NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907152327|ref|XP_036019254|]
View 

transcription termination factor 2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
563-813 3.45e-144

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: 432.67  E-value: 3.45e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKEKERSEPVT-WLSKNDSSVFTSSGTLIVC 641
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIPTTKQEGevpganlsvegTSAPLLQ 721
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEES-----------RSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  722 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 801
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1907152327  802 LSILTKSLLLRR 813
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
550-1107 7.26e-113

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 366.47  E-value: 7.26e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  550 TAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTKKnqqkskEKERSEPVtwlsknds 629
Cdd:COG0553    229 EALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELK------ERGLARPV-------- 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  630 svftssgtLIVCPASLIHHWKNEVEKrvTSNRLRIYLYHGP-NRSRHAKVLSTYDIVITTYSLLAKEIpttkqegevpga 708
Cdd:COG0553    294 --------LIVAPTSLVGNWQRELAK--FAPGLRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI------------ 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  709 nlsvegtsAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF- 784
Cdd:COG0553    352 --------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFr 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  785 SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVALPARRCQLHRLKLSEDERAVYDIFLARSRsalQSYLK 864
Cdd:COG0553    424 ERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYEAVLEYLR---RELEG 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  865 RQEGRgshhgrspdnpfsrvaqefgssvsqgcpaadsqrpSTVHVLSQLLRLRQCCCHLSLLksaldpteleseglvlsL 944
Cdd:COG0553    495 AEGIR-----------------------------------RRGLILAALTRLRQICSHPALL-----------------L 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  945 EEQLSAltlskvdvsepsptvslngtcfkaelfddTRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLKK 1024
Cdd:COG0553    523 EEGAEL-----------------------------SGRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLEE 571
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327 1025 NRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQKKDV 1104
Cdd:COG0553    572 RGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651

                   ...
gi 1907152327 1105 VIH 1107
Cdd:COG0553    652 QVY 654
zf-GRF super family cl46396
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-44 7.28e-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: 43.93  E-value: 7.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907152327    4 VKCPeHGDACFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
563-813 3.45e-144

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: 432.67  E-value: 3.45e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKEKERSEPVT-WLSKNDSSVFTSSGTLIVC 641
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIPTTKQEGevpganlsvegTSAPLLQ 721
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEES-----------RSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  722 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 801
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1907152327  802 LSILTKSLLLRR 813
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
550-1107 7.26e-113

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 366.47  E-value: 7.26e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  550 TAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTKKnqqkskEKERSEPVtwlsknds 629
Cdd:COG0553    229 EALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELK------ERGLARPV-------- 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  630 svftssgtLIVCPASLIHHWKNEVEKrvTSNRLRIYLYHGP-NRSRHAKVLSTYDIVITTYSLLAKEIpttkqegevpga 708
Cdd:COG0553    294 --------LIVAPTSLVGNWQRELAK--FAPGLRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI------------ 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  709 nlsvegtsAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF- 784
Cdd:COG0553    352 --------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFr 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  785 SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVALPARRCQLHRLKLSEDERAVYDIFLARSRsalQSYLK 864
Cdd:COG0553    424 ERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYEAVLEYLR---RELEG 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  865 RQEGRgshhgrspdnpfsrvaqefgssvsqgcpaadsqrpSTVHVLSQLLRLRQCCCHLSLLksaldpteleseglvlsL 944
Cdd:COG0553    495 AEGIR-----------------------------------RRGLILAALTRLRQICSHPALL-----------------L 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  945 EEQLSAltlskvdvsepsptvslngtcfkaelfddTRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLKK 1024
Cdd:COG0553    523 EEGAEL-----------------------------SGRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLEE 571
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327 1025 NRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQKKDV 1104
Cdd:COG0553    572 RGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651

                   ...
gi 1907152327 1105 VIH 1107
Cdd:COG0553    652 QVY 654
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
566-926 2.55e-75

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 250.68  E-value: 2.55e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekersepvtwlskndssvFTSSGTLIVCPASL 645
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSNRLRIYLYHGPNRSRHA-----KVLSTYDIVITTYSLLAKEipttkqegevpganlsvegtSAPLL 720
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGE 800
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  801 -----RLSILTKSLLLRRTKDQLDSTgkplvaLPARRCQLHRLKLSEDERAVYDIFLarsrsalqsylkrqegrgshhgr 875
Cdd:pfam00176  201 kkgvsRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL----------------------- 251
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907152327  876 spdnPFSRVAQEFGSSVSQGCPAAdsqrpstvhVLSQLLRLRQCCCHLSLL 926
Cdd:pfam00176  252 ----LKKDLNAIKTGEGGREIKAS---------LLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
983-1107 3.13e-50

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: 173.43  E-value: 3.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  983 STKVSSLLAELEAIQKGpgSQKSVIVSQWTSMLQVVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLL 1062
Cdd:cd18793     10 SGKLEALLELLEELREP--GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907152327 1063 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQKKDVVIH 1107
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVY 132
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
548-1104 4.35e-31

