NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1399623113|gb|PYH35024|]
View 

hypothetical protein BO87DRAFT_396216 [Aspergillus neoniger CBS 115656]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13756248)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to DNA repair and recombination protein RAD54 that plays a role in homologous recombination related repair of DNA double-strand breaks

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
208-453 2.54e-135

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


The actual alignment was detected with superfamily member cd18067:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 243  Bit Score: 419.95  E-value: 2.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvTTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCK-PEIDKAIVVSPSSLVKNWANELG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDaITPFAVDGKaSKTELISQMKQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18067     80 KWLGGR-LQPLAIDGG-SKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIVN 447
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18067    238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
122-705 7.26e-118

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 388.43  E-value: 7.26e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  122 RQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKPKLDEPLVHKSLADILGLKKKTEGRPKVPvvid 201
Cdd:COG0553    160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  202 PRLAKVLRPHQVEGVKFLYRCttgmvDKNANGCIMADGMGLGKTLQCISLmwtlLKQSPEAGvtTIQKCIIACPSSLVGN 281
Cdd:COG0553    236 AGLKATLRPYQLEGAAWLLFL-----RRLGLGGLLADDMGLGKTIQALAL----LLELKERG--LARPVLIVAPTSLVGN 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  282 WANELVKWLgkDAITPFAVDGKASKTELISQMKQwaiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKN 361
Cdd:COG0553    305 WQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKN 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  362 KESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRdaagteedlkkgDERLAE 441
Cdd:COG0553    373 PATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALER 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  442 LSSIVNKFIIRRT-NDILsKYLPVKYEHVVFCNMSEFQLGLYKHFIQSpEIKSLLRGKGSQP----LKAIGLLKKLCNHP 516
Cdd:COG0553    441 LRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSHP 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  517 DLLNlsndlpgceytfpedyvppeargRDRDIKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDLFEKLCRTRGY 596
Cdd:COG0553    519 ALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERGI 574
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  597 GSLRLDGTMTVGKRQKLVDKFNnpNGEEF-VFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 675
Cdd:COG0553    575 EYAYLHGGTSAEERDELVDRFQ--EGPEApVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1399623113  676 VYRFIATGSIEEKIFQRQSHKQSLSSCVVD 705
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
1386-1564 1.56e-115

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


:

Pssm-ID: 463395  Cd Length: 179  Bit Score: 362.19  E-value: 1.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1386 RHLLEVRGNLIIRQLCMNLSPERIYRTLADCLEKEEDIEFASIMVQNLNNNLITAPELSELRKRLRNLDAKDGQMFFVAL 1465
Cdd:pfam11916    1 RRLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRNLDSEEDRELFSTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1466 FRSWCHNAVSTFSLCLLAQAYEQAYNLLQVFAELEMTVNMLIQIDKLVQLLESPVFTYLRLQLLEPERYPYLYKCLYGVL 1545
Cdd:pfam11916   81 YKSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLL 160
                          170
                   ....*....|....*....
gi 1399623113 1546 MLLPQSSAFAALKNRLNSV 1564
Cdd:pfam11916  161 MLLPQSSAFNTLRNRLQSV 179
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
16-187 5.65e-90

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


:

Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 5.65e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   16 STNSVDRLSKPFKCPGLATATRASDKPARKRRKVNYAGADGTVDDD-SVKPYTN-EDRLALATRDANRFPSFKVKDKEMT 93
Cdd:pfam08658    1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdSDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   94 FRQRFKIPLINKSSDAYNSSRPAPTLGMRQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKP---- 169
Cdd:pfam08658   81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKPEEEEEAEEEEEEEEPeeka 160
                          170       180
                   ....*....|....*....|
gi 1399623113  170 --KLDEPLVHKSLADILGLK 187
Cdd:pfam08658  161 rkKLDNPLPHKSLAEILGIK 180
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
870-952 3.89e-45

Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. This domain appears to be the one responsible for binding to Fab1. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


:

Pssm-ID: 403838  Cd Length: 97  Bit Score: 158.14  E-value: 3.89e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  870 HARNGG--------------VAPYLKEIVPPVLACFSDQDARVRYYACESMYNIAKVAKGEVLLFFNEIFDALSKLASDS 935
Cdd:pfam12755    1 NARKGGliglaataialgkdIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80
                           90
                   ....*....|....*..
gi 1399623113  936 ELSVKNGAELLDRLVKD 952
Cdd:pfam12755   81 DPSVKNGAELLDRLLKD 97
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
208-453 2.54e-135

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: 419.95  E-value: 2.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvTTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCK-PEIDKAIVVSPSSLVKNWANELG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDaITPFAVDGKaSKTELISQMKQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18067     80 KWLGGR-LQPLAIDGG-SKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIVN 447
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18067    238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
122-705 7.26e-118

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 388.43  E-value: 7.26e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  122 RQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKPKLDEPLVHKSLADILGLKKKTEGRPKVPvvid 201
Cdd:COG0553    160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  202 PRLAKVLRPHQVEGVKFLYRCttgmvDKNANGCIMADGMGLGKTLQCISLmwtlLKQSPEAGvtTIQKCIIACPSSLVGN 281
Cdd:COG0553    236 AGLKATLRPYQLEGAAWLLFL-----RRLGLGGLLADDMGLGKTIQALAL----LLELKERG--LARPVLIVAPTSLVGN 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  282 WANELVKWLgkDAITPFAVDGKASKTELISQMKQwaiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKN 361
Cdd:COG0553    305 WQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKN 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  362 KESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRdaagteedlkkgDERLAE 441
Cdd:COG0553    373 PATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALER 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  442 LSSIVNKFIIRRT-NDILsKYLPVKYEHVVFCNMSEFQLGLYKHFIQSpEIKSLLRGKGSQP----LKAIGLLKKLCNHP 516
Cdd:COG0553    441 LRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSHP 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  517 DLLNlsndlpgceytfpedyvppeargRDRDIKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDLFEKLCRTRGY 596
Cdd:COG0553    519 ALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERGI 574
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  597 GSLRLDGTMTVGKRQKLVDKFNnpNGEEF-VFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 675
Cdd:COG0553    575 EYAYLHGGTSAEERDELVDRFQ--EGPEApVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1399623113  676 VYRFIATGSIEEKIFQRQSHKQSLSSCVVD 705
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
1386-1564 1.56e-115

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 463395  Cd Length: 179  Bit Score: 362.19  E-value: 1.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1386 RHLLEVRGNLIIRQLCMNLSPERIYRTLADCLEKEEDIEFASIMVQNLNNNLITAPELSELRKRLRNLDAKDGQMFFVAL 1465
Cdd:pfam11916    1 RRLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRNLDSEEDRELFSTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1466 FRSWCHNAVSTFSLCLLAQAYEQAYNLLQVFAELEMTVNMLIQIDKLVQLLESPVFTYLRLQLLEPERYPYLYKCLYGVL 1545
Cdd:pfam11916   81 YKSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLL 160
                          170
                   ....*....|....*....
gi 1399623113 1546 MLLPQSSAFAALKNRLNSV 1564
Cdd:pfam11916  161 MLLPQSSAFNTLRNRLQSV 179
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
211-519 3.86e-90

