NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|701401011|ref|XP_009996559|]
View 

PREDICTED: chromodomain-helicase-DNA-binding protein 1-like [Chaetura pelagica]

Protein Classification

DEAD/DEAH box helicase; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1( 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; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1) is a DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
5-473 2.50e-136

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 430.76  E-value: 2.50e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    5 LLAAVACIQ--LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLT--KKITDKErfLILCPLSVLSNWKE 80
Cdd:PLN03142  159 LLVQPSCIKgkMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeyRGITGPH--MVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   81 ELERFAPGLSFVTYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSE 160
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  161 FSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQ--GIEKESEPAKELHSLLQPFLLRRVKSEVAAEL 238
Cdd:PLN03142  317 FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAE--TFDEWFQisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGL 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  239 PKKVEVVLYHGMSALQRKYYKAILTKDLDAFESETGRKvTLQNVLIQLRKCVAHPYLFNGVEP-EPFEIGDHIVEASGKM 317
Cdd:PLN03142  395 PPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERK-RLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  318 CLLDKLLSFLYAGGHRVLLFSQMTQLLDILQDYMDYR---------------------------------------GGVG 358
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRgyqycridgntggedrdasidafnkpgsekfvfllstraGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  359 MNLTAADTVIFTDSDFNPQNDLQAIARAHRIGQHKPVKIIRLIGRDTVEEIIYRRAASKLQLTNAIVEGGHFAlgapKPQ 438
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLA----EQK 629
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 701401011  439 GAAELQLSEILKFGLDKLLSSEGSTIQDVELENIL 473
Cdd:PLN03142  630 TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRII 664
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
648-797 4.56e-90

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: 280.68  E-value: 4.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 648 IKYVMGDVTYPKAEE-EDAIIVHCLDDSGHWGRGGLFTALEARSYQPRKIYEMAGKMKDLELGGTLLFPIDDKKSRKKGQ 726
Cdd:cd03331    2 INYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGGR 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 727 DLLALIVAQHRDRSNNLSGIKLSALEKGLKKIYLAAKKRNATVHLPRIGYATKGFNWYGTERLIRKYLATR 797
Cdd:cd03331   82 DYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
5-473 2.50e-136

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 430.76  E-value: 2.50e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    5 LLAAVACIQ--LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLT--KKITDKErfLILCPLSVLSNWKE 80
Cdd:PLN03142  159 LLVQPSCIKgkMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeyRGITGPH--MVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   81 ELERFAPGLSFVTYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSE 160
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  161 FSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQ--GIEKESEPAKELHSLLQPFLLRRVKSEVAAEL 238
Cdd:PLN03142  317 FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAE--TFDEWFQisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGL 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  239 PKKVEVVLYHGMSALQRKYYKAILTKDLDAFESETGRKvTLQNVLIQLRKCVAHPYLFNGVEP-EPFEIGDHIVEASGKM 317
Cdd:PLN03142  395 PPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERK-RLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  318 CLLDKLLSFLYAGGHRVLLFSQMTQLLDILQDYMDYR---------------------------------------GGVG 358
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRgyqycridgntggedrdasidafnkpgsekfvfllstraGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  359 MNLTAADTVIFTDSDFNPQNDLQAIARAHRIGQHKPVKIIRLIGRDTVEEIIYRRAASKLQLTNAIVEGGHFAlgapKPQ 438
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLA----EQK 629
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 701401011  439 GAAELQLSEILKFGLDKLLSSEGSTIQDVELENIL 473
Cdd:PLN03142  630 TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRII 664
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
14-229 2.47e-120

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: 362.14  E-value: 2.47e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 174 IQNSLQELYSLLSLIEPDIFPREEVKEFVEYYQGIEKESEPAKELHSLLQPFLLRR 229
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
13-426 5.46e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 375.33  E-value: 5.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLtKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:COG0553  241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLqqnmKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:COG0553  320 VLDGTRERAKGA----NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGT 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 173 PIQNSLQELYSLLSLIEPDIFPREevKEFVEYYQG-IEKESEPAKE-LHSLLQPFLLRRVKSEVAAELPKKVEVVLYHGM 250
Cdd:COG0553  396 PVENRLEELWSLLDFLNPGLLGSL--KAFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 251 SALQRKYYKAILTKDLDAFESETG--RKVTLQNVLIQLRKCVAHPYLFNGvEPEPFEIGdhiveaSGKMCLLDKLLSFLY 328
Cdd:COG0553  474 TPEQRALYEAVLEYLRRELEGAEGirRRGLILAALTRLRQICSHPALLLE-EGAELSGR------SAKLEALLELLEELL 546
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 329 AGGHRVLLFSQMTQLLDILQDYMDYR--------------------------------------GGVGMNLTAADTVIFT 370
Cdd:COG0553  547 AEGEKVLVFSQFTDTLDLLEERLEERgieyaylhggtsaeerdelvdrfqegpeapvflislkaGGEGLNLTAADHVIHY 626
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 371 DSDFNPQNDLQAIARAHRIGQHKPVKIIRLIGRDTVEEIIYRRAASKLQLTNAIVE 426
Cdd:COG0553  627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
648-797 4.56e-90

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: 280.68  E-value: 4.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 648 IKYVMGDVTYPKAEE-EDAIIVHCLDDSGHWGRGGLFTALEARSYQPRKIYEMAGKMKDLELGGTLLFPIDDKKSRKKGQ 726
Cdd:cd03331    2 INYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGGR 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 727 DLLALIVAQHRDRSNNLSGIKLSALEKGLKKIYLAAKKRNATVHLPRIGYATKGFNWYGTERLIRKYLATR 797
Cdd:cd03331   82 DYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
17-296 2.21e-85