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 132.62  E-value: 4.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  548 GETAVAEDPAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltkknqqkskekersepVTWLSKN 627
Cdd:PLN03142   155 GGTRLLVQPSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISL------------------LGYLHEY 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  628 DSsvfTSSGTLIVCPASLIHHWKNEVEKRVTSnrLRIYLYHG-PNRSRHAK----VLSTYDIVITTYSLLAKEipttkqe 702
Cdd:PLN03142   216 RG---ITGPHMVVAPKSTLGNWMNEIRRFCPV--LRAVKFHGnPEERAHQReellVAGKFDVCVTSFEMAIKE------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  703 gevpganlsvegtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF- 781
Cdd:PLN03142   284 -------------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFs 350
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  782 --DEFSLWKSQvdNGSMKGGERLSILTKSL---LLRRTKDQLDStgkplvALPARRCQLHRLKLSEDERAVYdiflarsR 856
Cdd:PLN03142   351 saETFDEWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEK------GLPPKKETILKVGMSQMQKQYY-------K 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  857 SALQSYLKrqegrgshhgrspdnpfsrvaqefgsSVSQGcpaADSQRpstvhVLSQLLRLRQCCCHLSLLKSAldptele 936
Cdd:PLN03142   416 ALLQKDLD--------------------------VVNAG---GERKR-----LLNIAMQLRKCCNHPYLFQGA------- 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  937 seglvlsleeqlsaltlskvdvsEPSPTVSLNgtcfkAELFDDTRRSTKVSSLLAELEaiQKGpgsQKSVIVSQWTSMLQ 1016
Cdd:PLN03142   455 -----------------------EPGPPYTTG-----EHLVENSGKMVLLDKLLPKLK--ERD---SRVLIFSQMTRLLD 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327 1017 VVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1095
Cdd:PLN03142   502 ILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRA 581

                   ....*....
gi 1907152327 1096 YRVGQKKDV 1104
Cdd:PLN03142   582 HRIGQKKEV 590
DEXDc smart00487
DEAD-like helicases superfamily;
562-791 2.79e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.02  E-value: 2.79e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327   562 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTKKNQQKSKekersepvtwlskndssvftssGTLIVC 641
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGG----------------------RVLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327   642 P-ASLIHHWKNEVEKRVTSNRLR-IYLYHGPNRSRHAKVLST--YDIVITTYSLLAKEIPttkqegevpganlsvegtSA 717
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLE------------------ND 123
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152327   718 PLLQVVWARIILDEAHNVKNP--RVQTSIAVCKLQAQA-RWAVTGTPIQNNLLDMYSLMK-FLRCSPFDEFSLWKSQV 791
Cdd:smart00487  124 KLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
985-1099 2.02e-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: 2.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  985 KVSSLLAELEAIQKGpgsqKSVIVSQWTSMLQVVALhLKKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAG 1064
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRK--GKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907152327 1065 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1099
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1016-1099 1.40e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 72.63  E-value: 1.40e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  1016 QVVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1095
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1907152327  1096 YRVG 1099
Cdd:smart00490   79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
553-761 1.07e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.27  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  553 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekersepvtwlskndssvf 632
Cdd:COG1061     71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  633 tssgTLIVCP-ASLIHHWKNEVEKrvtsnRLRIYLYHGPNRSRHakvlstYDIVITTYSLLAKeipttkqegevpgaNLS 711
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKDSD------APITVATYQSLAR--------------RAH 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907152327  712 VEgtsapLLQVVWARIILDEAHNVKNPRVQTSIAvcKLQAQARWAVTGTP 761
Cdd:COG1061    181 LD-----ELGDRFGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-44 7.28e-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: 43.93  E-value: 7.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907152327    4 VKCPeHGDACFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
563-813 3.45e-144

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: 432.67  E-value: 3.45e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKEKERSEPVT-WLSKNDSSVFTSSGTLIVC 641
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIPTTKQEGevpganlsvegTSAPLLQ 721
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEES-----------RSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  722 VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGER 801
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1907152327  802 LSILTKSLLLRR 813
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
550-1107 7.26e-113

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 366.47  E-value: 7.26e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  550 TAVAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTKKnqqkskEKERSEPVtwlsknds 629
Cdd:COG0553    229 EALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELK------ERGLARPV-------- 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  630 svftssgtLIVCPASLIHHWKNEVEKrvTSNRLRIYLYHGP-NRSRHAKVLSTYDIVITTYSLLAKEIpttkqegevpga 708
Cdd:COG0553    294 --------LIVAPTSLVGNWQRELAK--FAPGLRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDI------------ 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  709 nlsvegtsAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL---RCSPFDEF- 784
Cdd:COG0553    352 --------ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFr 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  785 SLWKSQVDNGSMKGGERLSILTKSLLLRRTKDQLdstgkpLVALPARRCQLHRLKLSEDERAVYDIFLARSRsalQSYLK 864
Cdd:COG0553    424 ERFARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYEAVLEYLR---RELEG 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  865 RQEGRgshhgrspdnpfsrvaqefgssvsqgcpaadsqrpSTVHVLSQLLRLRQCCCHLSLLksaldpteleseglvlsL 944
Cdd:COG0553    495 AEGIR-----------------------------------RRGLILAALTRLRQICSHPALL-----------------L 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  945 EEQLSAltlskvdvsepsptvslngtcfkaelfddTRRSTKVSSLLAELEAIQKgpGSQKSVIVSQWTSMLQVVALHLKK 1024
Cdd:COG0553    523 EEGAEL-----------------------------SGRSAKLEALLELLEELLA--EGEKVLVFSQFTDTLDLLEERLEE 571
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327 1025 NRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQKKDV 1104
Cdd:COG0553    572 RGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651

                   ...
gi 1907152327 1105 VIH 1107
Cdd:COG0553    652 QVY 654
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
563-813 6.88e-102

