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Conserved domains on  [gi|145362201|ref|NP_973689|]
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SNF2 domain-containing protein / helicase domain-containing protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase; macro domain-containing protein( domain architecture ID 13327344)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA| macro domain-containing protein may bind compounds such as O-acetyl-ADP-ribose, mono- and poly-ADP-ribose, and catalyze reactions such as O-acetyl-ADP-ribose deacetylation and reversal of ADP-ribosylation of mono-ADP-ribosylated substrates; similar to viral non-structural protein 3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
46-537 7.07e-135

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 418.09  E-value: 7.07e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  46 GVTATLKPHQVEGVSWLIQKYLLGVNVVLeLDQMGLGKTLQAISFLSYLKFRqGLPGPFLVLCPLSVTDGWVSEINRFTP 125
Cdd:COG0553  237 GLKATLRPYQLEGAAWLLFLRRLGLGGLL-ADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 126 NLEVLRYVGDKycrldmrksmydhVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNvL 205
Cdd:COG0553  315 GLRVLVLDGTR-------------ERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAK-A 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketgdglSGLDVSNDKETYKSLKFILGAFMLRRT 285
Cdd:COG0553  381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF-------ARPIEKGDEEALERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 286 KSLLIESgnlvLPPLTELTVMVPLVSLQKKIYTSILRKELpGLLELSSGGSNHTSLQNIVIQLRKACSHPYLFPgiepep 365
Cdd:COG0553  454 KEDVLKD----LPEKTEETLYVELTPEQRALYEAVLEYLR-RELEGAEGIRRRGLILAALTRLRQICSHPALLL------ 522
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 366 fEEGEHLVQASGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAIKNFSakter 445
Cdd:COG0553  523 -EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ----- 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 446 gldsevDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLVTEHSVEEVILRRA 525
Cdd:COG0553  597 ------EGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
                        490
                 ....*....|..
gi 145362201 526 ERKLQLSHNVVG 537
Cdd:COG0553  671 EEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
705-864 2.82e-75

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


:

Pssm-ID: 394880  Cd Length: 152  Bit Score: 242.16  E-value: 2.82e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 705 SVNFVFGDCTNPSTVSHEPAIIFSCVDDSGNWGRGGMFDALSKLSNTVPTAYHRASEFKDLHLGDLHLIKIDDNDDQQNt 784
Cdd:cd03331    1 DINYVSGDVTHPQTTSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 785 qasKPLWVAVAVTQSYNsrRKVPRSSISIPDLESCLAKASFSASQKSASLHMPRIGYQDGSDrsQWYTVERLLRKYSSIF 864
Cdd:cd03331   80 ---GRDYVALIVAQHRD--RSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGF--NWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
46-537 7.07e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 418.09  E-value: 7.07e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  46 GVTATLKPHQVEGVSWLIQKYLLGVNVVLeLDQMGLGKTLQAISFLSYLKFRqGLPGPFLVLCPLSVTDGWVSEINRFTP 125
Cdd:COG0553  237 GLKATLRPYQLEGAAWLLFLRRLGLGGLL-ADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 126 NLEVLRYVGDKycrldmrksmydhVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNvL 205
Cdd:COG0553  315 GLRVLVLDGTR-------------ERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAK-A 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketgdglSGLDVSNDKETYKSLKFILGAFMLRRT 285
Cdd:COG0553  381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF-------ARPIEKGDEEALERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 286 KSLLIESgnlvLPPLTELTVMVPLVSLQKKIYTSILRKELpGLLELSSGGSNHTSLQNIVIQLRKACSHPYLFPgiepep 365
Cdd:COG0553  454 KEDVLKD----LPEKTEETLYVELTPEQRALYEAVLEYLR-RELEGAEGIRRRGLILAALTRLRQICSHPALLL------ 522
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 366 fEEGEHLVQASGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAIKNFSakter 445
Cdd:COG0553  523 -EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ----- 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 446 gldsevDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLVTEHSVEEVILRRA 525
Cdd:COG0553  597 ------EGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
                        490
                 ....*....|..
gi 145362201 526 ERKLQLSHNVVG 537
Cdd:COG0553  671 EEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
38-584 1.38e-133

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 424.98  E-value: 1.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   38 TPPDCsefgVTATLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWV 117
Cdd:PLN03142  161 VQPSC----IKGKMRDYQLAGLNWLIRLYENGINGILA-DEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWM 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  118 SEINRFTPNLEVLRYVGDKycrlDMRKSMYDHVKKSSKghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNP 197
Cdd:PLN03142  236 NEIRRFCPVLRAVKFHGNP----EERAHQREELLVAGK-----FDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  198 NSVLYNVLlEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGlsgldvsNDKETYKSLKFIL 277
Cdd:PLN03142  307 NSLLSKTM-RLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEN-------DQQEVVQQLHKVL 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  278 GAFMLRRTKSLlIESGnlvLPPLTELTVMVPLVSLQKKIYTSILRKELpgllELSSGGSNHTSLQNIVIQLRKACSHPYL 357
Cdd:PLN03142  379 RPFLLRRLKSD-VEKG---LPPKKETILKVGMSQMQKQYYKALLQKDL----DVVNAGGERKRLLNIAMQLRKCCNHPYL 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  358 FPGIEP-EPFEEGEHLVQASGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAI 436
Cdd:PLN03142  451 FQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASI 530
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  437 KNFSAktergldsevDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLVTEHS 516
Cdd:PLN03142  531 DAFNK----------PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYT 600
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  517 VEEVILRRAERKLQLSHNVV--GDNMEEKEEDGGDLRSLVfglqRFDPEEIHNEESDNLKMVEISSLAEK 584
Cdd:PLN03142  601 IEEKVIERAYKKLALDALVIqqGRLAEQKTVNKDELLQMV----RYGAEMVFSSKDSTITDEDIDRIIAK 666
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
51-284 6.94e-116

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: 351.74  E-value: 6.94e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLlGVNVVLELDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18006    1 LRPYQLEGVNWLLQCRA-EQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKSMYDhvkksskghFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEQFL 210
Cdd:cd18006   80 TYMGDKEKRLDLQQDIKS---------TNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362201 211 iPRRLLITGTPIQNNLTELWALMHFCMPLVFG--TLDQFLSAFKETGDGLsgldvsndkETYKSLKFILGAFMLRR 284
Cdd:cd18006  151 -DFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYSETDDES---------ETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
705-864 2.82e-75

