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Conserved domains on  [gi|672043626|ref|XP_008759576|]
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chromodomain-helicase-DNA-binding protein 1-like isoform X5 [Rattus norvegicus]

Protein Classification

DEXHc_CHD1L and Macro_Poa1p-like_SNF2 domain-containing protein( domain architecture ID 13327344)

DEXHc_CHD1L and Macro_Poa1p-like_SNF2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-519 8.35e-138

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: 434.61  E-value: 8.35e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:PLN03142  197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVE 159
Cdd:PLN03142  277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFD 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  160 DFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKL 239
Cdd:PLN03142  357 EWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRL 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  240 QNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSY 318
Cdd:PLN03142  435 LNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQY 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  319 ERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIR 396
Cdd:PLN03142  515 CRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFR 594

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  397 LIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-- 472
Cdd:PLN03142  595 FCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEea 670

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  473 -----TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYSkEPSKEDRK 519
Cdd:PLN03142  671 taeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI-DPPKRERK 729
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 648-798 6.97e-85

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: 266.82  E-value: 6.97e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 648 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 726
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043626 727 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 798
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-519 8.35e-138

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 434.61  E-value: 8.35e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:PLN03142  197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVE 159
Cdd:PLN03142  277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFD 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  160 DFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKL 239
Cdd:PLN03142  357 EWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRL 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  240 QNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSY 318
Cdd:PLN03142  435 LNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQY 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  319 ERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIR 396
Cdd:PLN03142  515 CRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFR 594

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  397 LIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-- 472
Cdd:PLN03142  595 FCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEea 670

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  473 -----TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYSkEPSKEDRK 519
Cdd:PLN03142  671 taeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI-DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 1-423 8.55e-112

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 356.46  E-value: 8.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEerarRQQDLRQESGFHVLLTT 80
Cdd:COG0553  269 MGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE----RAKGANPFEDADLVITS 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:COG0553  344 YGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL--GSLKA 421

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 161 FVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDA 228
Cdd:COG0553  422 FRERFARpIEKGDEEALERLRRL-------LrpfllrrtKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEG 494

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 229 FENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQ 308
Cdd:COG0553  495 AEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLE 566

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 309 DYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 387
Cdd:COG0553  567 ERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIG 646

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 672043626 388 QNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 423
Cdd:COG0553  647 QTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 1-177 1.33e-101

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: 313.22  E-value: 1.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd18006   28 MGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVED 160
Cdd:cd18006  108 YEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDD 187

                        170
                 ....*....|....*..
gi 672043626 161 FVQCYQDIEKESKSASE 177
Cdd:cd18006  188 FIKAYSETDDESETVEE 204
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 648-798 6.97e-85

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: 266.82  E-value: 6.97e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 648 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 726
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043626 727 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 798
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 1-256 2.18e-62

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: 211.77  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    1 MGLGKTCQTIALLIYLVG-RLNDEGPFLILCPLSVLSNWKEEMERFA--PGLSCVTYTGDKEERARRQQDLRQESGFHVL 77
Cdd:pfam00176  26 MGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVVVLHGNKRPQERWKNDPNFLADFDVV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   78 LTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQ 157
Cdd:pfam00176 106 ITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  158 VED--FVQCYQdIEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA 234
Cdd:pfam00176 186 TFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEG 264

                         250       260
                  ....*....|....*....|....*
gi 672043626  235 ---KKVKLQNVLTQLRKCVDHPYLF 256
Cdd:pfam00176 265 greIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
1-161 8.14e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 91.40  E-value: 8.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626     1 MGLGKT-CQTIALLIYLvgRLNDEGPFLILCPLSVL-SNWKEEMERFAP---GLSCVTYTGDKEERARRQQdlrQESGFH 75
Cdd:smart00487  33 TGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLGPslgLKVVGLYGGDSKREQLRKL---ESGKTD 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    76 VLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLSEF-SVVFRLLLTGTP---IQNSLQELYSLLSV 147
Cdd:smart00487 108 ILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVF 187

                          170
                   ....*....|....
gi 672043626   148 VEPDLFCREQVEDF 161
Cdd:smart00487 188 IDVGFTPLEPIEQF 201
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 1-519 8.35e-138