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: 321.16  E-value: 6.88e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTKKNQQKSKEKERSEPvtwlSKNDSSVFTSSGTLIVCP 642
Cdd:cd18008      1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILATRPQDPKIPEELEEN----SSDPKKLYLSKTTLIVVP 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIPttkqEGEVPGANLSVEGTSAPLLQV 722
Cdd:cd18008     71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFP----KNKKGGGRDSKEKEASPLHRI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  723 VWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQV----DNGSMKG 798
Cdd:cd18008    147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDIskpfSKNDRKA 226
                          250
                   ....*....|....*
gi 1907152327  799 GERLSILTKSLLLRR 813
Cdd:cd18008    227 LERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
566-926 2.55e-75

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 250.68  E-value: 2.55e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekersepvtwlskndssvFTSSGTLIVCPASL 645
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSNRLRIYLYHGPNRSRHA-----KVLSTYDIVITTYSLLAKEipttkqegevpganlsvegtSAPLL 720
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSMKGGE 800
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  801 -----RLSILTKSLLLRRTKDQLDSTgkplvaLPARRCQLHRLKLSEDERAVYDIFLarsrsalqsylkrqegrgshhgr 875
Cdd:pfam00176  201 kkgvsRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL----------------------- 251
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907152327  876 spdnPFSRVAQEFGSSVSQGCPAAdsqrpstvhVLSQLLRLRQCCCHLSLL 926
Cdd:pfam00176  252 ----LKKDLNAIKTGEGGREIKAS---------LLNILMRLRKICNHPGLI 289
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
563-813 5.05e-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: 220.03  E-value: 5.05e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRE-----------------------SQK--PQ---GGILADDMGLGKTLTMIALILTKKnqqkske 614
Cdd:cd18071      1 LLPHQKQALAWMVSREnsqdlppfweeavglflntitnfSQKkrPElvrGGILADDMGLGKTLTTISLILANF------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  615 kersepvtwlskndssvftssgTLIVCPASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAK 694
Cdd:cd18071     74 ----------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLAS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  695 EipttkqEGEVPganlsvegtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMK 774
Cdd:cd18071    132 D------FGAKG---------DSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLS 196
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1907152327  775 FLRCSPFDEFSLWKS----QVDNGSMKGGERLSILTKSLLLRR 813
Cdd:cd18071    197 FLHLKPFSNPEYWRRliqrPLTMGDPTGLKRLQVLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
563-812 6.48e-56

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: 194.48  E-value: 6.48e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTKKNQQKSKEKE--RSEPVTWLSKNDS--SVFTSSGTL 638
Cdd:cd18070      1 LLPYQRRAVNWMLVP------GGILADEMGLGKTVEVLALILLHPRPDNDLDAAddDSDEMVCCPDCLVaeTPVSSKATL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  639 IVCPASLIHHWKNEVEKRVTSNrLRIYLYHGPNR-----SRHAKVLSTYDIVITTYSLLAKEIPTTKQEGEVPGANLS-- 711
Cdd:cd18070     75 IVCPSAILAQWLDEINRHVPSS-LKVLTYQGVKKdgalaSPAPEILAEYDIVVTTYDVLRTELHYAEANRSNRRRRRQkr 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  712 VEGTSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQV 791
Cdd:cd18070    154 YEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARVL 233
                          250       260
                   ....*....|....*....|...
gi 1907152327  792 DN--GSMKGGERLSILTKSLLLR 812
Cdd:cd18070    234 IRpqGRNKAREPLAALLKELLWR 256
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
563-781 2.36e-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: 187.39  E-value: 2.36e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTKKNQQKSKEKersepvtwlskndssvftssgTLIVCP 642
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLQAIAFLAYLLKEGKERGP---------------------VLVVCP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEKRVTSnrLRIYLYHGPNRSRHA----KVLSTYDIVITTYSLLAKEIpttkqegevpganlsvegtsAP 718
Cdd:cd17919     59 LSVLENWEREFEKWTPD--LRVVVYHGSQRERAQirakEKLDKFDVVLTTYETLRRDK--------------------AS 116
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152327  719 LLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCsPF 781
Cdd:cd17919    117 LRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP-PF 178
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
567-815 5.53e-54

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 187.77  E-value: 5.53e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  567 QKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALILtkknqqKSKEKERSEPVtwlskndssvftssgtLIVCPASLI 646
Cdd:cd18012      9 QKEGFNWL-SFLRHYGLGGILADDMGLGKTLQTLALLL------SRKEEGRKGPS----------------LVVAPTSLI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  647 HHWKNEVEKRVTSnrLRIYLYHGPNRSRHAKV-LSTYDIVITTYSLLAKEIPTtkqegevpganlsvegtsapLLQVVWA 725
Cdd:cd18012     66 YNWEEEAAKFAPE--LKVLVIHGTKRKREKLRaLEDYDLVITSYGLLRRDIEL--------------------LKEVKFH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  726 RIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLrcSP-----FDEFS-LWKSQVDNGSMKGG 799
Cdd:cd18012    124 YLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPgllgsYKRFKkRFAKPIEKDGDEEA 201
                          250
                   ....*....|....*..
gi 1907152327  800 -ERLSILTKSLLLRRTK 815
Cdd:cd18012    202 lEELKKLISPFILRRLK 218
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
983-1107 3.13e-50

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: 173.43  E-value: 3.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  983 STKVSSLLAELEAIQKGpgSQKSVIVSQWTSMLQVVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQVMLISLL 1062
Cdd:cd18793     10 SGKLEALLELLEELREP--GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907152327 1063 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQKKDVVIH 1107
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVY 132
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
585-776 1.38e-36