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: 273.41  E-value: 2.21e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   17 YQIEGVKWLVQCHE-VQHGCILGDEMGLGKTCQTISLLLYLTK-KITDKERFLILCPLSVLSNWKEELERFA--PGLSFV 92
Cdd:pfam00176   1 YQIEGVNWMLSLENnLGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   93 TYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  173 PIQNSLQELYSLLSLIEPDIFprEEVKEF-----VEYYQGIEKESepAKELHSLLQPFLLRRVKSEVAAELPKKVEVVLY 247
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPF--GSLSTFrnwfdRPIERGGGKKG--VSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILF 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 701401011  248 HGMSALQRKYYKA-ILTKDLDAFESETGRKV---TLQNVLIQLRKCVAHPYLF 296
Cdd:pfam00176 237 CRLSKLQRKLYQTfLLKKDLNAIKTGEGGREikaSLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
12-201 9.46e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 9.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    12 IQLRPYQIEGVKWLVQCHevqHGCILGDEMGLGKT-CQTISLLLYLTKKitDKERFLILCPLSVL-SNWKEELERFAPGL 89
Cdd:smart00487   7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTlAALLPALEALKRG--KGGRVLVLVPTRELaEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    90 SF--VTYIGNKEERPKLQQNMKEQSHfpVLLTTYEICLKDAA--FLKSFNWAALVVDEAHRLKNQS--SLLYKTLSEF-S 162
Cdd:smart00487  82 GLkvVGLYGGDSKREQLRKLESGKTD--ILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 701401011   163 VGFTLLLTGTP---IQNSLQELYSLLSLIEPDIFPREEVKEF 201
Cdd:smart00487 160 NVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
5-473 2.50e-136

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 430.76  E-value: 2.50e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    5 LLAAVACIQ--LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLT--KKITDKErfLILCPLSVLSNWKE 80
Cdd:PLN03142  159 LLVQPSCIKgkMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeyRGITGPH--MVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   81 ELERFAPGLSFVTYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSE 160
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  161 FSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQ--GIEKESEPAKELHSLLQPFLLRRVKSEVAAEL 238
Cdd:PLN03142  317 FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAE--TFDEWFQisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGL 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  239 PKKVEVVLYHGMSALQRKYYKAILTKDLDAFESETGRKvTLQNVLIQLRKCVAHPYLFNGVEP-EPFEIGDHIVEASGKM 317
Cdd:PLN03142  395 PPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERK-RLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKM 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  318 CLLDKLLSFLYAGGHRVLLFSQMTQLLDILQDYMDYR---------------------------------------GGVG 358
Cdd:PLN03142  474 VLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRgyqycridgntggedrdasidafnkpgsekfvfllstraGGLG 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  359 MNLTAADTVIFTDSDFNPQNDLQAIARAHRIGQHKPVKIIRLIGRDTVEEIIYRRAASKLQLTNAIVEGGHFAlgapKPQ 438
Cdd:PLN03142  554 INLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLA----EQK 629
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 701401011  439 GAAELQLSEILKFGLDKLLSSEGSTIQDVELENIL 473
Cdd:PLN03142  630 TVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRII 664
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
14-229 2.47e-120

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: 362.14  E-value: 2.47e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 174 IQNSLQELYSLLSLIEPDIFPREEVKEFVEYYQGIEKESEPAKELHSLLQPFLLRR 229
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
13-426 5.46e-119

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 375.33  E-value: 5.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLtKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:COG0553  241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVL 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLqqnmKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:COG0553  320 VLDGTRERAKGA----NPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGT 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 173 PIQNSLQELYSLLSLIEPDIFPREevKEFVEYYQG-IEKESEPAKE-LHSLLQPFLLRRVKSEVAAELPKKVEVVLYHGM 250
Cdd:COG0553  396 PVENRLEELWSLLDFLNPGLLGSL--KAFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVEL 473
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 251 SALQRKYYKAILTKDLDAFESETG--RKVTLQNVLIQLRKCVAHPYLFNGvEPEPFEIGdhiveaSGKMCLLDKLLSFLY 328
Cdd:COG0553  474 TPEQRALYEAVLEYLRRELEGAEGirRRGLILAALTRLRQICSHPALLLE-EGAELSGR------SAKLEALLELLEELL 546
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 329 AGGHRVLLFSQMTQLLDILQDYMDYR--------------------------------------GGVGMNLTAADTVIFT 370
Cdd:COG0553  547 AEGEKVLVFSQFTDTLDLLEERLEERgieyaylhggtsaeerdelvdrfqegpeapvflislkaGGEGLNLTAADHVIHY 626
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 371 DSDFNPQNDLQAIARAHRIGQHKPVKIIRLIGRDTVEEIIYRRAASKLQLTNAIVE 426
Cdd:COG0553  627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
648-797 4.56e-90

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: 280.68  E-value: 4.56e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 648 IKYVMGDVTYPKAEE-EDAIIVHCLDDSGHWGRGGLFTALEARSYQPRKIYEMAGKMKDLELGGTLLFPIDDKKSRKKGQ 726
Cdd:cd03331    2 INYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGGR 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 727 DLLALIVAQHRDRSNNLSGIKLSALEKGLKKIYLAAKKRNATVHLPRIGYATKGFNWYGTERLIRKYLATR 797
Cdd:cd03331   82 DYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
17-296 2.21e-85