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: 294.98  E-value: 3.86e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  211 HQVEGVKFLYRCTTGMVdknaNGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIqkciIACPSSLVGNWANELVKWL 290
Cdd:pfam00176    1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTL----IVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  291 GKDAITPFAVDGKASKTE--LISQMKQWAiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTWT 368
Cdd:pfam00176   73 SPPALRVVVLHGNKRPQErwKNDPNFLAD--------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  369 ALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGrdaagteedlkKGDERLAELSSIVNK 448
Cdd:pfam00176  145 ALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKP 213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1399623113  449 FIIRRTNDILSKYLPVKYEHVVFCNMSEFQLGLYKHFIQSPEIKSLLRGKG-----SQPLKAIGLLKKLCNHPDLL 519
Cdd:pfam00176  214 FLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGgreikASLLNILMRLRKICNHPGLI 289
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
16-187 5.65e-90

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 5.65e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   16 STNSVDRLSKPFKCPGLATATRASDKPARKRRKVNYAGADGTVDDD-SVKPYTN-EDRLALATRDANRFPSFKVKDKEMT 93
Cdd:pfam08658    1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdSDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   94 FRQRFKIPLINKSSDAYNSSRPAPTLGMRQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKP---- 169
Cdd:pfam08658   81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKPEEEEEAEEEEEEEEPeeka 160
                          170       180
                   ....*....|....*....|
gi 1399623113  170 --KLDEPLVHKSLADILGLK 187
Cdd:pfam08658  161 rkKLDNPLPHKSLAEILGIK 180
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
208-704 5.65e-69

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 253.95  E-value: 5.65e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRcttgMVDKNANGcIMADGMGLGKTLQCISLMWTLlkqSPEAGVTTIQkcIIACPSSLVGNWANELV 287
Cdd:PLN03142   170 MRDYQLAGLNWLIR----LYENGING-ILADEMGLGKTLQTISLLGYL---HEYRGITGPH--MVVAPKSTLGNWMNEIR 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLgkDAITPFAVDGKASKTELIsqmKQWAIASGRSivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:PLN03142   240 RFC--PVLRAVKFHGNPEERAHQ---REELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELpilrgrdaaGTEEDLKkgdERLAELSSIVN 447
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  448 KFIIRRTNDILSKYLPVKYEHVVFCNMSEFQLGLYKHFIQSpEIKSLLRGKGSQPLKAIGL-LKKLCNHPDLLNLSNdlP 526
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK-DLDVVNAGGERKRLLNIAMqLRKCCNHPYLFQGAE--P 456
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  527 GCEYTFPEDYVPPeargrdrdikswySGKMMVLDRMLARIRQdtNDKIVLI-SNYTQTLDLFEKLCRTRGYGSLRLDGTM 605
Cdd:PLN03142   457 GPPYTTGEHLVEN-------------SGKMVLLDKLLPKLKE--RDSRVLIfSQMTRLLDILEDYLMYRGYQYCRIDGNT 521
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  606 TVGKRQKLVDKFNNPNGEEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATGSI 685
Cdd:PLN03142   522 GGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTI 601
                          490
                   ....*....|....*....
gi 1399623113  686 EEKIFQRQSHKQSLSSCVV 704
Cdd:PLN03142   602 EEKVIERAYKKLALDALVI 620
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
552-680 7.99e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 7.99e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  552 YSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDLFEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNPNgEEFVFLLSS 631
Cdd:cd18793      9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLST 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1399623113  632 KAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFI 680
Cdd:cd18793     87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
870-952 3.89e-45

Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. This domain appears to be the one responsible for binding to Fab1. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 403838  Cd Length: 97  Bit Score: 158.14  E-value: 3.89e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  870 HARNGG--------------VAPYLKEIVPPVLACFSDQDARVRYYACESMYNIAKVAKGEVLLFFNEIFDALSKLASDS 935
Cdd:pfam12755    1 NARKGGliglaataialgkdIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80
                           90
                   ....*....|....*..
gi 1399623113  936 ELSVKNGAELLDRLVKD 952
Cdd:pfam12755   81 DPSVKNGAELLDRLLKD 97
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
554-669 1.76e-23

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: 96.90  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  554 GKMMVLDRMLARIRqdtNDKIVLISNYTQTLDLfEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNpngEEFVFLLSSKA 633
Cdd:pfam00271    1 EKLEALLELLKKER---GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1399623113  634 GGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDG 669
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
200-399 1.18e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.87  E-value: 1.18e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   200 IDPRLAKVLRPHQVEGVKFLYrcttgmvdKNANGCIMADGMGLGKTLQ-CISLMWTLLKQSPeagvttiQKCIIACP-SS 277
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALL--------SGLRDVILAAPTGSGKTLAaLLPALEALKRGKG-------GRVLVLVPtRE 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   278 LVGNWANELVKWLGKDAITPFAVDGKASKTELISQMKqwaiasgrSIVRPVLIISYETLR--LYVDTLRDSPIGLLLCDE 355
Cdd:smart00487   66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLE--------SGKTDILVTTPGRLLdlLENDKLSLSNVDLVILDE 137
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1399623113   356 GHRLKN---KESLTWTALNGLNVQRRVILSGTP---IQNDLSEYFALLHF 399
Cdd:smart00487  138 AHRLLDggfGDQLEKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVF 187
HELICc smart00490
helicase superfamily c-terminal domain;
585-669 1.75e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 1.75e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   585 DLFEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNPngeEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALAR 664
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1399623113   665 VWRDG 669
Cdd:smart00490   78 AGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
208-473 2.50e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.42  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCttgMVDKNANGCIMADgMGLGKTLqcisLMWTLLKQspeagVTTIQKCIIACPS-SLVGNWANEL 286
Cdd:COG1061     81 LRPYQQEALEALLAA---LERGGGRGLVVAP-TGTGKTV----LALALAAE-----LLRGKRVLVLVPRrELLEQWAEEL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  287 VKWLGKdaitPFAVDGKasktelisqmkqwaiasgRSIVRPVLIISYETL--RLYVDTLRDSpIGLLLCDEGHRLknkES 364
Cdd:COG1061    148 RRFLGD----PLAGGGK------------------KDSDAPITVATYQSLarRAHLDELGDR-FGLVIIDEAHHA---GA 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  365 LTWTA-LNGLNVQRRVILSGTPIQND-LSEYFALLhfanpnllgsqneFRKRFELPIlrgRDAA-----------GTEED 431
Cdd:COG1061    202 PSYRRiLEAFPAAYRLGLTATPFRSDgREILLFLF-------------DGIVYEYSL---KEAIedgylappeyyGIRVD 265
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1399623113  432 LKKGDERLAELSSIVNKFII---RRTNDILSKYLP--VKYEHV-VFCN 473
Cdd:COG1061    266 LTDERAEYDALSERLREALAadaERKDKILRELLRehPDDRKTlVFCS 313
 
Name Accession Description Interval E-value
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
208-453 2.54e-135

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: 419.95  E-value: 2.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvTTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCK-PEIDKAIVVSPSSLVKNWANELG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDaITPFAVDGKaSKTELISQMKQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18067     80 KWLGGR-LQPLAIDGG-SKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIVN 447
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVN 237

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18067    238 RCIIRR 243
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
122-705 7.26e-118

