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Conserved domains on  [gi|672043624|ref|XP_008759575|]
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chromodomain-helicase-DNA-binding protein 1-like isoform X4 [Rattus norvegicus]

Protein Classification

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
70-616 1.62e-148

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: 464.27  E-value: 1.62e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   70 RLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC 148
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  149 VTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTG 228
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  229 TPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGM 307
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGM 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  308 SALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYS 386
Cdd:PLN03142  407 SQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKE 485
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  387 GGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFV 464
Cdd:PLN03142  486 RDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILY 565
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  465 DSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILK 544
Cdd:PLN03142  566 DSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVR 641
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  545 FGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYS 607
Cdd:PLN03142  642 YGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI 721

                  ....*....
gi 672043624  608 kEPSKEDRK 616
Cdd:PLN03142  722 -DPPKRERK 729
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
745-852 1.32e-60

macrodomain superfamily; 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. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


The actual alignment was detected with superfamily member cd03331:

Pssm-ID: 469581  Cd Length: 152  Bit Score: 202.49  E-value: 1.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 745 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 823
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100
                 ....*....|....*....|....*....
gi 672043624 824 QDLLALVVAQHRDRTNVLSGIKMAALEEG 852
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETG 109
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
70-616 1.62e-148

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 464.27  E-value: 1.62e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   70 RLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC 148
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  149 VTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTG 228
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  229 TPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGM 307
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGM 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  308 SALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYS 386
Cdd:PLN03142  407 SQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKE 485
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  387 GGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFV 464
Cdd:PLN03142  486 RDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILY 565
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  465 DSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILK 544
Cdd:PLN03142  566 DSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVR 641
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  545 FGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYS 607
Cdd:PLN03142  642 YGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI 721

                  ....*....
gi 672043624  608 kEPSKEDRK 616
Cdd:PLN03142  722 -DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-520 3.14e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 384.96  E-value: 3.14e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   2 LLRRVNARELCPLAAARGSEGAGPWAEPFGMAGGSPRFLQALRAGDRPEPVRTRVQEQDLQEW---------GLTGiRLR 72
Cdd:COG0553  165 LALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLrealeslpaGLKA-TLR 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  73 SYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYT 152
Cdd:COG0553  244 PYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLD 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 153 GDKEerarRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQ 232
Cdd:COG0553  323 GTRE----RAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVE 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 233 NSLQELYSLLSVVEPDLFcrEQVEDFVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQVATELPKKTEVVI 303
Cdd:COG0553  399 NRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALERLRRL-------LrpfllrrtKEDVLKDLPEKTEETL 469
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 304 YHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRL 380
Cdd:COG0553  470 YVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLEL 541
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 381 LAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAGGVGMNLTAAD 459
Cdd:COG0553  542 LEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAAD 621
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672043624 460 TVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 520
Cdd:COG0553  622 HVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
71-274 3.74e-121

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: 365.22  E-value: 3.74e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 230
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 672043624 231 IQNSLQELYSLLSVVEPDLFCREQVEDFVQCYQDIEKESKSASE 274
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEE 204
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
74-353 1.05e-75

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: 248.75  E-value: 1.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   74 YQLEGVNWLVQCFHG-QNGCILGDEMGLGKTCQTIALLIYLVG-RLNDEGPFLILCPLSVLSNWKEEMERFA--PGLSCV 149
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  150 TYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGT 229
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  230 PIQNSLQELYSLLSVVEPDLFCREQVED--FVQCYQdIEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGM 307
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 672043624  308 SALQKKYYKA-ILMKDLDAFENETA---KKVKLQNVLTQLRKCVDHPYLF 353
Cdd:pfam00176 240 SKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
745-852 1.32e-60

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: 202.49  E-value: 1.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 745 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 823
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100
                 ....*....|....*....|....*....
gi 672043624 824 QDLLALVVAQHRDRTNVLSGIKMAALEEG 852
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETG 109
DEXDc smart00487
DEAD-like helicases superfamily;
66-258 8.56e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.51  E-value: 8.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624    66 LTGIRLRSYQLEGVNWLVQcfhGQNGCILGDEMGLGKT-CQTIALLIYLvgRLNDEGPFLILCPLSVL-SNWKEEMERFA 143
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLS---GLRDVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   144 P---GLSCVTYTGDKEERARRQQdlrQESGFHVLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLS 216
Cdd:smart00487  79 PslgLKVVGLYGGDSKREQLRKL---ESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 672043624   217 EF-SVVFRLLLTGTP---IQNSLQELYSLLSVVEPDLFCREQVEDF 258
Cdd:smart00487 156 LLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
70-616 1.62e-148