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 242.16  E-value: 2.82e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 705 SVNFVFGDCTNPSTVSHEPAIIFSCVDDSGNWGRGGMFDALSKLSNTVPTAYHRASEFKDLHLGDLHLIKIDDNDDQQNt 784
Cdd:cd03331    1 DINYVSGDVTHPQTTSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 785 qasKPLWVAVAVTQSYNsrRKVPRSSISIPDLESCLAKASFSASQKSASLHMPRIGYQDGSDrsQWYTVERLLRKYSSIF 864
Cdd:cd03331   80 ---GRDYVALIVAQHRD--RSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGF--NWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
54-358 1.00e-69

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: 232.57  E-value: 1.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   54 HQVEGVSWLIQKY-LLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPG-PFLVLCPLSVTDGWVSEINRFT--PNLEV 129
Cdd:pfam00176   1 YQIEGVNWMLSLEnNLGRGGILA-DEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  130 LRYVGDKycrldmrksMYDHVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqF 209
Cdd:pfam00176  80 VVLHGNK---------RPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS-L 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketgdgLSGLDVSNDKETYKSLKFILGAFMLRRTKSLL 289
Cdd:pfam00176 150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWF------DRPIERGGGKKGVSRLHKLLKPFLLRRTKKDV 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  290 ieSGNlvLPPLTELTVMVPLVSLQKKIYTSILRKELPGLLELSSGGS-NHTSLQNIVIQLRKACSHPYLF 358
Cdd:pfam00176 224 --EKS--LPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGReIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
50-238 7.02e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.18  E-value: 7.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201    50 TLKPHQVEGVSWLIQkyllGVNVVLELDQMGLGKTLQAISFLSYlKFRQGLPGPFLVLCPL-SVTDGWVSEINRFTPNL- 127
Cdd:smart00487   8 PLRPYQKEAIEALLS----GLRDVILAAPTGSGKTLAALLPALE-ALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   128 --EVLRYVGDkycrldmrkSMYDHVKKSSKGhflPFDVLLTTYDIAL--VDQDFLSQIPWQYAIIDEAQRLKNPN--SVL 201
Cdd:smart00487  83 lkVVGLYGGD---------SKREQLRKLESG---KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGfgDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 145362201   202 YNVLLEQFLIPRRLLITGTP---IQNNLTELWALMHFCMP 238
Cdd:smart00487 151 EKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
46-537 7.07e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 418.09  E-value: 7.07e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  46 GVTATLKPHQVEGVSWLIQKYLLGVNVVLeLDQMGLGKTLQAISFLSYLKFRqGLPGPFLVLCPLSVTDGWVSEINRFTP 125
Cdd:COG0553  237 GLKATLRPYQLEGAAWLLFLRRLGLGGLL-ADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 126 NLEVLRYVGDKycrldmrksmydhVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNvL 205
Cdd:COG0553  315 GLRVLVLDGTR-------------ERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAK-A 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketgdglSGLDVSNDKETYKSLKFILGAFMLRRT 285
Cdd:COG0553  381 VRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERF-------ARPIEKGDEEALERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 286 KSLLIESgnlvLPPLTELTVMVPLVSLQKKIYTSILRKELpGLLELSSGGSNHTSLQNIVIQLRKACSHPYLFPgiepep 365
Cdd:COG0553  454 KEDVLKD----LPEKTEETLYVELTPEQRALYEAVLEYLR-RELEGAEGIRRRGLILAALTRLRQICSHPALLL------ 522
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 366 fEEGEHLVQASGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAIKNFSakter 445
Cdd:COG0553  523 -EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQ----- 596
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 446 gldsevDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLVTEHSVEEVILRRA 525
Cdd:COG0553  597 ------EGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELL 670
                        490
                 ....*....|..
gi 145362201 526 ERKLQLSHNVVG 537
Cdd:COG0553  671 EEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
38-584 1.38e-133

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 424.98  E-value: 1.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   38 TPPDCsefgVTATLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWV 117
Cdd:PLN03142  161 VQPSC----IKGKMRDYQLAGLNWLIRLYENGINGILA-DEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWM 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  118 SEINRFTPNLEVLRYVGDKycrlDMRKSMYDHVKKSSKghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNP 197
Cdd:PLN03142  236 NEIRRFCPVLRAVKFHGNP----EERAHQREELLVAGK-----FDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  198 NSVLYNVLlEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGlsgldvsNDKETYKSLKFIL 277
Cdd:PLN03142  307 NSLLSKTM-RLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGEN-------DQQEVVQQLHKVL 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  278 GAFMLRRTKSLlIESGnlvLPPLTELTVMVPLVSLQKKIYTSILRKELpgllELSSGGSNHTSLQNIVIQLRKACSHPYL 357
Cdd:PLN03142  379 RPFLLRRLKSD-VEKG---LPPKKETILKVGMSQMQKQYYKALLQKDL----DVVNAGGERKRLLNIAMQLRKCCNHPYL 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  358 FPGIEP-EPFEEGEHLVQASGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAI 436
Cdd:PLN03142  451 FQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASI 530
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  437 KNFSAktergldsevDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLVTEHS 516
Cdd:PLN03142  531 DAFNK----------PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYT 600
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  517 VEEVILRRAERKLQLSHNVV--GDNMEEKEEDGGDLRSLVfglqRFDPEEIHNEESDNLKMVEISSLAEK 584
Cdd:PLN03142  601 IEEKVIERAYKKLALDALVIqqGRLAEQKTVNKDELLQMV----RYGAEMVFSSKDSTITDEDIDRIIAK 666
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
51-284 6.94e-116

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: 351.74  E-value: 6.94e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLlGVNVVLELDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18006    1 LRPYQLEGVNWLLQCRA-EQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKSMYDhvkksskghFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEQFL 210
Cdd:cd18006   80 TYMGDKEKRLDLQQDIKS---------TNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362201 211 iPRRLLITGTPIQNNLTELWALMHFCMPLVFG--TLDQFLSAFKETGDGLsgldvsndkETYKSLKFILGAFMLRR 284
Cdd:cd18006  151 -DFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYSETDDES---------ETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
705-864 2.82e-75