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 388.43  E-value: 7.26e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  122 RQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKPKLDEPLVHKSLADILGLKKKTEGRPKVPvvid 201
Cdd:COG0553    160 GRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLP---- 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  202 PRLAKVLRPHQVEGVKFLYRCttgmvDKNANGCIMADGMGLGKTLQCISLmwtlLKQSPEAGvtTIQKCIIACPSSLVGN 281
Cdd:COG0553    236 AGLKATLRPYQLEGAAWLLFL-----RRLGLGGLLADDMGLGKTIQALAL----LLELKERG--LARPVLIVAPTSLVGN 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  282 WANELVKWLgkDAITPFAVDGKASKTELISQMKQwaiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKN 361
Cdd:COG0553    305 WQRELAKFA--PGLRVLVLDGTRERAKGANPFED----------ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKN 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  362 KESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRdaagteedlkkgDERLAE 441
Cdd:COG0553    373 PATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGD------------EEALER 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  442 LSSIVNKFIIRRT-NDILsKYLPVKYEHVVFCNMSEFQLGLYKHFIQSpEIKSLLRGKGSQP----LKAIGLLKKLCNHP 516
Cdd:COG0553    441 LRRLLRPFLLRRTkEDVL-KDLPEKTEETLYVELTPEQRALYEAVLEY-LRRELEGAEGIRRrgliLAALTRLRQICSHP 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  517 DLLNlsndlpgceytfpedyvppeargRDRDIKSWYSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDLFEKLCRTRGY 596
Cdd:COG0553    519 ALLL-----------------------EEGAELSGRSAKLEALLELLEELL-AEGEKVLVFSQFTDTLDLLEERLEERGI 574
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  597 GSLRLDGTMTVGKRQKLVDKFNnpNGEEF-VFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCF 675
Cdd:COG0553    575 EYAYLHGGTSAEERDELVDRFQ--EGPEApVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1399623113  676 VYRFIATGSIEEKIFQRQSHKQSLSSCVVD 705
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
1386-1564 1.56e-115

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 463395  Cd Length: 179  Bit Score: 362.19  E-value: 1.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1386 RHLLEVRGNLIIRQLCMNLSPERIYRTLADCLEKEEDIEFASIMVQNLNNNLITAPELSELRKRLRNLDAKDGQMFFVAL 1465
Cdd:pfam11916    1 RRLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRNLDSEEDRELFSTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113 1466 FRSWCHNAVSTFSLCLLAQAYEQAYNLLQVFAELEMTVNMLIQIDKLVQLLESPVFTYLRLQLLEPERYPYLYKCLYGVL 1545
Cdd:pfam11916   81 YKSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLL 160
                          170
                   ....*....|....*....
gi 1399623113 1546 MLLPQSSAFAALKNRLNSV 1564
Cdd:pfam11916  161 MLLPQSSAFNTLRNRLQSV 179
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
208-453 2.45e-110

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: 350.43  E-value: 2.45e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPeAGVTTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18004      1 LRPHQREGVQFLYDCLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGP-YGKPTAKKALIVCPSSLVGNWKAEFD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGKASKTELISQmkqwaiASGRSIVRPVLIISYETLRLYVDTL-RDSPIGLLLCDEGHRLKNKESLT 366
Cdd:cd18004     80 KWLGLRRIKVVTADGNAKDVKASLD------FFSSASTYPVLIISYETLRRHAEKLsKKISIDLLICDEGHRLKNSESKT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  367 WTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIV 446
Cdd:cd18004    154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                   ....*..
gi 1399623113  447 NKFIIRR 453
Cdd:cd18004    234 SRFILRR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
211-519 3.86e-90

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: 294.98  E-value: 3.86e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  211 HQVEGVKFLYRCTTGMVdknaNGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIqkciIACPSSLVGNWANELVKWL 290
Cdd:pfam00176    1 YQIEGVNWMLSLENNLG----RGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTL----IVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  291 GKDAITPFAVDGKASKTE--LISQMKQWAiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTWT 368
Cdd:pfam00176   73 SPPALRVVVLHGNKRPQErwKNDPNFLAD--------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  369 ALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGrdaagteedlkKGDERLAELSSIVNK 448
Cdd:pfam00176  145 ALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG-----------GGKKGVSRLHKLLKP 213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1399623113  449 FIIRRTNDILSKYLPVKYEHVVFCNMSEFQLGLYKHFIQSPEIKSLLRGKG-----SQPLKAIGLLKKLCNHPDLL 519
Cdd:pfam00176  214 FLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGgreikASLLNILMRLRKICNHPGLI 289
Rad54_N pfam08658
Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.
16-187 5.65e-90

Rad54 N terminal; This is the N terminal of the DNA repair protein Rad54.


Pssm-ID: 430137  Cd Length: 180  Bit Score: 289.93  E-value: 5.65e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   16 STNSVDRLSKPFKCPGLATATRASDKPARKRRKVNYAGADGTVDDD-SVKPYTN-EDRLALATRDANRFPSFKVKDKEMT 93
Cdd:pfam08658    1 VPDSLDRLTKPFKVPGSATPTRASDRPARKRRKVSYAGADGDAEDGdSDKPYTNvERRLALATRRVNKFPVFRVKDKETV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   94 FRQRFKIPLINKSSDAYNSSRPAPTLGMRQGATFVVKPLHDPSGEFAIVLYDPTVDDVNEPESKEEATADAEEQKP---- 169
Cdd:pfam08658   81 FRKSFSVPLKNKKQGAYNPRRPPPTLGTRRGAIFVPRPLHDPTGEFAIVLYDPTVDDRDKPEEEEEAEEEEEEEEPeeka 160
                          170       180
                   ....*....|....*....|
gi 1399623113  170 --KLDEPLVHKSLADILGLK 187
Cdd:pfam08658  161 rkKLDNPLPHKSLAEILGIK 180
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
208-453 5.36e-79

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: 260.93  E-value: 5.36e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18066      1 LRPHQREGIEFLYECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGKPVIKRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGKASKTELISqmkqwaiasgrSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18066     81 KWLGSERIKVFTVDQDHKVEEFIA-----------SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTT 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIVN 447
Cdd:cd18066    150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTG 229

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18066    230 LFILRR 235
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
208-704 5.65e-69

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 253.95  E-value: 5.65e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRcttgMVDKNANGcIMADGMGLGKTLQCISLMWTLlkqSPEAGVTTIQkcIIACPSSLVGNWANELV 287
Cdd:PLN03142   170 MRDYQLAGLNWLIR----LYENGING-ILADEMGLGKTLQTISLLGYL---HEYRGITGPH--MVVAPKSTLGNWMNEIR 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLgkDAITPFAVDGKASKTELIsqmKQWAIASGRSivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:PLN03142   240 RFC--PVLRAVKFHGNPEERAHQ---REELLVAGKF---DVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELpilrgrdaaGTEEDLKkgdERLAELSSIVN 447
Cdd:PLN03142   312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQI---------SGENDQQ---EVVQQLHKVLR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  448 KFIIRRTNDILSKYLPVKYEHVVFCNMSEFQLGLYKHFIQSpEIKSLLRGKGSQPLKAIGL-LKKLCNHPDLLNLSNdlP 526
Cdd:PLN03142   380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK-DLDVVNAGGERKRLLNIAMqLRKCCNHPYLFQGAE--P 456
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  527 GCEYTFPEDYVPPeargrdrdikswySGKMMVLDRMLARIRQdtNDKIVLI-SNYTQTLDLFEKLCRTRGYGSLRLDGTM 605
Cdd:PLN03142   457 GPPYTTGEHLVEN-------------SGKMVLLDKLLPKLKE--RDSRVLIfSQMTRLLDILEDYLMYRGYQYCRIDGNT 521
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  606 TVGKRQKLVDKFNNPNGEEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFIATGSI 685
Cdd:PLN03142   522 GGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTI 601
                          490
                   ....*....|....*....
gi 1399623113  686 EEKIFQRQSHKQSLSSCVV 704
Cdd:PLN03142   602 EEKVIERAYKKLALDALVI 620
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
208-433 1.65e-61