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 464.27  E-value: 1.62e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   70 RLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC 148
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  149 VTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTG 228
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  229 TPIQNSLQELYSLLSVVEPDLFCR-EQVEDFVQCYQDiEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGM 307
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGM 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  308 SALQKKYYKAILMKDLDAFeNETAKKVKLQNVLTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAFLYS 386
Cdd:PLN03142  407 SQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKE 485
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  387 GGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGK--QPIFVFLLSTRAGGVGMNLTAADTVIFV 464
Cdd:PLN03142  486 RDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILY 565
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  465 DSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHftLGAQKPAAEADLQlsEILK 544
Cdd:PLN03142  566 DSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGR--LAEQKTVNKDELL--QMVR 641
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  545 FGLDKLLSSEGSSMDEIDLKSIL--GE-------TKDGQWTPDALPAAAEGES--------REQEEGKNHMYLFEGRDYS 607
Cdd:PLN03142  642 YGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTAelydfddeDDKDENKLDFKKIVSDNWI 721

                  ....*....
gi 672043624  608 kEPSKEDRK 616
Cdd:PLN03142  722 -DPPKRERK 729
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-520 3.14e-122

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 384.96  E-value: 3.14e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   2 LLRRVNARELCPLAAARGSEGAGPWAEPFGMAGGSPRFLQALRAGDRPEPVRTRVQEQDLQEW---------GLTGiRLR 72
Cdd:COG0553  165 LALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLrealeslpaGLKA-TLR 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  73 SYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVTYT 152
Cdd:COG0553  244 PYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLD 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 153 GDKEerarRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQ 232
Cdd:COG0553  323 GTRE----RAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVE 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 233 NSLQELYSLLSVVEPDLFcrEQVEDFVQCYQD-IEKESKSASELHRLLrpfllrrV--------KAQVATELPKKTEVVI 303
Cdd:COG0553  399 NRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALERLRRL-------LrpfllrrtKEDVLKDLPEKTEETL 469
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 304 YHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnVLTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRL 380
Cdd:COG0553  470 YVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLEL 541
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 381 LAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAGGVGMNLTAAD 459
Cdd:COG0553  542 LEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAAD 621
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672043624 460 TVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 520
Cdd:COG0553  622 HVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
71-274 3.74e-121

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: 365.22  E-value: 3.74e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 230
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 672043624 231 IQNSLQELYSLLSVVEPDLFCREQVEDFVQCYQDIEKESKSASE 274
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEE 204
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
71-252 1.22e-78

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: 252.49  E-value: 1.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQDLRQESgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 230
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDK-FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                        170       180
                 ....*....|....*....|..
gi 672043624 231 IQNSLQELYSLLSVVEPDLFCR 252
Cdd:cd17919  160 LQNNLEELWALLDFLDPPFLLR 181
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
74-353 1.05e-75

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: 248.75  E-value: 1.05e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   74 YQLEGVNWLVQCFHG-QNGCILGDEMGLGKTCQTIALLIYLVG-RLNDEGPFLILCPLSVLSNWKEEMERFA--PGLSCV 149
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  150 TYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGT 229
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  230 PIQNSLQELYSLLSVVEPDLFCREQVED--FVQCYQdIEKESKSASELHRLLRPFLLRRVKAQVATELPKKTEVVIYHGM 307
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPFGSLSTFRnwFDRPIE-RGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 672043624  308 SALQKKYYKA-ILMKDLDAFENETA---KKVKLQNVLTQLRKCVDHPYLF 353
Cdd:pfam00176 240 SKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
71-273 4.70e-73

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: 238.79  E-value: 4.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd17993    2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERAR-RQQDLRQESG----FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLL 225
Cdd:cd17993   82 YLGDIKSRDTiREYEFYFSQTkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 672043624 226 LTGTPIQNSLQELYSLLSVVEPDLF-CREQVEDfvqcYQDIEKESKSAS 273
Cdd:cd17993  162 ITGTPLQNSLKELWALLHFLMPGKFdIWEEFEE----EHDEEQEKGIAD 206
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
71-269 1.12e-67

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 224.43  E-value: 1.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPgLSCVT 150
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQ-----------DLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 219
Cdd:cd17995   80 YHGSGESRQIIQQyemyfkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 672043624 220 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREqvEDFVQCYQDIEKES 269
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSS--EEFLEEFGDLKTAE 207
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
70-258 6.34e-65

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: 216.80  E-value: 6.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  70 RLRSYQLEGVNWLVQCFH-GQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC 148
Cdd:cd17997    3 TMRDYQIRGLNWLISLFEnGING-ILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 149 VTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTG 228
Cdd:cd17997   82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 672043624 229 TPIQNSLQELYSLLSVVEPDLFcrEQVEDF 258
Cdd:cd17997  162 TPLQNNLHELWALLNFLLPDVF--TSSEDF 189
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
68-274 5.28e-64

