NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|52545542|emb|CAH56404|]
View 

hypothetical protein, partial [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 80-596 5.99e-165

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: 513.19  E-value: 5.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    80 GTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYV 159
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   160 VTYTGDKESRSVIRENEFsfednairsgkkvfrmkkeVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:PLN03142  248 VKFHGNPEERAHQREELL-------------------VAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   240 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRRLKA 316
Cdd:PLN03142  309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRRLKS 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   317 DVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNskGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLpngsy 396
Cdd:PLN03142  389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVN--AGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT----- 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   397 DGSSLVKSSGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQF 476
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   477 CFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVR 556
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 52545542   557 PGLGSKSGSMTKQELDDILKFGTEELFK--------DDVEGMMSQGQR 596
Cdd:PLN03142  622 QGRLAEQKTVNKDELLQMVRYGAEMVFSskdstitdEDIDRIIAKGEE 669
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
 771-911 1.08e-79

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


:

Pssm-ID: 461920  Cd Length: 137  Bit Score: 256.14  E-value: 1.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    771 GQSGRRQSRRQLKSDRDKPLPpLLARVGGNIEVLGFNARQRKAFLNAIMRWGMppqDAFNSHWLVRDLRGKSEKEFRAYV 850
Cdd:pfam06461    1 PQTGRRPYRRRARVDKDEPLP-LMEGEGGSIEVLGFNARQRKAFLNALMRYGM---GNFDWKEFVRDLRGKTEKEIKAYG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52545542    851 SLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDL 911
Cdd:pfam06461   77 SLFLRHICEPGADNSETFADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DUF1087 pfam06465
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
 680-733 1.22e-21

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


:

Pssm-ID: 461922  Cd Length: 60  Bit Score: 89.02  E-value: 1.22e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 52545542    680 EDGVEEVEREIIKQE-ENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNY 733
Cdd:pfam06465    1 AAAEEEAQKEVIKEEnESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVS 55
CD_CSD super family cl28914
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 1-24 3.14e-04

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.


The actual alignment was detected with superfamily member cd18662:

Pssm-ID: 475127 [Multi-domain]  Cd Length: 55  Bit Score: 39.56  E-value: 3.14e-04
                         10        20
                 ....*....|....*....|....
gi 52545542    1 YDQCTWEIDDIDIPYYDNLKQAYW 24
Cdd:cd18662   31 YDQSTWESEDDDIPDYEKHIQEYW 54
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 80-596 5.99e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.19  E-value: 5.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    80 GTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYV 159
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   160 VTYTGDKESRSVIRENEFsfednairsgkkvfrmkkeVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:PLN03142  248 VKFHGNPEERAHQREELL-------------------VAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   240 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRRLKA 316
Cdd:PLN03142  309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRRLKS 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   317 DVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNskGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLpngsy 396
Cdd:PLN03142  389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVN--AGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT----- 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   397 DGSSLVKSSGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQF 476
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   477 CFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVR 556
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 52545542   557 PGLGSKSGSMTKQELDDILKFGTEELFK--------DDVEGMMSQGQR 596
Cdd:PLN03142  622 QGRLAEQKTVNKDELLQMVRYGAEMVFSskdstitdEDIDRIIAKGEE 669
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 82-313 4.65e-163

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: 479.56  E-value: 4.65e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18057   81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 79-555 1.12e-132

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 417.32  E-value: 1.12e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   79 GGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHsKGPYLVSAPLSTIINWEREFEMWAPDFY 158
Cdd:COG0553  239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLVGNWQRELAKFAPGLR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  159 VVTYTGDKESRSVIREnefsFEDnairsgkkvfrmkkevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:COG0553  318 VLVLDGTRERAKGANP----FED-------------------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPA 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  239 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD-ISKEDQ--IKKLHDLLGPHMLRRLK 315
Cdd:COG0553  375 TKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARpIEKGDEeaLERLRRLLRPFLLRRTK 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  316 ADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALN-SKGGGNQVSLLNIMMDLKKCCNHPYLFPVaaveapvlpng 394
Cdd:COG0553  455 EDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEgAEGIRRRGLILAALTRLRQICSHPALLLE----------- 523

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  395 syDGSSLVKSSGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNA-PGA 473
Cdd:COG0553  524 --EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEgPEA 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  474 QQfcFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHL 553
Cdd:COG0553  602 PV--FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAES 679


                 ..
gi 52545542  554 VV 555
Cdd:COG0553  680 VL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 85-381 5.65e-86

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: 279.18  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     85 YQLEGLNWLRFSWAQ-GTDTILADEMGLGKTVQTIVFLYSLYKEGHSKG-PYLVSAPLSTIINWEREFEMWA--PDFYVV 160
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    161 TYTGDKESRSVIREnefsfednairsgkkvfrmKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSK 240
Cdd:pfam00176   81 VLHGNKRPQERWKN-------------------DPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSK 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    241 FFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISKEDQ---IKKLHDLLGPHMLRRLKA 316
Cdd:pfam00176  142 LSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFdRPIERGGGkkgVSRLHKLLKPFLLRRTKK 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52545542    317 DVFKNMPAKTELIVRVELSQMQKKYYK-FILTRNFEALNSKGGGNQV--SLLNIMMDLKKCCNHPYLF 381
Cdd:pfam00176  222 DVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIkaSLLNILMRLRKICNHPGLI 289
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
 771-911 1.08e-79