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 434.61  E-value: 8.35e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:PLN03142  197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVE 159
Cdd:PLN03142  277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFD 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  160 DFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKL 239
Cdd:PLN03142  357 EWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRL 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  240 QNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSY 318
Cdd:PLN03142  435 LNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQY 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  319 ERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIR 396
Cdd:PLN03142  515 CRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFR 594

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  397 LIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-- 472
Cdd:PLN03142  595 FCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEea 670

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  473 -----TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYSkEPSKEDRK 519
Cdd:PLN03142  671 taeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI-DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 1-423 8.55e-112

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 356.46  E-value: 8.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEerarRQQDLRQESGFHVLLTT 80
Cdd:COG0553  269 MGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE----RAKGANPFEDADLVITS 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:COG0553  344 YGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLL--GSLKA 421

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 161 FVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDA 228
Cdd:COG0553  422 FRERFARpIEKGDEEALERLRRL-------LrpfllrrtKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEG 494

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 229 FENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQ 308
Cdd:COG0553  495 AEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLE 566

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 309 DYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 387
Cdd:COG0553  567 ERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIG 646

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 672043626 388 QNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 423
Cdd:COG0553  647 QTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 1-177 1.33e-101

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: 313.22  E-value: 1.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd18006   28 MGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVED 160
Cdd:cd18006  108 YEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDD 187

                        170
                 ....*....|....*..
gi 672043626 161 FVQCYQDIEKESKSASE 177
Cdd:cd18006  188 FIKAYSETDDESETVEE 204
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 648-798 6.97e-85

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: 266.82  E-value: 6.97e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 648 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 726
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043626 727 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 798
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 1-256 2.18e-62

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: 211.77  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    1 MGLGKTCQTIALLIYLVG-RLNDEGPFLILCPLSVLSNWKEEMERFA--PGLSCVTYTGDKEERARRQQDLRQESGFHVL 77
Cdd:pfam00176  26 MGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVVVLHGNKRPQERWKNDPNFLADFDVV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   78 LTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQ 157
Cdd:pfam00176 106 ITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  158 VED--FVQCYQdIEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA 234
Cdd:pfam00176 186 TFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEG 264

                         250       260
                  ....*....|....*....|....*
gi 672043626  235 ---KKVKLQNVLTQLRKCVDHPYLF 256
Cdd:pfam00176 265 greIKASLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 1-155 3.49e-62

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: 207.42  E-value: 3.49e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESgFHVLLTT 80
Cdd:cd17919   28 MGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVVYHGSQRERAQIRAKEKLDK-FDVVLTT 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR 155
Cdd:cd17919  107 YETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFLLR 181
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 1-176 4.42e-59

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: 200.27  E-value: 4.42e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERAR-RQQDLRQESG----FH 75
Cdd:cd17993   29 MGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIVYLGDIKSRDTiREYEFYFSQTkklkFN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  76 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF-C 154
Cdd:cd17993  109 VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFdI 188

                        170       180
                 ....*....|....*....|..
gi 672043626 155 REQVEDfvqcYQDIEKESKSAS 176
Cdd:cd17993  189 WEEFEE----EHDEEQEKGIAD 206
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 274-398 3.37e-53

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: 180.75  E-value: 3.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 274 SGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAG 352
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672043626 353 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 398
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 1-163 5.28e-53

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: 184.11  E-value: 5.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTT 80
Cdd:cd17996   31 MGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIVYKGTPDVRKKLQSQIRA-GKFNVLLTT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE-FSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVE 159
Cdd:cd17996  110 YEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIF--KSCK 187


                 ....
gi 672043626 160 DFVQ 163
Cdd:cd17996  188 TFEQ 191
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 1-161 5.50e-52

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: 180.98  E-value: 5.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd17997   31 MGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLIGDKEERADIIRDVLLPGKFDVCITS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:cd17997  111 YEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVF--TSSED 188


                 .
gi 672043626 161 F 161
Cdd:cd17997  189 F 189
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 1-177 1.11e-51

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: 180.66  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDeGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEER--ARRQQDLRQESG--FHV 76
Cdd:cd18009   31 MGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSVPVLLYHGTKEERerLRKKIMKREGTLqdFPV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  77 LLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR- 155
Cdd:cd18009  110 VVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDl 189