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: 214.94  E-value: 5.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  68 GIRLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDeGPFLILCPLSVLSNWKEEMERFAPGL 146
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWeNGING-ILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 147 SCVTYTGDKEER--ARRQQDLRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVF 222
Cdd:cd18009   79 PVLLYHGTKEERerLRKKIMKREGTLqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDN 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672043624 223 RLLLTGTPIQNSLQELYSLLSVVEPDLFCR----EQVEDFVQCYQDIEKESKSASE 274
Cdd:cd18009  159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDlssfESWFDFSSLSDNAADISNLSEE 214
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
71-260 1.57e-62

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: 210.69  E-value: 1.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQ-NGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCV 149
Cdd:cd17996    4 LKEYQLKGLQWMVSLYNNNlNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 150 TYTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE-FSVVFRLLLTG 228
Cdd:cd17996   83 VYKGTPDVRKKLQSQIRA-GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTG 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043624 229 TPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQ 260
Cdd:cd17996  162 TPLQNNLPELWALLNFLLPKIF--KSCKTFEQ 191
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
48-258 2.66e-61

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 207.55  E-value: 2.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  48 RPEPVRTRVQEQDLqewGLTGIRLRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILC 127
Cdd:cd18054    1 RPRFVALKKQPSYI---GGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 128 PLSVLSNWKEEMERFAPGLSCVTYTGDKEERA--RRQQDLRQESG---FHVLLTTYEICLKDASFLKSFSWSVLAVDEAH 202
Cdd:cd18054   78 PLSTLTSWQREFEIWAPEINVVVYIGDLMSRNtiREYEWIHSQTKrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAH 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672043624 203 RLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 258
Cdd:cd18054  158 RLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF--EFWEDF 211
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
745-852 1.32e-60

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: 202.49  E-value: 1.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 745 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEARSAEPRKIYELAGKMKDLSLGDVLLFPIDDKESRDKG 823
Cdd:cd03331    1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100
                 ....*....|....*....|....*....
gi 672043624 824 QDLLALVVAQHRDRTNVLSGIKMAALEEG 852
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETG 109
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
71-270 6.64e-56

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 191.11  E-value: 6.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDkeerarrqqdlrqesgfHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 230
Cdd:cd17994   81 YVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 672043624 231 IQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 270
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERF--NNLQGFLEEFADISKEDQ 181
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
71-268 3.62e-54

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: 187.17  E-value: 3.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQ-CFHGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCV 149
Cdd:cd18003    1 LREYQHIGLDWLATlYEKNLNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 150 TYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGT 229
Cdd:cd18003   80 TYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672043624 230 PIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKE 268
Cdd:cd18003  160 PLQNSLMELWSLMHFLMPHIF--QSHQEFKEWFSNPLTA 196
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
71-250 7.83e-54

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: 186.23  E-value: 7.83e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYlVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18012    5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARrqqdLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTP 230
Cdd:cd18012   84 IHGTKRKREK----LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                        170       180
                 ....*....|....*....|
gi 672043624 231 IQNSLQELYSLLSVVEPDLF 250
Cdd:cd18012  160 IENHLGELWSIFDFLNPGLL 179
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
71-273 1.69e-53

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


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 185.79  E-value: 1.69e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCV 149
Cdd:cd18002    1 LKEYQLKGLNWLANLYeQGING-ILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 150 TYTGDKEERA------RRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFR 223
Cdd:cd18002   80 PYWGNPKDRKvlrkfwDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672043624 224 LLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCY-QDIEKESKSAS 273
Cdd:cd18002  160 LLLTGTPIQNSMAELWALLHFIMPTLF--DSHDEFNEWFsKDIESHAENKT 208
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
71-250 2.29e-53

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: 183.74  E-value: 2.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVgRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERAR-RQQDLRQESGFHVLLTTYEICL---KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLL 226
Cdd:cd17998   80 YYGSQEERKHlRYDILKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                        170       180
                 ....*....|....*....|....
gi 672043624 227 TGTPIQNSLQELYSLLSVVEPDLF 250
Cdd:cd17998  160 TGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
65-250 2.75e-53

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: 185.25  E-value: 2.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  65 GLTGIRLRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAP 144
Cdd:cd18053   15 GHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 145 GLSCVTYTGDKEER--ARRQQDLRQESG---FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 219
Cdd:cd18053   95 QMNAVVYLGDINSRnmIRTHEWMHPQTKrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFK 174
                        170       180       190
                 ....*....|....*....|....*....|.
gi 672043624 220 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18053  175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKF 205
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
371-495 5.14e-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: 5.14e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 371 SGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQP-IFVFLLSTRAG 449
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 672043624 450 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 495
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
63-258 3.20e-49

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: 174.47  E-value: 3.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  63 EWGltgiRLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMER 141
Cdd:cd18064   12 KWG----KLRDYQVRGLNWLISLYeNGING-ILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 142 FAPGLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVV 221
Cdd:cd18064   87 WVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 672043624 222 FRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 258
Cdd:cd18064  167 NRLLLTGTPLQNNLHELWALLNFLLPDVF--NSAEDF 201
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
71-270 4.54e-49

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: 173.27  E-value: 4.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERA-----------------RRQQDLRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 211
Cdd:cd18055   81 YTGDKDSRAiirenefsfddnavkggKKAFKMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672043624 212 HRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 270
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
71-270 9.71e-49

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: 172.56  E-value: 9.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQD-----------------LRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 211
Cdd:cd18057   81 YTGDKESRSVIRENefsfednairsgkkvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672043624 212 HRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 270
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ 217
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
66-258 7.23e-48

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: 170.20  E-value: 7.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  66 LTGIRLRSYQLEGVNWLVQCF-HGQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAP 144
Cdd:cd18065   11 VKGGTLRDYQVRGLNWMISLYeNGVNG-ILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 145 GLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRL 224
Cdd:cd18065   90 SLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL 169
                        170       180       190
                 ....*....|....*....|....*....|....
gi 672043624 225 LLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDF 258
Cdd:cd18065  170 LLTGTPLQNNLHELWALLNFLLPDVF--NSADDF 201
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
71-270 2.96e-47

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: 168.32  E-value: 2.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERA-----------------RRQQDLRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 211
Cdd:cd18056   81 YVGDKDSRAiirenefsfednairggKKASRMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672043624 212 HRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCYQDIEKESK 270
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF--HNLEGFLEEFADIAKEDQ 217
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
71-270 1.64e-44

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: 160.21  E-value: 1.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSC 148
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLseIFLMGI---RGPFLIIAPLSTITNWEREFRTWTE-MNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 149 VTYTGDKEERARRQQD---LRQESG--------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 217
Cdd:cd18058   77 IVYHGSQISRQMIQQYemyYRDEQGnplsgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 672043624 218 FSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 270
Cdd:cd18058  157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTEEQ 207
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
71-250 5.27e-44

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: 159.37  E-value: 5.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQ-----NGCILGDEMGLGKTCQTIALLIYLVGRLNDEGP----FLILCPLSVLSNWKEEMER 141
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRrgyggGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 142 FAPG--LSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDAS-FLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEF 218
Cdd:cd18004   81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKALNSL 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043624 219 SVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18004  161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGIL 192
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
71-250 7.86e-44

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: 159.08  E-value: 7.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDE--------------------GPFLILCPLS 130
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 131 VLSNWKEEMERFAP-GLSCVTYTGDKEERARRQQDLRQEsgfhVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSS 209
Cdd:cd18005   81 VLYNWKDELDTWGHfEVGVYHGSRKDDELEGRLKAGRLE----VVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 672043624 210 LLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18005  157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGAL 197
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
71-270 3.01e-42

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 153.67  E-value: 3.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSC 148
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLqeVYNVGI---HGPFLVIAPLSTITNWEREFNTWTE-MNT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 149 VTYTGDKEERARRQQD---LRQESG--------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 217
Cdd:cd18060   77 IVYHGSLASRQMIQQYemyCKDSRGrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 672043624 218 FSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQveDFVQCYQDIEKESK 270
Cdd:cd18060  157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSES--EFLKDFGDLKTEEQ 207
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
71-250 4.54e-42

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: 154.07  E-value: 4.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18063   24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVV-FRLLLTGT 229
Cdd:cd18063  104 YKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGT 182
                        170       180
                 ....*....|....*....|.
gi 672043624 230 PIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18063  183 PLQNKLPELWALLNFLLPTIF 203
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
71-250 6.45e-42

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: 153.66  E-value: 6.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSCVT 150
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL-SEFSVVFRLLLTGT 229
Cdd:cd18062  104 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGT 182
                        170       180
                 ....*....|....*....|.
gi 672043624 230 PIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18062  183 PLQNKLPELWALLNFLLPTIF 203
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
71-270 1.11e-41

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: 152.11  E-value: 1.11e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLILCPLSVLSNWKEEMERFAPgLSC 148
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLyeIYLKGI---HGPFLVIAPLSTIPNWEREFRTWTE-LNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 149 VTYTGDKEERARRQ-----------QDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 217
Cdd:cd18059   77 VVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 672043624 218 FSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 270
Cdd:cd18059  157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTEEQ 207
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
71-252 9.97e-41

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 148.24  E-value: 9.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQcFHGQN-GCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGL--- 146
Cdd:cd18000    1 LFKYQQTGVQWLWE-LHCQRvGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvv 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 147 ---SCVTYTGDKEERARRQQDLRQESGF----HVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 219
Cdd:cd18000   80 vlhSSGSGTGSEEKLGSIERKSQLIRKVvgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 672043624 220 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR 252
Cdd:cd18000  160 TPHRLILSGTPIQNNLKELWSLFDFVFPPYLLR 192
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
71-251 5.23e-38

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: 141.74  E-value: 5.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIAlliYLVGrLNDEGPF---LILCPLSVLSNWKEEMERFAPGLS 147
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICA---FLSG-MFDSGLIksvLVVMPTSLIPHWVKEFAKWTPGLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 148 CVTYTG-DKEERARRQQDLRQESGfhVLLTTYEICLKDASFLKS-----FSWSVLAVDEAHRLKNQSSLLHRTLSEFSVV 221
Cdd:cd18001   77 VKVFHGtSKKERERNLERIQRGGG--VLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAK 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 672043624 222 FRLLLTGTPIQNSLQELYSLLsvvepDLFC 251
Cdd:cd18001  155 NRIILTGTPIQNNLKELWALF-----DFAC 179
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
71-270 6.70e-38

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 141.30  E-value: 6.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCILGDEMGLGKTCQTIALLiYLVGRLNDEGPFLILCPLSVLSNWKEEMeRFAPGLSCVT 150
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 151 YTGDKEERARRQQD-----------LRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 219
Cdd:cd18061   79 YHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 672043624 220 VVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCREQVedFVQCYQDIEKESK 270
Cdd:cd18061  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTEEQ 207
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
71-241 3.33e-36

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: 136.71  E-value: 3.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVqcF------HGqngcILGDEMGLGKTCQTIALL---IYLVGRLNDEGPF--LILCPLSVLSNWKEEM 139
Cdd:cd17999    1 LRPYQQEGINWLA--FlnkynlHG----ILCDDMGLGKTLQTLCILasdHHKRANSFNSENLpsLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 140 ERFAP--GLSCVTYTGDKEERARrqqdLRQESGFH-VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLS 216
Cdd:cd17999   75 KKYFPnaFLKPLAYVGPPQERRR----LREQGEKHnVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVK 150
                        170       180
                 ....*....|....*....|....*
gi 672043624 217 EFSVVFRLLLTGTPIQNSLQELYSL 241
Cdd:cd17999  151 QLKANHRLILSGTPIQNNVLELWSL 175
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
71-252 1.42e-35

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: 135.11  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCfhgqnGCILGDEMGLGKTCQTIALL-----------------IYLVGRLNDEGPFLILCPLSVLS 133
Cdd:cd18008    1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 134 NWKEEMERF--APGLSCVTYTGDKeeRARRQQDLRQesgFHVLLTTYEI----------------CLKDASFLKSFSWSV 195
Cdd:cd18008   76 QWKDEIEKHtkPGSLKVYVYHGSK--RIKSIEELSD---YDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYR 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672043624 196 LAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFCR 252
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGD 207
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
71-274 1.02e-32

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: 127.02  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVN--W--LVQCFHGQ---NGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFA 143
Cdd:cd18007    1 LKPHQVEGVRflWsnLVGTDVGSdegGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 144 P-------GLSCVTYTGDKEERARRQQDLRQESGfhVLLTTYEICLKDAS--------FLKSFSW------SVLAVDEAH 202
Cdd:cd18007   81 PpdlrpllVLVSLSASKRADARLRKINKWHKEGG--VLLIGYELFRNLASnattdprlKQEFIAAlldpgpDLLVLDEGH 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672043624 203 RLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcrEQVEDFVQCY-QDIEKESKSASE 274
Cdd:cd18007  159 RLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYL--GTLKEFKKKFvKPIEAGQCVDST 229
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
71-249 2.40e-30

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: 120.27  E-value: 2.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQ-----NGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFL----ILCPLSVLSNWKEEMER 141
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRrirgsHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 142 F-APGLSCVTYTG-DKEERARRQQDLRQESGFH----VLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL 215
Cdd:cd18067   81 WlGGRLQPLAIDGgSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 672043624 216 SEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDL 249
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
71-247 2.08e-29

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: 117.25  E-value: 2.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQN-----GCILGDEMGLGKTCQTIALlIYLVGRLNDEGP------FLILCPLSVLSNWKEEM 139
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRvnerfGAILADEMGLGKTLQCISL-IWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 140 ERFAPGLSCVTYTGDKEERARrqqDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 219
Cdd:cd18066   80 QKWLGSERIKVFTVDQDHKVE---EFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLS 156
                        170       180
                 ....*....|....*....|....*...
gi 672043624 220 VVFRLLLTGTPIQNSLQELYSLLSVVEP 247
Cdd:cd18066  157 CERRIILTGTPIQNDLQEFFALIDFVNP 184
DEXDc smart00487
DEAD-like helicases superfamily;
66-258 8.56e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.51  E-value: 8.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624    66 LTGIRLRSYQLEGVNWLVQcfhGQNGCILGDEMGLGKT-CQTIALLIYLvgRLNDEGPFLILCPLSVL-SNWKEEMERFA 143
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLS---GLRDVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   144 P---GLSCVTYTGDKEERARRQQdlrQESGFHVLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLS 216
Cdd:smart00487  79 PslgLKVVGLYGGDSKREQLRKL---ESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 672043624   217 EF-SVVFRLLLTGTP---IQNSLQELYSLLSVVEPDLFCREQVEDF 258
Cdd:smart00487 156 LLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
71-263 9.96e-29

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: 114.61  E-value: 9.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQcfhgQNG-CILGDEMGLGKTCQTIALLIYlvgrLNDEGPFLILCPLSVLSNWKEEMERFAPGLS-- 147
Cdd:cd18010    1 LLPFQREGVCFALR----RGGrVLIADEMGLGKTVQAIAIAAY----YREEWPLLIVCPSSLRLTWADEIERWLPSLPpd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 148 ---CVTYTGDKEERARRQqdlrqesgfhVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSVVFR- 223
Cdd:cd18010   73 diqVIVKSKDGLRDGDAK----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKA--KRTKAALPLLKRa 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 672043624 224 ---LLLTGTPIQNSLQELYSLLSVVEPDLFcREQVEDFVQCYQ 263
Cdd:cd18010  141 krvILLSGTPALSRPIELFTQLDALDPKLF-GRFHDFGRRYCA 182
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
91-243 2.70e-28

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: 114.10  E-value: 2.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  91 GCILGDEMGLGKTCQTIALLIYlvgrlndeGPFLILCPLSVLSNWKEEM-ERFAPG-LSCVTYTGdkeerARRQQDLRQE 168
Cdd:cd18071   50 GGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHG-----GERNRDPKLL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 169 SGFHVLLTTYEICL-----KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLS 243
Cdd:cd18071  117 SKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLS 196
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
71-250 7.61e-24

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: 100.44  E-value: 7.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQcfHGQNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLILCPLSVLSNWKEEM-ERFA-PGLSC 148
Cdd:cd18011    1 PLPHQIDAVLRALR--KPPVRLLLADEVGLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELqDKFGlPFLIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 149 VTYTGDKEERARRQQDLRqesgFHVLLTTYEIcLKD----ASFLKSFSWSVLAVDEAHRLKN----QSSLLHRTLSEFSV 220
Cdd:cd18011   78 DRETAAQLRRLIGNPFEE----FPIVIVSLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAK 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 672043624 221 VFR--LLLTGTPIQNSLQELYSLLSVVEPDLF 250
Cdd:cd18011  153 RARhvLLLTATPHNGKEEDFRALLSLLDPGRF 184
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
372-484 1.43e-23

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 96.13  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  372 GKLHLLDRLLAFlySGGHRVLLFSQMTHMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGKQPIFVfLLSTRAGGV 451
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 672043624  452 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 484
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
71-251 1.76e-19

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: 88.94  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQcfhgqNGCILGDEMGLGKTCQTIALLI------------YLVGRLNDE-------------GPFLI 125
Cdd:cd18070    1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILlhprpdndldaaDDDSDEMVCcpdclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 126 LCPLSVLSNWKEEMERFAP-GLSCVTYTGDKEERARRQQDLRQESGFHVLLTTYEICLKDASFLKSFS------------ 192
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkrye 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 193 -----------WSVLaVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFC 251
Cdd:cd18070  156 appsplvlvewWRVC-LDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
HELICc smart00490
helicase superfamily c-terminal domain;
402-484 3.56e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 3.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   402 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgKQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 481
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 672043624   482 RIG 484
Cdd:smart00490  80 RAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
71-249 2.74e-18

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: 85.32  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCF---------HGQNGCILGDEMGLGKTCQTIALL--IYLVGRLNDEGPFLILCPLSVLSNWKEEM 139
Cdd:cd18068    1 LKPHQVDGVQFMWDCCceslkktkkSPGSGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 140 ERFAPGL--------SCVTYTGDKEERARRQQDLRQESGfhVLLTTYEIC--------------LKDaSFLKSF---SWS 194
Cdd:cd18068   81 EKWQEGLkdeekievNELATYKRPQERSYKLQRWQEEGG--VMIIGYDMYrilaqernvksrekLKE-IFNKALvdpGPD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672043624 195 VLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSLLSVVEPDL 249
Cdd:cd18068  158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNL 212
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
91-274 1.48e-17

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: 82.91  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  91 GCILGDEMGLGKTCQTIALLIYLVGRLN-----------------DEGPF-----LILCPLSVLSNWKEEMERFAPG--L 146
Cdd:cd18072   22 GGILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVVCPASLVHQWKNEVESRVASnkL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 147 SCVTYTGdkeerARRQQDLRQESGFHVLLTTYEICLKD---------ASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 217
Cdd:cd18072  102 RVCLYHG-----PNRERIGEVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVCK 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672043624 218 FSVVFRLLLTGTPIQNSLQELYSLLSVVEPDLFcreqvEDFVQCYQDIEKESKSASE 274
Cdd:cd18072  177 LRAHARWALTGTPIQNNLLDMYSLLKFLRCSPF-----DDLKVWKKQVDNKSRKGGE 228
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
91-248 2.01e-17

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


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 82.17  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  91 GCILGDEMGLGKTCQTIALlIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLSC----------VTYTGD--KEER 158
Cdd:cd18069   30 GCILAHSMGLGKTLQVISF-LDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEAlpnvrprpfkVFILNDehKTTA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 159 ARRQ--QDLRQESGfhVLLTTYEIC-LKDASflksfswSVLAVDEAHRLKNQSSLLHRTLSEFSVVFRLLLTGTPIQNSL 235
Cdd:cd18069  109 ARAKviEDWVKDGG--VLLMGYEMFrLRPGP-------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNL 179
                        170
                 ....*....|...
gi 672043624 236 QELYSLLSVVEPD 248
Cdd:cd18069  180 IEYWCMVDFVRPD 192
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
37-641 9.74e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.14  E-value: 9.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  37 PRFLQALRAGDRPEPvrtrvqeqdlqewglTGIRLRSYQLEGVNWLVQCF--HGQNGCIlgdEM--GLGKTcqTIALLIy 112
Cdd:COG1061   62 LAEAEALEAGDEASG---------------TSFELRPYQQEALEALLAALerGGGRGLV---VAptGTGKT--VLALAL- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 113 lVGRLNDEGPFLILCP-LSVLSNWKEEMERFapglscvtyTGDKEERARRQqdlrqESGFHVLLTTYEIcLKDASFLKSF 191
Cdd:COG1061  121 -AAELLRGKRVLVLVPrRELLEQWAEELRRF---------LGDPLAGGGKK-----DSDAPITVATYQS-LARRAHLDEL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 192 S--WSVLAVDEAHRLknQSSLLHRTLSEFSVVFRLLLTGTPIQNSLQELYSllsvvepDLFCReqvedfvqcyqdiekes 269
Cdd:COG1061  185 GdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATPFRSDGREILL-------FLFDG----------------- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 270 ksaselhrllrpfllrrvkaqVATELPKKTevviyhgmsALQKKYYK-AILMKDLDAFENETAKKVKLQNVLTQLrkcVD 348
Cdd:COG1061  239 ---------------------IVYEYSLKE---------AIEDGYLApPEYYGIRVDLTDERAEYDALSERLREA---LA 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 349 HpylfdgvepepfevgehliEASGKLHLLDRLLAFlYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERH 428
Cdd:COG1061  286 A-------------------DAERKDKILRELLRE-HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKERE 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 429 LAIKNFGKQPIfVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKS-VKVIRLIGRDTVEEIVYRK 507
Cdd:COG1061  346 EILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAK 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 508 AASKLQLTNMVIEGGHFTLGAQKPAAEADLQLSEILKFGLDKLLSSEGSSMDEIDLKSILGETKDGQWTPDALPAAAEGE 587
Cdd:COG1061  425 DLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGK 504
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672043624 588 SREQEEGKNHMYLFEGRDYSKEPSKEDRKSFEQLVNLQKTLLEKTSHGGRSLRN 641
Cdd:COG1061  505 AEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKE 558
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
71-240 7.61e-13

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 68.53  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQcfHGQNGCILgdEMGLGKTCQTIALLIYLVgRLNDEGPFLILCPLSVLSN-WKEEMERFApGLSCV 149
Cdd:cd18013    1 PHPYQKVAINFIIE--HPYCGLFL--DMGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWN-HLRNL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 150 TY---TGDKEERARRQQdlrqeSGFHVLLTTYE----ICLKdasFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSVVF 222
Cdd:cd18013   75 TVsvaVGTERQRSKAAN-----TPADLYVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRP 144
                        170       180
                 ....*....|....*....|..
gi 672043624 223 R----LLLTGTPIQNSLQELYS 240
Cdd:cd18013  145 VikrlIGLTGTPSPNGLMDLWA 166
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
71-230 7.25e-11

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: 61.17  E-value: 7.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  71 LRSYQLEGVNWLVQCFHGQNGCIlgdEM--GLGKTCQTIALLIYLVgrlndEGPFLILCP-LSVLSNWKEEmerfapgls 147
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKER--------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 148 CVTYTGDKEERARRQQDLRQESGFHVLLTTY---EICLKDASFLKSFsWSVLAVDEAHRLKnqSSLLHRTLSEFSVVFRL 224
Cdd:cd17926   64 FEDFLGDSSIGLIGGGKKKDFDDANVVVATYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRL 140

                 ....*.
gi 672043624 225 LLTGTP 230
Cdd:cd17926  141 GLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
69-231 1.22e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 60.76  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   69 IRLRSYQLEGV-NWLVQCFHGQ-NGCIlgdEM--GLGKTcQTIALLIYLVGRLNDEGPFLILCP-LSVLSNWKEEMERFA 143
Cdd:pfam04851   2 LELRPYQIEAIeNLLESIKNGQkRGLI---VMatGSGKT-LTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  144 PG--LSCVTYTGDKeerarrqqDLRQESGFHVLLTTY-----EICLKDASFLKSFsWSVLAVDEAHRLknqSSLLHRTLS 216
Cdd:pfam04851  78 PNyvEIGEIISGDK--------KDESVDDNKIVVTTIqslykALELASLELLPDF-FDVIIIDEAHRS---GASSYRNIL 145
                         170
                  ....*....|....*.
gi 672043624  217 E-FSVVFRLLLTGTPI 231
Cdd:pfam04851 146 EyFKPAFLLGLTATPE 161
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
745-852 1.39e-08

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: 54.18  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 745 SINYVSGDVTHPQageEDAVIVHCVDDSGRWGRGGLFTALE--ARSAEPRKIYELAGkmkdlsLGDVLLFPiddkesRDK 822
Cdd:cd02901    1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKkpGRVEELRAQCKKKL------LGGVAVLK------RDG 65
                         90       100       110
                 ....*....|....*....|....*....|
gi 672043624 823 GQDLLALVVAQHRDRTNvlsgIKMAALEEG 852
Cdd:cd02901   66 VKRYIYYLITKKSYGPK----PTYEALRSS 91
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
90-229 3.27e-08

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 53.56  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  90 NGCILGDEMGLGKTcqTIALLIyLVGRLNDEGP-FLILCPLSVLSN-WKEEM-ERFAPGLSCVTYTGDKEERARRQQDLR 166
Cdd:cd00046    2 ENVLITAPTGSGKT--LAALLA-ALLLLLKKGKkVLVLVPTKALALqTAERLrELFGPGIRVAVLVGGSSAEEREKNKLG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672043624 167 QEsgfHVLLTTYEICLKDASFLKSFS---WSVLAVDEAHRL------KNQSSLLHRTLsEFSVVFRLLLTGT 229
Cdd:cd00046   79 DA---DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsrgALILDLAVRKA-GLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
99-233 7.70e-07

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 49.93  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   99 GLGKTcqTIALL--IYLVGRLNDEGPFLILCPLSVL-----SNWKEEMERFAPGLSCVtYTGDKeerarRQQDLRQESGF 171
Cdd:pfam00270  24 GSGKT--LAFLLpaLEALDKLDNGPQALVLAPTRELaeqiyEELKKLGKGLGLKVASL-LGGDS-----RKEQLEKLKGP 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672043624  172 HVLLTTYEIC---LKDASFLKSFSWsvLAVDEAHRL--KNQSSLLHRTLSEFSVVFR-LLLTGTPIQN 233
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNLKL--LVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATLPRN 161
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
335-503 1.66e-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: 50.79  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  335 KLQNVLTQLRKCVDHPYLF-DGVEPEPF---EVGEHLIEASGKLHLLDRLLAFL----YSGGHRVLLFSQMTHMLDILQD 406
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624  407 YMDYRGYSYERVDG-SVRGEERHLAIKNFGKQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 479
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207
                         170       180
                  ....*....|....*....|....
gi 672043624  480 AHRIGQNKSVKVIRLIGRDTVEEI 503
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
439-495 9.78e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.54  E-value: 9.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672043624 439 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 495
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
101-202 6.38e-03

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 38.72  E-value: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624 101 GKT-CQTIALLIYLvgrLNDEGP-FLILCPLSVLSNWKEE-----MERFAPGLSCVTYTGDKEERARRQQdLRQESgfHV 173
Cdd:cd17923   27 GKSlCYQLPILEAL---LRDPGSrALYLYPTKALAQDQLRslrelLEQLGLGIRVATYDGDTPREERRAI-IRNPP--RI 100
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 672043624 174 LLTTYE----ICLKDASFLKSF--SWSVLAVDEAH 202
Cdd:cd17923  101 LLTNPDmlhyALLPHHDRWARFlrNLRYVVLDEAH 135
AAA_22 pfam13401
AAA domain;
86-242 7.70e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672043624   86 FHGQNGCILGDEmGLGKTcqtiALLIYLVGRLNDEGPFLILCPLSVLSNWKEEMERFAPGLscvtytGDKEERARRQQDL 165
Cdd:pfam13401   3 FGAGILVLTGES-GTGKT----TLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRAL------GLPLSGRLSKEEL 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672043624  166 RQEsgFHVLLTTYeiclkdasflksFSWSVLAVDEAHRLKNQS-SLLHRTLSEFSVVFRLLLTGTPiqnslqELYSLL 242
Cdd:pfam13401  72 LAA--LQQLLLAL------------AVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLILVGTP------ELRELL 129
 
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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