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 138.25  E-value: 1.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  585 GILADDMGLGKTLTMIALILTKknQQKSKEKERSEPVTwlskndssvftssgTLIVCPASLIHHWKNEVEKRVTSNRLRI 664
Cdd:cd17999     22 GILCDDMGLGKTLQTLCILASD--HHKRANSFNSENLP--------------SLVVCPPTLVGHWVAEIKKYFPNAFLKP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  665 YLYHGP--NRSRHAKVLSTYDIVITTYSLLAKEIpttkqegEVpganlsvegtsapLLQVVWARIILDEAHNVKNPRVQT 742
Cdd:cd17999     86 LAYVGPpqERRRLREQGEKHNVIVASYDVLRNDI-------EV-------------LTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907152327  743 SIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 776
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL 179
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
563-821 3.43e-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: 131.73  E-value: 3.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWReSQKPQGGILADDMGLGKTLTMIAL---ILTKKNQQKskEKERSEPVTWLSKNDSSVFTSSgtLI 639
Cdd:cd18005      1 LRDYQREGVEFMYDL-YKNGRGGILGDDMGLGKTVQVIAFlaaVLGKTGTRR--DRENNRPRFKKKPPASSAKKPV--LI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  640 VCPASLIHHWKNEVEkrvTSNRLRIYLYHGPNRSRHAKV---LSTYDIVITTYSLLAKEIPTtkqegevpganlsvegts 716
Cdd:cd18005     76 VAPLSVLYNWKDELD---TWGHFEVGVYHGSRKDDELEGrlkAGRLEVVVTTYDTLRRCIDS------------------ 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  717 apLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNgSM 796
Cdd:cd18005    135 --LNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSE-PI 211
                          250       260
                   ....*....|....*....|....*.
gi 1907152327  797 KGGERLSILTKSLLL-RRTKDQLDST 821
Cdd:cd18005    212 KRGQRHTATARELRLgRKRKQELAVK 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
566-776 1.23e-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: 129.80  E-value: 1.23e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALIltkknqqkskekersepvtwlskndSSVFTSS---GTLIVCP 642
Cdd:cd18001      4 HQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAFL-------------------------SGMFDSGlikSVLVVMP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEKRvtSNRLRIYLYHGPNRSRHAK----VLSTYDIVITTYSLLakeIPTTKQegevpganLSVEGTSap 718
Cdd:cd18001     58 TSLIPHWVKEFAKW--TPGLRVKVFHGTSKKERERnlerIQRGGGVLLTTYGMV---LSNTEQ--------LSADDHD-- 122
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152327  719 llQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 776
Cdd:cd18001    123 --EFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
566-775 1.98e-31

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 122.05  E-value: 1.98e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALILtkknqqkskekersepvtwlSKNDSSVFTSSgTLIVCPASL 645
Cdd:cd18000      4 YQQTGVQWLWELHCQR-VGGILGDEMGLGKTIQIIAFLA--------------------ALHHSKLGLGP-SLIVCPATV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEK-----RVT-------SNRLRIYLYHGPNRSRHA-KVLSTYDIVITTYSLLAKEipttkqegevpganlsv 712
Cdd:cd18000     62 LKQWVKEFHRwwppfRVVvlhssgsGTGSEEKLGSIERKSQLIrKVVGDGGILITTYEGFRKH----------------- 124
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152327  713 egtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKF 775
Cdd:cd18000    125 ---KDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDF 184
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
548-1104 4.35e-31

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 132.62  E-value: 4.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  548 GETAVAEDPAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltkknqqkskekersepVTWLSKN 627
Cdd:PLN03142   155 GGTRLLVQPSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISL------------------LGYLHEY 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  628 DSsvfTSSGTLIVCPASLIHHWKNEVEKRVTSnrLRIYLYHG-PNRSRHAK----VLSTYDIVITTYSLLAKEipttkqe 702
Cdd:PLN03142   216 RG---ITGPHMVVAPKSTLGNWMNEIRRFCPV--LRAVKFHGnPEERAHQReellVAGKFDVCVTSFEMAIKE------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  703 gevpganlsvegtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF- 781
Cdd:PLN03142   284 -------------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFs 350
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  782 --DEFSLWKSQvdNGSMKGGERLSILTKSL---LLRRTKDQLDStgkplvALPARRCQLHRLKLSEDERAVYdiflarsR 856
Cdd:PLN03142   351 saETFDEWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEK------GLPPKKETILKVGMSQMQKQYY-------K 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  857 SALQSYLKrqegrgshhgrspdnpfsrvaqefgsSVSQGcpaADSQRpstvhVLSQLLRLRQCCCHLSLLKSAldptele 936
Cdd:PLN03142   416 ALLQKDLD--------------------------VVNAG---GERKR-----LLNIAMQLRKCCNHPYLFQGA------- 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  937 seglvlsleeqlsaltlskvdvsEPSPTVSLNgtcfkAELFDDTRRSTKVSSLLAELEaiQKGpgsQKSVIVSQWTSMLQ 1016
Cdd:PLN03142   455 -----------------------EPGPPYTTG-----EHLVENSGKMVLLDKLLPKLK--ERD---SRVLIFSQMTRLLD 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327 1017 VVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHSQGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1095
Cdd:PLN03142   502 ILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRA 581

                   ....*....
gi 1907152327 1096 YRVGQKKDV 1104
Cdd:PLN03142   582 HRIGQKKEV 590
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
566-813 3.92e-29