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


Pssm-ID: 461920  Cd Length: 137  Bit Score: 256.14  E-value: 1.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    771 GQSGRRQSRRQLKSDRDKPLPpLLARVGGNIEVLGFNARQRKAFLNAIMRWGMppqDAFNSHWLVRDLRGKSEKEFRAYV 850
Cdd:pfam06461    1 PQTGRRPYRRRARVDKDEPLP-LMEGEGGSIEVLGFNARQRKAFLNALMRYGM---GNFDWKEFVRDLRGKTEKEIKAYG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52545542    851 SLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDL 911
Cdd:pfam06461   77 SLFLRHICEPGADNSETFADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DEXDc smart00487
DEAD-like helicases superfamily;
76-284 6.95e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.34  E-value: 6.95e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542      76 DSTGGTLHPYQLEGLNWLRFSWaqgTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPL-STIINWEREFEMWA 154
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTrELAEQWAEELKKLG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     155 PDFY--VVTYTGDKESRSVIREnefsfednaIRSGkkvfrmkkevqiKFHVLLTSYELIT--IDQAILGSIEWACLVVDE 230
Cdd:smart00487   79 PSLGlkVVGLYGGDSKREQLRK---------LESG------------KTDILVTTPGRLLdlLENDKLSLSNVDLVILDE 137

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542     231 AHRLKNNqsKFFRVLNSY-----KIDYKLLLTGTP---LQNNLEELFHLLNFLTPERFNNLE 284
Cdd:smart00487  138 AHRLLDG--GFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DUF1087 pfam06465
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
 680-733 1.22e-21

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


Pssm-ID: 461922  Cd Length: 60  Bit Score: 89.02  E-value: 1.22e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 52545542    680 EDGVEEVEREIIKQE-ENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNY 733
Cdd:pfam06465    1 AAAEEEAQKEVIKEEnESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVS 55
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
 1-24 3.14e-04

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 39.56  E-value: 3.14e-04
                         10        20
                 ....*....|....*....|....
gi 52545542    1 YDQCTWEIDDIDIPYYDNLKQAYW 24
Cdd:cd18662   31 YDQSTWESEDDDIPDYEKHIQEYW 54
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 80-596 5.99e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.19  E-value: 5.99e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    80 GTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYV 159
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   160 VTYTGDKESRSVIRENEFsfednairsgkkvfrmkkeVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:PLN03142  248 VKFHGNPEERAHQREELL-------------------VAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENS 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   240 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ---IKKLHDLLGPHMLRRLKA 316
Cdd:PLN03142  309 LLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRRLKS 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   317 DVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNskGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLpngsy 396
Cdd:PLN03142  389 DVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVN--AGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYT----- 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   397 DGSSLVKSSGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQF 476
Cdd:PLN03142  462 TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKF 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   477 CFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVR 556
Cdd:PLN03142  542 VFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ 621

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 52545542   557 PGLGSKSGSMTKQELDDILKFGTEELFK--------DDVEGMMSQGQR 596
Cdd:PLN03142  622 QGRLAEQKTVNKDELLQMVRYGAEMVFSskdstitdEDIDRIIAKGEE 669
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 82-313 4.65e-163

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: 479.56  E-value: 4.65e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18057   81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 82-313 2.29e-156

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: 462.17  E-value: 2.29e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18055   81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 82-313 1.36e-148

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: 442.20  E-value: 1.36e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18056   81 YVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 82-313 2.21e-141

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: 421.85  E-value: 2.21e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDkesrsvirenefsfednairsgkkvfrmkkevqikfHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd17994   81 YVGD------------------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKF 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd17994  125 FRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 79-555 1.12e-132

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 417.32  E-value: 1.12e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   79 GGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHsKGPYLVSAPLSTIINWEREFEMWAPDFY 158
Cdd:COG0553  239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLVGNWQRELAKFAPGLR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  159 VVTYTGDKESRSVIREnefsFEDnairsgkkvfrmkkevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:COG0553  318 VLVLDGTRERAKGANP----FED-------------------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPA 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  239 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD-ISKEDQ--IKKLHDLLGPHMLRRLK 315
Cdd:COG0553  375 TKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARpIEKGDEeaLERLRRLLRPFLLRRTK 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  316 ADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALN-SKGGGNQVSLLNIMMDLKKCCNHPYLFPVaaveapvlpng 394
Cdd:COG0553  455 EDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEgAEGIRRRGLILAALTRLRQICSHPALLLE----------- 523

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  395 syDGSSLVKSSGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNA-PGA 473
Cdd:COG0553  524 --EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEgPEA 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  474 QQfcFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHL 553
Cdd:COG0553  602 PV--FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAES 679


                 ..
gi 52545542  554 VV 555
Cdd:COG0553  680 VL 681
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 82-313 2.26e-100

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: 315.34  E-value: 2.26e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 161
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd17995   80 YHGSGESRQIIQQYEMYFKDAQGRKKKGVY--------KFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd17995  152 LQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 81-313 1.35e-96

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: 305.05  E-value: 1.35e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   81 TLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVV 160
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  161 TYTGDKESRSVIRENEFSFEdnairSGKKvfrmkkevqIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSK 240
Cdd:cd17993   81 VYLGDIKSRDTIREYEFYFS-----QTKK---------LKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52545542  241 FFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd17993  147 LYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 85-381 5.65e-86