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: 273.41  E-value: 2.21e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   17 YQIEGVKWLVQCHE-VQHGCILGDEMGLGKTCQTISLLLYLTK-KITDKERFLILCPLSVLSNWKEELERFA--PGLSFV 92
Cdd:pfam00176   1 YQIEGVNWMLSLENnLGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   93 TYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  173 PIQNSLQELYSLLSLIEPDIFprEEVKEF-----VEYYQGIEKESepAKELHSLLQPFLLRRVKSEVAAELPKKVEVVLY 247
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPF--GSLSTFrnwfdRPIERGGGKKG--VSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILF 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 701401011  248 HGMSALQRKYYKA-ILTKDLDAFESETGRKV---TLQNVLIQLRKCVAHPYLF 296
Cdd:pfam00176 237 CRLSKLQRKLYQTfLLKKDLNAIKTGEGGREikaSLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
14-195 2.42e-75

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: 242.86  E-value: 2.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERpKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd17919   81 YHGSQRER-AQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                        170       180
                 ....*....|....*....|..
gi 701401011 174 IQNSLQELYSLLSLIEPDIFPR 195
Cdd:cd17919  160 LQNNLEELWALLDFLDPPFLLR 181
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
13-229 1.85e-71

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: 233.79  E-value: 1.85e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLQQ-----NMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTL 167
Cdd:cd17993   81 VYLGDIKSRDTIREyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701401011 168 LLTGTPIQNSLQELYSLLSLIEPDIFpreEVKEFVEYYQGIEKESEpAKELHSLLQPFLLRR 229
Cdd:cd17993  161 LITGTPLQNSLKELWALLHFLMPGKF---DIWEEFEEEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
13-231 6.67e-69

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: 227.20  E-value: 6.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLT--KKITDKerFLILCPLSVLSNWKEELERFAPGLS 90
Cdd:cd17997    3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKhyKNINGP--HLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  91 FVTYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLT 170
Cdd:cd17997   81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701401011 171 GTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQ---GIEKESEPAKELHSLLQPFLLRRVK 231
Cdd:cd17997  161 GTPLQNNLHELWALLNFLLPDVFTSSE--DFDEWFNvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
14-229 7.34e-67

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: 221.74  E-value: 7.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPgLSFVT 93
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQ----NMKEQS-------HFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFS 162
Cdd:cd17995   80 YHGSGESRQIIQQyemyFKDAQGrkkkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701401011 163 VGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQGIEKESEPAKeLHSLLQPFLLRR 229
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE--EFLEEFGDLKTAEQVEK-LQALLKPYMLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
13-231 3.69e-66

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: 220.34  E-value: 3.69e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKErFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd18009    3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGP-FLVIAPLSTLPNWVNEFARFTPSVPVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKL--QQNMKEQSH--FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLL 168
Cdd:cd18009   82 LYHGTKEERERLrkKIMKREGTLqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701401011 169 LTGTPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYY------QGIEKESEPAKE--------LHSLLQPFLLRRVK 231
Cdd:cd18009  162 LTGTPLQNNLSELWSLLNFLLPDVF--DDLSSFESWFdfsslsDNAADISNLSEEreqnivhmLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
13-231 2.96e-63

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: 212.23  E-value: 2.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLQQNMKeQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSE-FSVGFTLLLTG 171
Cdd:cd17996   83 VYKGTPDVRKKLQSQIR-AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701401011 172 TPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQ------GIEKESEPAKE--------LHSLLQPFLLRRVK 231
Cdd:cd17996  162 TPLQNNLPELWALLNFLLPKIF--KSCKTFEQWFNtpfantGEQVKIELNEEetlliirrLHKVLRPFLLRRLK 233
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
13-231 9.10e-62

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: 207.42  E-value: 9.10e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKeRFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd18012    4 TLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKG-PSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLQQNMKEQshfpVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:cd18012   83 VIHGTKRKREKLRALEDYD----LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701401011 173 PIQNSLQELYSLLSLIEPDIFPREevKEFVEYYQG-IEK--ESEPAKELHSLLQPFLLRRVK 231
Cdd:cd18012  159 PIENHLGELWSIFDFLNPGLLGSY--KRFKKRFAKpIEKdgDEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
12-229 2.51e-61

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: 207.17  E-value: 2.51e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  12 IQLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSF 91
Cdd:cd18054   19 LELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 VTYIGNKEERPKLQQ-----NMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFT 166
Cdd:cd18054   99 VVYIGDLMSRNTIREyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHR 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701401011 167 LLLTGTPIQNSLQELYSLLSLIEPDIFpreevkefvEYYQGIEKESEPAKE-----LHSLLQPFLLRR 229
Cdd:cd18054  179 LLITGTPLQNSLKELWSLLHFIMPEKF---------EFWEDFEEDHGKGREngyqsLHKVLEPFLLRR 237
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
14-229 2.81e-57

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: 195.65  E-value: 2.81e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd18003   81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701401011 174 IQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQGIEKE-SEPAKE--------LHSLLQPFLLRR 229
Cdd:cd18003  161 LQNSLMELWSLMHFLMPHIF--QSHQEFKEWFSNPLTAmSEGSQEeneelvrrLHKVLRPFLLRR 223
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
14-229 1.17e-56

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: 192.65  E-value: 1.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKeerpklqqnmkeqshfpVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd17994   81 YVGDH-----------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 174 IQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQGIEKEsEPAKELHSLLQPFLLRR 229
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERF--NNLQGFLEEFADISKE-DQIKKLHDLLGPHMLRR 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
14-229 7.17e-53

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


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 183.47  E-value: 7.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMK------EQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTL 167
Cdd:cd18002   81 YWGNPKDRKVLRKFWDrknlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 168 LLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYY-QGIEKESEPA--------KELHSLLQPFLLRR 229
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFDSHD--EFNEWFsKDIESHAENKtglnehqlKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
13-241 6.76e-52

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


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 181.40  E-value: 6.76e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd18064   15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGT 172
Cdd:cd18064   95 CLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGT 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 173 PIQNSLQELYSLLSLIEPDIFprEEVKEFVEYY--QGIEKESEPAKELHSLLQPFLLRRVKSEVAAELPKK 241
Cdd:cd18064  175 PLQNNLHELWALLNFLLPDVF--NSAEDFDSWFdtNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
12-229 1.17e-51