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: 117.00  E-value: 3.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWL----LWRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekersepvtwlSKNDSSvfTSSGTLIVC 641
Cdd:cd18004      4 HQREGVQFLydclTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQ---------------GPYGKP--TAKKALIVC 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVL-----STYDIVITTYSLLAKEIPTTKQegevpganlsveGTS 716
Cdd:cd18004     67 PSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKASLDffssaSTYPVLIISYETLRRHAEKLSK------------KIS 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  717 APLLqvvwariILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVDNGSM 796
Cdd:cd18004    135 IDLL-------ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIL 207
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907152327  797 KGGER----------------LSILTKSLLLRR 813
Cdd:cd18004    208 RSRDPdaseedkelgaersqeLSELTSRFILRR 240
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
566-813 1.32e-28

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: 114.76  E-value: 1.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALIltkknQQKSKEKERSEPvtwlskndssvftssgTLIVCPASL 645
Cdd:cd18003      4 YQHIGLDWLA-TLYEKNLNGILADEMGLGKTIQTIALL-----AHLACEKGNWGP----------------HLIVVPTSV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSnrLRIYLYHGPNRSRHAK-----VLSTYDIVITTYSLLAKEIPTTKQegevpganlsvegtsapll 720
Cdd:cd18003     62 MLNWEMEFKRWCPG--FKILTYYGSAKERKLKrqgwmKPNSFHVCITSYQLVVQDHQVFKR------------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 qVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKSQVDNGSMK 797
Cdd:cd18003    121 -KKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFqshQEFKEWFSNPLTAMSE 199
                          250       260
                   ....*....|....*....|....
gi 1907152327  798 GGE--------RLSILTKSLLLRR 813
Cdd:cd18003    200 GSQeeneelvrRLHKVLRPFLLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
566-815 1.58e-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: 111.64  E-value: 1.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALILTKKNQQKskekersepvtwlskndssvfTSSGTLIVCPA 643
Cdd:cd17997      7 YQIRGLNWLI---SLFENGinGILADEMGLGKTLQTISLLGYLKHYKN---------------------INGPHLIIVPK 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  644 SLIHHWKNEVEKRVTSnrLRIYLYHGPNRSRHA---KVLST--YDIVITTYSLLAKEipttkqegevpganlsvegtSAP 718
Cdd:cd17997     63 STLDNWMREFKRWCPS--LRVVVLIGDKEERADiirDVLLPgkFDVCITSYEMVIKE--------------------KTV 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  719 LLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKS--QVDN 793
Cdd:cd17997    121 LKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFtssEDFDEWFNvnNCDD 200
                          250       260
                   ....*....|....*....|..
gi 1907152327  794 GSMKGGERLSILTKSLLLRRTK 815
Cdd:cd17997    201 DNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
563-785 7.36e-24

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: 101.60  E-value: 7.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLlWR-------ESQKPQGGILADDMGLGKTLTMIALILTKKNQQKSKEKersepvtwlskndssvftss 635
Cdd:cd18007      1 LKPHQVEGVRFL-WSnlvgtdvGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSR-------------------- 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  636 gTLIVCPASLIHHWKNEVEKRVTSNRLRIYLYHGpnRSRHAKVLSTYD----------IVITTYSLLAKEI----PTTKQ 701
Cdd:cd18007     60 -PLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVS--LSASKRADARLRkinkwhkeggVLLIGYELFRNLAsnatTDPRL 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  702 EGEVPGANLsVEGTSApllqvvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR---C 778
Cdd:cd18007    137 KQEFIAALL-DPGPDL---------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARpkyL 206

                   ....*..
gi 1907152327  779 SPFDEFS 785
Cdd:cd18007    207 GTLKEFK 213
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
566-780 3.97e-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: 99.53  E-value: 3.97e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKP----QGGILADDMGLGKTLTMIALILTKKNQQKSKEKersePVTwlskndssvftsSGTLIVC 641
Cdd:cd18066      4 HQREGIEFLYECVMGMRvnerFGAILADEMGLGKTLQCISLIWTLLRQGPYGGK----PVI------------KRALIVT 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIpttkqeGEVPGANLSVegtsapllq 721
Cdd:cd18066     68 PGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSL------DQISKLNFDL--------- 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152327  722 vvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFlrCSP 780
Cdd:cd18066    133 -----VICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF--VNP 184
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
567-813 4.77e-23

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: 98.86  E-value: 4.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  567 QKQALAWLL--WRESQkpqGGILADDMGLGKTLTMIALIltkknqqkskekersepvtwlskndSSVFTSSGT----LIV 640
Cdd:cd17995      5 QLEGVNWLLfnWYNRR---NCILADEMGLGKTIQSIAFL-------------------------EHLYQVEGIrgpfLVI 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  641 CPASLIHHWKNEVEKRVTSN------------RLRIY-LYHGPNRSRHAKVLSTYDIVITTYSLLAKEIPTTKQegevpg 707
Cdd:cd17995     57 APLSTIPNWQREFETWTDMNvvvyhgsgesrqIIQQYeMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRK------ 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  708 anlsvegtsapllqVVWARIILDEAHNVKNprVQTSIAVC--KLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---D 782
Cdd:cd17995    131 --------------IPWRVVVVDEAHRLKN--RNSKLLQGlkKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFpssE 194
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907152327  783 EFslwksQVDNGSMKGGE---RLSILTKSLLLRR 813
Cdd:cd17995    195 EF-----LEEFGDLKTAEqveKLQALLKPYMLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
563-815 1.89e-22

