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Conserved domains on  [gi|312922352|ref|NP_001099924|]
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transcription termination factor 2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
550-800 3.91e-142

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: 427.67  E-value: 3.91e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKE-KDRSLPVMWLSKNDSSVFTSTGTLIVC 628
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEeEKEKALTEWESKKDSTLVPSAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAKEIPTAKHEGEvpgaklsvegiSAPLLQ 708
Cdd:cd18072    81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEESR-----------SSPLFR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 788
Cdd:cd18072   150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                         250
                  ....*....|..
gi 312922352  789 LSILTKSLLLRR 800
Cdd:cd18072   230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
536-1122 5.59e-127

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.61  E-value: 5.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  536 KTAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILtkknQQKSKEKDRSlpvmwlsknd 615
Cdd:COG0553   228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL----ELKERGLARP---------- 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  616 ssvftstgTLIVCPASLIHHWKNEIEKRVNSnkLRIYLYHGP-NRIQHAKVLSTYDIVITTYSLLAKEIptakhegevpg 694
Cdd:COG0553   293 --------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI----------- 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  695 aklsvegisAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF 771
Cdd:COG0553   352 ---------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAF 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  772 -SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVPLPARSCQLHRLKLSEDERAVYDvflarsrsALQSYL 850
Cdd:COG0553   423 rERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYL 488
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  851 kRQEGRGSHPGRspenpfsrvaqefgsgvpqcstaadsrrpSTVHVLSQLLRLRQCCCHLSLLKSvlDPKELEseglvls 930
Cdd:COG0553   489 -RRELEGAEGIR-----------------------------RRGLILAALTRLRQICSHPALLLE--EGAELS------- 529
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  931 leeqlsaltlskvdvsepsptvslngtcfkvelfddiRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLR 1010
Cdd:COG0553   530 -------------------------------------GRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLE 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352 1011 KNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQEKD 1090
Cdd:COG0553   571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                         570       580       590
                  ....*....|....*....|....*....|..
gi 312922352 1091 VVMHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1122
Cdd:COG0553   651 VQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
zf-GRF super family cl46396
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
6-44 3.95e-06

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


The actual alignment was detected with superfamily member pfam06839:

Pssm-ID: 480736  Cd Length: 45  Bit Score: 44.70  E-value: 3.95e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 312922352     6 CPeHGAVCFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    3 CP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
550-800 3.91e-142

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: 427.67  E-value: 3.91e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKE-KDRSLPVMWLSKNDSSVFTSTGTLIVC 628
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEeEKEKALTEWESKKDSTLVPSAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAKEIPTAKHEGEvpgaklsvegiSAPLLQ 708
Cdd:cd18072    81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEESR-----------SSPLFR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 788
Cdd:cd18072   150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                         250
                  ....*....|..
gi 312922352  789 LSILTKSLLLRR 800
Cdd:cd18072   230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
536-1122 5.59e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.61  E-value: 5.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  536 KTAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILtkknQQKSKEKDRSlpvmwlsknd 615
Cdd:COG0553   228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL----ELKERGLARP---------- 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  616 ssvftstgTLIVCPASLIHHWKNEIEKRVNSnkLRIYLYHGP-NRIQHAKVLSTYDIVITTYSLLAKEIptakhegevpg 694
Cdd:COG0553   293 --------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI----------- 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  695 aklsvegisAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF 771
Cdd:COG0553   352 ---------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAF 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  772 -SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVPLPARSCQLHRLKLSEDERAVYDvflarsrsALQSYL 850
Cdd:COG0553   423 rERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYL 488
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  851 kRQEGRGSHPGRspenpfsrvaqefgsgvpqcstaadsrrpSTVHVLSQLLRLRQCCCHLSLLKSvlDPKELEseglvls 930
Cdd:COG0553   489 -RRELEGAEGIR-----------------------------RRGLILAALTRLRQICSHPALLLE--EGAELS------- 529
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  931 leeqlsaltlskvdvsepsptvslngtcfkvelfddiRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLR 1010
Cdd:COG0553   530 -------------------------------------GRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLE 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352 1011 KNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQEKD 1090
Cdd:COG0553   571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                         570       580       590
                  ....*....|....*....|....*....|..
gi 312922352 1091 VVMHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1122
Cdd:COG0553   651 VQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
553-913 1.13e-74

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: 249.14  E-value: 1.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   553 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekdrslpvmwlskndssvFTSTGTLIVCPASL 632
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   633 IHHWKNEIEKRVNSNKLRIYLYHGPNR-----IQHAKVLSTYDIVITTYSLLAKeiptakhegevpgaklsvegISAPLL 707
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRpqerwKNDPNFLADFDVVITTYETLRK--------------------HKELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   708 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGE 787
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   788 -----RLSILTKSLLLRRTKDQLDSTgkplvpLPARSCQLHRLKLSEDERAVYDVFLaRSRSALQsyLKRQEGrGSHPGR 862
Cdd:pfam00176  201 kkgvsRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-LKKDLNA--IKTGEG-GREIKA 270
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 312922352   863 SpenpfsrvaqefgsgvpqcstaadsrrpstvhVLSQLLRLRQCCCHLSLL 913
Cdd:pfam00176  271 S--------------------------------LLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
970-1097 8.56e-51

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: 175.36  E-value: 8.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  970 STKVSSLLAELEAIQKGpgSQKSVIVSQWTSMLQVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLL 1049
Cdd:cd18793    10 SGKLEALLELLEELREP--GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 312922352 1050 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQEKDVVMHRFV 1097
Cdd:cd18793    88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
535-1113 2.46e-35

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 146.10  E-value: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  535 GKTAVAEDPAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALIltkknQQKSKEKDRSLPVMwlskn 614
Cdd:PLN03142  155 GGTRLLVQPSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISLL-----GYLHEYRGITGPHM----- 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  615 dssvftstgtlIVCPASLIHHWKNEIEKRVNSnkLRIYLYHG-PNRIQHAK----VLSTYDIVITTYSLLAKEIPTAKhe 689
Cdd:PLN03142  224 -----------VVAPKSTLGNWMNEIRRFCPV--LRAVKFHGnPEERAHQReellVAGKFDVCVTSFEMAIKEKTALK-- 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  690 gevpgaKLSvegisapllqvvWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF- 768
Cdd:PLN03142  289 ------RFS------------WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFs 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  769 --DEFSLWKSQvdNGSMKGGERLSILTKSL---LLRRTKDQLDSTgkplvpLPARSCQLHRLKLSEDERAVYdvflarsR 843
Cdd:PLN03142  351 saETFDEWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------K 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  844 SALQSYLKrqegrgshpgrspenpfsrvaqefgsgvpQCSTAADSRRpstvhVLSQLLRLRQCCCHLSLLKSvldpkele 923
Cdd:PLN03142  416 ALLQKDLD-----------------------------VVNAGGERKR-----LLNIAMQLRKCCNHPYLFQG-------- 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  924 seglvlsleeqlsaltlskvdvSEPSPTVS----LNGTCFKVELFDdirrstkvsSLLAELEaiQKGpgsQKSVIVSQWT 999
Cdd:PLN03142  454 ----------------------AEPGPPYTtgehLVENSGKMVLLD---------KLLPKLK--ERD---SRVLIFSQMT 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352 1000 SMLQVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQA 1078
Cdd:PLN03142  498 RLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQA 577
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 312922352 1079 CDRIYRVGQEKDVVMHRFVCEGTVEEKILQLQEKK 1113
Cdd:PLN03142  578 QDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXDc smart00487
DEAD-like helicases superfamily;
549-778 3.69e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 95.64  E-value: 3.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352    549 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTKKNQQKSKekdrslpvmwlskndssvftstGTLIVC 628
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGG----------------------RVLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352    629 P-ASLIHHWKNEIEKRVNSNKLR-IYLYHGPNRIQHAKVLST--YDIVITTYSLLAKEIPtakhegevpgaklsvegiSA 704
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLE------------------ND 123
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312922352    705 PLLQVVWARIILDEAHNVKNP--RVQTSIAVCKLQAQA-RWAVTGTPIQNNLLDMYSLMK-FLRCSPFDEFSLWKSQV 778
Cdd:smart00487  124 KLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
972-1086 2.08e-18