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: 180.63  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  12 IQLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSF 91
Cdd:cd18053   19 LELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 VTYIGNKEERPKLQQN--MKEQSH---FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFT 166
Cdd:cd18053   99 VVYLGDINSRNMIRTHewMHPQTKrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHR 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701401011 167 LLLTGTPIQNSLQELYSLLSLIEPDIFPREEVkefVEYYQGIEKESEPAkELHSLLQPFLLRR 229
Cdd:cd18053  179 LLITGTPLQNSLKELWSLLHFIMPEKFSSWED---FEEEHGKGREYGYA-SLHKELEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
14-193 1.25e-50

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: 175.65  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLtKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYL-KEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKEQ-SHFPVLLTTYEICL---KDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLL 169
Cdd:cd17998   80 YYGSQEERKHLRYDILKGlEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                        170       180
                 ....*....|....*....|....
gi 701401011 170 TGTPIQNSLQELYSLLSLIEPDIF 193
Cdd:cd17998  160 TGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
14-229 2.03e-50

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: 176.79  E-value: 2.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQN-----------------MKEQSH--FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLL 154
Cdd:cd18057   81 YTGDKESRSVIRENefsfednairsgkkvfrMKKEAQikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701401011 155 YKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQGIEKESEpAKELHSLLQPFLLRR 229
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
14-229 5.42e-49

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: 172.94  E-value: 5.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQN-----------------MKEQS--HFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLL 154
Cdd:cd18056   81 YVGDKDSRAIIRENefsfednairggkkasrMKKEAsvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701401011 155 YKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQGIEKESEpAKELHSLLQPFLLRR 229
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF--HNLEGFLEEFADIAKEDQ-IKKLHDMLGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
14-229 1.27e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 171.73  E-value: 1.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQN-----------------MKEQSH--FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLL 154
Cdd:cd18055   81 YTGDKDSRAIIRENefsfddnavkggkkafkMKREAQvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701401011 155 YKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQGIEKESEpAKELHSLLQPFLLRR 229
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
14-229 2.62e-48

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: 171.31  E-value: 2.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQC-----HEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDK----ERFLILCPLSVLSNWKEELER 84
Cdd:cd18004    1 LRPHQREGVQFLYDCltgrrGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGkptaKKALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  85 FAPG--LSFVTYIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFL---KSFNwaALVVDEAHRLKNQSSLLYKTLS 159
Cdd:cd18004   81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLskkISID--LLICDEGHRLKNSESKTTKALN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 160 EFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPreEVKEFVEYYQG-IEKESEP-------------AKELHSLLQPF 225
Cdd:cd18004  159 SLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILG--SLASFRKVFEEpILRSRDPdaseedkelgaerSQELSELTSRF 236

                 ....
gi 701401011 226 LLRR 229
Cdd:cd18004  237 ILRR 240
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
14-231 2.81e-47

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: 168.27  E-value: 2.81e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18065   16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTP 173
Cdd:cd18065   96 LIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 174 IQNSLQELYSLLSLIEPDIFprEEVKEFVEYY--QGIEKESEPAKELHSLLQPFLLRRVK 231
Cdd:cd18065  176 LQNNLHELWALLNFLLPDVF--NSADDFDSWFdtKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
14-229 4.38e-47

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: 167.94  E-value: 4.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKI--------------------TDKERFLILCPLS 73
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  74 VLSNWKEELERFApglSFVTYI---GNKEErpKLQQNMKeQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQ 150
Cdd:cd18005   81 VLYNWKDELDTWG---HFEVGVyhgSRKDD--ELEGRLK-AGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 151 SSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIF-PREEVKEF----VEYYQG-------IEKESEPAKEL 218
Cdd:cd18005  155 KSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALgSRSQFKKHfsepIKRGQRhtatareLRLGRKRKQEL 234
                        250
                 ....*....|.
gi 701401011 219 HSLLQPFLLRR 229
Cdd:cd18005  235 AVKLSKFFLRR 245
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
14-229 1.04e-43

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: 157.90  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLlYLTKKITDKERFLILCPLSVLSNWKEELERFAPgLSFVT 93
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFL-SEIFLMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQ----NMKEQSH-------FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFS 162
Cdd:cd18058   79 YHGSQISRQMIQQyemyYRDEQGNplsgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701401011 163 VGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEVkeFVEYYQGIEKEsEPAKELHSLLQPFLLRR 229
Cdd:cd18058  159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
14-229 2.97e-42

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: 153.67  E-value: 2.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKkITDKERFLILCPLSVLSNWKEELERFAPgLSFVT 93
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQN----MKEQSH-------FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFS 162
Cdd:cd18060   79 YHGSLASRQMIQQYemycKDSRGRlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701401011 163 VGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREevKEFVEYYQGIEKEsEPAKELHSLLQPFLLRR 229
Cdd:cd18060  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSE--SEFLKDFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
14-229 5.34e-42

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: 153.30  E-value: 5.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLL--LYLTKKItdkERFLILCPLSVLSNWKEELERFAPGLSF 91
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLsgMFDSGLI---KSVLVVMPTSLIPHWVKEFAKWTPGLRV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 VTYIG-NKEERPKLQqnMKEQSHFPVLLTTYEICLKDAAFLKS-----FNWAALVVDEAHRLKNQSSLLYKTLSEFSVGF 165
Cdd:cd18001   78 KVFHGtSKKERERNL--ERIQRGGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKN 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701401011 166 TLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvKEFVEYYQ-----GIEKESEP---------AKELHSLLQPFLLRR 229
Cdd:cd18001  156 RIILTGTPIQNNLKELWALFDFACNGSLLGTR-KTFKMEFEnpitrGRDKDATQgekalgsevAENLRQIIKPYFLRR 232
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
13-231 5.00e-41

