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Conserved domains on  [gi|255089631|ref|XP_002506737|]
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SNF2 super family [Micromonas commoda]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
330-997 9.66e-125

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: 416.89  E-value: 9.66e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  330 QARREEKldAARRARGGSTIQSVEADAELAPSRE-WYGSEGDV------------LRGYQKEGVRWMAHnlvVRERGC-- 394
Cdd:PLN03142  117 QSASAKK--AKGRGRHASKLTEEEEDEEYLKEEEdGLGGSGGTrllvqpscikgkMRDYQLAGLNWLIR---LYENGIng 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  395 ILADEMGLGKTAQSLALIDYvLRAQRAsrleTRGPALVVVPLSTLVNWEREAARWVPGAHVVAYVGPPAARVCIRRHEIS 474
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGY-LHEYRG----ITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLV 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  475 YGdgrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyRADVVLTTYEMVQADRSALAKIPWSCLVIDEAHRLKN 554
Cdd:PLN03142  267 AG-----------------------------------------KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  555 SGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGAMTAARQ---VETLHKVLAPYLLR 631
Cdd:PLN03142  306 ENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLR 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  632 RLKQDVEHKLPPRVETLVECELMPLQKKCYRALFERNFSFLRQGSKDDRALanfsNLMMEVRKCCQHPFLLDGVEEAfvs 711
Cdd:PLN03142  385 RLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLL----NIAMQLRKCCNHPYLFQGAEPG--- 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  712 qqmskkggkrPAKTaTAAELVACSGKLQLLDKLLPRLKAGGHRALIFSQMTRVLDVLEDYCRNRGHSYERLDGGVTGRAR 791
Cdd:PLN03142  458 ----------PPYT-TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDR 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  792 QAAIDRFccgsnatDAGHSDEgaFLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQTKPVQVYRLVM 871
Cdd:PLN03142  527 DASIDAF-------NKPGSEK--FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCT 597
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  872 RATYERDMLDRAAMKLGLEQAIFSSNLNSGNGAIdNKErrgaaaEIERLLKHGAYGALSEDcaegdarTKAFAGEGIDDI 951
Cdd:PLN03142  598 EYTIEEKVIERAYKKLALDALVIQQGRLAEQKTV-NKD------ELLQMVRYGAEMVFSSK-------DSTITDEDIDRI 663
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 255089631  952 LARSERRVVEASDDDTSKSSDAQK-SMFATATFTG-EGGDGSDEIALD 997
Cdd:PLN03142  664 IAKGEEATAELDAKMKKFTEDAIKfKMDDTAELYDfDDEDDKDENKLD 711
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1482-1560 1.25e-24

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.


:

Pssm-ID: 461788  Cd Length: 83  Bit Score: 98.83  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  1482 KPLFRLTADEGLDEPIVAKSATAAWAEVLRRVTTVRRANGEEAK-KTAISGPEFFGYSLPHIRLLIEELPGVNDCTEYKP 1560
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKlPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYKF 80
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1421-1472 1.40e-10

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


:

Pssm-ID: 461787  Cd Length: 51  Bit Score: 57.90  E-value: 1.40e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  1421 GVTLESLGAVqPPDAPGFHSAAYILPVGYRTTRQYMRCDDPNgPRTRWVQEI 1472
Cdd:pfam05964    2 SLTVLSLGEI-VPDRPAFHTERYIYPVGYKSTRLYWSTKDPR-KRCRYTCEI 51
CD_CSD super family cl28914
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
172-219 1.69e-08

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 cd18660:

Pssm-ID: 475127 [Multi-domain]  Cd Length: 70  Bit Score: 52.75  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  172 VEKLLGWR----ASVDAVDADSGTPDEDGVDILVKWKGRALVHCSWVPLPAL 219
Cdd:cd18660     5 IEKILDHRpkgpVEEASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETL 56
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
330-997 9.66e-125

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 416.89  E-value: 9.66e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  330 QARREEKldAARRARGGSTIQSVEADAELAPSRE-WYGSEGDV------------LRGYQKEGVRWMAHnlvVRERGC-- 394
Cdd:PLN03142  117 QSASAKK--AKGRGRHASKLTEEEEDEEYLKEEEdGLGGSGGTrllvqpscikgkMRDYQLAGLNWLIR---LYENGIng 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  395 ILADEMGLGKTAQSLALIDYvLRAQRAsrleTRGPALVVVPLSTLVNWEREAARWVPGAHVVAYVGPPAARVCIRRHEIS 474
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGY-LHEYRG----ITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLV 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  475 YGdgrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyRADVVLTTYEMVQADRSALAKIPWSCLVIDEAHRLKN 554
Cdd:PLN03142  267 AG-----------------------------------------KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  555 SGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGAMTAARQ---VETLHKVLAPYLLR 631
Cdd:PLN03142  306 ENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLR 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  632 RLKQDVEHKLPPRVETLVECELMPLQKKCYRALFERNFSFLRQGSKDDRALanfsNLMMEVRKCCQHPFLLDGVEEAfvs 711
Cdd:PLN03142  385 RLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLL----NIAMQLRKCCNHPYLFQGAEPG--- 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  712 qqmskkggkrPAKTaTAAELVACSGKLQLLDKLLPRLKAGGHRALIFSQMTRVLDVLEDYCRNRGHSYERLDGGVTGRAR 791
Cdd:PLN03142  458 ----------PPYT-TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDR 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  792 QAAIDRFccgsnatDAGHSDEgaFLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQTKPVQVYRLVM 871
Cdd:PLN03142  527 DASIDAF-------NKPGSEK--FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCT 597
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  872 RATYERDMLDRAAMKLGLEQAIFSSNLNSGNGAIdNKErrgaaaEIERLLKHGAYGALSEDcaegdarTKAFAGEGIDDI 951
Cdd:PLN03142  598 EYTIEEKVIERAYKKLALDALVIQQGRLAEQKTV-NKD------ELLQMVRYGAEMVFSSK-------DSTITDEDIDRI 663
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 255089631  952 LARSERRVVEASDDDTSKSSDAQK-SMFATATFTG-EGGDGSDEIALD 997
Cdd:PLN03142  664 IAKGEEATAELDAKMKKFTEDAIKfKMDDTAELYDfDDEDDKDENKLD 711
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
288-895 5.71e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 390.35  E-value: 5.71e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  288 ERREALVRWGGGLGYEDATWEPVEWVESRSGGDVALRAYGAVQARREEKLDAARRARGGSTIQSVEADAELAPSREWYGS 367
Cdd:COG0553   154 LLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  368 EGD----VLRGYQKEGVRWMAHnLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRAsrletrGPALVVVPLSTLVNWE 443
Cdd:COG0553   234 LPAglkaTLRPYQLEGAAWLLF-LRRLGLGGLLADDMGLGKTIQALALLLELKERGLA------RPVLIVAPTSLVGNWQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  444 REAARWVPGAHVVAYVGPPAarvcirrheisygdgrlvtnegsdsdapnaeqrvesqsdngRVDRADGYRadvyRADVVL 523
Cdd:COG0553   307 RELAKFAPGLRVLVLDGTRE-----------------------------------------RAKGANPFE----DADLVI 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  524 TTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKD 603
Cdd:COG0553   342 TSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK-ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  604 EFESAFG---AMTAARQVETLHKVLAPYLLRRLKQDVEHKLPPRVETLVECELMPLQKKCYRALFERNFSFLRQGSKDDR 680
Cdd:COG0553   421 AFRERFArpiEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRR 500
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  681 ALANFSnLMMEVRKCCQHPFLLDGveeafvsqqmskkggkrpaktaTAAELVACSGKLQLLDKLLPRLKAGGHRALIFSQ 760
Cdd:COG0553   501 RGLILA-ALTRLRQICSHPALLLE----------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQ 557
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  761 MTRVLDVLEDYCRNRGHSYERLDGGVTGRARQAAIDRFccgsnatdagHSDEGAFLFLLSTRAGGQGINLVAADTVIVFD 840
Cdd:COG0553   558 FTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF----------QEGPEAPVFLISLKAGGEGLNLTAADHVIHYD 627
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 255089631  841 SDWNPQNDAQALARAHRIGQTKPVQVYRLVMRATYERDMLDRAAMKLGLEQAIFS 895
Cdd:COG0553   628 LWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
372-632 1.08e-91