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: 210.61  E-value: 1.65e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYR--CTTGMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPeagvtTIQKCIIACPSSLVGNWANE 285
Cdd:cd18007      1 LKPHQVEGVRFLWSnlVGTDVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-----RRSRPLVLCPASTLYNWEDE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  286 LVKWLGKDAItPFAVD--GKASKTEL--ISQMKQWAIASGrsivrpVLIISYETLR---------------LYVDTLRDS 346
Cdd:cd18007     76 FKKWLPPDLR-PLLVLvsLSASKRADarLRKINKWHKEGG------VLLIGYELFRnlasnattdprlkqeFIAALLDPG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  347 PiGLLLCDEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAA 426
Cdd:cd18007    149 P-DLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVD 227

                   ....*..
gi 1399623113  427 GTEEDLK 433
Cdd:cd18007    228 STEEDVR 234
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
208-453 1.03e-58

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: 202.99  E-value: 1.03e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTtgmvdKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIQKCI---------------I 272
Cdd:cd18005      1 LRDYQREGVEFMYDLY-----KNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRRDRENNRPRfkkkppassakkpvlI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  273 ACPSSLVGNWANELVKWlGKDAITPFAVDGKasKTELISQMKQwaiasGRSivrPVLIISYETLRLYVDTLRDSPIGLLL 352
Cdd:cd18005     76 VAPLSVLYNWKDELDTW-GHFEVGVYHGSRK--DDELEGRLKA-----GRL---EVVVTTYDTLRRCIDSLNSINWSAVI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  353 CDEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDL 432
Cdd:cd18005    145 ADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATAREL 224
                          250       260
                   ....*....|....*....|.
gi 1399623113  433 KKGDERLAELSSIVNKFIIRR 453
Cdd:cd18005    225 RLGRKRKQELAVKLSKFFLRR 245
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
208-402 8.06e-57

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: 195.09  E-value: 8.06e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTtgmvdKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd17919      1 LRPYQLEGLNFLLELY-----ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERG-----PVLVVCPLSVLENWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKdaITPFAVDGKASKTELISQMKQWAIAsgrsivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd17919     71 KWTPD--LRVVVYHGSQRERAQIRAKEKLDKF-------DVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLS 141
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANP 402
Cdd:cd17919    142 KALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
552-680 7.99e-56

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 190.00  E-value: 7.99e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  552 YSGKMMVLDRMLARIRqDTNDKIVLISNYTQTLDLFEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNPNgEEFVFLLSS 631
Cdd:cd18793      9 VSGKLEALLELLEELR-EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDP-DIRVFLLST 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1399623113  632 KAGGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDGQKKDCFVYRFI 680
Cdd:cd18793     87 KAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
208-433 7.47e-48

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: 171.61  E-value: 7.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKN----ANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIqkcIIACPSSLVGNWA 283
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESLKKTkkspGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSRV---LVVCPLNTVLNWL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  284 NELVKWL----GKDAITPFAVDGKASKTELISQMKQWAIASGrsivrpVLIISYETLRL----------------YVDTL 343
Cdd:cd18068     78 NEFEKWQeglkDEEKIEVNELATYKRPQERSYKLQRWQEEGG------VMIIGYDMYRIlaqernvksreklkeiFNKAL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  344 RDSPIGLLLCDEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGR 423
Cdd:cd18068    152 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQ 231
                          250
                   ....*....|
gi 1399623113  424 DAAGTEEDLK 433
Cdd:cd18068    232 CADSTLVDVR 241
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
870-952 3.89e-45

Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. This domain appears to be the one responsible for binding to Fab1. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 403838  Cd Length: 97  Bit Score: 158.14  E-value: 3.89e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  870 HARNGG--------------VAPYLKEIVPPVLACFSDQDARVRYYACESMYNIAKVAKGEVLLFFNEIFDALSKLASDS 935
Cdd:pfam12755    1 NARKGGliglaataialgkdIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80
                           90
                   ....*....|....*..
gi 1399623113  936 ELSVKNGAELLDRLVKD 952
Cdd:pfam12755   81 DPSVKNGAELLDRLLKD 97
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
208-454 1.92e-44

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: 160.81  E-value: 1.92e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRcttgMVDKNANGCiMADGMGLGKTLQCISLMwTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18012      5 LRPYQKEGFNWLSF----LRHYGLGGI-LADDMGLGKTLQTLALL-LSRKEEGRKG-----PSLVVAPTSLIYNWEEEAA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWlgkdaiTP----FAVDGKASKTELISQMKQwaiasgrsivRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKE 363
Cdd:cd18012     74 KF------APelkvLVIHGTKRKREKLRALED----------YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQ 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  364 SLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAagteedlkkgdERLAELS 443
Cdd:cd18012    138 TKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDE-----------EALEELK 206
                          250
                   ....*....|.
gi 1399623113  444 SIVNKFIIRRT 454
Cdd:cd18012    207 KLISPFILRRL 217
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
208-433 2.87e-44

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: 160.75  E-value: 2.87e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCT---TGMVDKNAN-GCIMADGMGLGKTLQCISLMWTLLKQspeagvTTIQKCIIACPSSLVGNWA 283
Cdd:cd18069      1 LKPHQIGGIRFLYDNIiesLERYKGSSGfGCILAHSMGLGKTLQVISFLDVLLRH------TGAKTVLAIVPVNTLQNWL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  284 NELVKWL------GKDAITPFAV----DGKASKTELISQMKQWAIASGrsivrpVLIISYETLRLyvdtlRDSPiGLLLC 353
Cdd:cd18069     75 SEFNKWLpppealPNVRPRPFKVfilnDEHKTTAARAKVIEDWVKDGG------VLLMGYEMFRL-----RPGP-DVVIC 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  354 DEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLK 433
Cdd:cd18069    143 DEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
208-453 1.09e-39

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: 147.88  E-value: 1.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrcttGMVDK-NANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIQKCIIACPSSLVGNWANEL 286
Cdd:cd17999      1 LRPYQQEGINWL-----AFLNKyNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPSLVVCPPTLVGHWVAEI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  287 VKWLGKDAITPFAVDGKASKTELISQMKQWAiasgrsivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLT 366
Cdd:cd17999     75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKH---------NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  367 WTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAELSSIV 446
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQV 225

                   ....*..
gi 1399623113  447 NKFIIRR 453
Cdd:cd17999    226 LPFLLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
208-453 2.64e-39

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: 146.75  E-value: 2.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRcttgmVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSpeagvtTIQKCIIACPSSLVGNWANELV 287
Cdd:cd18001      1 LYPHQREGVAWLWS-----LHDGGKGGILADDMGLGKTVQICAFLSGMFDSG------LIKSVLVVMPTSLIPHWVKEFA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWlgKDAITPFAVDGkASKTELISQMKqwAIASGRSivrpVLIISYETLRLYVDTLRDSPIG-----LLLCDEGHRLKNK 362
Cdd:cd18001     70 KW--TPGLRVKVFHG-TSKKERERNLE--RIQRGGG----VLLTTYGMVLSNTEQLSADDHDefkwdYVILDEGHKIKNS 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  363 ESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFA-NPNLLGSQNEFRKRFELPILRGRDAAGTEEDLKKGDERLAE 441
Cdd:cd18001    141 KTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAEN 220
                          250
                   ....*....|..
gi 1399623113  442 LSSIVNKFIIRR 453
Cdd:cd18001    221 LRQIIKPYFLRR 232
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
208-453 1.28e-37