                        170       180
                 ....*....|....*....|....*
gi 672043626 156 ---EQVEDFVQCYQDIEKESKSASE 177
Cdd:cd18009  190 ssfESWFDFSSLSDNAADISNLSEE 214
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 1-172 1.48e-50

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: 177.06  E-value: 1.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPgLSCVTYTGDKEERARRQQ-----------DLR 69
Cdd:cd17995   28 MGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVVYHGSGESRQIIQQyemyfkdaqgrKKK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  70 QESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVE 149
Cdd:cd17995  107 GVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLE 186

                        170       180
                 ....*....|....*....|...
gi 672043626 150 PDLFCREqvEDFVQCYQDIEKES 172
Cdd:cd17995  187 PEKFPSS--EEFLEEFGDLKTAE 207
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 1-161 3.21e-48

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: 170.96  E-value: 3.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERA--RRQQDLRQESG---FH 75
Cdd:cd18054   48 MGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNtiREYEWIHSQTKrlkFN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  76 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcr 155
Cdd:cd18054  128 ALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF-- 205


                 ....*.
gi 672043626 156 EQVEDF 161
Cdd:cd18054  206 EFWEDF 211
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 1-173 8.03e-46

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: 162.61  E-value: 8.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDkeerarrqqdlrqesgfHVLLTT 80
Cdd:cd17994   28 MGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVGD-----------------HVLLTS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:cd17994   91 YELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLQG 168

                        170
                 ....*....|...
gi 672043626 161 FVQCYQDIEKESK 173
Cdd:cd17994  169 FLEEFADISKEDQ 181
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 1-171 1.42e-44

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: 160.21  E-value: 1.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd18003   28 MGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILTYYGSAKERKLKRQGWMKPNSFHVCITS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:cd18003  108 YQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIF--QSHQE 185

                        170
                 ....*....|.
gi 672043626 161 FVQCYQDIEKE 171
Cdd:cd18003  186 FKEWFSNPLTA 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 1-176 1.56e-42

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: 154.58  E-value: 1.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERA------RRQQDLRQESGF 74
Cdd:cd18002   28 MGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWGNPKDRKvlrkfwDRKNLYTRDAPF 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  75 HVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFc 154
Cdd:cd18002  108 HVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLF- 186

                        170       180
                 ....*....|....*....|...
gi 672043626 155 rEQVEDFVQCY-QDIEKESKSAS 176
Cdd:cd18002  187 -DSHDEFNEWFsKDIESHAENKT 208
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 1-153 1.65e-42

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: 152.92  E-value: 1.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVgRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERAR-RQQDLRQESGFHVLLT 79
Cdd:cd17998   28 MGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGSQEERKHlRYDILKGLEDFDVIVT 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672043626  80 TYEICL---KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd17998  107 TYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 1-153 2.71e-41

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: 150.79  E-value: 2.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYlVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARrqqdLRQESGFHVLLTT 80
Cdd:cd18012   32 MGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVIHGTKRKREK----LRALEDYDLVITS 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd18012  107 YGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLL 179
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 1-173 3.42e-41

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: 150.93  E-value: 3.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERA-----------------R 63
Cdd:cd18055   28 MGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTGDKDSRAiirenefsfddnavkggK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  64 RQQDLRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQEL 141
Cdd:cd18055  108 KAFKMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEEL 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043626 142 YSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 173
Cdd:cd18055  188 FHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 1-153 6.49e-41

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: 150.20  E-value: 6.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEER--ARRQQDLRQESG---FH 75
Cdd:cd18053   48 MGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRnmIRTHEWMHPQTKrlkFN 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672043626  76 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd18053  128 ILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF 205
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 1-173 9.53e-41

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: 149.83  E-value: 9.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQD------------- 67
Cdd:cd18057   28 MGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENefsfednairsgk 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  68 ----LRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQEL 141
Cdd:cd18057  108 kvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEEL 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043626 142 YSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 173
Cdd:cd18057  188 FHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 1-161 1.06e-39

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: 147.12  E-value: 1.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd18064   43 MGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:cd18064  123 YEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVF--NSAED 200


                 .
gi 672043626 161 F 161
Cdd:cd18064  201 F 201
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 1-173 1.41e-39