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: 150.97  E-value: 5.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  13 QLRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFV 92
Cdd:cd18062   23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 TYIGNKEERPKLQQNMKeQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTL-SEFSVGFTLLLTG 171
Cdd:cd18062  103 SYKGSPAARRAFVPQLR-SGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTG 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 172 TPIQNSLQELYSLLSLIEPDIFPREEVKE------FVEYYQGIEKESEPA----KELHSLLQPFLLRRVK 231
Cdd:cd18062  182 TPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapFAMTGEKVDLNEEETiliiRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
14-231 1.78e-40

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: 149.44  E-value: 1.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKERFLILCPLSVLSNWKEELERFAPGLSFVT 93
Cdd:cd18063   24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQQNMKeQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVG-FTLLLTGT 172
Cdd:cd18063  104 YKGTPAMRRSLVPQLR-SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGT 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 173 PIQNSLQELYSLLSLIEPDIFprEEVKEFVEYYQG--------IEKESEPA----KELHSLLQPFLLRRVK 231
Cdd:cd18063  183 PLQNKLPELWALLNFLLPTIF--KSCSTFEQWFNApfamtgerVDLNEEETiliiRRLHKVLRPFLLRRLK 251
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
14-229 1.23e-39

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: 145.94  E-value: 1.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDKErFLILCPLSVLSNWKEELERFAPgLSFVT 93
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGP-FLVIAPLSTIPNWEREFRTWTE-LNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  94 YIGNKEERPKLQ-----------QNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFS 162
Cdd:cd18059   79 YHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701401011 163 VGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEVkeFVEYYQGIEKEsEPAKELHSLLQPFLLRR 229
Cdd:cd18059  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
14-229 4.47e-38

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: 142.10  E-value: 4.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQ-HGcILGDEMGLGKTCQTISLL---LYLTKKITDKERF--LILCPLSVLSNWKEELERFAP 87
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNlHG-ILCDDMGLGKTLQTLCILasdHHKRANSFNSENLpsLVVCPPTLVGHWVAEIKKYFP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  88 --GLSFVTYIGNKEERPKLQQNMKEQShfpVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGF 165
Cdd:cd17999   80 naFLKPLAYVGPPQERRRLREQGEKHN---VIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701401011 166 TLLLTGTPIQNSLQELYSLLSLIEPDIFPREevKEFVEYY----------QGIEKESEPAK----ELHSLLQPFLLRR 229
Cdd:cd17999  157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTE--KQFQRRFlkpilasrdsKASAKEQEAGAlaleALHKQVLPFLLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
14-229 8.76e-38

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: 140.91  E-value: 8.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLL--LYLTKKitdKERFLILCPLSVLSNWKEELeRFAPGLSF 91
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLyeILLTGI---RGPFLIIAPLSTIANWEREF-RTWTDLNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 VTYIGNKEERPKLQQN-----------MKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSE 160
Cdd:cd18061   77 VVYHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701401011 161 FSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEVkeFVEYYQGIEKEsEPAKELHSLLQPFLLRR 229
Cdd:cd18061  157 MNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
14-205 8.99e-38

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: 141.27  E-value: 8.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVK--W--LVQCHEVQ---HGCILGDEMGLGKTCQTISLL-LYLTKKITDKeRFLILCPLSVLSNWKEELERF 85
Cdd:cd18007    1 LKPHQVEGVRflWsnLVGTDVGSdegGGCILAHTMGLGKTLQVITFLhTYLAAAPRRS-RPLVLCPASTLYNWEDEFKKW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  86 APGLSFVTYIGN--------KEERPKLQQNMKEQShfpVLLTTYEICLK--------------DAAFLKSFNWAALVVDE 143
Cdd:cd18007   80 LPPDLRPLLVLVslsaskraDARLRKINKWHKEGG---VLLIGYELFRNlasnattdprlkqeFIAALLDPGPDLLVLDE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701401011 144 AHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFprEEVKEFVEYY 205
Cdd:cd18007  157 GHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYL--GTLKEFKKKF 216
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
14-229 2.73e-37

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 140.12  E-value: 2.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQChevqhGCILGDEMGLGKTCQTISLLL---YLTKKITDKERF--------------LILCPLSVLS 76
Cdd:cd18008    1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALILatrPQDPKIPEELEEnssdpkklylskttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  77 NWKEELERF--APGLSFVTYIGNKEERPKlqqnmKEQSHFPVLLTTYEI----------------CLKDAAFLKSFNWAA 138
Cdd:cd18008   76 QWKDEIEKHtkPGSLKVYVYHGSKRIKSI-----EELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 139 LVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREevKEFVEYYQGIEKESEPA--K 216
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDY--PWFNSDISKPFSKNDRKalE 228
                        250
                 ....*....|...
gi 701401011 217 ELHSLLQPFLLRR 229
Cdd:cd18008  229 RLQALLKPILLRR 241
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
14-190 5.08e-37

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: 137.46  E-value: 5.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCILGDEMGLGKTCQTISLL--LYLTKKITDkeRFLILCPLSVLSNWKEELERFAPGLSF 91
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLaaLHHSKLGLG--PSLIVCPATVLKQWVKEFHRWWPPFRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 V------------TYIGNKEERPKLQQNMKEQSHfpVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLS 159
Cdd:cd18000   79 VvlhssgsgtgseEKLGSIERKSQLIRKVVGDGG--ILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACK 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 701401011 160 EFSVGFTLLLTGTPIQNSLQELYSLLSLIEP 190
Cdd:cd18000  157 QLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
14-229 4.14e-36