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: 141.04  E-value: 1.28e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTtgmvdKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18006      1 LRPYQLEGVNWLLQCR-----AEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLG-----PFLVLCPLSVLDNWKEELN 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDgKASKTELISQMKQ---WAiasgrsivrpVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKES 364
Cdd:cd18006     71 RFAPDLSVITYMGD-KEKRLDLQQDIKStnrFH----------VLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNS 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  365 LTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQ--NEFRKRFelpilrgrdaagteEDLKKGDERLAEL 442
Cdd:cd18006    140 LLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDklDDFIKAY--------------SETDDESETVEEL 205
                          250
                   ....*....|.
gi 1399623113  443 SSIVNKFIIRR 453
Cdd:cd18006    206 HLLLQPFLLRR 216
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
208-453 1.70e-33

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: 129.68  E-value: 1.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTtgmvdKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiQKCIIAcPSSLVGNWANELV 287
Cdd:cd17995      1 LRDYQLEGVNWLLFNW-----YNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRG----PFLVIA-PLSTIPNWQREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITpFAVDGKASKTELISQMKQWAiASGRSIVRP----VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKE 363
Cdd:cd17995     71 TWTDMNVVV-YHGSGESRQIIQQYEMYFKD-AQGRKKKGVykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  364 SLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFelpilrgrdaagteEDLKKGDErLAELS 443
Cdd:cd17995    149 SKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF--------------GDLKTAEQ-VEKLQ 213
                          250
                   ....*....|
gi 1399623113  444 SIVNKFIIRR 453
Cdd:cd17995    214 ALLKPYMLRR 223
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
208-453 5.41e-32

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: 125.86  E-value: 5.41e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYrcttgmvdknANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIQKC------------IIACP 275
Cdd:cd18008      1 LLPYQKQGLAWML----------PRGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSsdpkklylskttLIVVP 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  276 SSLVGNWANELVKWLGKDAITPFAVDGkASKTELISQMKQWaiasgrSIVrpvlIISYETLR--------LYVDTLRDSP 347
Cdd:cd18008     71 LSLLSQWKDEIEKHTKPGSLKVYVYHG-SKRIKSIEELSDY------DIV----ITTYGTLAsefpknkkGGGRDSKEKE 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  348 IGLLLC--------DEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPI 419
Cdd:cd18008    140 ASPLHRirwyrvilDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1399623113  420 LRGRDAAgteedlkkgderLAELSSIVNKFIIRR 453
Cdd:cd18008    220 SKNDRKA------------LERLQALLKPILLRR 241
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
207-453 5.56e-32

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: 125.58  E-value: 5.56e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  207 VLRPHQVEGVKFLYRcttgMVDKNANGcIMADGMGLGKTLQCISLMWTLLkqspEAGVTTiqKCIIACPSSLVGNWANEL 286
Cdd:cd18009      3 VMRPYQLEGMEWLRM----LWENGING-ILADEMGLGKTIQTIALLAHLR----ERGVWG--PFLVIAPLSTLPNWVNEF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  287 VKWLGKDAITPFAVDgKASKTELISQMKQwaiASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLT 366
Cdd:cd18009     72 ARFTPSVPVLLYHGT-KEERERLRKKIMK---REGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  367 WTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILrgRDAAGTEEDLKKGDER--LAELSS 444
Cdd:cd18009    148 IQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSL--SDNAADISNLSEEREQniVHMLHA 225

                   ....*....
gi 1399623113  445 IVNKFIIRR 453
Cdd:cd18009    226 ILKPFLLRR 234
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
208-453 1.29e-31

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: 124.00  E-value: 1.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18003      1 LREYQHIGLDWL----ATLYEKNLNG-ILADEMGLGKTIQTIALLAHLACEKGNWG-----PHLIVVPTSVMLNWEMEFK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWL-GKDAITPFAvdgkaSKTELISQMKQWAiasgrsivRP----VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNK 362
Cdd:cd18003     71 RWCpGFKILTYYG-----SAKERKLKRQGWM--------KPnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNF 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  363 ESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPIlrgrdAAGTEEDLKKGDERLAEL 442
Cdd:cd18003    138 KSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL-----TAMSEGSQEENEELVRRL 212
                          250
                   ....*....|.
gi 1399623113  443 SSIVNKFIIRR 453
Cdd:cd18003    213 HKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
208-453 2.64e-28

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: 114.38  E-value: 2.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTgmvdkNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd17993      2 LRDYQLTGLNWLAHSWC-----KGNNGILADEMGLGKTVQTISFLSYLFHSQQQYG-----PFLVVVPLSTMPAWQREFA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLgkDAITPFAVDGKASKTELISQMkQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd17993     72 KWA--PDMNVIVYLGDIKSRDTIREY-EFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLY 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFrkrfelpilrgrdaagtEEDLKKGDER-LAELSSIV 446
Cdd:cd17993    149 EALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-----------------EEEHDEEQEKgIADLHKEL 211

                   ....*..
gi 1399623113  447 NKFIIRR 453
Cdd:cd17993    212 EPFILRR 218
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
208-462 1.09e-26

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: 110.15  E-value: 1.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd17996      4 LKEYQLKGLQWM----VSLYNNNLNG-ILADEMGLGKTIQTISLITYLMEKKKNNG-----PYLVIVPLSTLSNWVSEFE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKdaITPFAVDG-KASKTELISQMkqwaiasgRSIVRPVLIISYEtlrlYVdtLRDSPI------GLLLCDEGHRLK 360
Cdd:cd17996     74 KWAPS--VSKIVYKGtPDVRKKLQSQI--------RAGKFNVLLTTYE----YI--IKDKPLlskikwKYMIIDEGHRMK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  361 NKES-LTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPIlrgrdaAGTEEdlkKGDERL 439
Cdd:cd17996    138 NAQSkLTQTLNTYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPF------ANTGE---QVKIEL 208
                          250       260
                   ....*....|....*....|...
gi 1399623113  440 AELSSIVnkfIIRRTNDILSKYL 462
Cdd:cd17996    209 NEEETLL---IIRRLHKVLRPFL 228
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
208-453 1.77e-26

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: 109.37  E-value: 1.77e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYrcttgMVDKNANGCIMADGMGLGKTLQCIslmwTLLKQSPEAGVTTiqKCIIACPSSLVGNWANELV 287
Cdd:cd18060      1 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSI----AFLQEVYNVGIHG--PFLVIAPLSTITNWEREFN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITpfaVDGKASKTELISQMKQWAIAS-GRSIVRP----VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNK 362
Cdd:cd18060     70 TWTEMNTIV---YHGSLASRQMIQQYEMYCKDSrGRLIPGAykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  363 ESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFelpilrgrdaagteEDLKKgDERLAEL 442
Cdd:cd18060    147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF--------------GDLKT-EEQVQKL 211
                          250
                   ....*....|.
gi 1399623113  443 SSIVNKFIIRR 453
Cdd:cd18060    212 QAILKPMMLRR 222
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
208-453 4.03e-26

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: 108.36  E-value: 4.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCttgmVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18002      1 LKEYQLKGLNWLANL----YEQGING-ILADEMGLGKTVQSIAVLAHLAEEHNIWG-----PFLVIAPASTLHNWQQEIS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAvdGKASKTELISQMKQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18002     71 RFVPQFKVLPYW--GNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRW 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPIlRGRDAAGTEEDlkkgDERLAELSSIVN 447
Cdd:cd18002    149 KTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDI-ESHAENKTGLN----EHQLKRLHMILK 223

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18002    224 PFMLRR 229
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
208-454 1.95e-25