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: 81.87  E-value: 2.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   972 KVSSLLAELEAIQKGpgsqKSVIVSQWTSMLQVVALhLRKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAG 1051
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRK--GKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 312922352  1052 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1086
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1003-1086 1.45e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 72.63  E-value: 1.45e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   1003 QVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1082
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 312922352   1083 YRVG 1086
Cdd:smart00490   79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
540-748 8.94e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.65  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  540 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALIltkknqQKSKEKDRslpvmwlskndssvf 619
Cdd:COG1061    71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALA------AELLRGKR--------------- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  620 tstgTLIVCP-ASLIHHWKNEIEKRVNsnklRIYLYHGPNRIQhakvlstYDIVITTYSLLAKEIPTAKHEGEvpgakls 698
Cdd:COG1061   130 ----VLVLVPrRELLEQWAEELRRFLG----DPLAGGGKKDSD-------APITVATYQSLARRAHLDELGDR------- 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 312922352  699 vegisapllqvvWARIILDEAHNVKNPRVQTSIAvcKLQAQARWAVTGTP 748
Cdd:COG1061   188 ------------FGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
6-44 3.95e-06

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 44.70  E-value: 3.95e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 312922352     6 CPeHGAVCFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    3 CP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
550-800 3.91e-142

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: 427.67  E-value: 3.91e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKE-KDRSLPVMWLSKNDSSVFTSTGTLIVC 628
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEeEKEKALTEWESKKDSTLVPSAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAKEIPTAKHEGEvpgaklsvegiSAPLLQ 708
Cdd:cd18072    81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEESR-----------SSPLFR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 788
Cdd:cd18072   150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                         250
                  ....*....|..
gi 312922352  789 LSILTKSLLLRR 800
Cdd:cd18072   230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
536-1122 5.59e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.61  E-value: 5.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  536 KTAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILtkknQQKSKEKDRSlpvmwlsknd 615
Cdd:COG0553   228 REALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL----ELKERGLARP---------- 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  616 ssvftstgTLIVCPASLIHHWKNEIEKRVNSnkLRIYLYHGP-NRIQHAKVLSTYDIVITTYSLLAKEIptakhegevpg 694
Cdd:COG0553   293 --------VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI----------- 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  695 aklsvegisAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF 771
Cdd:COG0553   352 ---------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAF 422
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  772 -SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVPLPARSCQLHRLKLSEDERAVYDvflarsrsALQSYL 850
Cdd:COG0553   423 rERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYL 488
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  851 kRQEGRGSHPGRspenpfsrvaqefgsgvpqcstaadsrrpSTVHVLSQLLRLRQCCCHLSLLKSvlDPKELEseglvls 930
Cdd:COG0553   489 -RRELEGAEGIR-----------------------------RRGLILAALTRLRQICSHPALLLE--EGAELS------- 529
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  931 leeqlsaltlskvdvsepsptvslngtcfkvelfddiRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLR 1010
Cdd:COG0553   530 -------------------------------------GRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLE 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352 1011 KNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQEKD 1090
Cdd:COG0553   571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                         570       580       590
                  ....*....|....*....|....*....|..
gi 312922352 1091 VVMHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1122
Cdd:COG0553   651 VQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
550-800 4.79e-101

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: 319.23  E-value: 4.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTKKNQQKSKEKDRSLPvmwlSKNDSSVFTSTGTLIVCP 629
Cdd:cd18008     1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILATRPQDPKIPEELEEN----SSDPKKLYLSKTTLIVVP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAKEIPTAKHEGEVPgaklSVEGISAPLLQV 709
Cdd:cd18008    71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPKNKKGGGRD----SKEKEASPLHRI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  710 VWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQV----DNGSMKG 785
Cdd:cd18008   147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDIskpfSKNDRKA 226
                         250
                  ....*....|....*
gi 312922352  786 GERLSILTKSLLLRR 800
Cdd:cd18008   227 LERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
553-913 1.13e-74

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: 249.14  E-value: 1.13e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   553 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekdrslpvmwlskndssvFTSTGTLIVCPASL 632
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   633 IHHWKNEIEKRVNSNKLRIYLYHGPNR-----IQHAKVLSTYDIVITTYSLLAKeiptakhegevpgaklsvegISAPLL 707
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRpqerwKNDPNFLADFDVVITTYETLRK--------------------HKELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   708 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGE 787
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   788 -----RLSILTKSLLLRRTKDQLDSTgkplvpLPARSCQLHRLKLSEDERAVYDVFLaRSRSALQsyLKRQEGrGSHPGR 862
Cdd:pfam00176  201 kkgvsRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-LKKDLNA--IKTGEG-GREIKA 270
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 312922352   863 SpenpfsrvaqefgsgvpqcstaadsrrpstvhVLSQLLRLRQCCCHLSLL 913
Cdd:pfam00176  271 S--------------------------------LLNILMRLRKICNHPGLI 289
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
550-800 1.44e-65

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: 221.57  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRE-----------------------SQK--PQ---GGILADDMGLGKTLTMIALILTKKnqqkske 601
Cdd:cd18071     1 LLPHQKQALAWMVSREnsqdlppfweeavglflntitnfSQKkrPElvrGGILADDMGLGKTLTTISLILANF------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  602 kdrslpvmwlskndssvftstgTLIVCPASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAK 681
Cdd:cd18071    74 ----------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLAS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  682 EiptakhEGEVPgaklsvegiSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMK 761
Cdd:cd18071   132 D------FGAKG---------DSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLS 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 312922352  762 FLRCSPFDEFSLWKS----QVDNGSMKGGERLSILTKSLLLRR 800
Cdd:cd18071   197 FLHLKPFSNPEYWRRliqrPLTMGDPTGLKRLQVLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
550-799 2.27e-58