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: 296.47  E-value: 1.08e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVReRGCILADEMGLGKTAQSLALIDYVLraqraSRLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNR-RNCILADEMGLGKTIQSIAFLEHLY-----QVEGIRGPFLVIAPLSTIPNWQREFETWTD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 gAHVVAYVGPPAARVCIRRHEISYGDgrlvtnegsdsdapnaeqrvesqsDNGRVDRadgyraDVYRADVVLTTYEMVQA 531
Cdd:cd17995    75 -MNVVVYHGSGESRQIIQQYEMYFKD------------------------AQGRKKK------GVYKFDVLITTYEMVIA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFaKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd17995   124 DAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL-EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGD 202
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd17995   203 LKTAEQVEKLQALLKPYMLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
375-702 1.24e-77

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: 258.77  E-value: 1.24e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   375 YQKEGVRWMAHNLVVRERGCILADEMGLGKTAQSLALIDYVLRaqraSRLETRGPALVVVPLSTLVNWEREAARWVpgah 454
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKH----VDKNWGGPTLIVVPLSLLHNWMNEFERWV---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   455 vvayvGPPAARVCIrrheisYGDGrlvtnegsdsdapNAEQRVESQSDNGRVDRadgyradvyraDVVLTTYEMVQADRS 534
Cdd:pfam00176   73 -----SPPALRVVV------LHGN-------------KRPQERWKNDPNFLADF-----------DVVITTYETLRKHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   535 ALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG---- 610
Cdd:pfam00176  118 LLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR-WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpie 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   611 AMTAARQVETLHKVLAPYLLRRLKQDVEHKLPPRVETLVECELMPLQKKCY-RALFERNFSFLRQGSKDDRALANFSNLM 689
Cdd:pfam00176  197 RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGEGGREIKASLLNIL 276
                          330
                   ....*....|...
gi 255089631   690 MEVRKCCQHPFLL 702
Cdd:pfam00176  277 MRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
364-603 3.13e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.88  E-value: 3.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    364 WYGSEGDVLRGYQKEGVRWMAHNlvvrERGCILADEMGLGKT-AQSLALIDYVLRaqrasrlETRGPALVVVPLSTLV-N 441
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSG----LRDVILAAPTGSGKTlAALLPALEALKR-------GKGGRVLVLVPTRELAeQ 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    442 WEREAARWVPGAHVvayvgppaaRVCIRRHEISYGDGRLVTNEGsdsdapnaeqrvesqsdngrvdradgyradvyRADV 521
Cdd:smart00487   70 WAEELKKLGPSLGL---------KVVGLYGGDSKREQLRKLESG--------------------------------KTDI 108
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    522 VLTTYEMVQAD--RSALAKIPWSCLVIDEAHRLKNSGGKAQ--RDLRTLDFAKRVVLLTGTP---LQNDTAELWSLLNFV 594
Cdd:smart00487  109 LVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGFGDQleKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFI 188

                    ....*....
gi 255089631    595 DAGRFASKD 603
Cdd:smart00487  189 DVGFTPLEP 197
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1482-1560 1.25e-24

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.


Pssm-ID: 461788  Cd Length: 83  Bit Score: 98.83  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  1482 KPLFRLTADEGLDEPIVAKSATAAWAEVLRRVTTVRRANGEEAK-KTAISGPEFFGYSLPHIRLLIEELPGVNDCTEYKP 1560
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKlPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYKF 80
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
1484-1560 5.83e-12

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 197781  Cd Length: 86  Bit Score: 63.08  E-value: 5.83e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255089631   1484 LFRLTADEGLDEPIVAKSATAAWAEVLRRVTTVRRANGEEAKKTA-ISGPEFFGYSLPHIRLLIEELPGVNDCTEYKP 1560
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEgVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1421-1472 1.40e-10

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


Pssm-ID: 461787  Cd Length: 51  Bit Score: 57.90  E-value: 1.40e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  1421 GVTLESLGAVqPPDAPGFHSAAYILPVGYRTTRQYMRCDDPNgPRTRWVQEI 1472
Cdd:pfam05964    2 SLTVLSLGEI-VPDRPAFHTERYIYPVGYKSTRLYWSTKDPR-KRCRYTCEI 51
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
172-219 1.69e-08

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 52.75  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  172 VEKLLGWR----ASVDAVDADSGTPDEDGVDILVKWKGRALVHCSWVPLPAL 219
Cdd:cd18660     5 IEKILDHRpkgpVEEASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETL 56
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
330-997 9.66e-125

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 416.89  E-value: 9.66e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  330 QARREEKldAARRARGGSTIQSVEADAELAPSRE-WYGSEGDV------------LRGYQKEGVRWMAHnlvVRERGC-- 394
Cdd:PLN03142  117 QSASAKK--AKGRGRHASKLTEEEEDEEYLKEEEdGLGGSGGTrllvqpscikgkMRDYQLAGLNWLIR---LYENGIng 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  395 ILADEMGLGKTAQSLALIDYvLRAQRAsrleTRGPALVVVPLSTLVNWEREAARWVPGAHVVAYVGPPAARVCIRRHEIS 474
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGY-LHEYRG----ITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLV 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  475 YGdgrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyRADVVLTTYEMVQADRSALAKIPWSCLVIDEAHRLKN 554
Cdd:PLN03142  267 AG-----------------------------------------KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  555 SGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGAMTAARQ---VETLHKVLAPYLLR 631
Cdd:PLN03142  306 ENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLR 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  632 RLKQDVEHKLPPRVETLVECELMPLQKKCYRALFERNFSFLRQGSKDDRALanfsNLMMEVRKCCQHPFLLDGVEEAfvs 711
Cdd:PLN03142  385 RLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKRLL----NIAMQLRKCCNHPYLFQGAEPG--- 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  712 qqmskkggkrPAKTaTAAELVACSGKLQLLDKLLPRLKAGGHRALIFSQMTRVLDVLEDYCRNRGHSYERLDGGVTGRAR 791
Cdd:PLN03142  458 ----------PPYT-TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDR 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  792 QAAIDRFccgsnatDAGHSDEgaFLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQTKPVQVYRLVM 871
Cdd:PLN03142  527 DASIDAF-------NKPGSEK--FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCT 597
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  872 RATYERDMLDRAAMKLGLEQAIFSSNLNSGNGAIdNKErrgaaaEIERLLKHGAYGALSEDcaegdarTKAFAGEGIDDI 951
Cdd:PLN03142  598 EYTIEEKVIERAYKKLALDALVIQQGRLAEQKTV-NKD------ELLQMVRYGAEMVFSSK-------DSTITDEDIDRI 663
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 255089631  952 LARSERRVVEASDDDTSKSSDAQK-SMFATATFTG-EGGDGSDEIALD 997
Cdd:PLN03142  664 IAKGEEATAELDAKMKKFTEDAIKfKMDDTAELYDfDDEDDKDENKLD 711
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
288-895 5.71e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 390.35  E-value: 5.71e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  288 ERREALVRWGGGLGYEDATWEPVEWVESRSGGDVALRAYGAVQARREEKLDAARRARGGSTIQSVEADAELAPSREWYGS 367
Cdd:COG0553   154 LLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  368 EGD----VLRGYQKEGVRWMAHnLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRAsrletrGPALVVVPLSTLVNWE 443
Cdd:COG0553   234 LPAglkaTLRPYQLEGAAWLLF-LRRLGLGGLLADDMGLGKTIQALALLLELKERGLA------RPVLIVAPTSLVGNWQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  444 REAARWVPGAHVVAYVGPPAarvcirrheisygdgrlvtnegsdsdapnaeqrvesqsdngRVDRADGYRadvyRADVVL 523
Cdd:COG0553   307 RELAKFAPGLRVLVLDGTRE-----------------------------------------RAKGANPFE----DADLVI 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  524 TTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKD 603
Cdd:COG0553   342 TSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK-ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  604 EFESAFG---AMTAARQVETLHKVLAPYLLRRLKQDVEHKLPPRVETLVECELMPLQKKCYRALFERNFSFLRQGSKDDR 680
Cdd:COG0553   421 AFRERFArpiEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRR 500
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  681 ALANFSnLMMEVRKCCQHPFLLDGveeafvsqqmskkggkrpaktaTAAELVACSGKLQLLDKLLPRLKAGGHRALIFSQ 760
Cdd:COG0553   501 RGLILA-ALTRLRQICSHPALLLE----------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQ 557
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  761 MTRVLDVLEDYCRNRGHSYERLDGGVTGRARQAAIDRFccgsnatdagHSDEGAFLFLLSTRAGGQGINLVAADTVIVFD 840
Cdd:COG0553   558 FTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF----------QEGPEAPVFLISLKAGGEGLNLTAADHVIHYD 627
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 255089631  841 SDWNPQNDAQALARAHRIGQTKPVQVYRLVMRATYERDMLDRAAMKLGLEQAIFS 895
Cdd:COG0553   628 LWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
372-632 1.08e-91