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: 106.25  E-value: 1.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMwTLLKQ-----SPEagvttiqkcIIACPSSLVGNW 282
Cdd:cd17997      4 MRDYQIRGLNWL----ISLFENGING-ILADEMGLGKTLQTISLL-GYLKHykninGPH---------LIIVPKSTLDNW 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  283 ANELVKWLGKdaitPFAVDGKASKTElisqmkQWAIASGRSIVRP--VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLK 360
Cdd:cd17997     69 MREFKRWCPS----LRVVVLIGDKEE------RADIIRDVLLPGKfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  361 NKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFElpilrgrdaagTEEDLKKGDERLA 440
Cdd:cd17997    139 NEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN-----------VNNCDDDNQEVVQ 207
                          250
                   ....*....|....
gi 1399623113  441 ELSSIVNKFIIRRT 454
Cdd:cd17997    208 RLHKVLRPFLLRRI 221
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
208-453 2.33e-25

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: 105.75  E-value: 2.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRcttgmvdknANG-CIMADGMGLGKTLQCISLM------WTLLkqspeagvttiqkciIACPSSLVG 280
Cdd:cd18010      1 LLPFQREGVCFALR---------RGGrVLIADEMGLGKTVQAIAIAayyreeWPLL---------------IVCPSSLRL 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  281 NWANELVKWLGKDAITPFAVdgkasktelisqmkqwaIASGRSIVRP----VLIISYETLRLYVDTLRDSPIGLLLCDEG 356
Cdd:cd18010     57 TWADEIERWLPSLPPDDIQV-----------------IVKSKDGLRDgdakVVIVSYDLLRRLEKQLLARKFKVVICDES 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  357 HRLKNKES-LTWTALNGLNVQRRVI-LSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPIL--RGRDAagteedl 432
Cdd:cd18010    120 HYLKNSKAkRTKAALPLLKRAKRVIlLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQggFGWDY------- 192
                          250       260
                   ....*....|....*....|..
gi 1399623113  433 kKGDERLAELSSIVNK-FIIRR 453
Cdd:cd18010    193 -SGSSNLEELHLLLLAtIMIRR 213
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
208-405 6.37e-25

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: 103.94  E-value: 6.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTtgmvDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGVTtiqkcIIACPSSLVGNWANELV 287
Cdd:cd18000      1 LFKYQQTGVQWLWELH----CQRVGG-ILGDEMGLGKTIQIIAFLAALHHSKLGLGPS-----LIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGKASKTELISQMKQWAIASGRSIVRP--VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESL 365
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVVGDggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1399623113  366 TWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLL 405
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
554-669 1.76e-23

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: 96.90  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  554 GKMMVLDRMLARIRqdtNDKIVLISNYTQTLDLfEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNpngEEFVFLLSSKA 633
Cdd:pfam00271    1 EKLEALLELLKKER---GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRK---GKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1399623113  634 GGCGLNLIGANRLVLFDPDWNPAADQQALARVWRDG 669
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
208-416 2.09e-23

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: 99.44  E-value: 2.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKnangcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDT-----ILADEMGLGKTIQTIVFLYSLYKEGHSKG-----PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGkasktelisqmkqwaiasgrsivrpVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd17994     71 MWAPDFYVVTYVGDH-------------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFF 125
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFE 416
Cdd:cd17994    126 RILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA 174
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
208-453 8.32e-22

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: 96.23  E-value: 8.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYR--CTTgmvdknaNGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANE 285
Cdd:cd18054     21 LRDYQLEGLNWLAHswCKN-------NSVILADEMGLGKTIQTISFLSYLFHQHQLYG-----PFLLVVPLSTLTSWQRE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  286 LVKWLGKDAITPFAVDGKASKTelISQMkQWAIASGRSIVRPVLIISYETLrlyvdtLRDSPI------GLLLCDEGHRL 359
Cdd:cd18054     89 FEIWAPEINVVVYIGDLMSRNT--IREY-EWIHSQTKRLKFNALITTYEIL------LKDKTVlgsinwAFLGVDEAHRL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  360 KNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFrkrfelpilrgrdaagtEEDLKKG-DER 438
Cdd:cd18054    160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF-----------------EEDHGKGrENG 222
                          250
                   ....*....|....*
gi 1399623113  439 LAELSSIVNKFIIRR 453
Cdd:cd18054    223 YQSLHKVLEPFLLRR 237
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
208-453 8.51e-22

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: 95.84  E-value: 8.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYrcttgMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVttiqkcIIACPSSLVGNWANELV 287
Cdd:cd18061      1 LREYQLEGLNWLL-----FNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPF------LIIAPLSTIANWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITpfaVDGKASKTELISQMKQWAIASGRSIVR-----PVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNK 362
Cdd:cd18061     70 TWTDLNVVV---YHGSLISRQMIQQYEMYFRDSQGRIIRgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNK 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  363 ESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFelpilrgrdaagteEDLKKgDERLAEL 442
Cdd:cd18061    147 NCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF--------------GDLKT-EEQVQKL 211
                          250
                   ....*....|.
gi 1399623113  443 SSIVNKFIIRR 453
Cdd:cd18061    212 QAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
208-411 9.30e-22

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: 95.90  E-value: 9.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKnangcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDT-----ILADEMGLGKTVQTAVFLYSLYKEGHSKG-----PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFA--VDGKASKTELISQMKQWAIASGRSIVR---------PVLIISYETLRLYVDTLRDSPIGLLLCDEG 356
Cdd:cd18056     71 MWAPDMYVVTYVgdKDSRAIIRENEFSFEDNAIRGGKKASRmkkeasvkfHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1399623113  357 HRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANP----NLLGSQNEF 411
Cdd:cd18056    151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPerfhNLEGFLEEF 209
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
208-453 9.83e-22

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: 95.48  E-value: 9.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYrcttgMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVTTIqkciiaCPSSLVGNWANELV 287
Cdd:cd18059      1 LREYQLEGVNWLL-----FNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVI------APLSTIPNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAvdGKASKTELISQMKQWAIASGRSIVRP----VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKE 363
Cdd:cd18059     70 TWTELNVVVYHG--SQASRRTIQLYEMYFKDPQGRVIKGSykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  364 SLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFelpilrgrdaagteEDLKKgDERLAELS 443
Cdd:cd18059    148 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF--------------GDLKT-EEQVQKLQ 212
                          250
                   ....*....|
gi 1399623113  444 SIVNKFIIRR 453
Cdd:cd18059    213 AILKPMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
200-399 1.18e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 94.87  E-value: 1.18e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   200 IDPRLAKVLRPHQVEGVKFLYrcttgmvdKNANGCIMADGMGLGKTLQ-CISLMWTLLKQSPeagvttiQKCIIACP-SS 277
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALL--------SGLRDVILAAPTGSGKTLAaLLPALEALKRGKG-------GRVLVLVPtRE 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   278 LVGNWANELVKWLGKDAITPFAVDGKASKTELISQMKqwaiasgrSIVRPVLIISYETLR--LYVDTLRDSPIGLLLCDE 355
Cdd:smart00487   66 LAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLE--------SGKTDILVTTPGRLLdlLENDKLSLSNVDLVILDE 137
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 1399623113   356 GHRLKN---KESLTWTALNGLNVQRRVILSGTP---IQNDLSEYFALLHF 399
Cdd:smart00487  138 AHRLLDggfGDQLEKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVF 187
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
208-411 1.44e-21