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 242.16  E-value: 2.82e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 705 SVNFVFGDCTNPSTVSHEPAIIFSCVDDSGNWGRGGMFDALSKLSNTVPTAYHRASEFKDLHLGDLHLIKIDDNDDQQNt 784
Cdd:cd03331    1 DINYVSGDVTHPQTTSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 785 qasKPLWVAVAVTQSYNsrRKVPRSSISIPDLESCLAKASFSASQKSASLHMPRIGYQDGSDrsQWYTVERLLRKYSSIF 864
Cdd:cd03331   80 ---GRDYVALIVAQHRD--RSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGF--NWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
54-358 1.00e-69

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: 232.57  E-value: 1.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   54 HQVEGVSWLIQKY-LLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPG-PFLVLCPLSVTDGWVSEINRFT--PNLEV 129
Cdd:pfam00176   1 YQIEGVNWMLSLEnNLGRGGILA-DEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  130 LRYVGDKycrldmrksMYDHVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqF 209
Cdd:pfam00176  80 VVLHGNK---------RPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKS-L 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketgdgLSGLDVSNDKETYKSLKFILGAFMLRRTKSLL 289
Cdd:pfam00176 150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWF------DRPIERGGGKKGVSRLHKLLKPFLLRRTKKDV 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  290 ieSGNlvLPPLTELTVMVPLVSLQKKIYTSILRKELPGLLELSSGGS-NHTSLQNIVIQLRKACSHPYLF 358
Cdd:pfam00176 224 --EKS--LPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGReIKASLLNILMRLRKICNHPGLI 289
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
50-286 3.70e-69

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


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 228.81  E-value: 3.70e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  50 TLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRqGLPGPFLVLCPLSVTDGWVSEINRFTPNLEV 129
Cdd:cd18009    3 VMRPYQLEGMEWLRMLWENGINGILA-DEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 130 LRYVGDKYCRLDMRKSMYDHvkkssKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLlEQF 209
Cdd:cd18009   81 LLYHGTKEERERLRKKIMKR-----EGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQEL-KTF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAF-----KETGDGLSGLDVSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18009  155 NSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfsslSDNAADISNLSEEREQNIVHMLHAILKPFLLRR 234

                 ..
gi 145362201 285 TK 286
Cdd:cd18009  235 LK 236
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
51-241 1.55e-68

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: 225.14  E-value: 1.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLeLDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGIL-ADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsmydhvkkssKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlLEQFL 210
Cdd:cd17919   80 VYHGSQRERAQIRA----------KEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKA-LKALR 148
                        170       180       190
                 ....*....|....*....|....*....|.
gi 145362201 211 IPRRLLITGTPIQNNLTELWALMHFCMPLVF 241
Cdd:cd17919  149 AKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
50-284 3.75e-64

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: 214.53  E-value: 3.75e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  50 TLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEV 129
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILA-DEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 130 LRYVGDKYCRLDMRKSMYDHvkksSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqF 209
Cdd:cd17993   80 IVYLGDIKSRDTIREYEFYF----SQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-F 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362201 210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFlsaFKETGDGlsgldvsNDKEtYKSLKFILGAFMLRR 284
Cdd:cd17993  155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF---EEEHDEE-------QEKG-IADLHKELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
50-286 3.05e-62

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: 209.49  E-value: 3.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  50 TLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEV 129
Cdd:cd17997    3 TMRDYQIRGLNWLISLFENGINGILA-DEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 130 LRYVGDKycrlDMRKSMYDHVKKSSKghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlLEQF 209
Cdd:cd17997   82 VVLIGDK----EERADIIRDVLLPGK-----FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI-VRLF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFK-ETGDGlsgldvsNDKETYKSLKFILGAFMLRRTK 286
Cdd:cd17997  152 NSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNvNNCDD-------DNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
50-286 3.10e-58

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: 199.13  E-value: 3.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  50 TLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEV 129
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILA-DEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 130 LRYVGDKycrlDMRKSMYDHVKKSSkghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEQF 209
Cdd:cd17996   82 IVYKGTP----DVRKKLQSQIRAGK------FNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 210 LIPRRLLITGTPIQNNLTELWALMHFCMPLVF---GTLDQFLSA-FKETGDglSGLDVSNDKETY---KSLKFILGAFML 282
Cdd:cd17996  152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIFkscKTFEQWFNTpFANTGE--QVKIELNEEETLliiRRLHKVLRPFLL 229

                 ....
gi 145362201 283 RRTK 286
Cdd:cd17996  230 RRLK 233
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
51-284 5.50e-58

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: 197.86  E-value: 5.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTpNLEVL 130
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILA-DEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRlDMRK--SMYDHV--KKSSKGhFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLL 206
Cdd:cd17995   79 VYHGSGESR-QIIQqyEMYFKDaqGRKKKG-VYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 207 eQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketGDGLSGLDVSndketykSLKFILGAFMLRR 284
Cdd:cd17995  157 -KLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---GDLKTAEQVE-------KLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
51-284 1.29e-57

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: 197.34  E-value: 1.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILA-DEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsMYDhvKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLeQFL 210
Cdd:cd18002   80 PYWGNPKDRKVLRK-FWD--RKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLL-SFH 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362201 211 IPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGLSGLDVSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18002  156 CRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
49-286 1.87e-57

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: 196.25  E-value: 1.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  49 ATLKPHQVEGVSWLiqKYL--LGVNVVLElDQMGLGKTLQAISFLSYLKfRQGLPGPFLVLCPLSVTDGWVSEINRFTPN 126
Cdd:cd18012    3 ATLRPYQKEGFNWL--SFLrhYGLGGILA-DDMGLGKTLQTLALLLSRK-EEGRKGPSLVVAPTSLIYNWEEEAAKFAPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 127 LEVLRYVGDKycrldmrksmydhVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLL 206
Cdd:cd18012   79 LKVLVIHGTK-------------RKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 207 E---QFliprRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETgdglsgLDVSNDKETYKSLKFILGAFMLR 283
Cdd:cd18012  146 AlkaDH----RLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP------IEKDGDEEALEELKKLISPFILR 215

                 ...
gi 145362201 284 RTK 286
Cdd:cd18012  216 RLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
51-284 9.53e-56

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: 192.14  E-value: 9.53e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18054   21 LRDYQLEGLNWLAHSWCKNNSVILA-DEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsmYDHVKKSSKGhfLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqFL 210
Cdd:cd18054  100 VYIGDLMSRNTIRE--YEWIHSQTKR--LKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLID-FK 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362201 211 IPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLsafKETGDGlsgldvsnDKETYKSLKFILGAFMLRR 284
Cdd:cd18054  175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFE---EDHGKG--------RENGYQSLHKVLEPFLLRR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
370-512 1.01e-50