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: 296.47  E-value: 1.08e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVReRGCILADEMGLGKTAQSLALIDYVLraqraSRLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNR-RNCILADEMGLGKTIQSIAFLEHLY-----QVEGIRGPFLVIAPLSTIPNWQREFETWTD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 gAHVVAYVGPPAARVCIRRHEISYGDgrlvtnegsdsdapnaeqrvesqsDNGRVDRadgyraDVYRADVVLTTYEMVQA 531
Cdd:cd17995    75 -MNVVVYHGSGESRQIIQQYEMYFKD------------------------AQGRKKK------GVYKFDVLITTYEMVIA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFaKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd17995   124 DAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL-EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGD 202
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd17995   203 LKTAEQVEKLQALLKPYMLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
375-702 1.24e-77

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: 258.77  E-value: 1.24e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   375 YQKEGVRWMAHNLVVRERGCILADEMGLGKTAQSLALIDYVLRaqraSRLETRGPALVVVPLSTLVNWEREAARWVpgah 454
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKH----VDKNWGGPTLIVVPLSLLHNWMNEFERWV---- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   455 vvayvGPPAARVCIrrheisYGDGrlvtnegsdsdapNAEQRVESQSDNGRVDRadgyradvyraDVVLTTYEMVQADRS 534
Cdd:pfam00176   73 -----SPPALRVVV------LHGN-------------KRPQERWKNDPNFLADF-----------DVVITTYETLRKHKE 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   535 ALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG---- 610
Cdd:pfam00176  118 LLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR-WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpie 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   611 AMTAARQVETLHKVLAPYLLRRLKQDVEHKLPPRVETLVECELMPLQKKCY-RALFERNFSFLRQGSKDDRALANFSNLM 689
Cdd:pfam00176  197 RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGEGGREIKASLLNIL 276
                          330
                   ....*....|...
gi 255089631   690 MEVRKCCQHPFLL 702
Cdd:pfam00176  277 MRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
372-595 2.98e-65

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: 218.97  E-value: 2.98e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVReRGCILADEMGLGKTAQSLALIDYVLRAQRAsrletRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd17919     1 LRPYQLEGLNFLLELYENG-PGGILADEMGLGKTLQAIAFLAYLLKEGKE-----RGPVLVVCPLSVLENWEREFEKWTP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEisygdgrlvtnegsdsdapnaeqrvesqsdngrvdradgyraDVYRADVVLTTYEMVQA 531
Cdd:cd17919    75 DLRVVVYHGSQRERAQIRAKE------------------------------------------KLDKFDVVLTTYETLRR 112
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVD 595
Cdd:cd17919   113 DKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTPLQNNLEELWALLDFLD 175
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
372-632 1.68e-63

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: 215.30  E-value: 1.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIDYVLRAQRASrletrGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd17993     2 LRDYQLTGLNWLAHSWC-KGNNGILADEMGLGKTVQTISFLSYLFHSQQQY-----GPFLVVVPLSTMPAWQREFAKWAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEISYGDGRLVtnegsdsdapnaeqrvesqsdngrvdradgyradvyRADVVLTTYEMVQA 531
Cdd:cd17993    76 DMNVIVYLGDIKSRDTIREYEFYFSQTKKL------------------------------------KFNVLLTTYEIILK 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd17993   120 DKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNR-LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDE 198
                         250       260
                  ....*....|....*....|.
gi 255089631  612 mTAARQVETLHKVLAPYLLRR 632
Cdd:cd17993   199 -EQEKGIADLHKELEPFILRR 218
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
369-634 2.11e-59

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: 204.14  E-value: 2.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  369 GDVLRGYQKEGVRWMAhNLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRasrleTRGPALVVVPLSTLVNWEREAAR 448
Cdd:cd17996     1 GGTLKEYQLKGLQWMV-SLYNNNLNGILADEMGLGKTIQTISLITYLMEKKK-----NNGPYLVIVPLSTLSNWVSEFEK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  449 WVPGAHVVAYVGPPAARvcirrheisygdgrlvtnegsdsdapnaeQRVESQSDNGRVDradgyradvyradVVLTTYEM 528
Cdd:cd17996    75 WAPSVSKIVYKGTPDVR-----------------------------KKLQSQIRAGKFN-------------VLLTTYEY 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  529 VQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESA 608
Cdd:cd17996   113 IIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQW 192
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 255089631  609 FG---AMTAAR------QVET------LHKVLAPYLLRRLK 634
Cdd:cd17996   193 FNtpfANTGEQvkielnEEETlliirrLHKVLRPFLLRRLK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
735-870 1.49e-58

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: 197.70  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  735 SGKLQLLDKLLPRLKAGGHRALIFSQMTRVLDVLEDYCRNRGHSYERLDGGVTGRARQAAIDRFccgsnatdagHSDEGA 814
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF----------NEDPDI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 255089631  815 FLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQTKPVQVYRLV 870
Cdd:cd18793    80 RVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
369-634 4.25e-55

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: 192.22  E-value: 4.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  369 GDVLRGYQKEGVRWMahnLVVRERGC--ILADEMGLGKTAQSLALIDYVLRAqrasrlETRGPALVVVPLSTLVNWEREA 446
Cdd:cd18009     1 GGVMRPYQLEGMEWL---RMLWENGIngILADEMGLGKTIQTIALLAHLRER------GVWGPFLVIAPLSTLPNWVNEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  447 ARWVPGAHVVAYVGPPAARVCIRRheisygdgRLVTNEGSDSDAPnaeqrvesqsdngrvdradgyradvyradVVLTTY 526
Cdd:cd18009    72 ARFTPSVPVLLYHGTKEERERLRK--------KIMKREGTLQDFP-----------------------------VVVTSY 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  527 EMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFE 606
Cdd:cd18009   115 EIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL-LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFE 193
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 255089631  607 SAFG------------AMTAARQ---VETLHKVLAPYLLRRLK 634
Cdd:cd18009   194 SWFDfsslsdnaadisNLSEEREqniVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
369-634 9.47e-55

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: 190.61  E-value: 9.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  369 GDVLRGYQKEGVRWMAHnlvVRERGC--ILADEMGLGKTAQSLALIDYvLRAQRasrlETRGPALVVVPLSTLVNWEREA 446
Cdd:cd17997     1 GGTMRDYQIRGLNWLIS---LFENGIngILADEMGLGKTLQTISLLGY-LKHYK----NINGPHLIIVPKSTLDNWMREF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  447 ARWVPGAHVVAYVGPPAARVCIRRHEISYGDgrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyrADVVLTTY 526
Cdd:cd17997    73 KRWCPSLRVVVLIGDKEERADIIRDVLLPGK-----------------------------------------FDVCITSY 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  527 EMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFE 606
Cdd:cd17997   112 EMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR-LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFD 190
                         250       260       270
                  ....*....|....*....|....*....|..
gi 255089631  607 SAFGAMTAARQ----VETLHKVLAPYLLRRLK 634
Cdd:cd17997   191 EWFNVNNCDDDnqevVQRLHKVLRPFLLRRIK 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
372-632 9.53e-53

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: 184.87  E-value: 9.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVRERgCILADEMGLGKTAQSLALIDYVLRAQrasrleTRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQN-CILADEMGLGKTIQSIAFLQEVYNVG------IHGPFLVIAPLSTITNWEREFNTWTE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 gAHVVAYVGPPAARVCIRRHEISYGD--GRLVtnegsdsdaPNAeqrvesqsdngrvdradgyradvYRADVVLTTYEMV 529
Cdd:cd18060    74 -MNTIVYHGSLASRQMIQQYEMYCKDsrGRLI---------PGA-----------------------YKFDALITTFEMI 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  530 QADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAF 609
Cdd:cd18060   121 LSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
                         250       260
                  ....*....|....*....|...
gi 255089631  610 GAMTAARQVETLHKVLAPYLLRR 632
Cdd:cd18060   200 GDLKTEEQVQKLQAILKPMMLRR 222
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
372-634 4.45e-52

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: 182.77  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMA----HNLvvrerGCILADEMGLGKTAQSLALIDYVLRAQRAsrletrGPALVVVPLSTLVNWEREAA 447
Cdd:cd18012     5 LRPYQKEGFNWLSflrhYGL-----GGILADDMGLGKTLQTLALLLSRKEEGRK------GPSLVVAPTSLIYNWEEEAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  448 RWVPGAHVVAYVGPPAARVcirrheisygdgrlvtnegsdsdapnAEQRVESqsdngrvdradgyradvyrADVVLTTYE 527
Cdd:cd18012    74 KFAPELKVLVIHGTKRKRE--------------------------KLRALED-------------------YDLVITSYG 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  528 MVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFES 607
Cdd:cd18012   109 LLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALK-ADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKK 187
                         250       260       270
                  ....*....|....*....|....*....|.
gi 255089631  608 AFGA----MTAARQVETLHKVLAPYLLRRLK 634
Cdd:cd18012   188 RFAKpiekDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
364-632 9.63e-52

