RTLIVVPtDALLDQWKERFEDFL------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  538 yHGSQISRQmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPELKKI--HWSCVVIDEAHRLknrNCKLLEGLKL 615
Cdd:cd17926     69 -GDSSIGLI------------GGGKKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILK 132
                          170
                   ....*....|....
gi 1958762180  616 MALEHKVL-LTGTP 628
Cdd:cd17926    133 ELNAKYRLgLTATP 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
461-636 1.30e-05

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: 46.85  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  461 REYQLEGMNWLLfnwyNRKNCILADEMGLGKT-IQSIAFLSEIFVRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAI-- 536
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLkv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  537 --VYHGSQISRQMiqqyemvyrdaqgNPLSGVfkfHVVITTFEMILADCPE---LKKIhwSCVVIDEAHRL--KNRNCKL 609
Cdd:pfam00270   77 asLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 1958762180  610 LEGLKLMALEHK-VLLTGTPLQNsVEEL 636
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
292-353 2.01e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 43.33  E-value: 2.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  292 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 353
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
375-427 2.05e-05

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 43.23  E-value: 2.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958762180  375 EIDRILevahtkDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEFES 427
Cdd:cd00024      2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
372-427 3.50e-05

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


Pssm-ID: 349311  Cd Length: 59  Bit Score: 42.64  E-value: 3.50e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762180  372 DYIEIDRILEvahTKDAETGEEVTH--YLVKWCSLPYEESTWELEEDV---DPAKVKEFES 427
Cdd:cd18664      1 EFHVVERIIA---SQRASLEDGTSQlqYLVKWRRLNYDECTWEDATLIaklAPEQVDHFQN 58
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
373-427 7.00e-05

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


Pssm-ID: 349308  Cd Length: 58  Bit Score: 41.90  E-value: 7.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  373 YIEIDRIleVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD---PAKVKEFES 427
Cdd:cd18661      2 YQIVERI--IAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHS 57
CDC27 pfam09507
DNA polymerase subunit Cdc27; This protein forms the C subunit of DNA polymerase delta. It ...
21-259 1.51e-04

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: 45.97  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180   21 SPMSDASVNFDYKSPSPfDCSPDQGENIEEAANHCLPQKDFYTTEEEADTL-FSRKLMSHNGMEDNGGRGTGVKKKRKKK 99
Cdd:pfam09507  122 GPIVNPNVKRRSGLGIP-PPPPPASPPLETTAPGKTPPVGKPSAAPETSPAkSEKKKKSAAKSQDASKETTPEKAEKAPS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGEQEGTKASKDREPKPK-RKREPKEPKEPRRAKEPKRAKEPKEAKQKDgvkkPRKPREASGT-KEGKEKRSCTDCGPR 177
Cdd:pfam09507  201 VKAPSLKRSPSAKSNIMSAfFKAKPKNKKKKTSASEQKVQEESAEESGKE----DVTLEDDSAAeEEEDEQLPTKKDKRR 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  178 TKPKKASKDQGPTPVERKKKGKR---------KNETTVESLELDQSL-------PNPSLQSPEEPSESADSQ--KRRSGR 239
Cdd:pfam09507  277 QKRGESSDSEESTRESRKEKRERlkkmmeddsDDDEMEDVPESPVATeeeetgsPPPLLKKEVEKEEVTESGdgRRRKRR 356
                          250       260
                   ....*....|....*....|
gi 1958762180  240 QVKRRKynedldfKVVDDDG 259
Cdd:pfam09507  357 KVMKKK-------TFKDEEG 369
PTZ00121 PTZ00121
MAEBL; Provisional
100-284 2.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGEQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPK---EAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGP 176
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  177 RTKPKKASKDQGPTP---VERKKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSgrqvKRRKYNEDLDFK 253
Cdd:PTZ00121  1566 AEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE----EEKKKVEQLKKK 1641
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958762180  254 VVDDDGETIAVLGAGRTSALSASTLAWQAEE 284
Cdd:PTZ00121  1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
849-901 3.59e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 3.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  849 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 901
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
CHROMO smart00298
Chromatin organization modifier domain;
375-426 3.92e-04

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 39.50  E-value: 3.92e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958762180   375 EIDRILEVAHTKDAETgeevtHYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 426
Cdd:smart00298    3 EVEKILDHRWKKKGEL-----EYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
PTZ00121 PTZ00121
MAEBL; Provisional
103-249 6.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  103 EQEGTKASKDREPKPKRKREPK------------EPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASgtKEGKEKRS 170
Cdd:PTZ00121  1239 AEEAKKAEEERNNEEIRKFEEArmahfarrqaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK--KKAEEAKK 1316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  171 CTDCGPRTKPKKASKDQGPTPVERKKK----GKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVK---- 242
Cdd:PTZ00121  1317 ADEAKKKAEEAKKKADAAKKKAEEAKKaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadea 1396

                   ....*..
gi 1958762180  243 RRKYNED 249
Cdd:PTZ00121  1397 KKKAEED 1403
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
115-234 1.01e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.60  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  115 PKPKRKREPKEPKePRRAKEPKRAKePKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPVER 194
Cdd:NF033839   383 PKPEVKPQPEKPK-PEVKPQPEKPK-PEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETP 460
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958762180  195 KKKGKRKNET-------TVESLELDQSLPNPSLQSPEEPSE-SADSQK 234
Cdd:NF033839   461 KPEVKPQPEKpkpevkpQPEKPKPDNSKPQADDKKPSTPNNlSKDKQP 508
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
375-424 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: 38.42  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958762180  375 EIDRILevahtkdAETGEE-VTHYLVKWCSLPYEESTWELEEDVDPAKVKE 424
Cdd:cd18966      2 EVERIL-------AERRDDgGKRYLVKWEGYPLEEATWEPEENIGDEELLK 45
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
278-338 1.09e-03

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: 39.24  E-value: 1.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762180  278 LAWQAEEPPEDDAnIIEKILASKTVQEVHPGEPPFDLELFyVKYRNFSYLHCKWATMEELE 338
Cdd:cd18667      9 LTWRWAEPPYPEP-LPEKPDEDPYPPPPRKLQPRPEREFF-VKWHGMSYWHCEWVSELQLE 67
CF222 pfam15661
C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in ...
100-246 1.73e-03

C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 618 and 652 amino acids in length.