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: 279.18  E-value: 5.65e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     85 YQLEGLNWLRFSWAQ-GTDTILADEMGLGKTVQTIVFLYSLYKEGHSKG-PYLVSAPLSTIINWEREFEMWA--PDFYVV 160
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    161 TYTGDKESRSVIREnefsfednairsgkkvfrmKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSK 240
Cdd:pfam00176   81 VLHGNKRPQERWKN-------------------DPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSK 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    241 FFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISKEDQ---IKKLHDLLGPHMLRRLKA 316
Cdd:pfam00176  142 LSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFdRPIERGGGkkgVSRLHKLLKPFLLRRTKK 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52545542    317 DVFKNMPAKTELIVRVELSQMQKKYYK-FILTRNFEALNSKGGGNQV--SLLNIMMDLKKCCNHPYLF 381
Cdd:pfam00176  222 DVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIkaSLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 82-277 5.78e-83

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: 266.74  E-value: 5.78e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRenefsfednairsgkkvfrmKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd17919   81 YHGSQRERAQIR--------------------AKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQL 140

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 277
Cdd:cd17919  141 SKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
 771-911 1.08e-79

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


Pssm-ID: 461920  Cd Length: 137  Bit Score: 256.14  E-value: 1.08e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    771 GQSGRRQSRRQLKSDRDKPLPpLLARVGGNIEVLGFNARQRKAFLNAIMRWGMppqDAFNSHWLVRDLRGKSEKEFRAYV 850
Cdd:pfam06461    1 PQTGRRPYRRRARVDKDEPLP-LMEGEGGSIEVLGFNARQRKAFLNALMRYGM---GNFDWKEFVRDLRGKTEKEIKAYG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52545542    851 SLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDL 911
Cdd:pfam06461   77 SLFLRHICEPGADNSETFADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 66-313 2.91e-79

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: 258.78  E-value: 2.91e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   66 VKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIIN 145
Cdd:cd18054    5 VALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  146 WEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAirsgkkvfrmkkevQIKFHVLLTSYELITIDQAILGSIEWAC 225
Cdd:cd18054   85 WQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTK--------------RLKFNALITTYEILLKDKTVLGSINWAF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  226 LVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHDL 305
Cdd:cd18054  151 LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-GRENGYQSLHKV 229


                 ....*...
gi 52545542  306 LGPHMLRR 313
Cdd:cd18054  230 LEPFLLRR 237
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 79-315 3.03e-73

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: 242.29  E-value: 3.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   79 GGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFY 158
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  159 VVTYTGDKESRSVIRENefsfednairsgkkvfRMKKEVQI-KFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNN 237
Cdd:cd18009   80 VLLYHGTKEERERLRKK----------------IMKREGTLqDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  238 QSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFL------------EEFADISKEDQ---IKKL 302
Cdd:cd18009  144 NCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFEswfdfsslsdnaADISNLSEEREqniVHML 223

                        250
                 ....*....|...
gi 52545542  303 HDLLGPHMLRRLK 315
Cdd:cd18009  224 HAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 79-315 9.98e-72

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: 238.04  E-value: 9.98e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   79 GGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFY 158
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  159 VVTYTGDKESRsvirenefsfednairsgKKVFrmKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:cd17996   81 KIVYKGTPDVR------------------KKLQ--SQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  239 SKFFRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA------------DISKEDQ---IKKL 302
Cdd:cd17996  141 SKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETlliIRRL 220

                        250
                 ....*....|...
gi 52545542  303 HDLLGPHMLRRLK 315
Cdd:cd17996  221 HKVLRPFLLRRLK 233
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 82-313 5.77e-70

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: 232.63  E-value: 5.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 161
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMG-IRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18058   79 YHGSQISRQMIQQYEMYYRDEQGNPLSGIF--------KFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18058  151 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 82-313 2.94e-67

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: 225.30  E-value: 2.94e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 161
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKG-IHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18059   79 YHGSQASRRTIQLYEMYFKDPQGRVIKGSY--------KFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18059  151 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 82-313 7.01e-67

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: 223.85  E-value: 7.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDnairsgkkvfrmkkevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNR-------------------FHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLL 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 313
Cdd:cd18006  142 HKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSETDDESEtVEELHLLLQPFLLRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 79-315 1.53e-66

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


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 222.97  E-value: 1.53e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   79 GGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFY 158
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  159 VVTYTGDKESRSVIRENEFsfednairsgkkvfrmkkeVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:cd17997   81 VVVLIGDKEERADIIRDVL-------------------LPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  239 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFaDISKEDQ-----IKKLHDLLGPHMLRR 313
Cdd:cd17997  142 SKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF-NVNNCDDdnqevVQRLHKVLRPFLLRR 220


                 ..
gi 52545542  314 LK 315
Cdd:cd17997  221 IK 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 82-313 2.87e-65

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: 219.54  E-value: 2.87e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 161
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18060   79 YHGSLASRQMIQQYEMYCKDSRGRLIPGAY--------KFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18060  151 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 82-313 2.19e-64

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: 217.18  E-value: 2.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 161
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEFSFEDNAIRSGKKVFRmkkevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18061   79 YHGSLISRQMIQQYEMYFRDSQGRIIRGAYR--------FQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 313
Cdd:cd18061  151 LEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 66-313 8.64e-63