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: 97.46  E-value: 1.89e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALIltkknqQKSKEKERSEPVtwlskndssvftssgtLIV 640
Cdd:cd18009      4 MRPYQLEGMEWLrmLW---ENGINGILADEMGLGKTIQTIALL------AHLRERGVWGPF----------------LVI 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  641 CPASLIHHWKNEVEKRVTSnrLRIYLYHGPNRSR---------HAKVLSTYDIVITTYSLLAKEipttkqegevpganls 711
Cdd:cd18009     59 APLSTLPNWVNEFARFTPS--VPVLLYHGTKEERerlrkkimkREGTLQDFPVVVTSYEIAMRD---------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  712 vegtsAPLLQ-VVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQ 790
Cdd:cd18009    121 -----RKALQhYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESW 195
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907152327  791 VDNGSMKGGE----------------RLSILTKSLLLRRTK 815
Cdd:cd18009    196 FDFSSLSDNAadisnlseereqnivhMLHAILKPFLLRRLK 236
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
566-813 2.27e-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: 96.74  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLL-WRESQkpQGGILADDMGLGKTLTMIALILTKKNQQKSKEKersepvtwlskndssvftssgTLIVCPAS 644
Cdd:cd18006      4 YQLEGVNWLLqCRAEQ--HGCILGDEMGLGKTCQTISLLWYLAGRLKLLGP---------------------FLVLCPLS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  645 LIHHWKNEVeKRVTSNrLRIYLYHGPNRSR-----HAKVLSTYDIVITTYSLLAKEipttkqegevpganlsvegtSAPL 719
Cdd:cd18006     61 VLDNWKEEL-NRFAPD-LSVITYMGDKEKRldlqqDIKSTNRFHVLLTTYEICLKD--------------------ASFL 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  720 LQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF-----DEFSLWKSQVDNG 794
Cdd:cd18006    119 KSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdklDDFIKAYSETDDE 198
                          250
                   ....*....|....*....
gi 1907152327  795 SmKGGERLSILTKSLLLRR 813
Cdd:cd18006    199 S-ETVEELHLLLQPFLLRR 216
DEXDc smart00487
DEAD-like helicases superfamily;
562-791 2.79e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.02  E-value: 2.79e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327   562 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTKKNQQKSKekersepvtwlskndssvftssGTLIVC 641
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGG----------------------RVLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327   642 P-ASLIHHWKNEVEKRVTSNRLR-IYLYHGPNRSRHAKVLST--YDIVITTYSLLAKEIPttkqegevpganlsvegtSA 717
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLE------------------ND 123
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152327   718 PLLQVVWARIILDEAHNVKNP--RVQTSIAVCKLQAQA-RWAVTGTPIQNNLLDMYSLMK-FLRCSPFDEFSLWKSQV 791
Cdd:smart00487  124 KLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
566-815 7.26e-22

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: 95.51  E-value: 7.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekersepvTWL--SKNDSSVFtssgtLIVCPA 643
Cdd:cd17996      7 YQLKGLQWMVSLYNNN-LNGILADEMGLGKTIQTISLI------------------TYLmeKKKNNGPY-----LVIVPL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  644 SLIHHWKNEVEKRVTSnrLRIYLYHGPNRSRHAK----VLSTYDIVITTYSLLAKEIPTtkqegevpganlsvegtsapL 719
Cdd:cd17996     63 STLSNWVSEFEKWAPS--VSKIVYKGTPDVRKKLqsqiRAGKFNVLLTTYEYIIKDKPL--------------------L 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  720 LQVVWARIILDEAHNVKNprvqtsiAVCKL--------QAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-- 783
Cdd:cd17996    121 SKIKWKYMIIDEGHRMKN-------AQSKLtqtlntyyHARYRLLLTGTPLQNNLPELWALLNFLlpkifkSCKTFEQwf 193
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907152327  784 ---FSLWKSQvDNGSMKGGERLSI---LTKSL---LLRRTK 815
Cdd:cd17996    194 ntpFANTGEQ-VKIELNEEETLLIirrLHKVLrpfLLRRLK 233
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
562-815 1.06e-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: 92.39  E-value: 1.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  562 PLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekeRSEPvtwlskndssvftsSGTLIVC 641
Cdd:cd18065     15 TLRDYQVRGLNWMI-SLYENGVNGILADEMGLGKTLQTIALLGYLKHY-------RNIP--------------GPHMVLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTSnrLRIYLYHGPNRSRHAKVLST-----YDIVITTYSLLAKEIPTTKQegevpganlsvegts 716
Cdd:cd18065     73 PKSTLHNWMNEFKRWVPS--LRAVCLIGDKDARAAFIRDVmmpgeWDVCVTSYEMVIKEKSVFKK--------------- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  717 apllqVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWKSQVDN 793
Cdd:cd18065    136 -----FNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaDDFDSWFDTKNC 210
                          250       260
                   ....*....|....*....|...
gi 1907152327  794 -GSMKGGERLSILTKSLLLRRTK 815
Cdd:cd18065    211 lGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
566-824 3.75e-20