Pssm-ID: 464786 [Multi-domain]  Cd Length: 608  Bit Score: 42.57  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPGEqegtKASKdrepKPKRKREPKEPKE-PRRAKEP---KRAKEPKEAKQKDGVKKPrKPREASGTkEGKEKRSCTDCG 175
Cdd:pfam15661  110 EPKE----KASR----RAKGKEGLPQPAEtPEAPGEPaprKKAHDKKASRKKHSHKKH-VAEETKGA-QDQEAEGQEAGL 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  176 PRTKPKKASK--DQGPTPVER----------KKKGKRKNETTVESLELDQSLPNPSlqspeePSESADSQKRRSG--RQV 241
Cdd:pfam15661  180 PKTAAASRSEeaDLGPARRQDaiiqmivellKKVGDQWEEEQLQAPQPEVAPQNPA------PVVRKKSQEKKSSlkRAF 253

                   ....*
gi 1958762180  242 KRRKY 246
Cdd:pfam15661  254 SHKKH 258
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
397-425 1.79e-03

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 37.52  E-value: 1.79e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958762180  397 YLVKWCSLPYEESTWELEEDVDPAK-VKEF 425
Cdd:cd18975     18 YLIQWKGYPLEEASWELEDNIKNPRlIEEF 47
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
381-421 1.90e-03

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


Pssm-ID: 349330  Cd Length: 50  Bit Score: 37.46  E-value: 1.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958762180  381 EVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK 421
Cdd:cd18974      2 EVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAP 42
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
124-245 2.70e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.31  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  124 KEPKEPRRAKEPKRAKEPKEAKQKDGVK-------KPRKPREASGTKEGKEKRSCT---DCGPRTKPKKASKDQGPTPVE 193
Cdd:NF033838   195 EEAKEPRDEEKIKQAKAKVESKKAEATRlekiktdREKAEEEAKRRADAKLKEAVEknvATSEQDKPKRRAKRGVLGEPA 274
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  194 RKKKgKRKNETTVESLELDQSLPNPSLqSPEEPSESADSQKRRSGRQVKRRK 245
Cdd:NF033838   275 TPDK-KENDAKSSDSSVGEETLPSPSL-KPEKKVAEAEKKVEEAKKKAKDQK 324
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
115-242 2.70e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.06  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  115 PKPKRKREPKEPKE--PRRAKEPKRAKEPKEAKQKDGVK-KPRKPREASGTKEGKEKRSCtdcgpRTKPKKASKDQGPTP 191
Cdd:NF033839   328 PKPEVKPQPEKPKPevKPQLETPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPETPKPEV-----KPQPEKPKPEVKPQP 402
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958762180  192 VERKKKGKRKNETTVESLELDQSLPNPSLQ-SPEEPSESADSQKRRSGRQVK 242
Cdd:NF033839   403 EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPEKPKPEVK 454
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
395-417 2.79e-03

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


Pssm-ID: 349321  Cd Length: 53  Bit Score: 37.07  E-value: 2.79e-03
                           10        20
                   ....*....|....*....|...
gi 1958762180  395 THYLVKWCSLPYEESTWELEEDV 417
Cdd:cd18965     16 LEYLVKWHGLPESENTWEREKDI 38
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
100-242 4.51e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  100 EPG--EQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPR-KPREASGTKEGKEKRSCTDCGP 176
Cdd:NF033839   286 EPGnkKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEvKPQLETPKPEVKPQPEKPKPEV 365
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958762180  177 RTKPKKASKDQGPTPVERKKKGKRKNETTVESLELDQSLPNPSLQ-SPEEPSESADSQKRRSGRQVK 242
Cdd:NF033839   366 KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPEKPKPEVK 432
PTZ00121 PTZ00121
MAEBL; Provisional
104-248 4.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  104 QEGTKASKDREPKPKRKREpkepkEPRRAKEPKRAKEPK---EAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKP 180
Cdd:PTZ00121  1143 EEARKAEDAKRVEIARKAE-----DARKAEEARKAEDAKkaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  181 KKASKDQGPTPVERKKKGKRKNEttvESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:PTZ00121  1218 RKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
PTZ00121 PTZ00121
MAEBL; Provisional
104-242 5.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  104 QEGTKASKDREPKPKRKRE--PKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPK 181
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958762180  182 KASKDQGPTPVERKKKGKRKNETTVESLELDqslpnpslQSPEEPSESADSQKRRSGRQVK 242
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAK--------KKAEEDKKKADELKKAAAAKKK 1419
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
591-657 8.87e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 40.59  E-value: 8.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958762180  591 WSCVVIDEAHRL------KNRNCKLLEGLKlMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE 657
Cdd:PRK04914   273 WDLLVVDEAHHLvwseeaPSREYQVVEQLA-EVIPGVLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFVEE 344
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
116-248 9.44e-03

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 40.15  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762180  116 KPKRKREPKE---PKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPV 192
Cdd:NF040676   214 KPKEEVKVQEevkPKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKA 293
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958762180  193 ER--KKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNE 248
Cdd:NF040676   294 QEiaKAKEEEKAQEIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEA 351
 
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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