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: 174.20  E-value: 1.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 370 EHLVqaSGKLLVLDQLLKRLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAIKNFSakterglds 449
Cdd:cd18793    6 EEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFN--------- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145362201 450 evDGSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQISHVLSINLV 512
Cdd:cd18793   75 --EDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
51-284 2.64e-50

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: 176.39  E-value: 2.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILA-DEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRldmrksmydhvKKSSKGHFLP--FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEq 208
Cdd:cd18003   80 TYYGSAKER-----------KLKRQGWMKPnsFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362201 209 FLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGLSGLDVSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18003  148 FNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
51-241 8.95e-46

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: 162.55  E-value: 8.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKfRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILA-DEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDkycrLDMRKSMYDHVKKSSKGhflpFDVLLTTYDIAL---VDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLE 207
Cdd:cd17998   79 PYYGS----QEERKHLRYDILKGLED----FDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145362201 208 ---QFliprRLLITGTPIQNNLTELWALMHFCMPLVF 241
Cdd:cd17998  151 inaNF----RLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
49-286 1.80e-45

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


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 163.26  E-value: 1.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  49 ATLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLE 128
Cdd:cd18065   14 GTLRDYQVRGLNWMISLYENGVNGILA-DEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 129 VLRYVGDKycrlDMRKSMYDHVKKSSKghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEq 208
Cdd:cd18065   93 AVCLIGDK----DARAAFIRDVMMPGE-----WDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE- 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 209 FLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFkETGDGLSgldvsnDKETYKSLKFILGAFMLRRTK 286
Cdd:cd18065  163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF-DTKNCLG------DQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
51-299 1.93e-45

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


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 163.68  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18064   16 LRDYQVRGLNWLISLYENGINGILA-DEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKSMydhvkksskghFLP--FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEq 208
Cdd:cd18064   95 CLIGDKDQRAAFVRDV-----------LLPgeWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 209 FLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFkETGDGLSgldvsnDKETYKSLKFILGAFMLRRTKSL 288
Cdd:cd18064  163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-DTNNCLG------DQKLVERLHMVLRPFLLRRIKAD 235
                        250
                 ....*....|.
gi 145362201 289 LIESgnlvLPP 299
Cdd:cd18064  236 VEKS----LPP 242
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
51-284 4.43e-45

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 162.53  E-value: 4.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18053   21 LRDYQLNGLNWLAHSWCKGNSCILA-DEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKSMYDHVKKSSkghfLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqFL 210
Cdd:cd18053  100 VYLGDINSRNMIRTHEWMHPQTKR----LKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLID-FK 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362201 211 IPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLsafKETGDGlsgldvsnDKETYKSLKFILGAFMLRR 284
Cdd:cd18053  175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFE---EEHGKG--------REYGYASLHKELEPFLLRR 237
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
47-286 4.45e-45

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 162.92  E-value: 4.45e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  47 VTATLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPN 126
Cdd:cd18063   20 INGTLKHYQLQGLEWMVSLYNNNLNGILA-DEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 127 LEVLRYVGDKycrlDMRKSMYDHVKKSSkghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLL 206
Cdd:cd18063   99 VVKISYKGTP----AMRRSLVPQLRSGK------FNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 207 EQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVF---GTLDQFLSA-FKETGDGLSgldvSNDKET---YKSLKFILGA 279
Cdd:cd18063  169 THYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFkscSTFEQWFNApFAMTGERVD----LNEEETiliIRRLHKVLRP 244

                 ....*..
gi 145362201 280 FMLRRTK 286
Cdd:cd18063  245 FLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
43-286 3.76e-44

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 160.21  E-value: 3.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  43 SEFGVTATLKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINR 122
Cdd:cd18062   16 SSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILA-DEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 123 FTPNLEVLRYVGDKYCRldmrkSMYDHVKKSSKghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLY 202
Cdd:cd18062   95 WAPSVVKVSYKGSPAAR-----RAFVPQLRSGK-----FNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 203 NVLLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVF---GTLDQFLSA-FKETGDGLSgldvSNDKET---YKSLKF 275
Cdd:cd18062  165 QVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFkscSTFEQWFNApFAMTGEKVD----LNEEETiliIRRLHK 240
                        250
                 ....*....|.
gi 145362201 276 ILGAFMLRRTK 286
Cdd:cd18062  241 VLRPFLLRRLK 251
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
51-238 2.90e-41

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 149.78  E-value: 2.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNL--E 128
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILG-DEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 129 VLRYVGdKYCRLDMRKSMYDHVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLyNVLLEQ 208
Cdd:cd18000   80 VLHSSG-SGTGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI-TLACKQ 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 145362201 209 FLIPRRLLITGTPIQNNLTELWALMHFCMP 238
Cdd:cd18000  158 LRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
51-284 6.36e-41

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: 149.13  E-value: 6.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILA-DEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKycrldmrksmydhvkksskghflpfdVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlLEQFL 210
Cdd:cd17994   80 TYVGDH--------------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRI-LNSYK 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362201 211 IPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKetgdglsglDVSNDkETYKSLKFILGAFMLRR 284
Cdd:cd17994  133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA---------DISKE-DQIKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
51-284 3.09e-40

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: 148.24  E-value: 3.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLsYLKFRQG-LPGPFLVLCPLSVTDGWVSEINRFTPNLEV 129
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILA-DEMGLGKTIQTIVFL-YSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 130 LRYVGDKYCRLDMRKSMY---DHVKKSSKGHF-------LPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNS 199
Cdd:cd18055   79 VTYTGDKDSRAIIRENEFsfdDNAVKGGKKAFkmkreaqVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 200 VLYNVlLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKetgdglsglDVSNDKETyKSLKFILGA 279
Cdd:cd18055  159 KFFRV-LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA---------DISKEDQI-KKLHDLLGP 227

                 ....*
gi 145362201 280 FMLRR 284
Cdd:cd18055  228 HMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
51-284 5.16e-40

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: 147.52  E-value: 5.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILA-DEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRK---SMYDHVKKSSKGHF-------LPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSV 200
Cdd:cd18057   80 TYTGDKESRSVIREnefSFEDNAIRSGKKVFrmkkeaqIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 201 LYNVlLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKetgdglsglDVSNDKETyKSLKFILGAF 280
Cdd:cd18057  160 FFRV-LNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA---------DISKEDQI-KKLHDLLGPH 228