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: 213.37  E-value: 8.64e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   66 VKFDKQPWYIDSTGG-TLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTII 144
Cdd:cd18053    4 VALKKQPSYIGGHEGlELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  145 NWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAirsgkkvfrmkkevQIKFHVLLTSYELITIDQAILGSIEWA 224
Cdd:cd18053   84 SWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTK--------------RLKFNILLTTYEILLKDKSFLGGLNWA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  225 CLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHD 304
Cdd:cd18053  150 FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK-GREYGYASLHK 228


                 ....*....
gi 52545542  305 LLGPHMLRR 313
Cdd:cd18053  229 ELEPFLLRR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 405-531 1.98e-59

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: 199.63  E-value: 1.98e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  405 SGKLMLLQKMLKKLRDEGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGaQQFCFLLSTRA 484
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLSTKA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 52545542  485 GGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFV 531
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 82-313 5.84e-59

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: 201.81  E-value: 5.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENefSFEDNAirsgkkvfrmkkevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18003   81 YYGSAKERKLKRQG--WMKPNS-----------------FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD----ISKEDQ------IKKLHDLLGPHML 311
Cdd:cd18003  142 WQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNpltaMSEGSQeeneelVRRLHKVLRPFLL 221


                 ..
gi 52545542  312 RR 313
Cdd:cd18003  222 RR 223
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 80-315 3.15e-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: 199.71  E-value: 3.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   80 GTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYV 159
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEG-RKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  160 VTYTGDKESRSVIRENEfsfednairsgkkvfrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:cd18012   82 LVIHGTKRKREKLRALE-----------------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQT 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  240 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-DISK---EDQIKKLHDLLGPHMLRRLK 315
Cdd:cd18012  139 KTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkPIEKdgdEEALEELKKLISPFILRRLK 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 82-313 3.30e-55

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: 191.56  E-value: 3.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENefsfednaiRSGKKVFRMKKevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18002   81 YWGNPKDRKVLRKF---------WDRKNLYTRDA----PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  242 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-DIS---------KEDQIKKLHDLLGPHML 311
Cdd:cd18002  148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEshaenktglNEHQLKRLHMILKPFML 227


                 ..
gi 52545542  312 RR 313
Cdd:cd18002  228 RR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 67-325 2.80e-52

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: 183.71  E-value: 2.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   67 KFDKQPWYIdsTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINW 146
Cdd:cd18064    3 RFEDSPSYV--KWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  147 EREFEMWAPDFYVVTYTGDKESRSvirenefSFEDNAIRSGKkvfrmkkevqikFHVLLTSYELITIDQAILGSIEWACL 226
Cdd:cd18064   81 MAEFKRWVPTLRAVCLIGDKDQRA-------AFVRDVLLPGE------------WDVCVTSYEMLIKEKSVFKKFNWRYL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  227 VVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKLH 303
Cdd:cd18064  142 VIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLH 221

                        250       260
                 ....*....|....*....|..
gi 52545542  304 DLLGPHMLRRLKADVFKNMPAK 325
Cdd:cd18064  222 MVLRPFLLRRIKADVEKSLPPK 243
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 82-280 8.88e-52

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: 179.89  E-value: 8.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHsKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGDKESRSVIRENEfsfednairsgkkvfrmkKEVQIKFHVLLTSYELIT---IDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:cd17998   80 YYGSQEERKHLRYDI------------------LKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMT 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 52545542  239 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF 280
Cdd:cd17998  142 SERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 66-315 1.97e-51

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: 180.98  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   66 VKFDKQPWYIdsTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIIN 145
Cdd:cd18065    2 VRFEESPSYV--KGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  146 WEREFEMWAPDFYVVTYTGDKESRSVIRENEFsfednairsgkkvfrMKKEvqikFHVLLTSYELITIDQAILGSIEWAC 225
Cdd:cd18065   80 WMNEFKRWVPSLRAVCLIGDKDARAAFIRDVM---------------MPGE----WDVCVTSYEMVIKEKSVFKKFNWRY 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  226 LVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD---ISKEDQIKKL 302
Cdd:cd18065  141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERL 220

                        250
                 ....*....|...
gi 52545542  303 HDLLGPHMLRRLK 315
Cdd:cd18065  221 HAVLKPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 80-315 2.73e-50

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: 178.33  E-value: 2.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   80 GTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYV 159
Cdd:cd18063   22 GTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  160 VTYTGDKESRSVIRENefsfednaIRSGkkvfrmkkevqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:cd18063  102 ISYKGTPAMRRSLVPQ--------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  240 KFFRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDL 305
Cdd:cd18063  162 KLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgerVDLNEEETiliIRRLHKV 241

                        250
                 ....*....|
gi 52545542  306 LGPHMLRRLK 315
Cdd:cd18063  242 LRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 65-315 6.03e-49

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: 174.46  E-value: 6.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   65 TVKFDKQPWYIdsTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTII 144
Cdd:cd18062    9 TEKVEKQSSLL--VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  145 NWEREFEMWAPDFYVVTYTGDKESRSVIREnefsfednAIRSGkkvfrmkkevqiKFHVLLTSYELITIDQAILGSIEWA 224
Cdd:cd18062   87 NWVYEFDKWAPSVVKVSYKGSPAARRAFVP--------QLRSG------------KFNVLLTTYEYIIKDKQILAKIRWK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  225 CLVVDEAHRLKNNQSKFFRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADI 293
Cdd:cd18062  147 YMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDL 226