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: 146.36  E-value: 1.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERA-----------------R 63
Cdd:cd18056   28 MGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAiirenefsfednairggK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  64 RQQDLRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQEL 141
Cdd:cd18056  108 KASRMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEEL 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043626 142 YSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 173
Cdd:cd18056  188 FHLLNFLTPERF--HNLEGFLEEFADIAKEDQ 217
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 1-161 4.98e-39

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: 144.78  E-value: 4.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd18065   43 MGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVED 160
Cdd:cd18065  123 YEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVF--NSADD 200


                 .
gi 672043626 161 F 161
Cdd:cd18065  201 F 201
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 1-153 2.09e-33

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: 129.39  E-value: 2.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTT 80
Cdd:cd18062   51 MGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRS-GKFNVLLTT 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL-SEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd18062  130 YEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIF 203
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 1-153 2.60e-33

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: 129.03  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTT 80
Cdd:cd18063   51 MGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRS-GKFNVLLTT 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672043626  81 YEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVV-FRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd18063  130 YEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIF 203
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 1-173 1.12e-32

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: 126.31  E-value: 1.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSCVTYTGDKEERARRQQD---LRQESG-- 73
Cdd:cd18058   28 MGLGKTIQSITFLseIFLMGI---RGPFLIIAPLSTITNWEREFRTWTE-MNAIVYHGSQISRQMIQQYemyYRDEQGnp 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  74 ------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSV 147
Cdd:cd18058  104 lsgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNF 183

                        170       180
                 ....*....|....*....|....*.
gi 672043626 148 VEPDLFCREQVedFVQCYQDIEKESK 173
Cdd:cd18058  184 LEPSQFPSETT--FLEEFGDLKTEEQ 207
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 1-153 1.20e-32

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: 126.63  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGP----FLILCPLSVLSNWKEEMERFAPG--LSCVTYTGDKEERARRQQDLRQESGF 74
Cdd:cd18004   33 MGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDKWLGLrrIKVVTADGNAKDVKASLDFFSSASTY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  75 HVLLTTYEICLKDAS-FLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 153
Cdd:cd18004  113 PVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGIL 192
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 1-155 4.10e-31

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: 120.51  E-value: 4.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGL------SCVTYTGDKEERARRQQDLRQESGF 74
Cdd:cd18000   28 MGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvvvlhSSGSGTGSEEKLGSIERKSQLIRKV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  75 ----HVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEP 150
Cdd:cd18000  108 vgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187


                 ....*
gi 672043626 151 DLFCR 155
Cdd:cd18000  188 PYLLR 192
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 1-153 6.39e-31

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: 121.72  E-value: 6.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDE--------------------GPFLILCPLSVLSNWKEEMERFAP-GLSCVTYTGDKE 59
Cdd:cd18005   28 MGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLSVLYNWKDELDTWGHfEVGVYHGSRKDD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  60 ERARRQQDLRQEsgfhVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQ 139
Cdd:cd18005  108 ELEGRLKAGRLE----VVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMK 183

                        170
                 ....*....|....
gi 672043626 140 ELYSLLSVVEPDLF 153
Cdd:cd18005  184 ELWCLLDWAVPGAL 197
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 1-173 4.25e-30

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: 118.62  E-value: 4.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSCVTYTGDKEERARRQQD---LRQESG-- 73
Cdd:cd18060   28 MGLGKTIQSIAFLqeVYNVGI---HGPFLVIAPLSTITNWEREFNTWTE-MNTIVYHGSLASRQMIQQYemyCKDSRGrl 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  74 ------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSV 147
Cdd:cd18060  104 ipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHF 183

                        170       180
                 ....*....|....*....|....*.
gi 672043626 148 VEPDLFCREQveDFVQCYQDIEKESK 173
Cdd:cd18060  184 LEPSQFPSES--EFLKDFGDLKTEEQ 207
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 1-173 5.23e-30

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: 118.60  E-value: 5.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSCVTYTGDKEERARRQ-----------QD 67
Cdd:cd18059   28 MGLGKTIQSITFLyeIYLKGI---HGPFLVIAPLSTIPNWEREFRTWTE-LNVVVYHGSQASRRTIQlyemyfkdpqgRV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  68 LRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSV 147
Cdd:cd18059  104 IKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHF 183