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: 201.80  E-value: 2.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTKKNQQKSKEK--DRSLPVMWLSKNDS--SVFTSTGTL 625
Cdd:cd18070     1 LLPYQRRAVNWMLVP------GGILADEMGLGKTVEVLALILLHPRPDNDLDAadDDSDEMVCCPDCLVaeTPVSSKATL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  626 IVCPASLIHHWKNEIEKRVNSNkLRIYLYHGPNRI-----QHAKVLSTYDIVITTYSLLAKEI--PTAKHEGEVPGAKLS 698
Cdd:cd18070    75 IVCPSAILAQWLDEINRHVPSS-LKVLTYQGVKKDgalasPAPEILAEYDIVVTTYDVLRTELhyAEANRSNRRRRRQKR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  699 VEGISAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQV 778
Cdd:cd18070   154 YEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARVL 233
                         250       260
                  ....*....|....*....|...
gi 312922352  779 DN--GSMKGGERLSILTKSLLLR 799
Cdd:cd18070   234 IRpqGRNKAREPLAALLKELLWR 256
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
550-768 4.98e-54

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: 186.23  E-value: 4.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftstgTLIVCP 629
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLQAIAFLAYLLKEGKERGP---------------------VLVVCP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEKRVNSnkLRIYLYHGPNR----IQHAKVLSTYDIVITTYSLLAKEIptakhegevpgaklsvegisAP 705
Cdd:cd17919    59 LSVLENWEREFEKWTPD--LRVVVYHGSQReraqIRAKEKLDKFDVVLTTYETLRRDK--------------------AS 116
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922352  706 LLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCsPF 768
Cdd:cd17919   117 LRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP-PF 178
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
554-802 6.84e-53

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: 184.69  E-value: 6.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  554 QKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALILtkknqqKSKEKDRSLPVmwlskndssvftstgtLIVCPASLI 633
Cdd:cd18012     9 QKEGFNWL-SFLRHYGLGGILADDMGLGKTLQTLALLL------SRKEEGRKGPS----------------LVVAPTSLI 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  634 HHWKNEIEKRvnSNKLRIYLYHGPNR-IQHAKVLSTYDIVITTYSLLAKEIPTakhegevpgaklsvegisapLLQVVWA 712
Cdd:cd18012    66 YNWEEEAAKF--APELKVLVIHGTKRkREKLRALEDYDLVITSYGLLRRDIEL--------------------LKEVKFH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  713 RIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLrcSP-----FDEFS-LWKSQVDNGSMKGG 786
Cdd:cd18012   124 YLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPgllgsYKRFKkRFAKPIEKDGDEEA 201
                         250
                  ....*....|....*..
gi 312922352  787 -ERLSILTKSLLLRRTK 802
Cdd:cd18012   202 lEELKKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
970-1097 8.56e-51

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: 175.36  E-value: 8.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  970 STKVSSLLAELEAIQKGpgSQKSVIVSQWTSMLQVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLL 1049
Cdd:cd18793    10 SGKLEALLELLEELREP--GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 312922352 1050 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQEKDVVMHRFV 1097
Cdd:cd18793    88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
572-763 6.04e-37

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: 139.41  E-value: 6.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  572 GILADDMGLGKTLTMIALILTKKNQQKSKEKDRSLPVmwlskndssvftstgtLIVCPASLIHHWKNEIEKRVNSNKLRI 651
Cdd:cd17999    22 GILCDDMGLGKTLQTLCILASDHHKRANSFNSENLPS----------------LVVCPPTLVGHWVAEIKKYFPNAFLKP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  652 YLYHGP--NRIQHAKVLSTYDIVITTYSLLAKEIptakhegEVpgaklsvegisapLLQVVWARIILDEAHNVKNPRVQT 729
Cdd:cd17999    86 LAYVGPpqERRRLREQGEKHNVIVASYDVLRNDI-------EV-------------LTKIEWNYCVLDEGHIIKNSKTKL 145
                         170       180       190
                  ....*....|....*....|....*....|....
gi 312922352  730 SIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 763
Cdd:cd17999   146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL 179
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
535-1113 2.46e-35

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 146.10  E-value: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  535 GKTAVAEDPAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALIltkknQQKSKEKDRSLPVMwlskn 614
Cdd:PLN03142  155 GGTRLLVQPSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISLL-----GYLHEYRGITGPHM----- 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  615 dssvftstgtlIVCPASLIHHWKNEIEKRVNSnkLRIYLYHG-PNRIQHAK----VLSTYDIVITTYSLLAKEIPTAKhe 689
Cdd:PLN03142  224 -----------VVAPKSTLGNWMNEIRRFCPV--LRAVKFHGnPEERAHQReellVAGKFDVCVTSFEMAIKEKTALK-- 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  690 gevpgaKLSvegisapllqvvWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF- 768
Cdd:PLN03142  289 ------RFS------------WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFs 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  769 --DEFSLWKSQvdNGSMKGGERLSILTKSL---LLRRTKDQLDSTgkplvpLPARSCQLHRLKLSEDERAVYdvflarsR 843
Cdd:PLN03142  351 saETFDEWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------K 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  844 SALQSYLKrqegrgshpgrspenpfsrvaqefgsgvpQCSTAADSRRpstvhVLSQLLRLRQCCCHLSLLKSvldpkele 923
Cdd:PLN03142  416 ALLQKDLD-----------------------------VVNAGGERKR-----LLNIAMQLRKCCNHPYLFQG-------- 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  924 seglvlsleeqlsaltlskvdvSEPSPTVS----LNGTCFKVELFDdirrstkvsSLLAELEaiQKGpgsQKSVIVSQWT 999
Cdd:PLN03142  454 ----------------------AEPGPPYTtgehLVENSGKMVLLD---------KLLPKLK--ERD---SRVLIFSQMT 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352 1000 SMLQVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQA 1078
Cdd:PLN03142  498 RLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQA 577
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 312922352 1079 CDRIYRVGQEKDVVMHRFVCEGTVEEKILQLQEKK 1113
Cdd:PLN03142  578 QDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
550-808 4.89e-34

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: 131.35  E-value: 4.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWReSQKPQGGILADDMGLGKTLTMIALiLTKKNQQKSKEKDRSLPVMWLSKNDSSVFTSTGTLIVCP 629
Cdd:cd18005     1 LRDYQREGVEFMYDL-YKNGRGGILGDDMGLGKTVQVIAF-LAAVLGKTGTRRDRENNRPRFKKKPPASSAKKPVLIVAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEKRvnsNKLRIYLYHGPNR---IQHAKVLSTYDIVITTYSLLAKEIPTakhegevpgaklsvegisapL 706
Cdd:cd18005    79 LSVLYNWKDELDTW---GHFEVGVYHGSRKddeLEGRLKAGRLEVVVTTYDTLRRCIDS--------------------L 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  707 LQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNgSMKGG 786
Cdd:cd18005   136 NSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSE-PIKRG 214
                         250       260
                  ....*....|....*....|...
gi 312922352  787 ERLSILTKSLLL-RRTKDQLDST 808
Cdd:cd18005   215 QRHTATARELRLgRKRKQELAVK 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
553-763 2.44e-33