                        250       260
                 ....*....|....*....|....*
gi 52545542  294 SKEDQ---IKKLHDLLGPHMLRRLK 315
Cdd:cd18062  227 NEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 82-313 4.11e-43

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


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 157.54  E-value: 4.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLY-----------------KEGHS---KGPYLVSAPLS 141
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfkKKPPAssaKKPVLIVAPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  142 TIINWEREFEMWApDFYVVTYTGdkesrsvirenefsfednairSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSI 221
Cdd:cd18005   81 VLYNWKDELDTWG-HFEVGVYHG---------------------SRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSI 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  222 EWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD--------- 292
Cdd:cd18005  139 NWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrht 218

                        250       260
                 ....*....|....*....|....*..
gi 52545542  293 -----ISKEDQIKK-LHDLLGPHMLRR 313
Cdd:cd18005  219 atareLRLGRKRKQeLAVKLSKFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 82-277 1.03e-41

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: 151.32  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFyvvt 161
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPF---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 ytgdkesRSVIRENEFSFeDNAIRSGKKVFRMKKEVQIKF---HVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQ 238
Cdd:cd18000   77 -------RVVVLHSSGSG-TGSEEKLGSIERKSQLIRKVVgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPD 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 52545542  239 SKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 277
Cdd:cd18000  149 AEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 82-290 5.07e-39

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: 145.51  E-value: 5.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLnwlRFSWAQ--GTDT--------ILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFE 151
Cdd:cd18007    1 LKPHQVEGV---RFLWSNlvGTDVgsdegggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  152 MWAPDFYVVTYTGDkesrsvirenefsfEDNAIRSGKKVFRMKKevqiKFH----VLLTSYEL--------ITIDQAILG 219
Cdd:cd18007   78 KWLPPDLRPLLVLV--------------SLSASKRADARLRKIN----KWHkeggVLLIGYELfrnlasnaTTDPRLKQE 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52545542  220 SIEWAC------LVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 290
Cdd:cd18007  140 FIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 82-313 2.07e-37

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 140.88  E-value: 2.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWL-----RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGP----YLVSAPLSTIINWEREFEM 152
Cdd:cd18004    1 LRPHQREGVQFLydcltGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  153 WAPDFYVVTYTGDKESRSVIRENEFSFEDNAirsgkkvfrmkkevqikFHVLLTSYELITIDQAILGS-IEWACLVVDEA 231
Cdd:cd18004   81 WLGLRRIKVVTADGNAKDVKASLDFFSSAST-----------------YPVLIISYETLRRHAEKLSKkISIDLLICDEG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  232 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQI--- 299
Cdd:cd18004  144 HRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFeepilrsrdPDASEEDKElga 223

                        250
                 ....*....|....*..
gi 52545542  300 KKLHDL---LGPHMLRR 313
Cdd:cd18004  224 ERSQELselTSRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 82-313 2.67e-37

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: 140.50  E-value: 2.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFswaQGTdtILADEMGLGKTVQTIVFLYS------------LYKEGHSKGPY-----LVSAPLSTII 144
Cdd:cd18008    1 LLPYQKQGLAWMLP---RGG--ILADEMGLGKTIQALALILAtrpqdpkipeelEENSSDPKKLYlskttLIVVPLSLLS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  145 NWEREFEM--WAPDFYVVTYTGDKESRSvirenefsfednairsgkkvfrmkKEVQIKFHVLLTSYELITID-------- 214
Cdd:cd18008   76 QWKDEIEKhtKPGSLKVYVYHGSKRIKS------------------------IEELSDYDIVITTYGTLASEfpknkkgg 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  215 --------QAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGF 286
Cdd:cd18008  132 grdskekeASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF 211

                        250       260       270
                 ....*....|....*....|....*....|
gi 52545542  287 LEEFADISKEDQ---IKKLHDLLGPHMLRR 313
Cdd:cd18008  212 NSDISKPFSKNDrkaLERLQALLKPILLRR 241
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 82-313 7.96e-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: 138.64  E-value: 7.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS-------LYKEGHSkgPYLVSAPLSTIINWEREFEMWA 154
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkranSFNSENL--PSLVVCPPTLVGHWVAEIKKYF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  155 PDFY--VVTYTGDKESRSVIREnefsfednairsgkkvfrmkkevQIKFH-VLLTSYELITIDQAILGSIEWACLVVDEA 231
Cdd:cd17999   79 PNAFlkPLAYVGPPQERRRLRE-----------------------QGEKHnVIVASYDVLRNDIEVLTKIEWNYCVLDEG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  232 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA----------DISKEDQ--- 298
Cdd:cd17999  136 HIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrdskASAKEQEaga 215

                        250
                 ....*....|....*..
gi 52545542  299 --IKKLHDLLGPHMLRR 313
Cdd:cd17999  216 laLEALHKQVLPFLLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 82-313 5.70e-36

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: 136.35  E-value: 5.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPyLVSAPLSTIINWEREFEMWAPDFYVVT 161
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 YTGdkesrSVIRENEFSFEdnairsgkkvfrmkkEVQIKFHVLLTSYELITIDQAILGSIE-----WACLVVDEAHRLKN 236
Cdd:cd18001   80 FHG-----TSKKERERNLE---------------RIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKN 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  237 NQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPerfNNLEGFLEEF----------ADISKEDQIKK----- 301
Cdd:cd18001  140 SKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACN---GSLLGTRKTFkmefenpitrGRDKDATQGEKalgse 216