                        170       180
                 ....*....|....*....|....*.
gi 672043626 148 VEPDLFCREQVedFVQCYQDIEKESK 173
Cdd:cd18059  184 LEPSRFPSETT--FMQEFGDLKTEEQ 207
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 1-154 3.90e-28

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: 113.24  E-value: 3.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIAlliYLVGrLNDEGPF---LILCPLSVLSNWKEEMERFAPGLSCVTYTG-DKEERARRQQDLRQESGfhV 76
Cdd:cd18001   28 MGLGKTVQICA---FLSG-MFDSGLIksvLVVMPTSLIPHWVKEFAKWTPGLRVKVFHGtSKKERERNLERIQRGGG--V 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  77 LLTTYEICLKDASFLKS-----FSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLsvvepD 151
Cdd:cd18001  102 LLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALF-----D 176


                 ...
gi 672043626 152 LFC 154
Cdd:cd18001  177 FAC 179
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 1-177 9.48e-28

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: 112.38  E-value: 9.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAP-------GLSCVTYTGDKEERARRQQDLRQESG 73
Cdd:cd18007   35 MGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWLPpdlrpllVLVSLSASKRADARLRKINKWHKEGG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  74 fhVLLTTYEICLKDAS--------FLKSFSW------SVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQ 139
Cdd:cd18007  115 --VLLIGYELFRNLASnattdprlKQEFIAAlldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLK 192

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672043626 140 ELYSLLSVVEPDLFcrEQVEDFVQCY-QDIEKESKSASE 177
Cdd:cd18007  193 EYWTMVDFARPKYL--GTLKEFKKKFvKPIEAGQCVDST 229
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 1-155 1.69e-27

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: 111.61  E-value: 1.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL-----------------IYLVGRLNDEGPFLILCPLSVLSNWKEEMERF--APGLSCVTYTGdkeer 61
Cdd:cd18008   23 MGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLSQWKDEIEKHtkPGSLKVYVYHG----- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  62 ARRQQDLRQESGFHVLLTTYEI----------------CLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVF 125
Cdd:cd18008   98 SKRIKSIEELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAER 177

                        170       180       190
                 ....*....|....*....|....*....|
gi 672043626 126 RLLLTGTPIQNSLQELYSLLSVVEPDLFCR 155
Cdd:cd18008  178 RWCLTGTPIQNSLDDLYSLLRFLRVEPFGD 207
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 1-144 2.49e-27

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: 110.90  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL---IYLVGRLNDEGPF--LILCPLSVLSNWKEEMERFAP--GLSCVTYTGDKEERARrqqdLRQESG 73
Cdd:cd17999   28 MGLGKTLQTLCILasdHHKRANSFNSENLpsLVVCPPTLVGHWVAEIKKYFPnaFLKPLAYVGPPQERRR----LREQGE 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043626  74 FH-VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSL 144
Cdd:cd17999  104 KHnVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSL 175
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 1-173 1.39e-26

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: 108.55  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLiYLVGRLNDEGPFLILCPLSVLSNWKEEMeRFAPGLSCVTYTGDKEERARRQQD-----------LR 69
Cdd:cd18061   28 MGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriIR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  70 QESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVE 149
Cdd:cd18061  106 GAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLE 185

                        170       180
                 ....*....|....*....|....
gi 672043626 150 PDLFCREQVedFVQCYQDIEKESK 173
Cdd:cd18061  186 PLRFPSEST--FMQEFGDLKTEEQ 207
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 1-146 9.58e-26

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: 106.78  E-value: 9.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYlvgrlndeGPFLILCPLSVLSNWKEEM-ERFAPG-LSCVTYTGdkeerARRQQDLRQESGFHVLL 78
Cdd:cd18071   57 MGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHG-----GERNRDPKLLSKYDIVL 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672043626  79 TTYEICL-----KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLS 146
Cdd:cd18071  124 TTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLS 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 275-387 1.38e-23

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 96.13  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  275 GKLHLLDRLLAFlySGGHRVLLFSQMTHMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQPIFVfLLSTRAGGV 354
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 672043626  355 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 387
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 1-166 6.96e-22