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: 136.83  E-value: 4.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQ-----HGCILGDEMGLGKTCQTISLLLYLTKKITDK----ERFLILCPLSVLSNWKEELER 84
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRrirgsHGCIMADEMGLGKTLQCITLMWTLLRQSPQCkpeiDKAIVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  85 F-APGLSFVTYIG--NKEERPKLQQNMKEQSH---FPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTL 158
Cdd:cd18067   81 WlGGRLQPLAIDGgsKKEIDRKLVQWASQQGRrvsTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 159 SEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIF-PREEVKEFVEY-----------YQGIEKESEPAKELHSLLQPFL 226
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILgTAAEFKKNFELpilkgrdadasEKERQLGEEKLQELISIVNRCI 240

                 ...
gi 701401011 227 LRR 229
Cdd:cd18067  241 IRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
14-229 5.67e-32

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: 124.57  E-value: 5.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQC-----HEVQHGCILGDEMGLGKTCQTISLLLYLTKKITDK-----ERFLILCPLSVLSNWKEELE 83
Cdd:cd18066    1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGgkpviKRALIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  84 RFApGLSFVTYIGNKEERPklQQNMKEQSHFPVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSV 163
Cdd:cd18066   81 KWL-GSERIKVFTVDQDHK--VEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSC 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701401011 164 GFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEVKEFVeYYQGIEKESEP-------------AKELHSLLQPFLLRR 229
Cdd:cd18066  158 ERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKV-YEEPIVRSREPtatpeekklgearAAELTRLTGLFILRR 235
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
308-401 2.00e-31

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: 119.50  E-value: 2.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 308 DHIVeaSGKMCLLDKLLSFLYAGGHRVLLFSQMTQLLDILQDYMDYR--------------------------------- 354
Cdd:cd18793    6 EEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERgikylrldgstsskerqklvdrfnedpdirvfl 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 701401011 355 -----GGVGMNLTAADTVIFTDSDFNPQNDLQAIARAHRIGQHKPVKIIRLI 401
Cdd:cd18793   84 lstkaGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
33-195 1.83e-29

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: 117.57  E-value: 1.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  33 HGCILGDEMGLGKTCQTISLLLYltkkitdkERFLILCPLSVLSNWKEEL-ERFAPG-LSFVTYIGnkeerPKLQQNMKE 110
Cdd:cd18071   49 RGGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHG-----GERNRDPKL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 111 QSHFPVLLTTYEICL-----KDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLL 185
Cdd:cd18071  116 LSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL 195
                        170
                 ....*....|..
gi 701401011 186 SL--IEPDIFPR 195
Cdd:cd18071  196 SFlhLKPFSNPE 207
DEXDc smart00487
DEAD-like helicases superfamily;
12-201 9.46e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.13  E-value: 9.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    12 IQLRPYQIEGVKWLVQCHevqHGCILGDEMGLGKT-CQTISLLLYLTKKitDKERFLILCPLSVL-SNWKEELERFAPGL 89
Cdd:smart00487   7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTlAALLPALEALKRG--KGGRVLVLVPTRELaEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011    90 SF--VTYIGNKEERPKLQQNMKEQSHfpVLLTTYEICLKDAA--FLKSFNWAALVVDEAHRLKNQS--SLLYKTLSEF-S 162
Cdd:smart00487  82 GLkvVGLYGGDSKREQLRKLESGKTD--ILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 701401011   163 VGFTLLLTGTP---IQNSLQELYSLLSLIEPDIFPREEVKEF 201
Cdd:smart00487 160 NVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
14-229 1.79e-27

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: 110.76  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQchevqHG--CILGDEMGLGKTCQTISLLLYLtkkitdKERF--LILCPLSVLSNWKEELERFAPGL 89
Cdd:cd18010    1 LLPFQREGVCFALR-----RGgrVLIADEMGLGKTVQAIAIAAYY------REEWplLIVCPSSLRLTWADEIERWLPSL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  90 SfVTYI----GNKEERPKLQQNmkeqshfpVLLTTYEICLKDAAFLKSFNWAALVVDEAHRLKNQSSLLYKTLSEF--SV 163
Cdd:cd18010   70 P-PDDIqvivKSKDGLRDGDAK--------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRA 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701401011 164 GFTLLLTGTPIQNSLQELYSLLSLIEPDIFPREEvkEFVEYYQGIE--------KESEPAKELHSLL-QPFLLRR 229
Cdd:cd18010  141 KRVILLSGTPALSRPIELFTQLDALDPKLFGRFH--DFGRRYCAAKqggfgwdySGSSNLEELHLLLlATIMIRR 213
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
14-195 1.01e-26

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: 108.53  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVqhGCILGDEMGLGKTCQTISLLLYLtKKITDKERFLILCPLSVLSNWKEEL-ERFapGLSFV 92
Cdd:cd18011    1 PLPHQIDAVLRALRKPPV--RLLLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELqDKF--GLPFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  93 tyIGNKEERPKLQQNMKEQ-SHFPVLLTTYEIcLKD----AAFLKSFNWAALVVDEAHRLKN----QSSLLYKTLSEFSV 163
Cdd:cd18011   76 --ILDRETAAQLRRLIGNPfEEFPIVIVSLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAK 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 701401011 164 GFT--LLLTGTPIQNSLQELYSLLSLIEPDIFPR 195
Cdd:cd18011  153 RARhvLLLTATPHNGKEEDFRALLSLLDPGRFAV 186
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
14-201 1.38e-23