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: 129.03  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALiltkknqqkskekdrsLPVMWLSKNDSSVftstgtLIVCPASL 632
Cdd:cd18001     4 HQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAF----------------LSGMFDSGLIKSV------LVVMPTSL 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSnkLRIYLYHGP-----NRIQHaKVLSTYDIVITTYSLL---AKEIPTAKHEgevpgaklsvegisa 704
Cdd:cd18001    61 IPHWVKEFAKWTPG--LRVKVFHGTskkerERNLE-RIQRGGGVLLTTYGMVlsnTEQLSADDHD--------------- 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 312922352  705 pllQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 763
Cdd:cd18001   123 ---EFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
553-762 3.80e-32

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: 123.97  E-value: 3.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekdRSLpvmwlskNDSSVFTSTgTLIVCPASL 632
Cdd:cd18000     4 YQQTGVQWLWELHCQR-VGGILGDEMGLGKTIQIIAFL-------------AAL-------HHSKLGLGP-SLIVCPATV 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEK----------------RVNSNKLRIYLYhgpNRIQHAKVLSTYDIVITTYSLLAKEiptakhegevpgak 696
Cdd:cd18000    62 LKQWVKEFHRwwppfrvvvlhssgsgTGSEEKLGSIER---KSQLIRKVVGDGGILITTYEGFRKH-------------- 124
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312922352  697 lsvegiSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKF 762
Cdd:cd18000   125 ------KDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDF 184
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
553-800 5.09e-30

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: 119.70  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWL----LWRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekdrslpvmwlSKNDSSvfTSTGTLIVC 628
Cdd:cd18004     4 HQREGVQFLydclTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQ---------------GPYGKP--TAKKALIVC 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNKLRIYLYHGPNR-----IQHAKVLSTYDIVITTYSLLAKEIPTAKHegevpgaklsveGIS 703
Cdd:cd18004    67 PSSLVGNWKAEFDKWLGLRRIKVVTADGNAKdvkasLDFFSSASTYPVLIISYETLRRHAEKLSK------------KIS 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  704 APLLqvvwariILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSM 783
Cdd:cd18004   135 IDLL-------ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIL 207
                         250       260       270
                  ....*....|....*....|....*....|...
gi 312922352  784 KGGER----------------LSILTKSLLLRR 800
Cdd:cd18004   208 RSRDPdaseedkelgaersqeLSELTSRFILRR 240
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
553-802 3.65e-27

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: 110.87  E-value: 3.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALiltkknqqkskekdrsLPVMWLSKNDSSVFtstgtLIVCPA 630
Cdd:cd17997     7 YQIRGLNWLI---SLFENGinGILADEMGLGKTLQTISL----------------LGYLKHYKNINGPH-----LIIVPK 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  631 SLIHHWKNEIEKRVNSnkLRIYLYHGPNR-----IQHAKVLSTYDIVITTYSLLAKEiptakhegevpgaklsvegiSAP 705
Cdd:cd17997    63 STLDNWMREFKRWCPS--LRVVVLIGDKEeradiIRDVLLPGKFDVCITSYEMVIKE--------------------KTV 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  706 LLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKS--QVDN 780
Cdd:cd17997   121 LKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFtssEDFDEWFNvnNCDD 200
                         250       260
                  ....*....|....*....|..
gi 312922352  781 GSMKGGERLSILTKSLLLRRTK 802
Cdd:cd17997   201 DNQEVVQRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
553-800 6.91e-27

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: 110.13  E-value: 6.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltkknqqkskekdrsLPVMWLSKNDssvftsTGT-LIVCPAS 631
Cdd:cd18003     4 YQHIGLDWLA-TLYEKNLNGILADEMGLGKTIQTIAL----------------LAHLACEKGN------WGPhLIVVPTS 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  632 LIHHWKNEIEKRVNSnkLRIYLYHGPNRIQHAK-----VLSTYDIVITTYSLLAKEIPTAKhegevpgaklsvegisapl 706
Cdd:cd18003    61 VMLNWEMEFKRWCPG--FKILTYYGSAKERKLKrqgwmKPNSFHVCITSYQLVVQDHQVFK------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  707 lQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKSQVDNGSM 783
Cdd:cd18003   120 -RKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFqshQEFKEWFSNPLTAMS 198
                         250       260
                  ....*....|....*....|....*
gi 312922352  784 KGGE--------RLSILTKSLLLRR 800
Cdd:cd18003   199 EGSQeeneelvrRLHKVLRPFLLRR 223
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
553-767 2.33e-23

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: 100.30  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKP----QGGILADDMGLGKTLTMIALILTKKNQQKSKEKdrslPVMwlskndssvftsTGTLIVC 628
Cdd:cd18066     4 HQREGIEFLYECVMGMRvnerFGAILADEMGLGKTLQCISLIWTLLRQGPYGGK----PVI------------KRALIVT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLSTYDIVITTYSLLAKeiptakhegevpgaklSVEGISAPLLQ 708
Cdd:cd18066    68 PGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLR----------------SLDQISKLNFD 131
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 312922352  709 VVwariILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFlrCSP 767
Cdd:cd18066   132 LV----ICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF--VNP 184
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
550-772 2.48e-23

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: 100.06  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLlWR-------ESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftst 622
Cdd:cd18007     1 LKPHQVEGVRFL-WSnlvgtdvGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSR-------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  623 gTLIVCPASLIHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAK-VLSTYD-------IVITTYSLLAKEIPTAkheGEVPG 694
Cdd:cd18007    60 -PLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKRADaRLRKINkwhkeggVLLIGYELFRNLASNA---TTDPR 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  695 AKLSVEG---ISAPLLqvvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR---CSPF 768
Cdd:cd18007   136 LKQEFIAallDPGPDL------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARpkyLGTL 209

                  ....
gi 312922352  769 DEFS 772
Cdd:cd18007   210 KEFK 213
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
550-802 7.49e-23