                 ....
gi 145362201 281 MLRR 284
Cdd:cd18057  229 MLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
51-284 5.88e-40

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: 147.12  E-value: 5.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLkFRQGLPGPFLVLCPLSVTDGWVSEINRFTpNLEVL 130
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILA-DEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsmYDHVKKSSKGHFLP----FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlL 206
Cdd:cd18060   78 VYHGSLASRQMIQQ--YEMYCKDSRGRLIPgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDS-L 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 207 EQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLsafKETGDglsgldvSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18060  155 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFL---KDFGD-------LKTEEQVQKLQAILKPMMLRR 222
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
51-251 1.56e-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: 146.34  E-value: 1.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWL--IQKYllGVNVVLeLDQMGLGKTLQAISFLsYLKF--RQGLPGPF----LVLCPLSVTDGWVSEINR 122
Cdd:cd17999    1 LRPYQQEGINWLafLNKY--NLHGIL-CDDMGLGKTLQTLCIL-ASDHhkRANSFNSEnlpsLVVCPPTLVGHWVAEIKK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 123 FTPN--LEVLRYVGDKYCRLDMRKSMYDHvkksskghflpfDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSV 200
Cdd:cd17999   77 YFPNafLKPLAYVGPPQERRRLREQGEKH------------NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTK 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145362201 201 LYNVLLeQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAF 251
Cdd:cd17999  145 LSKAVK-QLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRF 194
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
51-284 2.19e-39

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: 146.37  E-value: 2.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYL---------------KFRQGLP-----GPFLVLCPL 110
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILG-DDMGLGKTVQVIAFLAAVlgktgtrrdrennrpRFKKKPPassakKPVLIVAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 111 SVTDGWVSEINRFTpNLEVLRYVGDKycRLDMRKSMYDHVKksskghflpFDVLLTTYDIALVDQDFLSQIPWQYAIIDE 190
Cdd:cd18005   80 SVLYNWKDELDTWG-HFEVGVYHGSR--KDDELEGRLKAGR---------LEVVVTTYDTLRRCIDSLNSINWSAVIADE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 191 AQRLKNPNSVLYNVLLEqFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKE---TGDGLSGL--DVSN 265
Cdd:cd18005  148 AHRIKNPKSKLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikRGQRHTATarELRL 226
                        250
                 ....*....|....*....
gi 145362201 266 DKETYKSLKFILGAFMLRR 284
Cdd:cd18005  227 GRKRKQELAVKLSKFFLRR 245
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
51-284 8.40e-38

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: 141.36  E-value: 8.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILA-DEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKSMYDHV-------KKSS---KGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSV 200
Cdd:cd18056   80 TYVGDKDSRAIIRENEFSFEdnairggKKASrmkKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 201 LYNVlLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKetgdglsglDVSNDKETyKSLKFILGAF 280
Cdd:cd18056  160 FFRV-LNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA---------DIAKEDQI-KKLHDMLGPH 228

                 ....
gi 145362201 281 MLRR 284
Cdd:cd18056  229 MLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
51-252 2.00e-36

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 137.50  E-value: 2.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLkFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVL 130
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILA-DDMGLGKTVQICAFLSGM-FDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGdkyCRLDMRKSMYDHVKKSskghflpFDVLLTTYDIALVDQDFLS-----QIPWQYAIIDEAQRLKNPNSVLYNVL 205
Cdd:cd18001   79 VFHG---TSKKERERNLERIQRG-------GGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 145362201 206 LEqflIP--RRLLITGTPIQNNLTELWALMHFcmpLVFGTLDQFLSAFK 252
Cdd:cd18001  149 RE---IPakNRIILTGTPIQNNLKELWALFDF---ACNGSLLGTRKTFK 191
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
51-284 3.98e-36

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: 136.33  E-value: 3.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLSYLkFRQGLPGPFLVLCPLSVTDGWVSEINRFTpNLEVL 130
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILA-DEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsmYDHVKKSSKGHFLP----FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlL 206
Cdd:cd18058   78 VYHGSQISRQMIQQ--YEMYYRDEQGNPLSgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEG-L 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 207 EQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFketGDglsgldvSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18058  155 KLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF---GD-------LKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
51-284 3.19e-34

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: 130.54  E-value: 3.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLsYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTpNLEVL 130
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILA-DEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRksMYDHVKKSSKGHFLP----FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVlL 206
Cdd:cd18059   78 VYHGSQASRRTIQ--LYEMYFKDPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEG-L 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 207 EQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETgdglsgldvsNDKETYKSLKFILGAFMLRR 284
Cdd:cd18059  155 KMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDL----------KTEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
51-284 3.69e-33

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: 128.17  E-value: 3.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKyLLGVNV-----VLELDQMGLGKTLQAISFLSYL----KFRQGLPGPFLVLCPLSVTDGWVSEIN 121
Cdd:cd18004    1 LRPHQREGVQFLYDC-LTGRRGyggggAILADEMGLGKTLQAIALVWTLlkqgPYGKPTAKKALIVCPSSLVGNWKAEFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 122 RFTPNLEVlryvgdKYCRLDMRKSmYDHVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQ-IPWQYAIIDEAQRLKNPNSV 200
Cdd:cd18004   80 KWLGLRRI------KVVTADGNAK-DVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 201 LYNvLLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETgdGLSGLDVSNDKETY-------KSL 273
Cdd:cd18004  153 TTK-ALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEP--ILRSRDPDASEEDKelgaersQEL 229
                        250
                 ....*....|.
gi 145362201 274 KFILGAFMLRR 284
Cdd:cd18004  230 SELTSRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
51-284 5.16e-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: 125.09  E-value: 5.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQK-YLLGvnvvlelDQMGLGKTLQAIS-----------------FLSYLKFRQGLPGPFLVLCPLSV 112
Cdd:cd18008    1 LLPYQKQGLAWMLPRgGILA-------DEMGLGKTIQALAlilatrpqdpkipeeleENSSDPKKLYLSKTTLIVVPLSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 113 TDGWVSEINRFT--PNLEVLRYVGDKycrldmrksmydhvKKSSKGHFLPFDVLLTTYDI----------------ALVD 174
Cdd:cd18008   74 LSQWKDEIEKHTkpGSLKVYVYHGSK--------------RIKSIEELSDYDIVITTYGTlasefpknkkgggrdsKEKE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 175 QDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqflIP--RRLLITGTPIQNNLTELWALMHF------CMPLVFgtlDQ 246
Cdd:cd18008  140 ASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCA---LKaeRRWCLTGTPIQNSLDDLYSLLRFlrvepfGDYPWF---NS 213
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 145362201 247 FLSAfketgdglsgLDVSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18008  214 DISK----------PFSKNDRKALERLQALLKPILLRR 241
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
51-284 1.93e-31

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: 122.81  E-value: 1.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLElDQMGLGKTLQAISFLsYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTpNLEVL 130
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILA-DEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 131 RYVGDKYCRLDMRKsmYDHVKKSSKGHFLP----FDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLl 206
Cdd:cd18061   78 VYHGSLISRQMIQQ--YEMYFRDSQGRIIRgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGL- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362201 207 EQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETgdglsgldvsNDKETYKSLKFILGAFMLRR 284
Cdd:cd18061  155 KLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDL----------KTEEQVQKLQAILKPMMLRR 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
51-253 5.70e-31

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: 122.01  E-value: 5.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQ-------KYLLGVNVVLElDQMGLGKTLQAISFL-SYLK-FRQGLPgpFLVLCPLSVTDGWVSEIN 121
Cdd:cd18007    1 LKPHQVEGVRFLWSnlvgtdvGSDEGGGCILA-HTMGLGKTLQVITFLhTYLAaAPRRSR--PLVLCPASTLYNWEDEFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 122 RFTPNLEV---LRYVGDKYCRLDMRKSMydhVKK--SSKGhflpfdVLLTTYD----IALVDQDFLSQIPWQYA------ 186
Cdd:cd18007   78 KWLPPDLRpllVLVSLSASKRADARLRK---INKwhKEGG------VLLIGYElfrnLASNATTDPRLKQEFIAalldpg 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145362201 187 ----IIDEAQRLKNPNSVLYNVLlEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKE 253
Cdd:cd18007  149 pdllVLDEGHRLKNEKSQLSKAL-SKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVK 218
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
51-284 2.88e-24

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: 102.55  E-value: 2.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQ----KYLLGVNVVLELDQMGLGKTLQAISFLSYLkFRQGlPGP------FLVLCPLSVTDGWVSEI 120
Cdd:cd18067    1 LRPHQREGVKFLYRcvtgRRIRGSHGCIMADEMGLGKTLQCITLMWTL-LRQS-PQCkpeidkAIVVSPSSLVKNWANEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 121 NRFT-PNLEVLRYVGdKYCRLDMRKSMydhVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNS 199
Cdd:cd18067   79 GKWLgGRLQPLAIDG-GSKKEIDRKLV---QWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 200 VLYNVLlEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFK------ETGDGlSGLDVSNDKETYKSL 273
Cdd:cd18067  155 QTYQAL-DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFElpilkgRDADA-SEKERQLGEEKLQEL 232
                        250
                 ....*....|.
gi 145362201 274 KFILGAFMLRR 284
Cdd:cd18067  233 ISIVNRCIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
51-284 3.37e-23

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: 98.43  E-value: 3.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQK---YLLGvnvvlelDQMGLGKTLQAISFLSYlkFRQglPGPFLVLCPLSVTDGWVSEINRFTPNL 127
Cdd:cd18010    1 LLPFQREGVCFALRRggrVLIA-------DEMGLGKTVQAIAIAAY--YRE--EWPLLIVCPSSLRLTWADEIERWLPSL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 128 EVlryvgdkycrldmrksMYDHV--KKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVL 205
Cdd:cd18010   70 PP----------------DDIQVivKSKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LEqfLI---PRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGLSGLDV---SNDKEtyksLKFILGA 279
Cdd:cd18010  134 LP--LLkraKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYsgsSNLEE----LHLLLLA 207

                 ....*.
gi 145362201 280 -FMLRR 284
Cdd:cd18010  208 tIMIRR 213
DEXDc smart00487
DEAD-like helicases superfamily;
50-238 7.02e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.18  E-value: 7.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201    50 TLKPHQVEGVSWLIQkyllGVNVVLELDQMGLGKTLQAISFLSYlKFRQGLPGPFLVLCPL-SVTDGWVSEINRFTPNL- 127
Cdd:smart00487   8 PLRPYQKEAIEALLS----GLRDVILAAPTGSGKTLAALLPALE-ALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   128 --EVLRYVGDkycrldmrkSMYDHVKKSSKGhflPFDVLLTTYDIAL--VDQDFLSQIPWQYAIIDEAQRLKNPN--SVL 201
Cdd:smart00487  83 lkVVGLYGGD---------SKREQLRKLESG---KTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDGGfgDQL 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 145362201   202 YNVLLEQFLIPRRLLITGTP---IQNNLTELWALMHFCMP 238
Cdd:smart00487 151 EKLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
377-501 3.42e-22

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: 92.27  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  377 GKLLVLDQLLKRlhDSGHRVLLFSQMTSTLDIlQDFMELRRYSYERLDGSVRAEERFAAIKNFSAKTERgldsevdgsna 456
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKID----------- 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 145362201  457 fvFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIG 501
Cdd:pfam00271  67 --VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
51-253 3.60e-22