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: 100.73  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQC-----HEVQH----GCILGDEMGLGKTCQTISLL--LYLTKKITDKERFLILCPLSVLSNWKEEL 82
Cdd:cd18068    1 LKPHQVDGVQFMWDCcceslKKTKKspgsGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  83 ERFAPGLS---------FVTYIGNKEERPKLQQNMKEQShfpVLLTTYE----ICLKDAAFLKS-----FNWAA------ 138
Cdd:cd18068   81 EKWQEGLKdeekievneLATYKRPQERSYKLQRWQEEGG---VMIIGYDmyriLAQERNVKSREklkeiFNKALvdpgpd 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701401011 139 -LVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFprEEVKEF 201
Cdd:cd18068  158 fVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLL--GTIKEF 219
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
14-229 1.03e-22

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: 97.94  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLvQCHEVQ--HGCILGDEMGLGKTCQTISLLLYlTKKITDKERF-----------------------LI 68
Cdd:cd18072    1 LLLHQKQALAWL-LWRERQkpRGGILADDMGLGKTLTMIALILA-QKNTQNRKEEekekalteweskkdstlvpsagtLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  69 LCPLSVLSNWKEELERFAPG--LSFVTYIGNKEERpklqqNMKEQSHFPVLLTTYEICLKDAAFLKS---------FNWA 137
Cdd:cd18072   79 VCPASLVHQWKNEVESRVASnkLRVCLYHGPNRER-----IGEVLRDYDIVITTYSLVAKEIPTYKEesrssplfrIAWA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 138 ALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIFpreevKEFVEYYQGIEKESEPAKE 217
Cdd:cd18072  154 RIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPF-----DDLKVWKKQVDNKSRKGGE 228
                        250
                 ....*....|...
gi 701401011 218 -LHSLLQPFLLRR 229
Cdd:cd18072  229 rLNILTKSLLLRR 241
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
14-228 1.22e-20

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: 92.41  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQchevqHGCILGDEMGLGKTCQTISLLLYLTKKITDKERF-------------------------LI 68
Cdd:cd18070    1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILLHPRPDNDLDAAdddsdemvccpdclvaetpvsskatLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  69 LCPLSVLSNWKEELERFAP-GLSFVTYIGNKEErpklqqnMKEQSHFP-------VLLTTYEICLKDAAF---------- 130
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKD-------GALASPAPeilaeydIVVTTYDVLRTELHYaeanrsnrrr 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 131 ------------LKSFNWAALVVDEAHRLKNQSSLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPDIF-PREE 197
Cdd:cd18070  149 rrqkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFcDSDW 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 701401011 198 VKEFVEYYQGIEKESEPakeLHSLLQPFLLR 228
Cdd:cd18070  229 WARVLIRPQGRNKAREP---LAALLKELLWR 256
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
647-797 5.06e-19

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: 83.84  E-value: 5.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 647 CIKYVMGDVTYPKaeeEDAIIVHCLDDSGHWGRGGLFTALE--ARSYQPRKIYemagkmKDLELGGTLLFPIDDKksrkk 724
Cdd:cd02901    1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKkpGRVEELRAQC------KKKLLGGVAVLKRDGV----- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 701401011 725 gQDLLALIVAQHRDRSNnlsgIKLSALEKGLKKI-YLAAKKRNATVHLPRIGYATKGFNWYGTERLIRKYLATR 797
Cdd:cd02901   67 -KRYIYYLITKKSYGPK----PTYEALRSSLEELrEHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
14-191 2.94e-16

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: 78.70  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWL----VQCHEVQH-----GCILGDEMGLGKTCQTISLLlYLTKKITDKERFLILCPLSVLSNWKEELER 84
Cdd:cd18069    1 LKPHQIGGIRFLydniIESLERYKgssgfGCILAHSMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNWLSEFNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  85 FAPGLS---------FVTYIGNKEERPKLQQ-NMKEQ--SHFPVLLTTYEIC-LKDAAFLksfnwaaLVVDEAHRLKNQS 151
Cdd:cd18069   80 WLPPPEalpnvrprpFKVFILNDEHKTTAARaKVIEDwvKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCH 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 701401011 152 SLLYKTLSEFSVGFTLLLTGTPIQNSLQELYSLLSLIEPD 191
Cdd:cd18069  153 ASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPD 192
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
14-189 1.93e-15

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 76.23  E-value: 1.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQcHEVqhGCILGDeMGLGKTCQTISLLLYLtkKITDKER-FLILCPLSVLSN-WKEELERFApGLSF 91
Cdd:cd18013    1 PHPYQKVAINFIIE-HPY--CGLFLD-MGLGKTVTTLTALSDL--QLDDFTRrVLVIAPLRVARStWPDEVEKWN-HLRN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  92 VTY---IGNKEERPKLQQnmkeqSHFPVLLTTYE----ICLKdaaFLKSFNWAALVVDEAHRLKNQSSLLYKTLseFSVG 164
Cdd:cd18013   74 LTVsvaVGTERQRSKAAN-----TPADLYVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRSKRFKAL--RKVR 143
                        170       180
                 ....*....|....*....|....*....
gi 701401011 165 F----TLLLTGTPIQNSLQELYSLLSLIE 189
Cdd:cd18013  144 PvikrLIGLTGTPSPNGLMDLWAQIALLD 172
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
14-173 6.25e-12

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: 63.86  E-value: 6.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  14 LRPYQIEGVKWLVQCHEVQHGCIlgdEM--GLGKTCQTISLLLYLTKkitdkERFLILCP-LSVLSNWKEELERFAPGls 90
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTALALIAYLKE-----LRTLIVVPtDALLDQWKERFEDFLGD-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  91 fvTYIGNKEERPKlqqnmKEQSHFPVLLTTY---EICLKDAAFLKSFnWAALVVDEAHRLKnqSSLLYKTLSEFSVGFTL 167
Cdd:cd17926   71 --SSIGLIGGGKK-----KDFDDANVVVATYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRL 140