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: 94.58  E-value: 6.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLvgrlNDEGPFLILCPLSVLSNWKEEMERFAPGLS-----CVTYTGDKEERARRQqdlrqesgfh 75
Cdd:cd18010   25 MGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLPpddiqVIVKSKDGLRDGDAK---------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  76 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSVVFR----LLLTGTPIQNSLQELYSLLSVVEPD 151
Cdd:cd18010   91 VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKA--KRTKAALPLLKRakrvILLSGTPALSRPIELFTQLDALDPK 168

                        170
                 ....*....|....*
gi 672043626 152 LFcREQVEDFVQCYQ 166
Cdd:cd18010  169 LF-GRFHDFGRRYCA 182
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 1-150 3.82e-21

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: 93.37  E-value: 3.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALlIYLVGRLNDEGP------FLILCPLSVLSNWKEEMERFAPGLSCVTYTGDKEERARrqqDLRQESGF 74
Cdd:cd18066   33 MGLGKTLQCISL-IWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVE---EFIASPLY 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672043626  75 HVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEP 150
Cdd:cd18066  109 SVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXDc smart00487
DEAD-like helicases superfamily;
1-161 8.14e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 91.40  E-value: 8.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626     1 MGLGKT-CQTIALLIYLvgRLNDEGPFLILCPLSVL-SNWKEEMERFAP---GLSCVTYTGDKEERARRQQdlrQESGFH 75
Cdd:smart00487  33 TGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLGPslgLKVVGLYGGDSKREQLRKL---ESGKTD 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    76 VLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLSEF-SVVFRLLLTGTP---IQNSLQELYSLLSV 147
Cdd:smart00487 108 ILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVF 187

                          170
                   ....*....|....
gi 672043626   148 VEPDLFCREQVEDF 161
Cdd:smart00487 188 IDVGFTPLEPIEQF 201
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 1-152 2.29e-20

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: 90.99  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLNDEGPFL----ILCPLSVLSNWKEEMERF-APGLSCVTYTG-DKEERARRQQDLRQESGF 74
Cdd:cd18067   33 MGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGKWlGGRLQPLAIDGgSKKEIDRKLVQWASQQGR 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  75 H----VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEP 150
Cdd:cd18067  113 RvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNP 192


                 ..
gi 672043626 151 DL 152
Cdd:cd18067  193 GI 194
HELICc smart00490
helicase superfamily c-terminal domain;
305-387 2.65e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.03  E-value: 2.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   305 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgKQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 384
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 672043626   385 RIG 387
Cdd:smart00490  80 RAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 2-153 4.57e-19

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 86.19  E-value: 4.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   2 GLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEM-ERFA-PGLSCVTYTGDKEERARRQQDLRqesgFHVLLT 79
Cdd:cd18011   27 GLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELqDKFGlPFLILDRETAAQLRRLIGNPFEE----FPIVIV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  80 TYEIcLKD----ASFLKSFSWSVLAVDEAHRLKN----QSSLLHRTLSEFSVVFR--LLLTGTPIQNSLQELYSLLSVVE 149
Cdd:cd18011  102 SLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLD 180


                 ....
gi 672043626 150 PDLF 153
Cdd:cd18011  181 PGRF 184
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 648-798 8.98e-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: 83.07  E-value: 8.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 648 SINYVSGDVTHPQageEDAVIVHCVDDSGRWGRGGLFTALE--ARSAEPRKIYELAGkmkdlsLGDVLLFPiddkesRDK 725
Cdd:cd02901    1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKkpGRVEELRAQCKKKL------LGGVAVLK------RDG 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672043626 726 GQDLLALVVAQHRDRTNvlsgIKMAALEEG-LKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 798
Cdd:cd02901   66 VKRYIYYLITKKSYGPK----PTYEALRSSlEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 1-152 2.36e-15

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: 76.47  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALL--IYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGL--------SCVTYTGDKEERARRQQDLRQ 70
Cdd:cd18068   37 MGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLkdeekievNELATYKRPQERSYKLQRWQE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  71 ESGfhVLLTTYEIC--------------LKDaSFLKSF---SWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 133
Cdd:cd18068  117 EGG--VMIIGYDMYrilaqernvksrekLKE-IFNKALvdpGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTP 193

                        170
                 ....*....|....*....
gi 672043626 134 IQNSLQELYSLLSVVEPDL 152
Cdd:cd18068  194 LQNNLIEYHCMVNFVKPNL 212
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 1-177 8.50e-15