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: 98.61  E-value: 7.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALiltkknqqkskekdrsLPVMWLSKNDSSVftstgtLIV 627
Cdd:cd18009     4 MRPYQLEGMEWLrmLW---ENGINGILADEMGLGKTIQTIAL----------------LAHLRERGVWGPF------LVI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  628 CPASLIHHWKNEIEKRVNSnkLRIYLYHGPN---------RIQHAKVLSTYDIVITTYSLLAKEiptakhegevpgakls 698
Cdd:cd18009    59 APLSTLPNWVNEFARFTPS--VPVLLYHGTKeererlrkkIMKREGTLQDFPVVVTSYEIAMRD---------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  699 vegisAPLLQ-VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQ 777
Cdd:cd18009   121 -----RKALQhYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESW 195
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 312922352  778 VDNGSMKGGE----------------RLSILTKSLLLRRTK 802
Cdd:cd18009   196 FDFSSLSDNAadisnlseereqnivhMLHAILKPFLLRRLK 236
DEXDc smart00487
DEAD-like helicases superfamily;
549-778 3.69e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 95.64  E-value: 3.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352    549 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTKKNQQKSKekdrslpvmwlskndssvftstGTLIVC 628
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGG----------------------RVLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352    629 P-ASLIHHWKNEIEKRVNSNKLR-IYLYHGPNRIQHAKVLST--YDIVITTYSLLAKEIPtakhegevpgaklsvegiSA 704
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLE------------------ND 123
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312922352    705 PLLQVVWARIILDEAHNVKNP--RVQTSIAVCKLQAQA-RWAVTGTPIQNNLLDMYSLMK-FLRCSPFDEFSLWKSQV 778
Cdd:smart00487  124 KLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
553-800 5.27e-22

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: 95.58  E-value: 5.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLL-WRESQkpQGGILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftstgTLIVCPAS 631
Cdd:cd18006     4 YQLEGVNWLLqCRAEQ--HGCILGDEMGLGKTCQTISLLWYLAGRLKLLGP---------------------FLVLCPLS 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  632 LIHHWKNEIEKRVNSNKLRIYLYHGPNRI---QHAKVLSTYDIVITTYSLLAKEiptakhegevpgaklsvegiSAPLLQ 708
Cdd:cd18006    61 VLDNWKEELNRFAPDLSVITYMGDKEKRLdlqQDIKSTNRFHVLLTTYEICLKD--------------------ASFLKS 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF-----DEFSLWKSQVDNGSm 783
Cdd:cd18006   121 FPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdklDDFIKAYSETDDES- 199
                         250
                  ....*....|....*..
gi 312922352  784 KGGERLSILTKSLLLRR 800
Cdd:cd18006   200 ETVEELHLLLQPFLLRR 216
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
554-800 1.08e-21

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: 95.01  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  554 QKQALAWLL--WRESQkpqGGILADDMGLGKTLTMIALIltkknqqkskekdrslpvmwlskndSSVFTSTGT----LIV 627
Cdd:cd17995     5 QLEGVNWLLfnWYNRR---NCILADEMGLGKTIQSIAFL-------------------------EHLYQVEGIrgpfLVI 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  628 CPASLIHHWKNEIEKRVNsnkLRIYLYHGP----NRIQH------------AKVLSTYDIVITTYsllakEIPTAKHEge 691
Cdd:cd17995    57 APLSTIPNWQREFETWTD---MNVVVYHGSgesrQIIQQyemyfkdaqgrkKKGVYKFDVLITTY-----EMVIADAE-- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  692 vpgaklsvegisaPLLQVVWARIILDEAHNVKNprVQTSIAVC--KLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF- 768
Cdd:cd17995   127 -------------ELRKIPWRVVVVDEAHRLKN--RNSKLLQGlkKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFp 191
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 312922352  769 --DEFslwksQVDNGSMKGGE---RLSILTKSLLLRR 800
Cdd:cd17995   192 ssEEF-----LEEFGDLKTAEqveKLQALLKPYMLRR 223
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
553-802 1.85e-21

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: 94.36  E-value: 1.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALI--LTKKnqqkskekdrslpvmwlsKNDSSVFtstgtLIVCPA 630
Cdd:cd17996     7 YQLKGLQWMVSLYNNN-LNGILADEMGLGKTIQTISLItyLMEK------------------KKNNGPY-----LVIVPL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  631 SLIHHWKNEIEKRVNSnkLRIYLYHGP----NRIQHAKVLSTYDIVITTYSLLAKEIPTakhegevpgaklsvegisapL 706
Cdd:cd17996    63 STLSNWVSEFEKWAPS--VSKIVYKGTpdvrKKLQSQIRAGKFNVLLTTYEYIIKDKPL--------------------L 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  707 LQVVWARIILDEAHNVKNprvqtsiAVCKL--------QAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-- 770
Cdd:cd17996   121 SKIKWKYMIIDEGHRMKN-------AQSKLtqtlntyyHARYRLLLTGTPLQNNLPELWALLNFLlpkifkSCKTFEQwf 193
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 312922352  771 ---FSLWKSQvDNGSMKGGERLSI---LTKSL---LLRRTK 802
Cdd:cd17996   194 ntpFANTGEQ-VKIELNEEETLLIirrLHKVLrpfLLRRLK 233
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
550-800 5.17e-21

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: 92.65  E-value: 5.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWREsqkpqGGIL-ADDMGLGKTLTMIAliltkknqqkskekdrslpVMWLSKNDSSVftstgtLIVC 628
Cdd:cd18010     1 LLPFQREGVCFALRRG-----GRVLiADEMGLGKTVQAIA-------------------IAAYYREEWPL------LIVC 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRvnsnkLRIYLYHGPNRIQHAK-VLSTYD--IVITTYSLLakeiptAKHEGEVPGAKLSVegisap 705
Cdd:cd18010    51 PSSLRLTWADEIERW-----LPSLPPDDIQVIVKSKdGLRDGDakVVIVSYDLL------RRLEKQLLARKFKV------ 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  706 llqvvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAV--TGTPIQNNLLDMYSLMKFLR---CSPFDEFSlwKSQVDN 780
Cdd:cd18010   114 --------VICDESHYLKNSKAKRTKAALPLLKRAKRVIllSGTPALSRPIELFTQLDALDpklFGRFHDFG--RRYCAA 183
                         250       260       270
                  ....*....|....*....|....*....|
gi 312922352  781 GSMKGG----------ERLSILTKSLLLRR 800
Cdd:cd18010   184 KQGGFGwdysgssnleELHLLLLATIMIRR 213
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
549-802 1.63e-20

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: 92.00  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  549 PLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekdRSLPvmwlskndssvftsTGTLIVC 628
Cdd:cd18065    15 TLRDYQVRGLNWMI-SLYENGVNGILADEMGLGKTLQTIALLGYLKHY-------RNIP--------------GPHMVLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSnkLRIYLYHGPNRIQHAKVLST-----YDIVITTYSLLAKEIPTAKhegevpgaklsvegis 703
Cdd:cd18065    73 PKSTLHNWMNEFKRWVPS--LRAVCLIGDKDARAAFIRDVmmpgeWDVCVTSYEMVIKEKSVFK---------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  704 apllQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKSQVDN 780
Cdd:cd18065   135 ----KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaDDFDSWFDTKNC 210
                         250       260
                  ....*....|....*....|...
gi 312922352  781 -GSMKGGERLSILTKSLLLRRTK 802
Cdd:cd18065   211 lGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
553-768 1.35e-19