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: 95.52  E-value: 1.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKnangcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDT-----ILADEMGLGKTVQTIVFLYSLYKEGHSKG-----PYLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGKASKT--ELISQMKQWAIASGRSIVR---------PVLIISYETLRLYVDTLRDSPIGLLLCDEG 356
Cdd:cd18057     71 MWAPDFYVVTYTGDKESRSVirENEFSFEDNAIRSGKKVFRmkkeaqikfHVLLTSYELITIDQAILGSIEWACLVVDEA 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1399623113  357 HRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANP----NLLGSQNEF 411
Cdd:cd18057    151 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPerfnNLEGFLEEF 209
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
208-453 6.12e-21

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: 93.18  E-value: 6.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYrcttgMVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGVttiqkcIIACPSSLVGNWANELV 287
Cdd:cd18058      1 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPF------LIIAPLSTITNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITpfaVDGKASKTELISQMK------QWAIASGRSIVRpVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKN 361
Cdd:cd18058     70 TWTEMNAIV---YHGSQISRQMIQQYEmyyrdeQGNPLSGIFKFQ-VVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  362 KESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFelpilrgrdaagteEDLKKgDERLAE 441
Cdd:cd18058    146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF--------------GDLKT-EEQVKK 210
                          250
                   ....*....|..
gi 1399623113  442 LSSIVNKFIIRR 453
Cdd:cd18058    211 LQSILKPMMLRR 222
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
208-403 2.01e-20

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: 90.91  E-value: 2.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrcttGMVDKNANGCIMADGMGLGKTLQCISLMwTLLKQSPEAGVTtiqkcIIACPSSLVGNWANELV 287
Cdd:cd17998      1 LKDYQLIGLNWL-----NLLYQKKLSGILADEMGLGKTIQVIAFL-AYLKEIGIPGPH-----LVVVPSSTLDNWLREFK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPF---AVDGKASKTELISQMKQWAI-------ASGRSIVRPVLiisyetlrlyvdtlRDSPIGLLLCDEGH 357
Cdd:cd17998     70 RWCPSLKVEPYygsQEERKHLRYDILKGLEDFDVivttynlATSNPDDRSFF--------------KRLKLNYVVYDEGH 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1399623113  358 RLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPN 403
Cdd:cd17998    136 MLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPK 181
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
208-415 3.11e-20

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: 91.61  E-value: 3.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTGMVDKnangcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDT-----ILADEMGLGKTIQTIVFLYSLYKEGHTKG-----PFLVSAPLSTIINWEREFQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFA--VDGKASKTELISQMKQWAIASGRSIVR---------PVLIISYETLRLYVDTLRDSPIGLLLCDEG 356
Cdd:cd18055     71 MWAPDFYVVTYTgdKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1399623113  357 HRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRF 415
Cdd:cd18055    151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
207-453 8.50e-20

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: 90.87  E-value: 8.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  207 VLRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANEL 286
Cdd:cd18062     23 VLKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRING-----PFLIIVPLSTLSNWVYEF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  287 VKWlgKDAITPFAVDGK-ASKTELISQMKqwaiaSGRSivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESL 365
Cdd:cd18062     93 DKW--APSVVKVSYKGSpAARRAFVPQLR-----SGKF---NVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  366 TWTALNGLNVQ-RRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILrgrdAAGTEEDLKKGDERLA--EL 442
Cdd:cd18062    163 LTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFA----MTGEKVDLNEEETILIirRL 238
                          250
                   ....*....|.
gi 1399623113  443 SSIVNKFIIRR 453
Cdd:cd18062    239 HKVLRPFLLRR 249
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
208-453 8.88e-20

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: 90.89  E-value: 8.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18063     24 LKHYQLQGLEWM----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNG-----PYLIIVPLSTLSNWTYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWlgKDAITPFAVDGK-ASKTELISQMKqwaiaSGRSivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLT 366
Cdd:cd18063     94 KW--APSVVKISYKGTpAMRRSLVPQLR-----SGKF---NVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  367 WTALNGLNVQ-RRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILrgrdAAGTEEDLKKGDERLA--ELS 443
Cdd:cd18063    164 TQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFA----MTGERVDLNEEETILIirRLH 239
                          250
                   ....*....|
gi 1399623113  444 SIVNKFIIRR 453
Cdd:cd18063    240 KVLRPFLLRR 249
HELICc smart00490
helicase superfamily c-terminal domain;
585-669 1.75e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 1.75e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113   585 DLFEKLCRTRGYGSLRLDGTMTVGKRQKLVDKFNNPngeEFVFLLSSKAGGCGLNLIGANRLVLFDPDWNPAADQQALAR 664
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1399623113   665 VWRDG 669
Cdd:smart00490   78 AGRAG 82
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
208-465 2.63e-19

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: 89.34  E-value: 2.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18064     16 LRDYQVRGLNWL----ISLYENGING-ILADEMGLGKTLQTISLLGYMKHYRNIPG-----PHMVLVPKSTLHNWMAEFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKdaitpfavdgkASKTELISQMKQWAiASGRSIVRP----VLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKE 363
Cdd:cd18064     86 RWVPT-----------LRAVCLIGDKDQRA-AFVRDVLLPgewdVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  364 SLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFElpilrgrdaagTEEDLkkGDERLAE-L 442
Cdd:cd18064    154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD-----------TNNCL--GDQKLVErL 220
                          250       260
                   ....*....|....*....|...
gi 1399623113  443 SSIVNKFIIRRTNDILSKYLPVK 465
Cdd:cd18064    221 HMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
230-453 3.56e-19

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: 88.68  E-value: 3.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  230 NANGCIMADGMGLGKTLQCISLMWTllkqspeagvttiQKCIIACPSSLVGNWANELVKWLGKDAITPFAVDGKASKTEL 309
Cdd:cd18071     47 LVRGGILADDMGLGKTLTTISLILA-------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  310 ISQMKQwaiasgrsivrPVLIISYETLRLYVDTLRDSPIGLL-----LCDEGHRLKNKESLTWTALNGLNVQRRVILSGT 384
Cdd:cd18071    114 KLLSKY-----------DIVLTTYNTLASDFGAKGDSPLHTInwlrvVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGT 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1399623113  385 PIQNDLSEYFALLHFANPNLLGSQNEFRKRFELPILRGRDAAgteedlkkgderLAELSSIVNKFIIRR 453
Cdd:cd18071    183 PIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTG------------LKRLQVLMKQITLRR 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
208-412 4.91e-19

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: 87.34  E-value: 4.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrcttgmVDKNANGCIMADGMGLGKTLQCISLMWTLLKQSPeagvttIQKCIIACPSSLVGNWANELv 287
Cdd:cd18011      1 PLPHQIDAVLRA-------LRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGD------AKRVLILCPASLVEQWQDEL- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 kwLGKDAITPFAVDGKASKTELISQMKQWAiasgrsiVRPVLIISYETLR---LYVDTLRDSPIGLLLCDEGHRLKNKES 364
Cdd:cd18011     67 --QDKFGLPFLILDRETAAQLRRLIGNPFE-------EFPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGG 137
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1399623113  365 LTWTALNGL------NVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFR 412
Cdd:cd18011    138 GKETKRYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
208-453 7.61e-19

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: 87.38  E-value: 7.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLyrctTGMVDKNANGcIMADGMGLGKTLQCISLMWTLLKQSPEAGVTtiqkcIIACPSSLVGNWANELV 287
Cdd:cd18065     16 LRDYQVRGLNWM----ISLYENGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPH-----MVLVPKSTLHNWMNEFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGKASKTELISQMK--QWaiasgrsivrPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESL 365
Cdd:cd18065     86 RWVPSLRAVCLIGDKDARAAFIRDVMMpgEW----------DVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  366 TWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRKRFElpilrgrdaagTEEDLkkGDERLAE-LSS 444
Cdd:cd18065    156 LSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCL--GDQKLVErLHA 222