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: 90.88  E-value: 3.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTKKNQqkskekeRSEPvtwlskndssvftsSGTLIVCPASL 645
Cdd:cd18064     19 YQVRGLNWLI-SLYENGINGILADEMGLGKTLQTISLLGYMKHY-------RNIP--------------GPHMVLVPKST 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSnrLRIYLYHGPNRSRHAKVLST-----YDIVITTYSLLAKEIPTTKQEGevpganlsvegtsapll 720
Cdd:cd18064     77 LHNWMAEFKRWVPT--LRAVCLIGDKDQRAAFVRDVllpgeWDVCVTSYEMLIKEKSVFKKFN----------------- 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 qvvWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF---DEFSLWkSQVDN--GS 795
Cdd:cd18064    138 ---WRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaEDFDSW-FDTNNclGD 213
                          250       260
                   ....*....|....*....|....*....
gi 1907152327  796 MKGGERLSILTKSLLLRRTKDQLDSTGKP 824
Cdd:cd18064    214 QKLVERLHMVLRPFLLRRIKADVEKSLPP 242
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
566-781 1.80e-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: 87.44  E-value: 1.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqQKSKEKERSEPvtwlskndssvftssgTLIVCPASL 645
Cdd:cd17998      4 YQLIGLNWLNLLYQKK-LSGILADEMGLGKTIQVIAFL------AYLKEIGIPGP----------------HLVVVPSST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSnrLRIYLYHGPN------RSRHAKVLSTYDIVITTYSLLakeipTTKQEGEVPGANLSvegtsapl 719
Cdd:cd17998     61 LDNWLREFKRWCPS--LKVEPYYGSQeerkhlRYDILKGLEDFDVIVTTYNLA-----TSNPDDRSFFKRLK-------- 125
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907152327  720 LQVVwariILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF 781
Cdd:cd17998    126 LNYV----VYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
563-813 6.85e-19

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: 86.49  E-value: 6.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWREsqkpqGGIL-ADDMGLGKTLTMIALILTKKNqqkskekerSEPVtwlskndssvftssgtLIVC 641
Cdd:cd18010      1 LLPFQREGVCFALRRG-----GRVLiADEMGLGKTVQAIAIAAYYRE---------EWPL----------------LIVC 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  642 PASLIHHWKNEVEKRVTS-NRLRIYLYHGpnrSRHAKVLSTYDIVITTYSLLAKEipttkqEGEVPGANLSVegtsapll 720
Cdd:cd18010     51 PSSLRLTWADEIERWLPSlPPDDIQVIVK---SKDGLRDGDAKVVIVSYDLLRRL------EKQLLARKFKV-------- 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 qvvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAV--TGTPIQNNLLDMYSLMKFLR---CSPFDEFSlwKSQVDNGS 795
Cdd:cd18010    114 ------VICDESHYLKNSKAKRTKAALPLLKRAKRVIllSGTPALSRPIELFTQLDALDpklFGRFHDFG--RRYCAAKQ 185
                          250       260
                   ....*....|....*....|....*...
gi 1907152327  796 MKGG----------ERLSILTKSLLLRR 813
Cdd:cd18010    186 GGFGwdysgssnleELHLLLLATIMIRR 213
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
985-1099 2.02e-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: 2.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  985 KVSSLLAELEAIQKGpgsqKSVIVSQWTSMLQVVALhLKKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAG 1064
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRK--GKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907152327 1065 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1099
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
566-813 2.17e-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: 85.63  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALIltkknQQKSKEKERSEPVtwlskndssvftssgtLIVCPA 643
Cdd:cd18002      4 YQLKGLNWLA---NLYEQGinGILADEMGLGKTVQSIAVL-----AHLAEEHNIWGPF----------------LVIAPA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  644 SLIHHWKNEVEKRVTsnRLRIYLYHGPNRSRhaKVL-------------STYDIVITTYSLLAKEIpttkqegevpganl 710
Cdd:cd18002     60 STLHNWQQEISRFVP--QFKVLPYWGNPKDR--KVLrkfwdrknlytrdAPFHVVITSYQLVVQDE-------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  711 svegtsAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFD---EFSLW 787
Cdd:cd18002    122 ------KYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDshdEFNEW 195
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907152327  788 KSQ-VDNGSMKGG-------ERLSILTKSLLLRR 813
Cdd:cd18002    196 FSKdIESHAENKTglnehqlKRLHMILKPFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
567-813 1.26e-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: 82.79  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  567 QKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALI--LTKKNQQkskekerSEPVtwlskndssvftssgtLIVCP 642
Cdd:cd17993      6 QLTGLNWLahSW---CKGNNGILADEMGLGKTVQTISFLsyLFHSQQQ-------YGPF----------------LVVVP 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEKRVTSnrLRIYLYHGPNRSRhaKVLSTYD------------IVITTYSLLAKEipttKQEgevpganl 710
Cdd:cd17993     60 LSTMPAWQREFAKWAPD--MNVIVYLGDIKSR--DTIREYEfyfsqtkklkfnVLLTTYEIILKD----KAF-------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  711 svegtsapLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRcsPfDEFSLWKS- 789
Cdd:cd17993    124 --------LGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLM--P-GKFDIWEEf 192
                          250       260
                   ....*....|....*....|....*.
gi 1907152327  790 --QVDNGSMKGGERLSILTKSLLLRR 813
Cdd:cd17993    193 eeEHDEEQEKGIADLHKELEPFILRR 218
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
563-776 1.31e-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: 1.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLwreSQKPQGGILADDMGLGKTLTMIALIltkknqqkskeKERsepvtWLSKNDSSVftssgtLIVCP 642
Cdd:cd18011      1 PLPHQIDAVLRAL---RKPPVRLLLADEVGLGKTIEAGLII-----------KEL-----LLRGDAKRV------LILCP 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEKRVTSNRLRIY-LYHGPNRSRHAKVLSTYDIVITTYSLLakeipttKQEGEVPGANLSVEgtsapllq 721
Cdd:cd18011     56 ASLVEQWQDELQDKFGLPFLILDrETAAQLRRLIGNPFEEFPIVIVSLDLL-------KRSEERRGLLLSEE-------- 120
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152327  722 vvWARIILDEAHNVKN---PRVQTSIAVCKLQAQARWAV---TGTPIQNNLLDMYSLMKFL 776
Cdd:cd18011    121 --WDLVVVDEAHKLRNsggGKETKRYKLGRLLAKRARHVlllTATPHNGKEEDFRALLSLL 179
HELICc smart00490
helicase superfamily c-terminal domain;
1016-1099 1.40e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 72.63  E-value: 1.40e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  1016 QVVALHLKKNRLTYATIDGSVNPKQRMDLVEAFNHsqGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRI 1095
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1907152327  1096 YRVG 1099
Cdd:smart00490   79 GRAG 82
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
566-813 5.32e-15