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: 182.51  E-value: 9.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  364 WYGSEGDVLRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIDYVLRAQrasrlETRGPALVVVPLSTLVNWE 443
Cdd:cd18054    13 YIGGENLELRDYQLEGLNWLAHSWC-KNNSVILADEMGLGKTIQTISFLSYLFHQH-----QLYGPFLLVVPLSTLTSWQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  444 REAARWVPGAHVVAYVGPPAARVCIRRHEIsygdgrlvtnegsdsdapnaeqrVESQSDNgrvdradgyradvYRADVVL 523
Cdd:cd18054    87 REFEIWAPEINVVVYIGDLMSRNTIREYEW-----------------------IHSQTKR-------------LKFNALI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  524 TTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLrtLDF-AKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASK 602
Cdd:cd18054   131 TTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL--IDFkSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFW 208
                         250       260       270
                  ....*....|....*....|....*....|..
gi 255089631  603 DEFESAFGamtAARQ--VETLHKVLAPYLLRR 632
Cdd:cd18054   209 EDFEEDHG---KGREngYQSLHKVLEPFLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
372-632 4.84e-51

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: 179.85  E-value: 4.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVReRGCILADEMGLGKTAQSLALIDYVLRaqrasrLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNR-KNCILADEMGLGKTIQSITFLSEIFL------MGIRGPFLIIAPLSTITNWEREFRTWTE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 gAHVVAYVGPPAARVCIRRHEISYGDGRLVTNEGsdsdapnaeqrvesqsdngrvdradgyradVYRADVVLTTYEMVQA 531
Cdd:cd18058    74 -MNAIVYHGSQISRQMIQQYEMYYRDEQGNPLSG------------------------------IFKFQVVITTFEMILA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd18058   123 DCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKV-LLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD 201
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd18058   202 LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
372-632 5.22e-51

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: 179.84  E-value: 5.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLA-LIDYVLRAqrasrleTRGPALVVVPLSTLVNWEREAARWV 450
Cdd:cd18059     1 LREYQLEGVNWLLFNWY-NTRNCILADEMGLGKTIQSITfLYEIYLKG-------IHGPFLVIAPLSTIPNWEREFRTWT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  451 PgAHVVAYVGPPAARVCIRRHEISYGDGRlvtnegsdsdapnaeqrvesqsdnGRVDRAdgyradVYRADVVLTTYEMVQ 530
Cdd:cd18059    73 E-LNVVVYHGSQASRRTIQLYEMYFKDPQ------------------------GRVIKG------SYKFHAIITTFEMIL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  531 ADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG 610
Cdd:cd18059   122 TDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG 200
                         250       260
                  ....*....|....*....|..
gi 255089631  611 AMTAARQVETLHKVLAPYLLRR 632
Cdd:cd18059   201 DLKTEEQVQKLQAILKPMMLRR 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
372-632 6.90e-51

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 179.47  E-value: 6.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAhNLVVRERGCILADEMGLGKTAQSLALIDYVlraqrASRLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18003     1 LREYQHIGLDWLA-TLYEKNLNGILADEMGLGKTIQTIALLAHL-----ACEKGNWGPHLIVVPTSVMLNWEMEFKRWCP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGppaarvcirrheisygdgrlvtnegsdsdapNAEQRVESqsdngrvdRADGYRADVYRadVVLTTYEMVQA 531
Cdd:cd18003    75 GFKILTYYG-------------------------------SAKERKLK--------RQGWMKPNSFH--VCITSYQLVVQ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSggKAQRDLRTLDF-AKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG 610
Cdd:cd18003   114 DHQVFKRKKWKYLILDEAHNIKNF--KSQRWQTLLNFnTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFS 191
                         250       260       270
                  ....*....|....*....|....*....|..
gi 255089631  611 ----AMTAARQVET------LHKVLAPYLLRR 632
Cdd:cd18003   192 npltAMSEGSQEENeelvrrLHKVLRPFLLRR 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
372-632 2.38e-50

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: 177.63  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIDYVlraqrASRLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18006     1 LRPYQLEGVNWLLQCRA-EQHGCILGDEMGLGKTCQTISLLWYL-----AGRLKLLGPFLVLCPLSVLDNWKEELNRFAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRheisygdgrlvtnegsdsdapnaeqrvESQSDNgrvdradgyradvyRADVVLTTYEMVQA 531
Cdd:cd18006    75 DLSVITYMGDKEKRLDLQQ---------------------------DIKSTN--------------RFHVLLTTYEICLK 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLdFAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASK--DEFESAF 609
Cdd:cd18006   114 DASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEF-SVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDklDDFIKAY 192
                         250       260
                  ....*....|....*....|....
gi 255089631  610 GAM-TAARQVETLHKVLAPYLLRR 632
Cdd:cd18006   193 SETdDESETVEELHLLLQPFLLRR 216
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
372-632 4.72e-50

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: 176.09  E-value: 4.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIdYVLRAQRasrlETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd17994     1 LHPYQLEGLNWLRFSWA-QGTDTILADEMGLGKTIQTIVFL-YSLYKEG----HSKGPFLVSAPLSTIINWEREFEMWAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGppaarvcirrheisygdgrlvtnegsdsdapnaeqrvesqsDNgrvdradgyradvyradVVLTTYEMVQA 531
Cdd:cd17994    75 DFYVVTYVG-----------------------------------------DH-----------------VLLTSYELISI 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd17994    97 DQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKL-LLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd17994   176 ISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
372-632 8.52e-49

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: 173.65  E-value: 8.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVReRGCILADEMGLGKTAQSLALIDYVLRAQrasrleTRGPALVVVPLSTLVNWEREAARWVp 451
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYEILLTG------IRGPFLIIAPLSTIANWEREFRTWT- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEISYGDGRlvtnegsdsdapnaeqrvesqsdnGRVDRAdgyradVYRADVVLTTYEMVQA 531
Cdd:cd18061    73 DLNVVVYHGSLISRQMIQQYEMYFRDSQ------------------------GRIIRG------AYRFQAIITTFEMILG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd18061   123 GCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKV-LLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd18061   202 LKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
372-632 1.88e-48

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: 172.89  E-value: 1.88e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIdYVLRAQRasrlETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18055     1 LHMYQLEGLNWLRFSWA-QGTDTILADEMGLGKTIQTIVFL-YSLYKEG----HTKGPFLVSAPLSTIINWEREFQMWAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEISYGDGrlVTNEGSDSDAPNAEQRVESQsdngrvdradgyradvyradVVLTTYEMVQA 531
Cdd:cd18055    75 DFYVVTYTGDKDSRAIIRENEFSFDDN--AVKGGKKAFKMKREAQVKFH--------------------VLLTSYELVTI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd18055   133 DQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKL-LLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd18055   212 ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
372-632 3.90e-47

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: 169.09  E-value: 3.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIdYVLRAQRASRletrGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18057     1 LHPYQLEGLNWLRFSWA-QGTDTILADEMGLGKTVQTIVFL-YSLYKEGHSK----GPYLVSAPLSTIINWEREFEMWAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEISYGDgrlvtnegsdsDAPNAEQRVESQSDNGRVdradgyradvyRADVVLTTYEMVQA 531
Cdd:cd18057    75 DFYVVTYTGDKESRSVIRENEFSFED-----------NAIRSGKKVFRMKKEAQI-----------KFHVLLTSYELITI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd18057   133 DQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKL-LLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd18057   212 ISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
372-632 2.92e-46

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: 166.39  E-value: 2.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSlALIDYVLRAQRASRletrGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18056     1 LHPYQLEGLNWLRFSWA-QGTDTILADEMGLGKTVQT-AVFLYSLYKEGHSK----GPFLVSAPLSTIINWEREFEMWAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRHEISYGDGRLvtNEGSDSDAPNAEQRVESQsdngrvdradgyradvyradVVLTTYEMVQA 531
Cdd:cd18056    75 DMYVVTYVGDKDSRAIIRENEFSFEDNAI--RGGKKASRMKKEASVKFH--------------------VLLTSYELITI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFGA 611
Cdd:cd18056   133 DMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHK-LLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD 211
                         250       260
                  ....*....|....*....|.
gi 255089631  612 MTAARQVETLHKVLAPYLLRR 632
Cdd:cd18056   212 IAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
366-632 2.38e-45

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: 164.07  E-value: 2.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  366 GSEGDVLRGYQKEGVRWMAHNLVvRERGCILADEMGLGKTAQSLALIDYVLRAQrasrlETRGPALVVVPLSTLVNWERE 445
Cdd:cd18053    15 GHEGLELRDYQLNGLNWLAHSWC-KGNSCILADEMGLGKTIQTISFLNYLFHEH-----QLYGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  446 AARWVPGAHVVAYVGPPAARVCIRRHEISYgdgrlvtnegsdsdaPNAEQrvesqsdngrvdradgyradvYRADVVLTT 525
Cdd:cd18053    89 IQTWAPQMNAVVYLGDINSRNMIRTHEWMH---------------PQTKR---------------------LKFNILLTT 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  526 YEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLrtLDF-AKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDE 604
Cdd:cd18053   133 YEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL--IDFkSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWED 210
                         250       260
                  ....*....|....*....|....*...
gi 255089631  605 FESAFGAMTAARQVeTLHKVLAPYLLRR 632
Cdd:cd18053   211 FEEEHGKGREYGYA-SLHKELEPFLLRR 237
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
357-644 2.54e-45

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


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 164.45  E-value: 2.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  357 ELAPSREWYGSegdvLRGYQKEGVRWMahnLVVRERGC--ILADEMGLGKTAQSLALIDYVLRAQRASrletrGPALVVV 434
Cdd:cd18064     5 EDSPSYVKWGK----LRDYQVRGLNWL---ISLYENGIngILADEMGLGKTLQTISLLGYMKHYRNIP-----GPHMVLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  435 PLSTLVNWEREAARWVPGAHVVAYVGPPAARVCIRRHEISYGDGrlvtnegsdsdapnaeqrvesqsdngrvdradgyra 514
Cdd:cd18064    73 PKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEW------------------------------------ 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  515 dvyraDVVLTTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFV 594
Cdd:cd18064   117 -----DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL-LLTGTPLQNNLHELWALLNFL 190
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 255089631  595 DAGRFASKDEFESAF---GAMTAARQVETLHKVLAPYLLRRLKQDVEHKLPPR 644
Cdd:cd18064   191 LPDVFNSAEDFDSWFdtnNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
372-634 1.59e-44

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: 162.15  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAhNLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRASrletrGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18063    24 LKHYQLQGLEWMV-SLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLN-----GPYLIIVPLSTLSNWTYEFDKWAP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARvcirrheisygdgrlvtnegsdsdapnaeQRVESQSDNGRVDradgyradvyradVVLTTYEMVQA 531
Cdd:cd18063    98 SVVKISYKGTPAMR-----------------------------RSLVPQLRSGKFN-------------VLLTTYEYIIK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG- 610
Cdd:cd18063   136 DKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNa 215
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 255089631  611 --AMTAARQ----------VETLHKVLAPYLLRRLK 634
Cdd:cd18063   216 pfAMTGERVdlneeetiliIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
371-634 5.83e-44

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: 160.60  E-value: 5.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  371 VLRGYQKEGVRWMAhNLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRASrletrGPALVVVPLSTLVNWEREAARWV 450
Cdd:cd18062    23 VLKQYQIKGLEWLV-SLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRIN-----GPFLIIVPLSTLSNWVYEFDKWA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  451 PGAHVVAYVGPPAARvcirrheisygdgrlvtnegsdsdapnaeQRVESQSDNGRVDradgyradvyradVVLTTYEMVQ 530
Cdd:cd18062    97 PSVVKVSYKGSPAAR-----------------------------RAFVPQLRSGKFN-------------VLLTTYEYII 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  531 ADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFESAFG 610
Cdd:cd18062   135 KDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN 214
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 255089631  611 ---AMTAARQ----------VETLHKVLAPYLLRRLK 634
Cdd:cd18062   215 apfAMTGEKVdlneeetiliIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
368-634 5.90e-44

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 159.80  E-value: 5.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  368 EGDVLRGYQKEGVRWMahnLVVRERGC--ILADEMGLGKTAQSLALIDYvLRAQRasrlETRGPALVVVPLSTLVNWERE 445
Cdd:cd18065    12 KGGTLRDYQVRGLNWM---ISLYENGVngILADEMGLGKTLQTIALLGY-LKHYR----NIPGPHMVLVPKSTLHNWMNE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  446 AARWVPGAHVVAYVGPPAARVCIRRHEISYGDGrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyraDVVLTT 525
Cdd:cd18065    84 FKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEW-----------------------------------------DVCVTS 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  526 YEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEF 605
Cdd:cd18065   123 YEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNR-LLLTGTPLQNNLHELWALLNFLLPDVFNSADDF 201
                         250       260       270
                  ....*....|....*....|....*....|..
gi 255089631  606 ESAF---GAMTAARQVETLHKVLAPYLLRRLK 634
Cdd:cd18065   202 DSWFdtkNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
372-632 6.28e-44

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: 160.24  E-value: 6.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMaHNLVVRERGCILADEMGLGKTAQSLALIDYVL--------------RAQRASRLETRG-PALVVVPL 436
Cdd:cd18005     1 LRDYQREGVEFM-YDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrpRFKKKPPASSAKkPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  437 STLVNWEREAARWvpgAHVVAYVgppaarvcirrheisygdgrlVTNEGSDSDApnaeqrvesqsdNGRVDRAdgyradv 516
Cdd:cd18005    80 SVLYNWKDELDTW---GHFEVGV---------------------YHGSRKDDEL------------EGRLKAG------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  517 yRADVVLTTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDA 596
Cdd:cd18005   117 -RLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELK-CKVRIGLTGTLLQNNMKELWCLLDWAVP 194
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 255089631  597 GRFASKDEFESAFG-------AMTA-ARQVET-------LHKVLAPYLLRR 632
Cdd:cd18005   195 GALGSRSQFKKHFSepikrgqRHTAtARELRLgrkrkqeLAVKLSKFFLRR 245
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
372-632 7.94e-41

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: 150.73  E-value: 7.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAhNLVVRERGCILADEMGLGKTAQSLALIDYVlraqrASRLETRGPALVVVPLSTLVNWEREAARWVP 451
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQGINGILADEMGLGKTVQSIAVLAHL-----AEEHNIWGPFLVIAPASTLHNWQQEISRFVP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  452 GAHVVAYVGPPAARVCIRRheisYGDGRLVTNEgsdsDAPnaeqrvesqsdngrvdradgyradvyrADVVLTTYEMVQA 531
Cdd:cd18002    75 QFKVLPYWGNPKDRKVLRK----FWDRKNLYTR----DAP---------------------------FHVVITSYQLVVQ 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  532 DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVvLLTGTPLQNDTAELWSLLNFVDAGRFASKDEF------ 605
Cdd:cd18002   120 DEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL-LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFnewfsk 198
                         250       260       270
                  ....*....|....*....|....*....|.
gi 255089631  606 --ESAFGAMTA--ARQVETLHKVLAPYLLRR 632
Cdd:cd18002   199 diESHAENKTGlnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
372-594 1.78e-37

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: 139.44  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMahNLVVRER-GCILADEMGLGKTAQSLALIDYVLRAQRasrletRGPALVVVPLSTLVNWEREAARWV 450
Cdd:cd17998     1 LKDYQLIGLNWL--NLLYQKKlSGILADEMGLGKTIQVIAFLAYLKEIGI------PGPHLVVVPSSTLDNWLREFKRWC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  451 PGAHVVAYVGPPAARVCIRrheisygdgrlvtnegsdsdapnaeQRVEsqsdngrvDRADGYradvyraDVVLTTYEMVQ 530
Cdd:cd17998    73 PSLKVEPYYGSQEERKHLR-------------------------YDIL--------KGLEDF-------DVIVTTYNLAT 112
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255089631  531 A---DRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRvVLLTGTPLQNDTAELWSLLNFV 594
Cdd:cd17998   113 SnpdDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFR-LLLTGTPLQNNLLELMSLLNFI 178
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
372-632 2.11e-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: 140.95  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMA----HNLvvreRGcILADEMGLGKTAQSLALIdYVLRAQRASRLETRG-PALVVVPlSTLV-NWERE 445
Cdd:cd17999     1 LRPYQQEGINWLAflnkYNL----HG-ILCDDMGLGKTLQTLCIL-ASDHHKRANSFNSENlPSLVVCP-PTLVgHWVAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  446 AARWVPGA--HVVAYVGPPAARVCIRrHEISygdgrlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyRADVVL 523
Cdd:cd17999    74 IKKYFPNAflKPLAYVGPPQERRRLR-EQGE-------------------------------------------KHNVIV 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  524 TTYEMVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKD 603
Cdd:cd17999   110 ASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK-ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEK 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 255089631  604 EFESAFG-AMTAAR--------------QVETLHKVLAPYLLRR 632
Cdd:cd17999   189 QFQRRFLkPILASRdskasakeqeagalALEALHKQVLPFLLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
372-609 6.84e-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: 139.73  E-value: 6.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVRE----RGCILADEMGLGKTAQSLALIDYVLRAQRASRLETRgPALVVVPLSTLVNWEREAA 447
Cdd:cd18004     1 LRPHQREGVQFLYDCLTGRRgyggGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPTAK-KALIVCPSSLVGNWKAEFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  448 RWVPGahvvayvgppaarvcirrheisygdgRLVTNEGSDSDAPNAEQRVESQSDNGRvdradgyradvyrADVVLTTYE 527
Cdd:cd18004    80 KWLGL--------------------------RRIKVVTADGNAKDVKASLDFFSSAST-------------YPVLIISYE 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  528 MVQADRSALAKIPwSC--LVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEF 605
Cdd:cd18004   121 TLRRHAEKLSKKI-SIdlLICDEGHRLKNSESKTTKALNSLP-CRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASF 198

                  ....
gi 255089631  606 ESAF 609
Cdd:cd18004   199 RKVF 202
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
372-632 1.65e-36

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: 138.96  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHnlvvreRGCILADEMGLGKTAQSLALI------------DYVLRAQRASRLETRGPALVVVPLSTL 439
Cdd:cd18008     1 LLPYQKQGLAWMLP------RGGILADEMGLGKTIQALALIlatrpqdpkipeELEENSSDPKKLYLSKTTLIVVPLSLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  440 VNWEREAARwvpgaHvvayVGPPAARVCIRrheisYGDGRLVTNEgsdsdapnaeqrvesqsdngrvdradgyraDVYRA 519
Cdd:cd18008    75 SQWKDEIEK-----H----TKPGSLKVYVY-----HGSKRIKSIE------------------------------ELSDY 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  520 DVVLTTYEMVQAD----------------RSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVlLTGTPLQND 583
Cdd:cd18008   111 DIVITTYGTLASEfpknkkgggrdskekeASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWC-LTGTPIQNS 189
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  584 TAELWSLLNFVDA---GRFASKDEFESAFGAMTAARQVETLHKVLAPYLLRR 632
Cdd:cd18008   190 LDDLYSLLRFLRVepfGDYPWFNSDISKPFSKNDRKALERLQALLKPILLRR 241
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
375-594 1.59e-34

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: 131.29  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  375 YQKEGVRWMaHNLVVRERGCILADEMGLGKTAQSLALidyvLRAQRASRLeTRGPALVVVPLSTLVNWEREAARWVPGAH 454
Cdd:cd18000     4 YQQTGVQWL-WELHCQRVGGILGDEMGLGKTIQIIAF----LAALHHSKL-GLGPSLIVCPATVLKQWVKEFHRWWPPFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  455 VVayvgppaarvcirrheisygdgrLVTNEGSDSDAPNAEQRVESQSDNGRVDRADGyradvyraDVVLTTYEMVQADRS 534
Cdd:cd18000    78 VV-----------------------VLHSSGSGTGSEEKLGSIERKSQLIRKVVGDG--------GILITTYEGFRKHKD 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255089631  535 ALAKIPWSCLVIDEAHRLKNSGGK---AQRDLRTldfAKRVvLLTGTPLQNDTAELWSLLNFV 594
Cdd:cd18000   127 LLLNHNWQYVILDEGHKIRNPDAEitlACKQLRT---PHRL-ILSGTPIQNNLKELWSLFDFV 185
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
375-632 1.64e-34

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: 132.88  E-value: 1.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  375 YQKEGVRWMaHNLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRASRletrgpALVVVPLSTLVNWEREAARWVPGAH 454
Cdd:cd18001     4 HQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS------VLVVMPTSLIPHWVKEFAKWTPGLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  455 VVAYVGP-PAARVCIRRHeisygdgrlVTNEGSdsdapnaeqrvesqsdngrvdradgyradvyradVVLTTYEMVQADR 533
Cdd:cd18001    77 VKVFHGTsKKERERNLER---------IQRGGG----------------------------------VLLTTYGMVLSNT 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  534 SALA-----KIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAG-----RFASKD 603
Cdd:cd18001   114 EQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSLREIP-AKNRIILTGTPIQNNLKELWALFDFACNGsllgtRKTFKM 192
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 255089631  604 EFESAFGAMTAARQV-----------ETLHKVLAPYLLRR 632
Cdd:cd18001   193 EFENPITRGRDKDATqgekalgsevaENLRQIIKPYFLRR 232
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
375-632 1.28e-33

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: 129.63  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  375 YQKEGVRWmahnlVVRERG-CILADEMGLGKTAQSLALIDYVlraqRASrletrGPALVVVPLSTLVNWEREAARWVPga 453
Cdd:cd18010     4 FQREGVCF-----ALRRGGrVLIADEMGLGKTVQAIAIAAYY----REE-----WPLLIVCPSSLRLTWADEIERWLP-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  454 hvvayvgppaarvcirrheisygdgrlvtnegsdSDAPNAEQRVESQSDNGRVDRADgyradvyradVVLTTYEMVQADR 533
Cdd:cd18010    68 ----------------------------------SLPPDDIQVIVKSKDGLRDGDAK----------VVIVSYDLLRRLE 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  534 SALAKIPWSCLVIDEAHRLKNSggKAQRD---LRTLDFAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEF----- 605
Cdd:cd18010   104 KQLLARKFKVVICDESHYLKNS--KAKRTkaaLPLLKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrryc 181
                         250       260       270
                  ....*....|....*....|....*....|..
gi 255089631  606 ---ESAFGAMT--AARQVETLHKVLAPYLLRR 632
Cdd:cd18010   182 aakQGGFGWDYsgSSNLEELHLLLLATIMIRR 213
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
372-609 3.03e-33

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: 129.33  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLV------VRERGCILADEMGLGKTAQSLALIDYVLR-AQRASRletrgpALVVVPLSTLVNWER 444
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVgtdvgsDEGGGCILAHTMGLGKTLQVITFLHTYLAaAPRRSR------PLVLCPASTLYNWED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  445 EAARWVPGAHVvayvgPPAARVCIRRHEISygDGRLVTnegsdsdapnaeqrVESQSDNGRVdRADGYRADVYRADVVLT 524
Cdd:cd18007    75 EFKKWLPPDLR-----PLLVLVSLSASKRA--DARLRK--------------INKWHKEGGV-LLIGYELFRNLASNATT 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  525 TYEMVQADRSALAKIPWSCLVIDEAHRLKNSGG---KAQRDLRTldfaKRVVLLTGTPLQNDTAELWSLLNFVDAGRFAS 601
Cdd:cd18007   133 DPRLKQEFIAALLDPGPDLLVLDEGHRLKNEKSqlsKALSKVKT----KRRILLTGTPLQNNLKEYWTMVDFARPKYLGT 208

                  ....*...
gi 255089631  602 KDEFESAF 609
Cdd:cd18007   209 LKEFKKKF 216
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
372-609 4.49e-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: 111.79  E-value: 4.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVRER----GCILADEMGLGKTAQSLALIDYVLRaQRASRLETRGPALVVVPLSTLVNWEREAA 447
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIrgshGCIMADEMGLGKTLQCITLMWTLLR-QSPQCKPEIDKAIVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  448 RWVpGAHVVayvgpPAArvcirrheisygdgrlVTNEGSDSDAPNAEQRVESQSdnGRVDRAdgyradvyradVVLTTYE 527
Cdd:cd18067    80 KWL-GGRLQ-----PLA----------------IDGGSKKEIDRKLVQWASQQG--RRVSTP-----------VLIISYE 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  528 MVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDfAKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKDEFES 607
Cdd:cd18067   125 TFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLN-TQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKK 203

                  ..
gi 255089631  608 AF 609
Cdd:cd18067   204 NF 205
DEXDc smart00487
DEAD-like helicases superfamily;
364-603 3.13e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.88  E-value: 3.13e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    364 WYGSEGDVLRGYQKEGVRWMAHNlvvrERGCILADEMGLGKT-AQSLALIDYVLRaqrasrlETRGPALVVVPLSTLV-N 441
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSG----LRDVILAAPTGSGKTlAALLPALEALKR-------GKGGRVLVLVPTRELAeQ 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    442 WEREAARWVPGAHVvayvgppaaRVCIRRHEISYGDGRLVTNEGsdsdapnaeqrvesqsdngrvdradgyradvyRADV 521
Cdd:smart00487   70 WAEELKKLGPSLGL---------KVVGLYGGDSKREQLRKLESG--------------------------------KTDI 108
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    522 VLTTYEMVQAD--RSALAKIPWSCLVIDEAHRLKNSGGKAQ--RDLRTLDFAKRVVLLTGTP---LQNDTAELWSLLNFV 594
Cdd:smart00487  109 LVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGFGDQleKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFI 188

                    ....*....
gi 255089631    595 DAGRFASKD 603
Cdd:smart00487  189 DVGFTPLEP 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
736-859 4.90e-25

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 101.13  E-value: 4.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631   736 GKLQLLDKLLPRLKagGHRALIFSQMTRVLDvLEDYCRNRGHSYERLDGGVTGRARQAAIDRFccgsnatdaghsDEGAF 815
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDF------------RKGKI 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 255089631   816 LFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIG 859
Cdd:pfam00271   66 DVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
FYRC pfam05965
F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1482-1560 1.25e-24

F/Y rich C-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00542.


Pssm-ID: 461788  Cd Length: 83  Bit Score: 98.83  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  1482 KPLFRLTADEGLDEPIVAKSATAAWAEVLRRVTTVRRANGEEAK-KTAISGPEFFGYSLPHIRLLIEELPGVNDCTEYKP 1560
Cdd:pfam05965    1 GPLFRVTVEEDPDESFEGSSPTKCWSMVLERVQELRREAGLKLKlPESISGEDMFGLTHPAVVRLIESLPGAEKCTNYKF 80
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
372-609 2.08e-24

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: 103.77  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLV---VRER-GCILADEMGLGKTAQSLALIDYVLRAQRASRLETRGPALVVVPLSTLVNWEREAA 447
Cdd:cd18066     1 LRPHQREGIEFLYECVMgmrVNERfGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  448 RWVPGAHVVAYVgppaarvcirrheisygdgrlvtnegSDSDAPnAEQRVESQsdngrvdradgyradVYraDVVLTTYE 527
Cdd:cd18066    81 KWLGSERIKVFT--------------------------VDQDHK-VEEFIASP---------------LY--SVLIISYE 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  528 MVQADRSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVlLTGTPLQNDTAELWSLLNFVDAGRFASKDEFES 607
Cdd:cd18066   117 MLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRII-LTGTPIQNDLQEFFALIDFVNPGILGSLSTYRK 195

                  ..
gi 255089631  608 AF 609
Cdd:cd18066   196 VY 197
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
372-609 2.79e-24

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: 102.97  E-value: 2.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAHNLVVR-ER-------GCILADEMGLGKTAQSLALIDYVLRAQRASRletrgpALVVVPLSTLVNWE 443
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESlERykgssgfGCILAHSMGLGKTLQVISFLDVLLRHTGAKT------VLAIVPVNTLQNWL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  444 REAARWVPGAHVVAYVGPPAARVCIrrheisYGDgrlvtnegsdsdapnaeqrvESQSDNGRVDRADGYRADvyrADVVL 523
Cdd:cd18069    75 SEFNKWLPPPEALPNVRPRPFKVFI------LND--------------------EHKTTAARAKVIEDWVKD---GGVLL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  524 TTYEMVQadrsaLAKIPwSCLVIDEAHRLKNSGGKAQRDLRTLDFAKRVVlLTGTPLQNDTAELWSLLNFVDAGRFASKD 603
Cdd:cd18069   126 MGYEMFR-----LRPGP-DVVICDEGHRIKNCHASTSQALKNIRSRRRIV-LTGYPLQNNLIEYWCMVDFVRPDFLGTRQ 198

                  ....*.
gi 255089631  604 EFESAF 609
Cdd:cd18069   199 EFSNMF 204
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
372-632 1.97e-23

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 100.06  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRwMAhnLVVRERGCILADEMGLGKTAQSLALIDYvlraqrasrLETRGPA---LVVVPlSTLV-NWereaa 447
Cdd:cd18011     1 PLPHQIDAVL-RA--LRKPPVRLLLADEVGLGKTIEAGLIIKE---------LLLRGDAkrvLILCP-ASLVeQW----- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  448 rwvpgahvvayvgppaarvcirRHEISY--GDGRLVtnegsdSDAPNAEQrveSQSDNGRVDRadgyradvyRADVVLTT 525
Cdd:cd18011    63 ----------------------QDELQDkfGLPFLI------LDRETAAQ---LRRLIGNPFE---------EFPIVIVS 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  526 YEMVQAD---RSALAKIPWSCLVIDEAHRLKNSGG-KAQRDLRTL----DFAKRVVLLTGTPLQNDTAELWSLLNFVDAG 597
Cdd:cd18011   103 LDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGgKETKRYKLGrllaKRARHVLLLTATPHNGKEEDFRALLSLLDPG 182
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 255089631  598 RFASKDEFesafgamtaaRQVETLHKVLAPYLLRR 632
Cdd:cd18011   183 RFAVLGRF----------LRLDGLREVLAKVLLRR 207
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
372-632 8.77e-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: 93.30  E-value: 8.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMAH-----------------------NLVVRER-----GCILADEMGLGKTAQSLALIdyvlraqrasr 423
Cdd:cd18071     1 LLPHQKQALAWMVSrensqdlppfweeavglflntitNFSQKKRpelvrGGILADDMGLGKTLTTISLI----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  424 leTRGPALVVVPLSTLVNWEREAARWVPGAHVVAYVgppaarvcirrheiSYGDGRlvtnegsdsdapnaeqrvesqsdN 503
Cdd:cd18071    70 --LANFTLIVCPLSVLSNWETQFEEHVKPGQLKVYT--------------YHGGER-----------------------N 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  504 GRVDRADGYradvyraDVVLTTYEMVQADRSA-----LAKIPWSCLVIDEAHRLKNSggKAQRDLRTLDF-AKRVVLLTG 577
Cdd:cd18071   111 RDPKLLSKY-------DIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNP--NAQQTKAVLNLsSERRWVLTG 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 255089631  578 TPLQNDTAELWSLLNFVDAGRFASKDEFESAFG---AMTAARQVETLHKVLAPYLLRR 632
Cdd:cd18071   182 TPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
372-609 4.58e-20

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 91.49  E-value: 4.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWM--AHNLVVRER------GCILADEMGLGKTAQSLALIDYVLRAQRASRLETrgpALVVVPLSTLVNWE 443
Cdd:cd18068     1 LKPHQVDGVQFMwdCCCESLKKTkkspgsGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSR---VLVVCPLNTVLNWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  444 REAARWVPGA---------HVVAYVGPPAAR-----------VCIrrheISYGDGRLVTNEgsdsDAPNAEQRVESQSDN 503
Cdd:cd18068    78 NEFEKWQEGLkdeekievnELATYKRPQERSyklqrwqeeggVMI----IGYDMYRILAQE----RNVKSREKLKEIFNK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  504 GRVDRAdgyradvyrADVVlttyemvqadrsalakipwsclVIDEAHRLKN---SGGKAQRDLRTldfaKRVVLLTGTPL 580
Cdd:cd18068   150 ALVDPG---------PDFV----------------------VCDEGHILKNeasAVSKAMNSIRT----KRRIVLTGTPL 194
                         250       260
                  ....*....|....*....|....*....
gi 255089631  581 QNDTAELWSLLNFVDAGRFASKDEFESAF 609
Cdd:cd18068   195 QNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
HELICc smart00490
helicase superfamily c-terminal domain;
766-859 1.51e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.57  E-value: 1.51e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631    766 DVLEDYCRNRGHSYERLDGGVTGRARQAAIDRFCcgsnatdaghsdEGAFLFLLSTRAGGQGINLVAADTVIVFDSDWNP 845
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN------------NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP 68
                            90
                    ....*....|....
gi 255089631    846 QNDAQALARAHRIG 859
Cdd:smart00490   69 ASYIQRIGRAGRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
375-632 7.59e-18

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 84.84  E-value: 7.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  375 YQKEGVRWMAHNLVVRERGCILADEMGLGKTAQSLALIDYVLRAQRASRLE-----------------TRGPALVVVPLS 437
Cdd:cd18072     4 HQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEkekalteweskkdstlvPSAGTLVVCPAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  438 TLVNWEREAARWVPGAhvvayvgppAARVCIRRheisygdgrlvtnegsdsdAPNAEQRVESQSDngrvdradgyradvY 517
Cdd:cd18072    84 LVHQWKNEVESRVASN---------KLRVCLYH-------------------GPNRERIGEVLRD--------------Y 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  518 raDVVLTTYEMV---------QADRSALAKIPWSCLVIDEAHRLKNSggKAQRDLRTLDF-AKRVVLLTGTPLQNDTAEL 587
Cdd:cd18072   122 --DIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIKNP--KVQASIAVCKLrAHARWALTGTPIQNNLLDM 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 255089631  588 WSLLNFVDAGRFaskDEFES-----AFGAMTAARQVETLHKVLapyLLRR 632
Cdd:cd18072   198 YSLLKFLRCSPF---DDLKVwkkqvDNKSRKGGERLNILTKSL---LLRR 241
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
372-603 3.87e-14

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: 74.30  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWMahnlvvRERGCILADEMGLGKTAQSLALI--------------------DYVLRAQRASRLETRGPAL 431
Cdd:cd18070     1 LLPYQRRAVNWM------LVPGGILADEMGLGKTVEVLALIllhprpdndldaadddsdemVCCPDCLVAETPVSSKATL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  432 VVVPLSTLVNWEREAARWVPGAHVVA-YVGPPAarvcirrheisygdgrlvtnegSDSDAPNAEQRVESQsdngrvdrad 510
Cdd:cd18070    75 IVCPSAILAQWLDEINRHVPSSLKVLtYQGVKK----------------------DGALASPAPEILAEY---------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  511 gyradvyraDVVLTTYEMVQAD----------------------RSALAKIPWSCLVIDEAHRLKNSGGKAQRDLRTLdF 568
Cdd:cd18070   123 ---------DIVVTTYDVLRTElhyaeanrsnrrrrrqkryeapPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRL-P 192
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 255089631  569 AKRVVLLTGTPLQNDTAELWSLLNFVDAGRFASKD 603
Cdd:cd18070   193 RVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSD 227
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
372-597 7.20e-13

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: 69.69  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  372 LRGYQKEGVRWmahnLVVRERGCILADeMGLGKTAQSLALIDYVLRAqrasrlETRGPALVVVPLSTLVN-WEREAARW- 449
Cdd:cd18013     1 PHPYQKVAINF----IIEHPYCGLFLD-MGLGKTVTTLTALSDLQLD------DFTRRVLVIAPLRVARStWPDEVEKWn 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  450 -VPGAHVVAYVGPPAARvcirrheisygdgrlvtnegsdSDAPNAEqrvesqsdngrvdradgyradvyrADVVLTTYEM 528
Cdd:cd18013    70 hLRNLTVSVAVGTERQR----------------------SKAANTP------------------------ADLYVINREN 103
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255089631  529 VQ-ADRSALAKIPWSCLVIDEAHRLKN---SGGKAQRDLRTLdfAKRVVLLTGTPLQNDTAELWSLLNFVDAG 597
Cdd:cd18013   104 LKwLVNKSGDPWPFDMVVIDELSSFKSprsKRFKALRKVRPV--IKRLIGLTGTPSPNGLMDLWAQIALLDQG 174
FYRC smart00542
FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region ...
1484-1560 5.83e-12

FY-rich domain, C-terminal region; is sometimes closely juxtaposed with the N-terminal region (FYRN), but sometimes is far distant. Unknown function, but occurs frequently in chromatin-associated proteins.


Pssm-ID: 197781  Cd Length: 86  Bit Score: 63.08  E-value: 5.83e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255089631   1484 LFRLTADEGLDEPIVAKSATAAWAEVLRRVTTVRRANGEEAKKTA-ISGPEFFGYSLPHIRLLIEELPGVNDCTEYKP 1560
Cdd:smart00542    1 LFRVEIESDPGEVFKGESPEKCWEMVLERVQEARIAADLLQLLPEgVSGEEMFGLSSPAVVKLIEALPGVHQCTNYWF 78
FYRN pfam05964
F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It ...
1421-1472 1.40e-10

F/Y-rich N-terminus; This region is normally found in the trithorax/ALL1 family proteins. It is similar to SMART:SM00541.


Pssm-ID: 461787  Cd Length: 51  Bit Score: 57.90  E-value: 1.40e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  1421 GVTLESLGAVqPPDAPGFHSAAYILPVGYRTTRQYMRCDDPNgPRTRWVQEI 1472
Cdd:pfam05964    2 SLTVLSLGEI-VPDRPAFHTERYIYPVGYKSTRLYWSTKDPR-KRCRYTCEI 51
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
320-983 1.26e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.65  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  320 DVALRAYGAVQARREEKLDAARRARGGSTIQSVEADAELAPSREWYGSEGDvLRGYQKEGV-RWMAHNLVVRERGCILAD 398
Cdd:COG1061    30 LLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE-LRPYQQEALeALLAALERGGGRGLVVAP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  399 eMGLGKTAQSLALIDyvlraqrasRLETRGPALVVVPLSTLVN-WEREAARWVPGAHVVAyvgppaarvciRRHEISYgd 477
Cdd:COG1061   109 -TGTGKTVLALALAA---------ELLRGKRVLVLVPRRELLEqWAEELRRFLGDPLAGG-----------GKKDSDA-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  478 grlvtnegsdsdapnaeqrvesqsdngrvdradgyradvyraDVVLTTYEMVqADRSALAKIP--WSCLVIDEAHRLkns 555
Cdd:COG1061   166 ------------------------------------------PITVATYQSL-ARRAHLDELGdrFGLVIIDEAHHA--- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  556 GGKAQRDLRTLDFAKRVVLLTGTPLQNDTAElwsllnfVDAGRFaskdeFESAFGaMTAARQVEtlHKVLAPYLLRRLKQ 635
Cdd:COG1061   200 GAPSYRRILEAFPAAYRLGLTATPFRSDGRE-------ILLFLF-----DGIVYE-YSLKEAIE--DGYLAPPEYYGIRV 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  636 DVEHKlpprvetlvecelmplqkkcyRALFERNfsflrqGSKDDRALANFSnlmmevrkccqhpflldgveeafvsqqms 715
Cdd:COG1061   265 DLTDE---------------------RAEYDAL------SERLREALAADA----------------------------- 288
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  716 kkggkrpaktataaelvacSGKLQLLDKLLPRLkAGGHRALIFSQMTRVLDVLEDYCRNRGHSYERLDGGVTGRARQAAI 795
Cdd:COG1061   289 -------------------ERKDKILRELLREH-PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEIL 348
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  796 DRFccgsnatdaghsDEGAFLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQTK-PVQVY------- 867
Cdd:COG1061   349 EAF------------RDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYdfvgndv 416
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  868 --------RLVMRATYERDMLDRaamKLGLEQAIFSSNLNSGNGAIDNKERRGAAAEIERLLKHGAYGALSEDCAEGDAR 939
Cdd:COG1061   417 pvleelakDLRDLAGYRVEFLDE---EESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALAL 493
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 255089631  940 TKAFAGEGIDDILARSERRVVEASDDDTSKSSDAQKSMFATATF 983
Cdd:COG1061   494 ELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLE 537
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
172-219 1.69e-08

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 52.75  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255089631  172 VEKLLGWR----ASVDAVDADSGTPDEDGVDILVKWKGRALVHCSWVPLPAL 219
Cdd:cd18660     5 IEKILDHRpkgpVEEASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETL 56
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
393-578 1.64e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 52.02  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  393 GCILADEMGLGKT-AQSLALIDYVLraqrasrlETRGPALVVVPLSTLVN-WEREAARWV-PGAHVVAYVGppaarvcir 469
Cdd:cd00046     3 NVLITAPTGSGKTlAALLAALLLLL--------KKGKKVLVLVPTKALALqTAERLRELFgPGIRVAVLVG--------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255089631  470 rheisygdgrlvtnegsdsdAPNAEQRvesqsdngrvdradgYRADVYRADVVLTTYEMVQADRSALAKI---PWSCLVI 546
Cdd:cd00046    66 --------------------GSSAEER---------------EKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIV 110
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 255089631  547 DEAHRLKNSGGKAQRDLRTLDFAK----RVVLLTGT 578
Cdd:cd00046   111 DEAHALLIDSRGALILDLAVRKAGlknaQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
513-579 1.44e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.16  E-value: 1.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255089631   513 RADVYRADVVLTTYEMVQA---DRSALAKIpwSCLVIDEAHRLKNSGGKAQ--RDLRTLDFAKRVVLLTGTP 579
Cdd:pfam00270   89 LEKLKGPDILVGTPGRLLDllqERKLLKNL--KLLVLDEAHRLLDMGFGPDleEILRRLPKKRQILLLSATL 158
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
815-870 4.67e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 4.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 255089631  815 FLFLLSTRAGGQGINLVAADTVIVFDSDWNPQNDAQALARAHRIGQtKPVQVYRLV 870
Cdd:cd18785    23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
167-213 6.28e-03

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 36.93  E-value: 6.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 255089631  167 EDATAVEKLLGWRasVDAVDADSGTPDEDGVDILVKWKGRALVHCSW 213
Cdd:cd18668     2 EDTMIIEKILASR--KKKKEKEEGAEEIEVEEYLVKYKNFSYLHCEW 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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