                 ....*.
gi 701401011 168 LLTGTP 173
Cdd:cd17926  141 GLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
12-174 1.37e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 63.46  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   12 IQLRPYQIEGVKWLVQCHEVQ--HGCIlgdEM--GLGKTCQTISLLLYLTKKiTDKERFLILCP-LSVLSNWKEELERFA 86
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTLTAAKLIARLFKK-GPIKKVLFLVPrKDLLEQALEEFKKFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   87 PGLSFVTYIGNKEERPKLQQNMKeqshfpVLLTTYE---ICLKDAAFLKSFN-WAALVVDEAHRLknqSSLLYKTLSEFS 162
Cdd:pfam04851  78 PNYVEIGEIISGDKKDESVDDNK------IVVTTIQslyKALELASLELLPDfFDVIIIDEAHRS---GASSYRNILEYF 148
                         170
                  ....*....|...
gi 701401011  163 VGFTLL-LTGTPI 174
Cdd:pfam04851 149 KPAFLLgLTATPE 161
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
12-173 3.21e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.51  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  12 IQLRPYQIEGV-KWLVQC-HEVQHGCIlgdEM--GLGKTcqTISLLLYltKKITDKERFLILCP-LSVLSNWKEELERFA 86
Cdd:COG1061   79 FELRPYQQEALeALLAALeRGGGRGLV---VAptGTGKT--VLALALA--AELLRGKRVLVLVPrRELLEQWAEELRRFL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  87 PGLSFVTYignkeerpklqqnmKEQSHFPVLLTTYEIcLKDAAFLKSF--NWAALVVDEAHRLknqSSLLY-KTLSEFSV 163
Cdd:COG1061  152 GDPLAGGG--------------KKDSDAPITVATYQS-LARRAHLDELgdRFGLVIIDEAHHA---GAPSYrRILEAFPA 213
                        170
                 ....*....|
gi 701401011 164 GFTLLLTGTP 173
Cdd:COG1061  214 AYRLGLTATP 223
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
315-390 5.39e-10

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: 57.22  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  315 GKMCLLDKLLSFlyAGGHRVLLFSQMTQLLD--ILQDYMDYR---------------------------------GGVGM 359
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEaeLLLEKEGIKvarlhgdlsqeereeiledfrkgkidvlvatdvAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 701401011  360 NLTAADTVIFTDSDFNPQNDLQAIARAHRIG 390
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
321-390 6.71e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 53.37  E-value: 6.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   321 DKLLSFLYAGGHRVLLF-SQMTQL--LDILQDYMDYR---------GGVGMNLTAADTVIFTDSDFNPQNDLQAIARAHR 388
Cdd:smart00490   1 EELAELLKELGIKVARLhGGLSQEerEEILDKFNNGKikvlvatdvAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 701401011   389 IG 390
Cdd:smart00490  81 AG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
33-172 1.60e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.55  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  33 HGCILGDEMGLGKT-CQTISLLLYLTKKitdKERFLILCPLSVLSN-WKEEL-ERFAPGLSFVTYIGnkEERPKLQQNMK 109
Cdd:cd00046    2 ENVLITAPTGSGKTlAALLAALLLLLKK---GKKVLVLVPTKALALqTAERLrELFGPGIRVAVLVG--GSSAEEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701401011 110 EQsHFPVLLTTYEICLKDAAFLKSF---NWAALVVDEAHRLKNQS-----SLLYKTLSEFSVGFTLLLTGT 172
Cdd:cd00046   77 LG-DADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALLIDSrgaliLDLAVRKAGLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
42-176 5.71e-05

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.16  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011   42 GLGKTcqTISLL--LYLTKKITDKERFLILCPLSVLSNWK-EELERFA--PGLSFVTYIGNKEerpkLQQNMKEQSHFPV 116
Cdd:pfam00270  24 GSGKT--LAFLLpaLEALDKLDNGPQALVLAPTRELAEQIyEELKKLGkgLGLKVASLLGGDS----RKEQLEKLKGPDI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011  117 LLTTYEIC---LKDAAFLKSFNWaaLVVDEAHRL--KNQSSLLYKTLSEFSVGF-TLLLTGTPIQN 176
Cdd:pfam00270  98 LVGTPGRLldlLQERKLLKNLKL--LVLDEAHRLldMGFGPDLEEILRRLPKKRqILLLSATLPRN 161
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
37-193 1.23e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 42.52  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011  37 LGDEMGLGKTCQT---ISLLLyLTKKItdkERFLILCPLSVLSNW-KEELERFapGLSFVTYignKEERpklQQNMKEQS 112
Cdd:PRK04914 174 LADEVGLGKTIEAgmiIHQQL-LTGRA---ERVLILVPETLQHQWlVEMLRRF--NLRFSLF---DEER---YAEAQHDA 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701401011 113 HFPVLLTTYEICLKDaaFLK----------SFNWAALVVDEAHRL---KNQSSLLY---KTLSEFSVGFtLLLTGTPIQN 176
Cdd:PRK04914 242 DNPFETEQLVICSLD--FLRrnkqrleqalAAEWDLLVVDEAHHLvwsEEAPSREYqvvEQLAEVIPGV-LLLTATPEQL 318
                        170
                 ....*....|....*..
gi 701401011 177 SLQELYSLLSLIEPDIF 193
Cdd:PRK04914 319 GQESHFARLRLLDPDRF 335
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
332-401 2.43e-03

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: 37.30  E-value: 2.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701401011 332 HRVLLFSQMTQLLDILQDYM------DYrGGVGMNLTAADTVIFTDSDFNPQNDLQAIARAHRIGQhKPVKIIRLI 401
Cdd:cd18785    4 VKIIVFTNSIEHAEEIASSLeilvatNV-LGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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