                        250
                 ....*....|....*.
gi 52545542  302 ----LHDLLGPHMLRR 313
Cdd:cd18001  217 vaenLRQIIKPYFLRR 232
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 406-520 5.74e-30

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: 114.62  E-value: 5.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    406 GKLMLLQKMLKKLRdeGHRLLIFSQMTKMLDLlEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPgaqQFCFLLSTRAG 485
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVA 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 52545542    486 GLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIG 520
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 82-313 1.43e-27

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: 112.56  E-value: 1.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLnwlRFSWAQGTDT--------ILADEMGLGKTVQTIVFLYSLYKEGHSKGPYL----VSAPLSTIINWERE 149
Cdd:cd18067    1 LRPHQREGV---KFLYRCVTGRrirgshgcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  150 FEMW-APDFYVVTYTGdKESRSVIRENEFSFEDNAIRSGKKVfrmkkevqikfhvLLTSYELITIDQAILGSIEWACLVV 228
Cdd:cd18067   78 LGKWlGGRLQPLAIDG-GSKKEIDRKLVQWASQQGRRVSTPV-------------LIISYETFRLHVEVLQKGEVGLVIC 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  229 DEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISK---- 295
Cdd:cd18067  144 DEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADASEkerq 223

                        250       260
                 ....*....|....*....|
gi 52545542  296 --EDQIKKLHDLLGPHMLRR 313
Cdd:cd18067  224 lgEEKLQELISIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 82-277 3.28e-26

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: 108.39  E-value: 3.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWL-------RFSWAQGTdtILADEMGLGKTVQTIVFLYSLYKEGHSKGP-----YLVSAPLSTIINWERE 149
Cdd:cd18066    1 LRPHQREGIEFLyecvmgmRVNERFGA--ILADEMGLGKTLQCISLIWTLLRQGPYGGKpvikrALIVTPGSLVKNWKKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  150 FEMW--APDFYVVTYTGDKESRSVIRENEFSfednairsgkkvfrmkkevqikfhVLLTSYELITIDQAILGSIEWACLV 227
Cdd:cd18066   79 FQKWlgSERIKVFTVDQDHKVEEFIASPLYS------------------------VLIISYEMLLRSLDQISKLNFDLVI 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 52545542  228 VDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 277
Cdd:cd18066  135 CDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 82-313 6.72e-26

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: 106.52  E-value: 6.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhskgPYLVSAPLSTIINWEREFEMWAPDfyvvt 161
Cdd:cd18010    1 LLPFQREGV---CFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEW----PLLIVCPSSLRLTWADEIERWLPS----- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  162 ytgdkesrsvirenEFSFEDNAIRSGKKVFRMKKevqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 241
Cdd:cd18010   69 --------------LPPDDIQVIVKSKDGLRDGD-----AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKR 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  242 FRVLNSY--KIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLE---------GFLEEFADISKEDQIKKLHDLLGPH- 309
Cdd:cd18010  130 TKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHdfgrrycaaKQGGFGWDYSGSSNLEELHLLLLATi 209


                 ....
gi 52545542  310 MLRR 313
Cdd:cd18010  210 MIRR 213
DEXDc smart00487
DEAD-like helicases superfamily;
76-284 6.95e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 103.34  E-value: 6.95e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542      76 DSTGGTLHPYQLEGLNWLRFSWaqgTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPL-STIINWEREFEMWA 154
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTrELAEQWAEELKKLG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     155 PDFY--VVTYTGDKESRSVIREnefsfednaIRSGkkvfrmkkevqiKFHVLLTSYELIT--IDQAILGSIEWACLVVDE 230
Cdd:smart00487   79 PSLGlkVVGLYGGDSKREQLRK---------LESG------------KTDILVTTPGRLLdlLENDKLSLSNVDLVILDE 137

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542     231 AHRLKNNqsKFFRVLNSY-----KIDYKLLLTGTP---LQNNLEELFHLLNFLTPERFNNLE 284
Cdd:smart00487  138 AHRLLDG--GFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
HELICc smart00490
helicase superfamily c-terminal domain;
436-520 2.60e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 97.67  E-value: 2.60e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     436 DLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPgaqQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSR 515
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77


                    ....*
gi 52545542     516 AHRIG 520
Cdd:smart00490   78 AGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 82-290 9.70e-23

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: 97.96  E-value: 9.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEM 152
Cdd:cd18069    1 LKPHQIGGIRFLydniiesleRYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSEFNK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  153 WAPDFyvvtytgdkESRSVIRENefSFEDNAIRSGKKVFRMKKEVQIKFH----VLLTSYELITIDQAIlgsiewACLVV 228
Cdd:cd18069   80 WLPPP---------EALPNVRPR--PFKVFILNDEHKTTAARAKVIEDWVkdggVLLMGYEMFRLRPGP------DVVIC 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52545542  229 DEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 290
Cdd:cd18069  143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 204
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 82-313 1.47e-22