                   ....*....
gi 1399623113  445 IVNKFIIRR 453
Cdd:cd18065    223 VLKPFLLRR 231
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
208-453 5.84e-18

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: 85.10  E-value: 5.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCTTgmvdkNANGCIMADGMGLGKTLQCISLMWTLLKQSPEAGvttiqKCIIACPSSLVGNWANELV 287
Cdd:cd18053     21 LRDYQLNGLNWLAHSWC-----KGNSCILADEMGLGKTIQTISFLNYLFHEHQLYG-----PFLLVVPLSTLTSWQREIQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAvdGKASKTELIsQMKQWAIASGRSIVRPVLIISYETLRLYVDTLRDSPIGLLLCDEGHRLKNKESLTW 367
Cdd:cd18053     91 TWAPQMNAVVYL--GDINSRNMI-RTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLY 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  368 TALNGLNVQRRVILSGTPIQNDLSEYFALLHFANPNLLGSQNEFRkrfelpilrgrdaagtEEDLKKGDERLAELSSIVN 447
Cdd:cd18053    168 KTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFE----------------EEHGKGREYGYASLHKELE 231

                   ....*.
gi 1399623113  448 KFIIRR 453
Cdd:cd18053    232 PFLLRR 237
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
208-401 7.16e-16

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: 79.06  E-value: 7.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVK-FLYRcttgmVDKNANGCIMADGMGLGKTLQCISL-----------------MWTLLKQSPEAGVTTIQK 269
Cdd:cd18072      1 LLLHQKQALAwLLWR-----ERQKPRGGILADDMGLGKTLTMIALilaqkntqnrkeeekekALTEWESKKDSTLVPSAG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  270 CIIACPSSLVGNWANELVKWLGKDAITPFAVDGkASKTELISQMKQWAIasgrsIVRPVLIISYEtLRLYVDTLRDSPIG 349
Cdd:cd18072     76 TLVVCPASLVHQWKNEVESRVASNKLRVCLYHG-PNRERIGEVLRDYDI-----VITTYSLVAKE-IPTYKEESRSSPLF 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1399623113  350 L-----LLCDEGHRLKNKESLTWTALNGLNVQRRVILSGTPIQNDLSEYFALLHFAN 401
Cdd:cd18072    149 RiawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
208-395 8.54e-08

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: 54.66  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFlyrcttgmVDKNANGCIMADgMGLGKTLQCISLMWTLLKQSPEAGVTTIQKCIIACPSslvgnWANELV 287
Cdd:cd18013      1 PHPYQKVAINF--------IIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARST-----WPDEVE 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  288 KWLGKDAITPFAVDGkaSKTELISqmkqwAIASGRSIvrpvLIISYETLRLYVDTLRDS-PIGLLLCDEGHRLKNKESLT 366
Cdd:cd18013     67 KWNHLRNLTVSVAVG--TERQRSK-----AANTPADL----YVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSKR 135
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1399623113  367 WTALNGLN--VQRRVILSGTPIQNDLSEYFA 395
Cdd:cd18013    136 FKALRKVRpvIKRLIGLTGTPSPNGLMDLWA 166
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
208-473 2.50e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.42  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFLYRCttgMVDKNANGCIMADgMGLGKTLqcisLMWTLLKQspeagVTTIQKCIIACPS-SLVGNWANEL 286
Cdd:COG1061     81 LRPYQQEALEALLAA---LERGGGRGLVVAP-TGTGKTV----LALALAAE-----LLRGKRVLVLVPRrELLEQWAEEL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  287 VKWLGKdaitPFAVDGKasktelisqmkqwaiasgRSIVRPVLIISYETL--RLYVDTLRDSpIGLLLCDEGHRLknkES 364
Cdd:COG1061    148 RRFLGD----PLAGGGK------------------KDSDAPITVATYQSLarRAHLDELGDR-FGLVIIDEAHHA---GA 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  365 LTWTA-LNGLNVQRRVILSGTPIQND-LSEYFALLhfanpnllgsqneFRKRFELPIlrgRDAA-----------GTEED 431
Cdd:COG1061    202 PSYRRiLEAFPAAYRLGLTATPFRSDgREILLFLF-------------DGIVYEYSL---KEAIedgylappeyyGIRVD 265
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1399623113  432 LKKGDERLAELSSIVNKFII---RRTNDILSKYLP--VKYEHV-VFCN 473
Cdd:COG1061    266 LTDERAEYDALSERLREALAadaERKDKILRELLRehPDDRKTlVFCS 313
ResIII pfam04851
Type III restriction enzyme, res subunit;
206-386 2.00e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 49.59  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  206 KVLRPHQVEGVKflyRCTTGMVDKNANGCI-MADGMGlgKTLQCISLMWTLLKQSPeagvttIQKCIIACPSslvgnwaN 284
Cdd:pfam04851    2 LELRPYQIEAIE---NLLESIKNGQKRGLIvMATGSG--KTLTAAKLIARLFKKGP------IKKVLFLVPR-------K 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  285 ELVKWLgKDAITPFAvDGKASKTELISQMKQWAIASGRSIVrpvlIISYETL--RLYVDTLRDSP--IGLLLCDEGHRLK 360
Cdd:pfam04851   64 DLLEQA-LEEFKKFL-PNYVEIGEIISGDKKDESVDDNKIV----VTTIQSLykALELASLELLPdfFDVIIIDEAHRSG 137
                          170       180
                   ....*....|....*....|....*..
gi 1399623113  361 nkeSLTWTA-LNGLNVQRRVILSGTPI 386
Cdd:pfam04851  138 ---ASSYRNiLEYFKPAFLLGLTATPE 161
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
208-399 1.03e-05

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: 48.88  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  208 LRPHQVEGVKFlyrcttgMVdknANGCIMADGMGLGKTLQCISLM----------------WTLLKQSPEAGVT-TIQKC 270
Cdd:cd18070      1 LLPYQRRAVNW-------ML---VPGGILADEMGLGKTVEVLALIllhprpdndldaadddSDEMVCCPDCLVAeTPVSS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  271 ---IIACPSSLVGNWANEL-------VKWLGKDAITPFAVDGKASKTELISQmkqwaiasgrSIVrpvlIISYETLR--L 338
Cdd:cd18070     71 katLIVCPSAILAQWLDEInrhvpssLKVLTYQGVKKDGALASPAPEILAEY----------DIV----VTTYDVLRteL 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399623113  339 YVDTLRDSPiglllcDEGHRLKNKESLTwTALngLNVQ-RRVIL----------------------------SGTPIQND 389
Cdd:cd18070    137 HYAEANRSN------RRRRRQKRYEAPP-SPL--VLVEwWRVCLdeaqmvesstskaaemarrlprvnrwcvSGTPIQRG 207
                          250
                   ....*....|
gi 1399623113  390 LSEYFALLHF 399
Cdd:cd18070    208 LDDLFGLLSF 217
HEAT pfam02985
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
883-913 2.59e-03

HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514).


Pssm-ID: 460773  Cd Length: 31  Bit Score: 36.74  E-value: 2.59e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1399623113  883 IVPPVLACFSDQDARVRYYACESMYNIAKVA 913
Cdd:pfam02985    1 LLPLLLKLLNDPSPEVREAAAEALGELAEVL 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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