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 74.82  E-value: 8.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVGRLN-----------------DEGPF-----LILCPLSVLSNWKEEMERFAPG--LSCVTYTG 56
Cdd:cd18072   29 MGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVVCPASLVHQWKNEVESRVASnkLRVCLYHG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  57 dkeerARRQQDLRQESGFHVLLTTYEICLKD---------ASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRL 127
Cdd:cd18072  109 -----PNRERIGEVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARW 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 672043626 128 LLTGTPIQNSLQELYSLLSVVEPDLFcreqvEDFVQCYQDIEKESKSASE 177
Cdd:cd18072  184 ALTGTPIQNNLLDMYSLLKFLRCSPF-----DDLKVWKKQVDNKSRKGGE 228
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 1-151 3.59e-14

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: 72.54  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALlIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC----------VTYTGD--KEERARRQ--Q 66
Cdd:cd18069   37 MGLGKTLQVISF-LDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEAlpnvrprpfkVFILNDehKTTAARAKviE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  67 DLRQESGfhVLLTTYEIC-LKDASflksfswSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLL 145
Cdd:cd18069  116 DWVKDGG--VLLMGYEMFrLRPGP-------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMV 186


                 ....*.
gi 672043626 146 SVVEPD 151
Cdd:cd18069  187 DFVRPD 192
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 1-154 3.33e-12

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: 67.37  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLI------------YLVGRLNDE-------------GPFLILCPLSVLSNWKEEMERFAPG-LSCVTY 54
Cdd:cd18070   23 MGLGKTVEVLALILlhprpdndldaaDDDSDEMVCcpdclvaetpvssKATLIVCPSAILAQWLDEINRHVPSsLKVLTY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  55 TGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFS-----------------------WSVLaVDEAHRLKNQS 111
Cdd:cd18070  103 QGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkryeappsplvlvewWRVC-LDEAQMVESST 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 672043626 112 SLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFC 154
Cdd:cd18070  182 SKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 1-143 3.24e-11

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: 63.91  E-value: 3.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTCQTIALLIYLVgRLNDEGPFLILCPLSVLSN-WKEEMERFApGLSCVTY---TGDKEERARRQQdlrqeSGFHV 76
Cdd:cd18013   24 MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWN-HLRNLTVsvaVGTERQRSKAAN-----TPADL 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672043626  77 LLTTYE----ICLKdasFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSVVFR----LLLTGTPIQNSLQELYS 143
Cdd:cd18013   97 YVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRPVikrlIGLTGTPSPNGLMDLWA 166
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-544 3.37e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 66.59  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   2 GLGKTcqTIALLIylVGRLNDEGPFLILCP-LSVLSNWKEEMERFapglscvtyTGDKEERARRQqdlrqESGFHVLLTT 80
Cdd:COG1061  110 GTGKT--VLALAL--AAELLRGKRVLVLVPrRELLEQWAEELRRF---------LGDPLAGGGKK-----DSDAPITVAT 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  81 YEIcLKDASFLKSFS--WSVLAVDEAHRLknQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSllsvvepDLFCReqv 158
Cdd:COG1061  172 YQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATPFRSDGREILL-------FLFDG--- 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 159 edfvqcyqdiekesksaselhrllrpfllrrvkaqVATELPKKTevviyhgmsALQKKYYK-AILMKDLDAFENETAKKV 237
Cdd:COG1061  239 -----------------------------------IVYEYSLKE---------AIEDGYLApPEYYGIRVDLTDERAEYD 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 238 KLQNVLTQLrkcVDHpylfdgvepepfevgehliEASGKLHLLDRLLAFlYSGGHRVLLFSQMTHMLDILQDYMDYRGYS 317
Cdd:COG1061  275 ALSERLREA---LAA-------------------DAERKDKILRELLRE-HPDDRKTLVFCSSVDHAEALAELLNEAGIR 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 318 YERVDGSVRGEERHLAIKNFGKQPIfVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKS-VKVIR 396
Cdd:COG1061  332 AAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYD 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626 397 LIGRDTVEEIVYRKAASKLQLTNMVIEGGHFTLGAQKPAAEADLQLSEILKFGLDKLLSSEGSSMDEIDLKSILGETKDG 476
Cdd:COG1061  411 FVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLA 490

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672043626 477 QWTPDALPAAAEGESREQEEGKNHMYLFEGRDYSKEPSKEDRKSFEQLVNLQKTLLEKTSHGGRSLRN 544
Cdd:COG1061  491 LALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKE 558
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 2-133 1.97e-07

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: 51.15  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   2 GLGKTCQTIALLIYLVgrlndEGPFLILCP-LSVLSNWKEEmerfapglsCVTYTGDKEERARRQQDLRQESGFHVLLTT 80
Cdd:cd17926   28 GSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKER---------FEDFLGDSSIGLIGGGKKKDFDDANVVVAT 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672043626  81 Y---EICLKDASFLKSFsWSVLAVDEAHRLKnqSSLLHRTLSEFSVVFRLLLTGTP 133
Cdd:cd17926   94 YqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 1-132 3.90e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 50.09  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   1 MGLGKTcqTIALLIyLVGRLNDEGP-FLILCPLSVLSN-WKEEM-ERFAPGLSCVTYTGDKEERARRQQDLRQEsgfHVL 77
Cdd:cd00046   10 TGSGKT--LAALLA-ALLLLLKKGKkVLVLVPTKALALqTAERLrELFGPGIRVAVLVGGSSAEEREKNKLGDA---DII 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672043626  78 LTTYEICLKDASFLKSFS---WSVLAVDEAHRL------KNQSSLLHRTLsEFSVVFRLLLTGT 132
Cdd:cd00046   84 IATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsrgALILDLAVRKA-GLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 2-136 9.85e-07

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: 49.55  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    2 GLGKTcqTIALL--IYLVGRLNDEGPFLILCPLSVL-----SNWKEEMERFAPGLSCVtYTGDKeerarRQQDLRQESGF 74
Cdd:pfam00270  24 GSGKT--LAFLLpaLEALDKLDNGPQALVLAPTRELaeqiyEELKKLGKGLGLKVASL-LGGDS-----RKEQLEKLKGP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672043626   75 HVLLTTYEIC---LKDASFLKSFSWsvLAVDEAHRL--KNQSSLLHRTLSEFSVVFR-LLLTGTPIQN 136
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNLKL--LVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATLPRN 161
ResIII pfam04851
Type III restriction enzyme, res subunit;
2-134 1.62e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626    2 GLGKTcQTIALLIYLVGRLNDEGPFLILCP-LSVLSNWKEEMERFAPG--LSCVTYTGDKeerarrqqDLRQESGFHVLL 78
Cdd:pfam04851  33 GSGKT-LTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNyvEIGEIISGDK--------KDESVDDNKIVV 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043626   79 TTY-----EICLKDASFLKSFsWSVLAVDEAHRLknqSSLLHRTLSE-FSVVFRLLLTGTPI 134
Cdd:pfam04851 104 TTIqslykALELASLELLPDF-FDVIIIDEAHRS---GASSYRNILEyFKPAFLLGLTATPE 161
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
 238-406 3.40e-06

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


Pssm-ID: 402894  Cd Length: 281  Bit Score: 49.63  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  238 KLQNVLTQLRKCVDHPYLF-DGVEPEPF---EVGEHLIEASGKLHLLDRLLAFL----YSGGHRVLLFSQMTHMLDILQD 309
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626  310 YMDYRGYSYERVDG-SVRGEERHLAIKNFGKQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 382
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207

                         170       180
                  ....*....|....*....|....
gi 672043626  383 AHRIGQNKSVKVIRLIGRDTVEEI 406
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 342-398 9.27e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.54  E-value: 9.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672043626 342 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 398
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 4-105 6.02e-03

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 38.72  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043626   4 GKT-CQTIALLIYLvgrLNDEGP-FLILCPLSVLSNWKEE-----MERFAPGLSCVTYTGDKEERARRQQdLRQESgfHV 76
Cdd:cd17923   27 GKSlCYQLPILEAL---LRDPGSrALYLYPTKALAQDQLRslrelLEQLGLGIRVATYDGDTPREERRAI-IRNPP--RI 100

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 672043626  77 LLTTYE----ICLKDASFLKSF--SWSVLAVDEAH 105
Cdd:cd17923  101 LLTNPDmlhyALLPHHDRWARFlrNLRYVVLDEAH 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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