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 96.97  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNW------LRFswaqgtdtILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEreFEMW-- 153
Cdd:cd18011    1 PLPHQIDAVLRalrkppVRL--------LLADEVGLGKTIEAGLIIKELLLRGDAK-RVLILCPASLVEQWQ--DELQdk 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  154 -APDFYVVtytgDKESRSVIRenefsfednaiRSGKKVFRMkkevqikFHVLLTSYELI---TIDQAILGSIEWACLVVD 229
Cdd:cd18011   70 fGLPFLIL----DRETAAQLR-----------RLIGNPFEE-------FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVD 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  230 EAHRLKNNQ----SKFFRVLN--SYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEfadiskedqiKKLH 303
Cdd:cd18011  128 EAHKLRNSGggkeTKRYKLGRllAKRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL----------DGLR 197

                        250
                 ....*....|
gi 52545542  304 DLLGPHMLRR 313
Cdd:cd18011  198 EVLAKVLLRR 207
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 82-292 9.02e-22

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 95.73  E-value: 9.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTIVFLYSLY----KEGHSKGpyLVSAPLSTIIN 145
Cdd:cd18068    1 LKPHQVDGV---QFMWdccceslkktkkSPGSGCILAHCMGLGKTLQVVTFLHTVLlcekLENFSRV--LVVCPLNTVLN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  146 WEREFEMWAP--------DFYVVTYTGDKESRSvIRENEFSFEDNAIRSGKKVFR-MKKEVQIKfhvllTSYELITIDQA 216
Cdd:cd18068   76 WLNEFEKWQEglkdeekiEVNELATYKRPQERS-YKLQRWQEEGGVMIIGYDMYRiLAQERNVK-----SREKLKEIFNK 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52545542  217 ILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPerfnNLEGFLEEFAD 292
Cdd:cd18068  150 ALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKP----NLLGTIKEFRN 221
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 104-287 1.07e-21

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: 95.23  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  104 ILADEMGLGKTVQTIVFLYSlykeghskGPYLVSAPLSTIINWEREFEMW----APDFYvvTYTGDKESRSVireNEFSF 179
Cdd:cd18071   52 ILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHvkpgQLKVY--TYHGGERNRDP---KLLSK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  180 EDnairsgkkvfrmkkevqikfhVLLTSYELITIDQAI-----LGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKL 254
Cdd:cd18071  119 YD---------------------IVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRW 177

                        170       180       190
                 ....*....|....*....|....*....|...
gi 52545542  255 LLTGTPLQNNLEELFHLLNFLTPERFNNLEGFL 287
Cdd:cd18071  178 VLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWR 210
DUF1087 pfam06465
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
 680-733 1.22e-21

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


Pssm-ID: 461922  Cd Length: 60  Bit Score: 89.02  E-value: 1.22e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 52545542    680 EDGVEEVEREIIKQE-ENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNY 733
Cdd:pfam06465    1 AAAEEEAQKEVIKEEnESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVS 55
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 82-313 3.90e-15

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 76.36  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQG-TDTILADEMGLGKTVQTI-VFLYSLYKEGHSKGP---------------------YLVSA 138
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKpRGGILADDMGLGKTLTMIaLILAQKNTQNRKEEEkekalteweskkdstlvpsagTLVVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  139 PLSTIINWEREFEmwapdfyvvtytgDKESRSVIRENEFSfEDNAIRSGKkVFRmkkevqiKFHVLLTSYELI------- 211
Cdd:cd18072   81 PASLVHQWKNEVE-------------SRVASNKLRVCLYH-GPNRERIGE-VLR-------DYDIVITTYSLVakeipty 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  212 --TIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEE 289
Cdd:cd18072  139 keESRSSPLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQ 218

                        250       260
                 ....*....|....*....|....
gi 52545542  290 FADISKEDQiKKLHDLLGPHMLRR 313
Cdd:cd18072  219 VDNKSRKGG-ERLNILTKSLLLRR 241
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
76-534 4.74e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.05  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   76 DSTGGTLHPYQLEGLNWLRFSWAQGTDTILAdEM--GLGKTVqTIVFLYSLYKEGhskGPYLVSAPLSTIIN-WEREFEM 152
Cdd:COG1061   75 SGTSFELRPYQQEALEALLAALERGGGRGLV-VAptGTGKTV-LALALAAELLRG---KRVLVLVPRRELLEqWAEELRR 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  153 WAPDFYVVtytgdkesrsvirenefsfednairSGKKvfrmkkevQIKFHVLLTSYELITIDQAI--LGSiEWACLVVDE 230
Cdd:COG1061  150 FLGDPLAG-------------------------GGKK--------DSDAPITVATYQSLARRAHLdeLGD-RFGLVIIDE 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  231 AHRLKNNQskFFRVLNSYKIDYKLLLTGTPlqnnleelfhllnfltpERFNNLEGFLEEFADISKEdqiKKLHDLLGPHM 310
Cdd:COG1061  196 AHHAGAPS--YRRILEAFPAAYRLGLTATP-----------------FRSDGREILLFLFDGIVYE---YSLKEAIEDGY 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  311 LRrlKADVFknmpaktelIVRVELSQMQKKYYKFIlTRNFEALNSKgggnqvsllnimmdlkkccnhpylfpvaaveapv 390
Cdd:COG1061  254 LA--PPEYY---------GIRVDLTDERAEYDALS-ERLREALAAD---------------------------------- 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  391 lpngsydgsslvkSSGKLMLLQKMLKKLRDeGHRLLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNA 470
Cdd:COG1061  288 -------------AERKDKILRELLREHPD-DRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD 353