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: 87.83  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqQKSKEKDRSLPvmwlskndssvftstgTLIVCPASL 632
Cdd:cd17998     4 YQLIGLNWLNLLYQKK-LSGILADEMGLGKTIQVIAFL------AYLKEIGIPGP----------------HLVVVPSST 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSnkLRIYLYHGPN------RIQHAKVLSTYDIVITTYSLlakeiptakhegeVPGAKLSVEGISAPL 706
Cdd:cd17998    61 LDNWLREFKRWCPS--LKVEPYYGSQeerkhlRYDILKGLEDFDVIVTTYNL-------------ATSNPDDRSFFKRLK 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922352  707 LQVVwariILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF 768
Cdd:cd17998   126 LNYV----VYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
553-811 1.49e-19

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: 89.34  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekdRSLPvmwlskndssvftsTGTLIVCPASL 632
Cdd:cd18064    19 YQVRGLNWLI-SLYENGINGILADEMGLGKTLQTISLLGYMKHY-------RNIP--------------GPHMVLVPKST 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSnkLRIYLYHGPNRIQHAKVLST-----YDIVITTYSLLAKEIPTAKhegevpgaklsvegisapll 707
Cdd:cd18064    77 LHNWMAEFKRWVPT--LRAVCLIGDKDQRAAFVRDVllpgeWDVCVTSYEMLIKEKSVFK-------------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  708 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWkSQVDN--GS 782
Cdd:cd18064   135 KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaEDFDSW-FDTNNclGD 213
                         250       260
                  ....*....|....*....|....*....
gi 312922352  783 MKGGERLSILTKSLLLRRTKDQLDSTGKP 811
Cdd:cd18064   214 QKLVERLHMVLRPFLLRRIKADVEKSLPP 242
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
972-1086 2.08e-18

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: 81.87  E-value: 2.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   972 KVSSLLAELEAIQKGpgsqKSVIVSQWTSMLQVVALhLRKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAG 1051
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRK--GKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 312922352  1052 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1086
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
553-800 3.40e-18

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: 84.86  E-value: 3.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALIltkknQQKSKEKDRSLPVmwlskndssvftstgtLIVCPA 630
Cdd:cd18002     4 YQLKGLNWLA---NLYEQGinGILADEMGLGKTVQSIAVL-----AHLAEEHNIWGPF----------------LVIAPA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  631 SLIHHWKNEIEKRVNsnKLRIYLYHGpnRIQHAKVL-------------STYDIVITTYSLLAKEiptAKHegevpgakl 697
Cdd:cd18002    60 STLHNWQQEISRFVP--QFKVLPYWG--NPKDRKVLrkfwdrknlytrdAPFHVVITSYQLVVQD---EKY--------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  698 svegisapLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFD---EFSLW 774
Cdd:cd18002   124 --------FQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDshdEFNEW 195
                         250       260       270
                  ....*....|....*....|....*....|....
gi 312922352  775 KSQ-VDNGSMKGG-------ERLSILTKSLLLRR 800
Cdd:cd18002   196 FSKdIESHAENKTglnehqlKRLHMILKPFMLRR 229
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
550-763 1.07e-17

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: 82.72  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLwreSQKPQGGILADDMGLGKTLTMIALIltkknqqksKEkdrslpvMWLSKNDSSVftstgtLIVCP 629
Cdd:cd18011     1 PLPHQIDAVLRAL---RKPPVRLLLADEVGLGKTIEAGLII---------KE-------LLLRGDAKRV------LILCP 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEKRVNSNKLRIY-LYHGPNRIQHAKVLSTYDIVITTYSLLakeiptaKHEGEVPGAKLSVEgisapllq 708
Cdd:cd18011    56 ASLVEQWQDELQDKFGLPFLILDrETAAQLRRLIGNPFEEFPIVIVSLDLL-------KRSEERRGLLLSEE-------- 120
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312922352  709 vvWARIILDEAHNVKN---PRVQTSIAVCKLQAQARWAV---TGTPIQNNLLDMYSLMKFL 763
Cdd:cd18011   121 --WDLVVVDEAHKLRNsggGKETKRYKLGRLLAKRARHVlllTATPHNGKEEDFRALLSLL 179
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
554-800 4.86e-17

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: 81.25  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  554 QKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALI--LTKKNQQkskekdrslpvmwlskndSSVFtstgtLIVCP 629
Cdd:cd17993     6 QLTGLNWLahSW---CKGNNGILADEMGLGKTVQTISFLsyLFHSQQQ------------------YGPF-----LVVVP 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEK-------------RVNSNKLRIY-LYHGPNRiqhaKVlsTYDIVITTYSLLAKEiptakhegevpga 695
Cdd:cd17993    60 LSTMPAWQREFAKwapdmnvivylgdIKSRDTIREYeFYFSQTK----KL--KFNVLLTTYEIILKD------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  696 klsvegiSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRcsPfDEFSLWK 775
Cdd:cd17993   121 -------KAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLM--P-GKFDIWE 190
                         250       260
                  ....*....|....*....|....*...
gi 312922352  776 S---QVDNGSMKGGERLSILTKSLLLRR 800
Cdd:cd17993   191 EfeeEHDEEQEKGIADLHKELEPFILRR 218
HELICc smart00490
helicase superfamily c-terminal domain;
1003-1086 1.45e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 72.63  E-value: 1.45e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352   1003 QVVALHLRKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1082
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 312922352   1083 YRVG 1086
Cdd:smart00490   79 GRAG 82
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
553-800 1.11e-14

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: 74.70  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekdrslpvmwlsKNDSSVFTSTGTLIVCPASL 632
Cdd:cd18060     4 YQLEGVNWLLFNWYNR-QNCILADEMGLGKTIQSIAFL----------------------QEVYNVGIHGPFLVIAPLST 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSNKLriyLYHGP----NRIQHAKVLST------------YDIVITTYSLLAKEIPTakhegevpgak 696
Cdd:cd18060    61 ITNWEREFNTWTEMNTI---VYHGSlasrQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPE----------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  697 lsvegisapLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF-DEFSLWK 775
Cdd:cd18060   127 ---------LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLK 197
                         250       260
                  ....*....|....*....|....*
gi 312922352  776 SQVDNGSMKGGERLSILTKSLLLRR 800
Cdd:cd18060   198 DFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
534-800 1.97e-14

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: 74.27  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  534 PGKTAVAEDPA---GLKVPLLLHQKQALAWLL--WRESQKPqggILADDMGLGKTLTMIALILTKKNQQKskekdrslpv 608
Cdd:cd18054     2 PRFVALKKQPSyigGENLELRDYQLEGLNWLAhsWCKNNSV---ILADEMGLGKTIQTISFLSYLFHQHQ---------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  609 mwlskndssvfTSTGTLIVCPASLIHHWKNEIEkrVNSNKLRIYLYHGP----NRI-------QHAKVLStYDIVITTYS 677
Cdd:cd18054    69 -----------LYGPFLLVVPLSTLTSWQREFE--IWAPEINVVVYIGDlmsrNTIreyewihSQTKRLK-FNALITTYE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  678 LLAKEiptakhegevpgaklsvegiSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMY 757
Cdd:cd18054   135 ILLKD--------------------KTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELW 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 312922352  758 SLMKFLRCSPFDEFSLWKSQVDNGSMKGGERLSILTKSLLLRR 800
Cdd:cd18054   195 SLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
571-762 4.87e-14

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: 73.27  E-value: 4.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  571 GGILADDMGLGKTLTMIALILT--KKNQQKSKEKDRSLpvmwlskndssvftstgtlIVCPASLIHHWKNEIEKRVNSNK 648
Cdd:cd18067    26 GCIMADEMGLGKTLQCITLMWTllRQSPQCKPEIDKAI-------------------VVSPSSLVKNWANELGKWLGGRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  649 LRIYLYHGPNR----------IQHAKVLSTyDIVITTYSLLAKEIpTAKHEGEVpgaklsvegisapllqvvwARIILDE 718
Cdd:cd18067    87 QPLAIDGGSKKeidrklvqwaSQQGRRVST-PVLIISYETFRLHV-EVLQKGEV-------------------GLVICDE 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 312922352  719 AHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKF 762
Cdd:cd18067   146 GHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNF 189
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
553-800 9.39e-14

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: 72.00  E-value: 9.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekdrslpvmwlskndSSVF---TSTGTLIVCP 629
Cdd:cd18058     4 YQLEGMNWLLFNWYNR-KNCILADEMGLGKTIQSITFL-------------------------SEIFlmgIRGPFLIIAP 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEKRVNSNKLriyLYHGPN-------------RIQHAKVLS---TYDIVITTYSLLAKEIPTAKhegevp 693
Cdd:cd18058    58 LSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemyyRDEQGNPLSgifKFQVVITTFEMILADCPELK------ 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  694 gaklsvegisapllQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSL 773
Cdd:cd18058   129 --------------KINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT 194
                         250       260       270
                  ....*....|....*....|....*....|
gi 312922352  774 WKSQVdnGSMKGGE---RLSILTKSLLLRR 800
Cdd:cd18058   195 FLEEF--GDLKTEEqvkKLQSILKPMMLRR 222
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
571-764 4.18e-12

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: 67.15  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  571 GGILADDMGLGKTLTMIALILTKKNQQKSKEkdrslpvmwlskndssvftstgTLIVCPASLIHHWKNEIEKRVNSnklr 650
Cdd:cd18069    30 GCILAHSMGLGKTLQVISFLDVLLRHTGAKT----------------------VLAIVPVNTLQNWLSEFNKWLPP---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  651 iYLYHGPNRIQHAKVLSTYDIVITTYSLlAKEIPTAKHEGEV-----------PGAKLsvegisapllqvvwarIILDEA 719
Cdd:cd18069    84 -PEALPNVRPRPFKVFILNDEHKTTAAR-AKVIEDWVKDGGVllmgyemfrlrPGPDV----------------VICDEG 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 312922352  720 HNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR 764
Cdd:cd18069   146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
552-776 1.89e-11

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: 64.38  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  552 LH--QKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALI--LTKKNQQKSkekdrslPVmwlskndssvftstgtLIV 627
Cdd:cd17994     1 LHpyQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLysLYKEGHSKG-------PF----------------LVS 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  628 CPASLIHHWKNEIEkrVNSNKLRIYLYHGPNriqhakvlstydIVITTYSLLAkeiptakhegevpgaklsvegISAPLL 707
Cdd:cd17994    57 APLSTIINWEREFE--MWAPDFYVVTYVGDH------------VLLTSYELIS---------------------IDQAIL 101
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  708 QVV-WARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLrcSPfDEFSLWKS 776
Cdd:cd17994   102 GSIdWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFL--TP-ERFNNLQG 168
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
553-802 1.99e-11

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: 65.47  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALILTKKNQQKskekdrslpvmwlskndssvfTSTGTLIVCPASL 632
Cdd:cd18063    27 YQLQGLEWMVSLYNNN-LNGILADEMGLGKTIQTIALITYLMEHKR---------------------LNGPYLIIVPLST 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSnKLRIYlYHGPNRIQHAKV----LSTYDIVITTYSLLAKEiptaKHegevpgaklsvegisaPLLQ 708
Cdd:cd18063    85 LSNWTYEFDKWAPS-VVKIS-YKGTPAMRRSLVpqlrSGKFNVLLTTYEYIIKD----KH----------------ILAK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQ-TSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-----FSLWKS 776
Cdd:cd18063   143 IRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGE 222
                         250       260
                  ....*....|....*....|....*....
gi 312922352  777 QVD---NGSMKGGERLSILTKSLLLRRTK 802
Cdd:cd18063   223 RVDlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
564-764 4.74e-11

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: 64.52  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  564 RESQKPQG--GILADDMGLGKTLTMIALILTKKNQQKSKEKDRslpvmwlskndssvftstgTLIVCPASLIHHWKNEIE 641
Cdd:cd18068    21 KKTKKSPGsgCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSR-------------------VLVVCPLNTVLNWLNEFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  642 KRV----NSNKLRIYLYHGPNRIQHAKVL-----STYDIVITTYSLLaKEIPTAKHEGEVPGAKlsvEGISAPLLQVVWA 712
Cdd:cd18068    82 KWQeglkDEEKIEVNELATYKRPQERSYKlqrwqEEGGVMIIGYDMY-RILAQERNVKSREKLK---EIFNKALVDPGPD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 312922352  713 RIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR 764
Cdd:cd18068   158 FVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
553-802 2.17e-10

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: 62.37  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALILTKKNQQKskekdrslpvmwlskndssvfTSTGTLIVCPASL 632
Cdd:cd18062    27 YQIKGLEWLVSLYNNN-LNGILADEMGLGKTIQTIALITYLMEHKR---------------------INGPFLIIVPLST 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSNKLRIYLYHGPNRIQHAKVLST--YDIVITTYSLLAKEiptaKHegevpgaklsvegisaPLLQVV 710
Cdd:cd18062    85 LSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSgkFNVLLTTYEYIIKD----KQ----------------ILAKIR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  711 WARIILDEAHNVKNPRVQ-TSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-----FSLWKSQV 778
Cdd:cd18062   145 WKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGEKV 224
                         250       260
                  ....*....|....*....|....*..
gi 312922352  779 D---NGSMKGGERLSILTKSLLLRRTK 802
Cdd:cd18062   225 DlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
553-800 8.69e-10

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: 60.45  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALI--LTKKNQQKSKekdrslpvmwlskndssvftstgTLIVCPA 630
Cdd:cd18053    24 YQLNGLNWLA-HSWCKGNSCILADEMGLGKTIQTISFLnyLFHEHQLYGP-----------------------FLLVVPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  631 SLIHHWKNEIEKRVNSNKLRIYL--YHGPNRIQHAKVLS------TYDIVITTYSLLAKEiptakhegevpgaklsvegi 702
Cdd:cd18053    80 STLTSWQREIQTWAPQMNAVVYLgdINSRNMIRTHEWMHpqtkrlKFNILLTTYEILLKD-------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  703 SAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGS 782
Cdd:cd18053   140 KSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR 219
                         250
                  ....*....|....*...
gi 312922352  783 MKGGERLSILTKSLLLRR 800
Cdd:cd18053   220 EYGYASLHKELEPFLLRR 237
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
553-763 8.86e-10