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: 96.45  E-value: 3.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKyLLGVNVV-----LELDQMGLGKTLQAISfLSYLKFRQGLPGP------FLVLCPLSVTDGWVSE 119
Cdd:cd18066    1 LRPHQREGIEFLYEC-VMGMRVNerfgaILADEMGLGKTLQCIS-LIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 120 INRFTPNLEVLRYVGDKycrldmrksmyDH-VKKSSKGHFlpFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNpN 198
Cdd:cd18066   79 FQKWLGSERIKVFTVDQ-----------DHkVEEFIASPL--YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKN-T 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145362201 199 SVLYNVLLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKE 253
Cdd:cd18066  145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEE 199
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
51-235 1.12e-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: 89.07  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQK----------------YLlgvNVVLEL---------------DQMGLGKTLQAISFLsylkfrqg 99
Cdd:cd18071    1 LLPHQKQALAWMVSRensqdlppfweeavglFL---NTITNFsqkkrpelvrggilaDDMGLGKTLTTISLI-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 100 LPGPFLVLCPLSVTDGWVSEINRFTP--NLEVLRYVGDKYCRldmrksmydHVKKSSKghflpFDVLLTTYDIALVDQDF 177
Cdd:cd18071   70 LANFTLIVCPLSVLSNWETQFEEHVKpgQLKVYTYHGGERNR---------DPKLLSK-----YDIVLTTYNTLASDFGA 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145362201 178 -----LSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqFLIPRRLLITGTPIQNNLTELWALMHF 235
Cdd:cd18071  136 kgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLN-LSSERRWVLTGTPIQNSPKDLGSLLSF 197
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
51-249 4.23e-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: 86.57  E-value: 4.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQK----YLLGvnvvlelDQMGLGKTLQAISFLSYLKFRqGLPGPFLVLCPLSVTDGWVSEI-NRFTP 125
Cdd:cd18011    1 PLPHQIDAVLRALRKppvrLLLA-------DEVGLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELqDKFGL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 126 NLEVLRyvgdkycRLDMRKSMYDHVKKsskghFLPFDVLLTTYDIALVD---QDFLSQIPWQYAIIDEAQRLKN---PNS 199
Cdd:cd18011   73 PFLILD-------RETAAQLRRLIGNP-----FEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNsggGKE 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145362201 200 VLYNVLLEQfLIPR---RLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLS 249
Cdd:cd18011  141 TKRYKLGRL-LAKRarhVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
HELICc smart00490
helicase superfamily c-terminal domain;
407-501 4.44e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 76.48  E-value: 4.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201   407 DILQDFMELRRYSYERLDGSVRAEERFAAIKNFSaktergldsevdgSNAFVFMISTRAGGVGLNLVAADTVIFYEQDWN 486
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN-------------NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWS 67
                           90
                   ....*....|....*
gi 145362201   487 PQVDKQALQRAHRIG 501
Cdd:smart00490  68 PASYIQRIGRAGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
51-252 4.95e-17

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


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 81.01  E-value: 4.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQkyllgvNVVLELDQ--------------MGLGKTLQAISFLsYLKFRQGLPGPFLVLCPLSVTDGW 116
Cdd:cd18069    1 LKPHQIGGIRFLYD------NIIESLERykgssgfgcilahsMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 117 VSEINRFTPNLEVLRYVGDKYCRLDMrksMYDHVKKSSKGHFLPFD------VLLTTYDIalvdqdFLSQIPWQYAIIDE 190
Cdd:cd18069   74 LSEFNKWLPPPEALPNVRPRPFKVFI---LNDEHKTTAARAKVIEDwvkdggVLLMGYEM------FRLRPGPDVVICDE 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145362201 191 AQRLKNPNSVLyNVLLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFK 252
Cdd:cd18069  145 GHRIKNCHAST-SQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
51-238 9.80e-17

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: 80.85  E-value: 9.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSW-LIQKYLLGvnvvlelDQMGLGKTLQAISF----------LSYLKFRQGLP---------------GPF 104
Cdd:cd18070    1 LLPYQRRAVNWmLVPGGILA-------DEMGLGKTVEVLALillhprpdndLDAADDDSDEMvccpdclvaetpvssKAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 105 LVLCPLSVTDGWVSEINRFTPN-LEVLRYVGDKycrldmrKSMYDHvkKSSKGHFLPFDVLLTTYDIALVDQDF------ 177
Cdd:cd18070   74 LIVCPSAILAQWLDEINRHVPSsLKVLTYQGVK-------KDGALA--SPAPEILAEYDIVVTTYDVLRTELHYaeanrs 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362201 178 ----------------LSQIPWQYAIIDEAQRLKNPNSVLYNVLLEqflIPR--RLLITGTPIQNNLTELWALMHFCMP 238
Cdd:cd18070  145 nrrrrrqkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARR---LPRvnRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
51-251 1.16e-16

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: 80.32  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKYLLGVNVVLELDQ--------MGLGKTLQAISFLSYLKFRQGLPG--PFLVLCPLSVTDGWVSEI 120
Cdd:cd18068    1 LKPHQVDGVQFMWDCCCESLKKTKKSPGsgcilahcMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 121 NRF------TPNLEVlrYVGDKYCRLDMRKSMYDHVKKSSKGHFLPFDV---------------LLTTYDIALVDQ--DF 177
Cdd:cd18068   81 EKWqeglkdEEKIEV--NELATYKRPQERSYKLQRWQEEGGVMIIGYDMyrilaqernvksrekLKEIFNKALVDPgpDF 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362201 178 LsqipwqyaIIDEAQRLKNPNSVLYNVLlEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAF 251
Cdd:cd18068  159 V--------VCDEGHILKNEASAVSKAM-NSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
51-253 1.37e-16

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: 79.70  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLIQKylLGVNVVLEldqMGLGKTLQAISFLSYLKFrQGLPGPFLVLCPLSVT-DGWVSEINRFT--PNL 127
Cdd:cd18013    1 PHPYQKVAINFIIEH--PYCGLFLD---MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWNhlRNL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 128 EVLRYVGDKycrldmrksmydhvKKSSKGHFLPFDVLLTTYDIaLVDQDFLSQIPWQYA--IIDEAQRLKNPNSVLYNVL 205
Cdd:cd18013   75 TVSVAVGTE--------------RQRSKAANTPADLYVINREN-LKWLVNKSGDPWPFDmvVIDELSSFKSPRSKRFKAL 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LE-QFLIPRRLLITGTPIQNNLTELWALMHFcmpLVFG-TLDQFLSAFKE 253
Cdd:cd18013  140 RKvRPVIKRLIGLTGTPSPNGLMDLWAQIAL---LDQGeRLGRSITAYRE 186
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
51-284 2.62e-13

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: 70.59  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGVSWLI----QKYLLGVNVvlelDQMGLGKTLQAISFLSYLKFRQGL----------------------PGPF 104
Cdd:cd18072    1 LLLHQKQALAWLLwrerQKPRGGILA----DDMGLGKTLTMIALILAQKNTQNRkeeekekalteweskkdstlvpSAGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 105 LVLCPLSVTDGWVSEINRftpnlevlryvgdKYCRLDMRKSMYDHVKKSSKGHFLP-FDVLLTTYDIAL---------VD 174
Cdd:cd18072   77 LVVCPASLVHQWKNEVES-------------RVASNKLRVCLYHGPNRERIGEVLRdYDIVITTYSLVAkeiptykeeSR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 175 QDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLeQFLIPRRLLITGTPIQNNLTELWALMHF--CMPLvfgtldQFLSAFK 252
Cdd:cd18072  144 SSPLFRIAWARIILDEAHNIKNPKVQASIAVC-KLRAHARWALTGTPIQNNLLDMYSLLKFlrCSPF------DDLKVWK 216
                        250       260       270
                 ....*....|....*....|....*....|..
gi 145362201 253 ETGDglsgldvSNDKETYKSLKFILGAFMLRR 284
Cdd:cd18072  217 KQVD-------NKSRKGGERLNILTKSLLLRR 241
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
50-676 1.33e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 48.87  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  50 TLKPHQVEGVSWLIQKYLLGVN-VVLELDqMGLGKTLQAISFLSYLKfrqgLPGPFLVLCP-LSVTDGWVSEINRFTPNL 127
Cdd:COG1061   80 ELRPYQQEALEALLAALERGGGrGLVVAP-TGTGKTVLALALAAELL----RGKRVLVLVPrRELLEQWAEELRRFLGDP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 128 EVlryvgdkycrldmrksmydhvkkSSKGHFLPFDVLLTTYDIaLVDQDFLSQIP--WQYAIIDEAQRLKNPNsvlYNVL 205
Cdd:COG1061  155 LA-----------------------GGGKKDSDAPITVATYQS-LARRAHLDELGdrFGLVIIDEAHHAGAPS---YRRI 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 206 LEQFLIPRRLLITGTPiqnnltelwalmhfcmplvfgtldqflsafkETGDGLSGLDVSNDKETYkslkfilgafmlRRT 285
Cdd:COG1061  208 LEAFPAAYRLGLTATP-------------------------------FRSDGREILLFLFDGIVY------------EYS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 286 KSLLIESGnlVLPPLTELTVMVPLVSLQKK--IYTSILRKELpgllelssggsnhtslqniviqlrkacshpylfpgiep 363
Cdd:COG1061  245 LKEAIEDG--YLAPPEYYGIRVDLTDERAEydALSERLREAL-------------------------------------- 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 364 epfeegehLVQASGKLLVLDQLLKRlHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDGSVRAEERFAAIKNFSAKT 443
Cdd:COG1061  285 --------AADAERKDKILRELLRE-HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGE 355
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 444 ERgldsevdgsnafvFMISTRAGGVGLNLVAADTVIF---------YEQdwnpqvdkqalqrahRIGQishvlsinlvte 514
Cdd:COG1061  356 LR-------------ILVTVDVLNEGVDVPRLDVAILlrptgspreFIQ---------------RLGR------------ 395
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 515 hsveevILRRAERKLQLS-HNVVGDNMEEKEEDGGDLRSLV-FGLQRFDPEEIHNEESDNLKMVEISSLAEKVVAIRQNV 592
Cdd:COG1061  396 ------GLRPAPGKEDALvYDFVGNDVPVLEELAKDLRDLAgYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEEL 469
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 593 EPDKEERRFEINSSDTLLGNTSSASLDSELDEASYLSWVEKLKEAARSSKDEKIIELGNRKNLSEERNLRIEAARKKAEE 672
Cdd:COG1061  470 ELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLE 549

                 ....
gi 145362201 673 KKLA 676
Cdd:COG1061  550 ELAA 553
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
51-221 1.65e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 45.76  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  51 LKPHQVEGV-SWLI-QKYLLGVnVVLEldqMGLGKTLQAISFLSYLKfrqglPGPFLVLCP-LSVTDGWVSEINRFTPNL 127
Cdd:cd17926    1 LRPYQEEALeAWLAhKNNRRGI-LVLP---TGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGDS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 128 EVLRYVGDKycrldmrksmydhvKKSSKGhflpFDVLLTTYDIALVDQDFLSQIPWQYA--IIDEAQRLknpNSVLYNVL 205
Cdd:cd17926   72 SIGLIGGGK--------------KKDFDD----ANVVVATYQSLSNLAEEEKDLFDQFGllIVDEAHHL---PAKTFSEI 130
                        170
                 ....*....|....*.
gi 145362201 206 LEQFLIPRRLLITGTP 221
Cdd:cd17926  131 LKELNAKYRLGLTATP 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
454-503 2.78e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 43.08  E-value: 2.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 145362201 454 SNAFVFMISTRAGGVGLNLVAADTVIFYEQDWNPQVDKQALQRAHRIGQI 503
Cdd:cd18785   20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
729-862 9.10e-05

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 43.01  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 729 CVDDSGNWGRGGmfdalsklsntvptayhrASEFKdlhlgdlhliKIDDNDDQQNTQASKPLWVAVAVTQSYNSRR---- 804
Cdd:cd02901   21 CCNCDGVMGKGI------------------ALQFK----------KKPGRVEELRAQCKKKLLGGVAVLKRDGVKRyiyy 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145362201 805 ----KVPRSSISIPDLESCLAK-ASFSASQKSASLHMPRIGYqdGSDRSQWYTVERLLRKYSS 862
Cdd:cd02901   73 litkKSYGPKPTYEALRSSLEElREHCRENGVTSVAMPRIGC--GLDGLDWEEVEPILKEVFD 133
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
460-600 6.39e-04

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 43.57  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201 460 MISTRAGGVGLNLVAADTVIFYEQDWNPQvdkQALQRAHRIGQIS--HVlsINLVTEHSVEEVILRRAERKLQLSHNVVG 537
Cdd:COG1111  415 LVATSVAEEGLDIPEVDLVIFYEPVPSEI---RSIQRKGRTGRKRegRV--VVLIAKGTRDEAYYWSSRRKEKKMKSILK 489
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145362201 538 D-NMEEKEEDGGDLRSLV-FGLQRFDPEEIHNEESDNLKM--VEISSLAEKVVAIRQNVEPDKEERR 600
Cdd:COG1111  490 KlKKLLDKQEKEKLKESAqATLDEFESIKELAEDEINEKDldEIESSENGAHVDWREPVLLQVIVST 556
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
307-425 1.22e-03

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 41.93  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362201  307 VPLVSLQKKIYTSILRKELPGLL------ELSSGGSNHTSLQNIVIQLRKACSHPYLF-PGIEPEPF---EEGEHLVQAS 376
Cdd:pfam11496  10 TPMTSYQKELTEQIVSLHYSDILkycetsDSKEDISLIKSMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTS 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145362201  377 GKLLVLDQLLK----RLHDSGHRVLLFSQMTSTLDILQDFMELRRYSYERLDG 425
Cdd:pfam11496  90 GKFLVLNDLVNllieRDRKEPINVAIVARSGKTLDLVEALLLGKGLSYKRYSG 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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