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52545542  471 pGAQQfcFLLSTRAGGLGINLATADTVIIYDsdwnPHND----IQAFSRAHRIGQNKK-VMIYRFVTRA 534
Cdd:COG1061  354 -GELR--ILVTVDVLNEGVDVPRLDVAILLR----PTGSprefIQRLGRGLRPAPGKEdALVYDFVGND 415
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 82-280 9.64e-11

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 63.52  E-value: 9.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRfsWAQGtdtILADEMGLGKTVQTI----------------------VFLYSLYKEGHSK---GPYLV 136
Cdd:cd18070    1 LLPYQRRAVNWML--VPGG---ILADEMGLGKTVEVLalillhprpdndldaadddsdeMVCCPDCLVAETPvssKATLI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  137 SAPLSTIINWEREFEMWAPDFYVV-TYTGDKESRSVIRE---------------NEFSFE---DNAIRSGKKVFRMKKEV 197
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPSSLKVlTYQGVKKDGALASPapeilaeydivvttyDVLRTElhyAEANRSNRRRRRQKRYE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  198 QIKfhvlltsyelitidqAILGSIEWACLVVDEAHRLKNNQSK-------FFRVlNSYKIdyklllTGTPLQNNLEELFH 270
Cdd:cd18070  156 APP---------------SPLVLVEWWRVCLDEAQMVESSTSKaaemarrLPRV-NRWCV------SGTPIQRGLDDLFG 213

                        250
                 ....*....|
gi 52545542  271 LLNFLTPERF 280
Cdd:cd18070  214 LLSFLGVEPF 223
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 82-269 1.82e-09

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 58.90  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGLNWLRFSWAQGtdtILADeMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIIN-WEREFEMWapdfyvv 160
Cdd:cd18013    1 PHPYQKVAINFIIEHPYCG---LFLD-MGLGKTVTTLTALSDLQLDD-FTRRVLVIAPLRVARStWPDEVEKW------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  161 tytgdkesrSVIRENEFSFednAIRSGKKvfrMKKEVQIKFHVLLTSYELIT-IDQAILGSIEWACLVVDEAHRLKNNQS 239
Cdd:cd18013   69 ---------NHLRNLTVSV---AVGTERQ---RSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFKSPRS 133

                        170       180       190
                 ....*....|....*....|....*....|..
gi 52545542  240 KFFRVLNSY--KIDYKLLLTGTPLQNNLEELF 269
Cdd:cd18013  134 KRFKALRKVrpVIKRLIGLTGTPSPNGLMDLW 165
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
222-329 3.12e-07

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 54.84  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   222 EWACLVVDEAHRL---KNNQSKFFRVLN--SYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEE---FADI 293
Cdd:PRK04914  272 EWDLLVVDEAHHLvwsEEAPSREYQVVEqlAEVIPGVLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFVEEqqqYRPV 351

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 52545542   294 SK------------EDQIKKLHDLLGPH----MLRRLKADVFKNMPAKTELI 329
Cdd:PRK04914  352 ADavqallageklsDDALNALGELLGEQdiepLLQAANSDSEEAQAARQELI 403
ResIII pfam04851
Type III restriction enzyme, res subunit;
81-260 4.72e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 47.67  E-value: 4.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542     81 TLHPYQLEGLNWLRFSWAQGTDTILAdEM--GLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIIN-WEREFEMWAPDf 157
Cdd:pfam04851    3 ELRPYQIEAIENLLESIKNGQKRGLI-VMatGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRKDLLEqALEEFKKFLPN- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542    158 yvvtytgdkesrsvirenefSFEDNAIRSGKKVFRMKKEVQIKFhvlltsyelITIdQAILGSIEWA----------CLV 227
Cdd:pfam04851   80 --------------------YVEIGEIISGDKKDESVDDNKIVV---------TTI-QSLYKALELAslellpdffdVII 129

                          170       180       190
                   ....*....|....*....|....*....|....
gi 52545542    228 VDEAHRLknnQSKFFR-VLNSYKIDYKLLLTGTP 260
Cdd:pfam04851  130 IDEAHRS---GASSYRnILEYFKPAFLLGLTATP 160
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 473-528 6.96e-05

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: 42.31  E-value: 6.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 52545542  473 AQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIY 528
Cdd:cd18785   20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 82-260 7.85e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 43.83  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542   82 LHPYQLEGL-NWLRFSWAQGTDTILAdeMGLGKTVqTIVFLYSLYKEGHSkgpyLVSAPLSTIIN-WEREFEMWAPDFYV 159
Cdd:cd17926    1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTL-TALALIAYLKELRT----LIVVPTDALLDqWKERFEDFLGDSSI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545542  160 vtytgdkesrsvirenefsfedNAIRSGKKvfrmkkEVQIKFHVLLTSYELITIDQAILGSI--EWACLVVDEAHRLknN 237
Cdd:cd17926   74 ----------------------GLIGGGKK------KDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL--P 123

                        170       180
                 ....*....|....*....|...
gi 52545542  238 QSKFFRVLNSYKIDYKLLLTGTP 260
Cdd:cd17926  124 AKTFSEILKELNAKYRLGLTATP 146
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
 1-24 3.14e-04

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 39.56  E-value: 3.14e-04
                         10        20
                 ....*....|....*....|....
gi 52545542    1 YDQCTWEIDDIDIPYYDNLKQAYW 24
Cdd:cd18662   31 YDQSTWESEDDDIPDYEKHIQEYW 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH