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Conserved domains on  [gi|1958755039|ref|XP_038959729|]
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chromodomain-helicase-DNA-binding protein 1-like isoform X6 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
 19-494 5.68e-122

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: 391.86  E-value: 5.68e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:PLN03142   240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKT 177
Cdd:PLN03142   320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  178 EVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLD 256
Cdd:PLN03142   399 ETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLD 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  257 RLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLT 334
Cdd:PLN03142   478 KLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLA 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  335 AADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEAD 414
Cdd:PLN03142   558 TADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDE 635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  415 LQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMY 477
Cdd:PLN03142   636 LL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFK 713

                          490
                   ....*....|....*..
gi 1958755039  478 LFEGRDYSkEPSKEDRK 494
Cdd:PLN03142   714 KIVSDNWI-DPPKRERK 729
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 623-773 7.85e-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: 266.43  E-value: 7.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 623 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 701
Cdd:cd03331     1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958755039 702 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 773
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 19-494 5.68e-122

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 391.86  E-value: 5.68e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:PLN03142   240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKT 177
Cdd:PLN03142   320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  178 EVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLD 256
Cdd:PLN03142   399 ETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLD 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  257 RLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLT 334
Cdd:PLN03142   478 KLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLA 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  335 AADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEAD 414
Cdd:PLN03142   558 TADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDE 635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  415 LQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMY 477
Cdd:PLN03142   636 LL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFK 713

                          490
                   ....*....|....*..
gi 1958755039  478 LFEGRDYSkEPSKEDRK 494
Cdd:PLN03142   714 KIVSDNWI-DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 18-398 2.05e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 299.06  E-value: 2.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEerarRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 97
Cdd:COG0553   310 AKFAPGLRVLVLDGTRE----RAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  98 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQ 168
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALERLRRL-------LrpfllrrtKED 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 169 VATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHL 245
Cdd:COG0553   457 VLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAEL 528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 246 IEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLST 324
Cdd:COG0553   529 SGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISL 608

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958755039 325 RAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 398
Cdd:COG0553   609 KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 623-773 7.85e-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: 266.43  E-value: 7.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 623 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 701
Cdd:cd03331     1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958755039 702 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 773
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 19-152 3.45e-70

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: 230.02  E-value: 3.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18006    71 RFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVEDFVQCYQDIEKESKSASE 152
Cdd:cd18006   151 DFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEE 204
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 8-231 1.22e-43

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: 159.77  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   8 WET---RWaWGRPArfapgLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKN 84
Cdd:pfam00176  64 WMNefeRW-VSPPA-----LRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  85 QSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVED--FVQCYQdIEKESKSASELHRLLRPFLL 162
Cdd:pfam00176 138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLL 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958755039 163 RRVKAQVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNVLTQLRKCVDHPYLF 231
Cdd:pfam00176 217 RRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
HELICc smart00490
helicase superfamily c-terminal domain;
280-362 2.56e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.03  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  280 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgKQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 359
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 1958755039  360 RIG 362
Cdd:smart00490  80 RAG 82
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 19-494 5.68e-122

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 391.86  E-value: 5.68e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:PLN03142   240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKT 177
Cdd:PLN03142   320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  178 EVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLD 256
Cdd:PLN03142   399 ETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLD 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  257 RLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLT 334
Cdd:PLN03142   478 KLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLA 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  335 AADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEAD 414
Cdd:PLN03142   558 TADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDE 635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  415 LQlsEILKFGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMY 477
Cdd:PLN03142   636 LL--QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFK 713

                          490
                   ....*....|....*..
gi 1958755039  478 LFEGRDYSkEPSKEDRK 494
Cdd:PLN03142   714 KIVSDNWI-DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 18-398 2.05e-90

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 299.06  E-value: 2.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEerarRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 97
Cdd:COG0553   310 AKFAPGLRVLVLDGTRE----RAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  98 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQ 168
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALERLRRL-------LrpfllrrtKED 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 169 VATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHL 245
Cdd:COG0553   457 VLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAEL 528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 246 IEASGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLST 324
Cdd:COG0553   529 SGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISL 608

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958755039 325 RAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 398
Cdd:COG0553   609 KAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 623-773 7.85e-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: 266.43  E-value: 7.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 623 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 701
Cdd:cd03331     1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958755039 702 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 773
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 19-152 3.45e-70

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: 230.02  E-value: 3.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18006    71 RFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVEDFVQCYQDIEKESKSASE 152
Cdd:cd18006   151 DFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEE 204
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 249-373 2.67e-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: 2.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 249 SGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAG 327
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958755039 328 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 373
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 8-231 1.22e-43

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: 159.77  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   8 WET---RWaWGRPArfapgLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKN 84
Cdd:pfam00176  64 WMNefeRW-VSPPA-----LRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  85 QSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVED--FVQCYQdIEKESKSASELHRLLRPFLL 162
Cdd:pfam00176 138 SKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLL 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958755039 163 RRVKAQVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNVLTQLRKCVDHPYLF 231
Cdd:pfam00176 217 RRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 13-151 1.13e-39

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: 145.96  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  13 AWGRP-ARFAPGLSCVTYTGDKEERAR-RQQDLRQESG----FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQS 86
Cdd:cd17993    65 AWQREfAKWAPDMNVIVYLGDIKSRDTiREYEFYFSQTkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDE 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755039  87 SLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF-CREQVEDfvqcYQDIEKESKSAS 151
Cdd:cd17993   145 SLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFdIWEEFEE----EHDEEQEKGIAD 206
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 18-130 6.69e-38

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: 139.62  E-value: 6.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEERARRQQDLRQESgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 97
Cdd:cd17919    70 EKWTPDLRVVVYHGSQRERAQIRAKEKLDK-FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958755039  98 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR 130
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDPPFLLR 181
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 19-136 2.47e-32

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: 125.13  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd17997    74 RWCPSLRVVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNS 153

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 136
Cdd:cd17997   154 RNRLLLTGTPLQNNLHELWALLNFLLPDVF--TSSEDF 189
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 24-147 3.37e-32

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: 124.67  E-value: 3.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  24 LSCVTYTGDKEERARRQQ-----------DLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRT 92
Cdd:cd17995    75 MNVVVYHGSGESRQIIQQyemyfkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQG 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958755039  93 LSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREqvEDFVQCYQDIEKES 147
Cdd:cd17995   155 LKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSS--EEFLEEFGDLKTAE 207
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 18-152 1.36e-31

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: 123.27  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEER--ARRQQDLRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL 93
Cdd:cd18009    72 ARFTPSVPVLLYHGTKEERerLRKKIMKREGTLqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQEL 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958755039  94 SEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR----EQVEDFVQCYQDIEKESKSASE 152
Cdd:cd18009   152 KTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDlssfESWFDFSSLSDNAADISNLSEE 214
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 10-136 3.94e-31

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: 122.04  E-value: 3.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  10 TRWAWGRPAR-FAPGLSCVTYTGDKEERA--RRQQDLRQESG---FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLK 83
Cdd:cd18054    81 TLTSWQREFEiWAPEINVVVYIGDLMSRNtiREYEWIHSQTKrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958755039  84 NQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 136
Cdd:cd18054   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF--EFWEDF 211
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 14-148 1.87e-30

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: 118.70  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRPARF-APGLSCVTYTGDkeerarrqqdlrqesgfHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRT 92
Cdd:cd17994    65 WEREFEMwAPDFYVVTYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRI 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755039  93 LSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 148
Cdd:cd17994   128 LNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLQGFLEEFADISKEDQ 181
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 18-138 8.28e-30

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: 118.24  E-value: 8.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE-F 96
Cdd:cd17996    73 EKWAPSVSKIVYKGTPDVRKKLQSQIRA-GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyY 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958755039  97 SVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQ 138
Cdd:cd17996   152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIF--KSCKTFEQ 191
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 20-148 1.42e-26

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: 108.95  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  20 FAPGLSCVTYTGDKEERA-----------------RRQQDLRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAH 80
Cdd:cd18055    72 WAPDFYVVTYTGDKDSRAiirenefsfddnavkggKKAFKMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAH 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755039  81 RLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 148
Cdd:cd18055   152 RLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 14-128 1.57e-26

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: 107.09  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRP-ARFAPGLSCVTYTGDKEERAR-RQQDLRQESGFHVLLTTYEICL---KDASFLKSFSWSVLAVDEAHRLKNQSSL 88
Cdd:cd17998    64 WLREfKRWCPSLKVEPYYGSQEERKHlRYDILKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSE 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958755039  89 LHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd17998   144 RYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 20-148 2.50e-26

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: 108.23  E-value: 2.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  20 FAPGLSCVTYTGDKEERARRQQD-----------------LRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAH 80
Cdd:cd18057    72 WAPDFYVVTYTGDKESRSVIRENefsfednairsgkkvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAH 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755039  81 RLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 148
Cdd:cd18057   152 RLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 13-128 3.76e-26

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: 107.83  E-value: 3.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  13 AWGRPAR-FAPGLSCVTYTGDKEER--ARRQQDLRQESG---FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQS 86
Cdd:cd18053    84 SWQREIQtWAPQMNAVVYLGDINSRnmIRTHEWMHPQTKrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958755039  87 SLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18053   164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF 205
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 19-146 5.45e-26

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: 106.67  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18003    71 RWCPGFKILTYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNT 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKE 146
Cdd:cd18003   151 QRRLLLTGTPLQNSLMELWSLMHFLMPHIF--QSHQEFKEWFSNPLTA 196
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 20-148 1.26e-25

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: 105.92  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  20 FAPGLSCVTYTGDKEERA-----------------RRQQDLRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAH 80
Cdd:cd18056    72 WAPDMYVVTYVGDKDSRAiirenefsfednairggKKASRMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAH 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755039  81 RLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 148
Cdd:cd18056   152 RLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF--HNLEGFLEEFADIAKEDQ 217
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 19-136 3.05e-25

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: 105.52  E-value: 3.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18064    86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 136
Cdd:cd18064   166 TNRLLLTGTPLQNNLHELWALLNFLLPDVF--NSAEDF 201
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 18-151 3.76e-24

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: 101.81  E-value: 3.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEERA------RRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHR 91
Cdd:cd18002    70 SRFVPQFKVLPYWGNPKDRKvlrkfwDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWK 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958755039  92 TLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCY-QDIEKESKSAS 151
Cdd:cd18002   150 TLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLF--DSHDEFNEWFsKDIESHAENKT 208
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 19-136 4.30e-24

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: 101.63  E-value: 4.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18065    86 RWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958755039  99 VFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 136
Cdd:cd18065   166 TNRLLLTGTPLQNNLHELWALLNFLLPDVF--NSADDF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 250-362 1.09e-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: 96.51  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 250 GKLHLLDRLLAFlySGGHRVLLFSQMTHMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQPIFVfLLSTRAGGV 329
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958755039 330 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 362
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 18-128 4.71e-22

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: 95.33  E-value: 4.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTGDKEERARrqqdLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 97
Cdd:cd18012    73 AKFAPELKVLVIHGTKRKREK----LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALK 148

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958755039  98 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18012   149 ADHRLALTGTPIENHLGELWSIFDFLNPGLL 179
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 14-148 4.93e-21

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 92.41  E-value: 4.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRPARFAPGLSCVTYTGDKEERARRQQD---LRQESG--------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRL 82
Cdd:cd18058    64 WEREFRTWTEMNAIVYHGSQISRQMIQQYemyYRDEQGnplsgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRL 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755039  83 KNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 148
Cdd:cd18058   144 KNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTEEQ 207
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 27-128 6.38e-20

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: 89.65  E-value: 6.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  27 VTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDAS-FLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLT 105
Cdd:cd18004    90 VTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLT 169

                          90       100
                  ....*....|....*....|...
gi 1958755039 106 GTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18004   170 GTPIQNDLDEFFALVDFVNPGIL 192
HELICc smart00490
helicase superfamily c-terminal domain;
280-362 2.56e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.03  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  280 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgKQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 359
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 1958755039  360 RIG 362
Cdd:smart00490  80 RAG 82
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 14-148 2.93e-19

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: 87.39  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRPARFAPGLSCVTYTGDKEERARRQ-----------QDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRL 82
Cdd:cd18059    64 WEREFRTWTELNVVVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRL 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755039  83 KNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 148
Cdd:cd18059   144 KNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTEEQ 207
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 623-773 8.27e-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: 83.46  E-value: 8.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 623 SINYVSGDVTHPQageEDAVIVHCVDDSGRWGRGGLFTALE--ARSAEPRKIYELAGkmkdlsLGDVLLFPiddkesRDK 700
Cdd:cd02901     1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKkpGRVEELRAQCKKKL------LGGVAVLK------RDG 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958755039 701 GQDLLALVVAQHRDRTNvlsgIKMAALEEGLKK-ILLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 773
Cdd:cd02901    66 VKRYIYYLITKKSYGPK----PTYEALRSSLEElREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 49-148 3.04e-18

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: 84.33  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  49 FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18060   110 FDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQF 189

                          90       100
                  ....*....|....*....|
gi 1958755039 129 CREQveDFVQCYQDIEKESK 148
Cdd:cd18060   190 PSES--EFLKDFGDLKTEEQ 207
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 18-129 6.72e-17

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: 80.88  E-value: 6.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  18 ARFAPGLSCVTYTG-DKEERARRQQDLRQESGfhVLLTTYEICLKDASFLKS-----FSWSVLAVDEAHRLKNQSSLLHR 91
Cdd:cd18001    69 AKWTPGLRVKVFHGtSKKERERNLERIQRGGG--VLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAK 146

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958755039  92 TLSEFSVVFRLLLTGTPIQNSLQELYSLLsvvepDLFC 129
Cdd:cd18001   147 SLREIPAKNRIILTGTPIQNNLKELWALF-----DFAC 179
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 19-128 1.96e-16

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: 79.72  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSV 98
Cdd:cd18063    94 KWAPSVVKISYKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYV 172

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958755039  99 V-FRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18063   173 ApRRILLTGTPLQNKLPELWALLNFLLPTIF 203
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 14-130 2.15e-16

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: 78.13  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRPARFAPGLSCVTYTGDKEERARRQQDLRQESGF----HVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 89
Cdd:cd18000    72 WWPPFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVvgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958755039  90 HRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR 130
Cdd:cd18000   152 TLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYLLR 192
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 19-128 2.82e-16

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: 79.32  E-value: 2.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAPGLSCVTYTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL-SEFS 97
Cdd:cd18062    94 KWAPSVVKVSYKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 172

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958755039  98 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18062   173 APRRLLLTGTPLQNKLPELWALLNFLLPTIF 203
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 19-119 5.86e-16

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: 77.78  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAP--GLSCVTYTGDKEERARrqqdLRQESGFH-VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 95
Cdd:cd17999    76 KYFPnaFLKPLAYVGPPQERRR----LREQGEKHnVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQ 151

                          90       100
                  ....*....|....*....|....
gi 1958755039  96 FSVVFRLLLTGTPIQNSLQELYSL 119
Cdd:cd17999   152 LKANHRLILSGTPIQNNVLELWSL 175
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 14-148 8.43e-16

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: 77.35  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  14 WGRPARFAPGLSCVTYTGDKEERARRQQD-----------LRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRL 82
Cdd:cd18061    64 WEREFRTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRL 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958755039  83 KNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 148
Cdd:cd18061   144 KNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTEEQ 207
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 11-128 1.77e-15

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: 76.65  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  11 RWAWGRparfapgLSCVTYTGDKEERARRQQDLRQEsgfhVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLH 90
Cdd:cd18005    91 TWGHFE-------VGVYHGSRKDDELEGRLKAGRLE----VVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLT 159

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958755039  91 RTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18005   160 QAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGAL 197
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 37-130 8.39e-14

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: 71.93  E-value: 8.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  37 ARRQQDLRQESGFHVLLTTYEI----------------CLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVF 100
Cdd:cd18008    98 SKRIKSIEELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAER 177

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958755039 101 RLLLTGTPIQNSLQELYSLLSVVEPDLFCR 130
Cdd:cd18008   178 RWCLTGTPIQNSLDDLYSLLRFLRVEPFGD 207
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 51-152 2.34e-13

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: 70.40  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  51 VLLTTYEICLKDAS--------FLKSFSW------SVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQEL 116
Cdd:cd18007   115 VLLIGYELFRNLASnattdprlKQEFIAAlldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEY 194

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958755039 117 YSLLSVVEPDLFcrEQVEDFVQCY-QDIEKESKSASE 152
Cdd:cd18007   195 WTMVDFARPKYL--GTLKEFKKKFvKPIEAGQCVDST 229
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 49-125 9.41e-13

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: 68.72  E-value: 9.41e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755039  49 FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEP 125
Cdd:cd18066   108 YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 37-121 1.08e-12

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: 68.65  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  37 ARRQQDLRQESGFHVLLTTYEICL-----KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQN 111
Cdd:cd18071   107 GERNRDPKLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQN 186

                          90
                  ....*....|
gi 1958755039 112 SLQELYSLLS 121
Cdd:cd18071   187 SPKDLGSLLS 196
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 51-127 1.12e-11

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: 65.57  E-value: 1.12e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755039  51 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDL 127
Cdd:cd18067   118 VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
DEXDc smart00487
DEAD-like helicases superfamily;
5-136 7.62e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.43  E-value: 7.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039    5 AASWETRWAwgRPARFAPGLSCVTYTGDKEERARRQQdlrQESGFHVLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRL 82
Cdd:smart00487  67 AEQWAEELK--KLGPSLGLKVVGLYGGDSKREQLRKL---ESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRL 141

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039   83 KNQS--SLLHRTLSEF-SVVFRLLLTGTP---IQNSLQELYSLLSVVEPDLFCREQVEDF 136
Cdd:smart00487 142 LDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 61-128 2.10e-08

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: 55.37  E-value: 2.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958755039  61 KDASFLKSFSWSVLAVDEAHRLKN----QSSLLHRTLSEFSVVFR--LLLTGTPIQNSLQELYSLLSVVEPDLF 128
Cdd:cd18011   111 ERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPGRF 184
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 77-127 5.23e-07

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: 51.81  E-value: 5.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958755039  77 DEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDL 127
Cdd:cd18068   162 DEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNL 212
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 51-141 6.55e-07

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: 51.05  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  51 VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSVVFR----LLLTGTPIQNSLQELYSLLSVVEPD 126
Cdd:cd18010    91 VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKA--KRTKAALPLLKRakrvILLSGTPALSRPIELFTQLDALDPK 168

                          90
                  ....*....|....*
gi 1958755039 127 LFcREQVEDFVQCYQ 141
Cdd:cd18010   169 LF-GRFHDFGRRYCA 182
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 37-152 7.42e-07

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: 51.33  E-value: 7.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  37 ARRQQDLRQESGFHVLLTTYEICLKD---------ASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGT 107
Cdd:cd18072   109 PNRERIGEVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGT 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958755039 108 PIQNSLQELYSLLSVVEPDLFcreqvEDFVQCYQDIEKESKSASE 152
Cdd:cd18072   189 PIQNNLLDMYSLLKFLRCSPF-----DDLKVWKKQVDNKSRKGGE 228
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
44-519 1.40e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.95  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  44 RQESGFHVLLTTYEIcLKDASFLKSFS--WSVLAVDEAHRLknQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSlls 121
Cdd:COG1061   160 KKDSDAPITVATYQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATPFRSDGREILL--- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 122 vvepDLFCReqvedfvqcyqdiekesksaselhrllrpfllrrvkaqVATELPKKTevviyhgmsALQKKYYK-AILMKD 200
Cdd:COG1061   234 ----FLFDG--------------------------------------IVYEYSLKE---------AIEDGYLApPEYYGI 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 201 LDAFENETAKKVKLQNVLTQLrkcVDHpylfdgvepepfevgehliEASGKLHLLDRLLAFlYSGGHRVLLFSQMTHMLD 280
Cdd:COG1061   263 RVDLTDERAEYDALSERLREA---LAA-------------------DAERKDKILRELLRE-HPDDRKTLVFCSSVDHAE 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 281 ILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQPIfVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHR 360
Cdd:COG1061   320 ALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLR 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 361 IGQNKS-VKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHFTLGAQKPAAEADLQLSEILKFGLDKLLSSEGSSMDEI 439
Cdd:COG1061   399 PAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLL 478

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 440 DLKSILGETKDGQWTPDALPAAAEGESREQEEGKNHMYLFEGRDYSKEPSKEDRKSFEQLVNLQKTLLEKTSHGGRSLRN 519
Cdd:COG1061   479 VLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKE 558
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
 213-381 1.98e-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: 50.40  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 213 KLQNVLTQLRKCVDHPYLF-DGVEPEPF---EVGEHLIEASGKLHLLDRLLAFL----YSGGHRVLLFSQMTHMLDILQD 284
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039 285 YMDYRGYSYERVDG-SVRGEERHLAIKNFGKQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 357
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207

                         170       180
                  ....*....|....*....|....
gi 1958755039 358 AHRIGQNKSVKVIRLIGRDTVEEI 381
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 36-126 2.62e-06

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: 49.43  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  36 RARRQQDLRQESGfhVLLTTYEIC-LKDASflksfswSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQ 114
Cdd:cd18069   110 RAKVIEDWVKDGG--VLLMGYEMFrLRPGP-------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180

                          90
                  ....*....|..
gi 1958755039 115 ELYSLLSVVEPD 126
Cdd:cd18069   181 EYWCMVDFVRPD 192
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 317-373 8.98e-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: 8.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755039 317 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 373
Cdd:cd18785    22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 19-129 3.42e-03

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: 40.02  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  19 RFAP-GLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFS-----------------------WSVL 74
Cdd:cd18070    91 RHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkryeappsplvlvewWRVC 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958755039  75 aVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFC 129
Cdd:cd18070   171 -LDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 26-108 3.77e-03

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: 38.44  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755039  26 CVTYTGDKEERARRQQDLRQESGFHVLLTTY---EICLKDASFLKSFsWSVLAVDEAHRLKnqSSLLHRTLSEFSVVFRL 102
Cdd:cd17926    64 FEDFLGDSSIGLIGGGKKKDFDDANVVVATYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRL 140


                  ....*.
gi 1958755039 103 LLTGTP 108
Cdd:cd17926   141 GLTATP 146
 
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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