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: 60.06  E-value: 8.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLwresQKPQGGILADdMGLGKTLTMIALIltkknqQKSKEKDRSLPVmwlskndssvftstgtLIVCPASL 632
Cdd:cd18013     4 YQKVAINFII----EHPYCGLFLD-MGLGKTVTTLTAL------SDLQLDDFTRRV----------------LVIAPLRV 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHH-WKNEIEKRVNSNKLRIYLYHGPNRiQHAKVLST-YDIVITTYSLLAKEIptAKHEGEVPgaklsvegisapllqvv 710
Cdd:cd18013    57 ARStWPDEVEKWNHLRNLTVSVAVGTER-QRSKAANTpADLYVINRENLKWLV--NKSGDPWP----------------- 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312922352  711 WARIILDEAHNVKNPRVQTSIAVCKLQAQARWAV--TGTPIQNNLLDMYSLMKFL 763
Cdd:cd18013   117 FDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIglTGTPSPNGLMDLWAQIALL 171
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
553-800 1.00e-09

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: 60.05  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLL--WRESQKpqgGILADDMGLGKTLTMIALILTkknqqkskekdrslpvMWLsKNDSSVFtstgtLIVCPA 630
Cdd:cd18059     4 YQLEGVNWLLfnWYNTRN---CILADEMGLGKTIQSITFLYE----------------IYL-KGIHGPF-----LVIAPL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  631 SLIHHWKNEIEkrvNSNKLRIYLYHGPN-------------RIQHAKVLS---TYDIVITTYSLLAKEIPTakhegevpg 694
Cdd:cd18059    59 STIPNWEREFR---TWTELNVVVYHGSQasrrtiqlyemyfKDPQGRVIKgsyKFHAIITTFEMILTDCPE--------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  695 aklsvegisapLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLW 774
Cdd:cd18059   127 -----------LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTF 195
                         250       260
                  ....*....|....*....|....*....
gi 312922352  775 KSQVdnGSMKGGE---RLSILTKSLLLRR 800
Cdd:cd18059   196 MQEF--GDLKTEEqvqKLQAILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
553-771 3.15e-09

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: 58.54  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftstgTLIVCPASL 632
Cdd:cd18057     4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTIVFLYSLYKEGHSKGP---------------------YLVSAPLST 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSNKLRIYLYHGPNR-IQHAKVLSTYDIVITTysllAKEIPTAKHEGEVPGAKL--SVEGIS---APL 706
Cdd:cd18057    62 IINWEREFEMWAPDFYVVTYTGDKESRsVIRENEFSFEDNAIRS----GKKVFRMKKEAQIKFHVLltSYELITidqAIL 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312922352  707 LQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEF 771
Cdd:cd18057   138 GSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNL 202
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
553-800 7.12e-09

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: 57.32  E-value: 7.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALILTkknqqkskekdrslpvmwlskndssvFTSTGT----LIVC 628
Cdd:cd18061     4 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFLYE--------------------------ILLTGIrgpfLIIA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  629 PASLIHHWKNEIEKRVNSNklrIYLYHGpnRIQHAKVLSTYDIVITTYSllAKEIPTAKHEGEVPGAKLSVEGISAPLLQ 708
Cdd:cd18061    57 PLSTIANWEREFRTWTDLN---VVVYHG--SLISRQMIQQYEMYFRDSQ--GRIIRGAYRFQAIITTFEMILGGCPELNA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  709 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVdnGSMKGGE- 787
Cdd:cd18061   130 IDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF--GDLKTEEq 207
                         250
                  ....*....|....*
gi 312922352  788 --RLSILTKSLLLRR 800
Cdd:cd18061   208 vqKLQAILKPMMLRR 222
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
540-748 8.94e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.65  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  540 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALIltkknqQKSKEKDRslpvmwlskndssvf 619
Cdd:COG1061    71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALA------AELLRGKR--------------- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  620 tstgTLIVCP-ASLIHHWKNEIEKRVNsnklRIYLYHGPNRIQhakvlstYDIVITTYSLLAKEIPTAKHEGEvpgakls 698
Cdd:COG1061   130 ----VLVLVPrRELLEQWAEELRRFLG----DPLAGGGKKDSD-------APITVATYQSLARRAHLDELGDR------- 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 312922352  699 vegisapllqvvWARIILDEAHNVKNPRVQTSIAvcKLQAQARWAVTGTP 748
Cdd:COG1061   188 ------------FGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
553-763 1.73e-08

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: 56.61  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  553 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftstgTLIVCPASL 632
Cdd:cd18056     4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTAVFLYSLYKEGHSKGP---------------------FLVSAPLST 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  633 IHHWKNEIEKRVNSNKLRIYLYHGPNR-IQHAKVLSTYDIVITTysllAKEIPTAKHEGEVPGAKL--SVEGIS---APL 706
Cdd:cd18056    62 IINWEREFEMWAPDMYVVTYVGDKDSRaIIRENEFSFEDNAIRG----GKKASRMKKEASVKFHVLltSYELITidmAIL 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 312922352  707 LQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 763
Cdd:cd18056   138 GSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFL 194
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
550-769 3.31e-08

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: 55.79  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  550 LLLHQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKKNQQKSKEKdrslpvmwlskndssvftstgTLIVCP 629
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYSLYKEGHTKGP---------------------FLVSAP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  630 ASLIHHWKNEIEkrVNSNKLRIYLYHG---PNRIQHAKVLSTYDIVITTysllAKEIPTAKHEGEVPGAKL--SVEGIS- 703
Cdd:cd18055    59 LSTIINWEREFQ--MWAPDFYVVTYTGdkdSRAIIRENEFSFDDNAVKG----GKKAFKMKREAQVKFHVLltSYELVTi 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312922352  704 --APLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFD 769
Cdd:cd18055   133 dqAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFN 200
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
6-44 3.95e-06

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 44.70  E-value: 3.95e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 312922352     6 CPeHGAVCFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    3 CP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
624-736 9.54e-03

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 38.44  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922352  624 TLIVCPASL-IHHWKNEIEKRVNSNKLRIYLYHGPNR-IQHAKVlstydIVITTYSLLAKEIPTAKHegevpgaklsVEG 701
Cdd:cd18029    54 TLVLCTSAVsVEQWRRQFLDWTTIDDEQIGRFTSDKKeIFPEAG-----VTVSTYSMLANTRKRSPE----------SEK 118
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 312922352  702 ISAPLLQVVWARIILDEAHNVKNP---RVQTSIAV-CKL 736
Cdd:cd18029   119 FMEFITEREWGLIILDEVHVVPAPmfrRVLTLQKAhCKL 157
 
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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