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: 75.48  E-value: 5.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekersepvtwlsKNDSSVFTSSGTLIVCPASL 645
Cdd:cd18060      4 YQLEGVNWLLFNWYNR-QNCILADEMGLGKTIQSIAFL----------------------QEVYNVGIHGPFLVIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSNRLriyLYHGPNRSRHakvlstydiVITTYSLLAKE-----IPTTKQEGEVPGANLSVEGTSAPLL 720
Cdd:cd18060     61 ITNWEREFNTWTEMNTI---VYHGSLASRQ---------MIQQYEMYCKDsrgrlIPGAYKFDALITTFEMILSDCPELR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPF-DEFSLWKSQVDNGSMKGG 799
Cdd:cd18060    129 EIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLKDFGDLKTEEQV 208
                          250
                   ....*....|....
gi 1907152327  800 ERLSILTKSLLLRR 813
Cdd:cd18060    209 QKLQAILKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
547-813 5.61e-15

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: 75.81  E-value: 5.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  547 PGETAVAEDPA---GLKVPLLLHQKQALAWLL--WRESQKPqggILADDMGLGKTLTMIALILTKKNQQKskekersepv 621
Cdd:cd18054      2 PRFVALKKQPSyigGENLELRDYQLEGLNWLAhsWCKNNSV---ILADEMGLGKTIQTISFLSYLFHQHQ---------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  622 twlskndssvfTSSGTLIVCPASLIHHWKNEVEkrVTSNRLRIYLYHGPNRSRhaKVLSTYD------------IVITTY 689
Cdd:cd18054     69 -----------LYGPFLLVVPLSTLTSWQREFE--IWAPEINVVVYIGDLMSR--NTIREYEwihsqtkrlkfnALITTY 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  690 SLLAKEipttkqegevpganlsvegtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDM 769
Cdd:cd18054    134 EILLKD--------------------KTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKEL 193
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907152327  770 YSLMKFLRCSPFDEFSLWKSQVDNGSMKGGERLSILTKSLLLRR 813
Cdd:cd18054    194 WSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
566-813 8.22e-15

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: 75.08  E-value: 8.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLtmialiltkknqqkskekersEPVTWLSKndssVF---TSSGTLIVCP 642
Cdd:cd18058      4 YQLEGMNWLLFNWYNR-KNCILADEMGLGKTI---------------------QSITFLSE----IFlmgIRGPFLIIAP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEkrvTSNRLRIYLYHGPNRSRH-------------AKVLS---TYDIVITTYSLLAKEIPTTKQegevp 706
Cdd:cd18058     58 LSTITNWEREFR---TWTEMNAIVYHGSQISRQmiqqyemyyrdeqGNPLSgifKFQVVITTFEMILADCPELKK----- 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  707 ganlsvegtsapllqVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSL 786
Cdd:cd18058    130 ---------------INWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT 194
                          250       260       270
                   ....*....|....*....|....*....|
gi 1907152327  787 WKSQVdnGSMKGGE---RLSILTKSLLLRR 813
Cdd:cd18058    195 FLEEF--GDLKTEEqvkKLQSILKPMMLRR 222
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
566-775 4.81e-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: 4.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLlWR--ESQKPQGG---ILADDMGLGKTLTMIALILT--KKNQQKSKEKERSepvtwlskndssvftssgtL 638
Cdd:cd18067      4 HQREGVKFL-YRcvTGRRIRGShgcIMADEMGLGKTLQCITLMWTllRQSPQCKPEIDKA-------------------I 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  639 IVCPASLIHHWKNEVEK----RVT-------------SNRLRIYLYHGPNRSRHAKVLStYDivitTYSLLAKEIpttkQ 701
Cdd:cd18067     64 VVSPSSLVKNWANELGKwlggRLQplaidggskkeidRKLVQWASQQGRRVSTPVLIIS-YE----TFRLHVEVL----Q 134
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152327  702 EGEVpganlsvegtsapllqvvwARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKF 775
Cdd:cd18067    135 KGEV-------------------GLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNF 189
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
584-777 1.13e-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: 68.69  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  584 GGILADDMGLGKTLTMIALILTKKNQQKSKEkersepvtwlskndssvftssgTLIVCPASLIHHWKNEVEKRVTSnrlr 663
Cdd:cd18069     30 GCILAHSMGLGKTLQVISFLDVLLRHTGAKT----------------------VLAIVPVNTLQNWLSEFNKWLPP---- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  664 iYLYHGPNRSRHAKVLSTYDIVITTYSLlAKEIPTTKQEGEV-----------PGANLsvegtsapllqvvwarIILDEA 732
Cdd:cd18069     84 -PEALPNVRPRPFKVFILNDEHKTTAAR-AKVIEDWVKDGGVllmgyemfrlrPGPDV----------------VICDEG 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907152327  733 HNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR 777
Cdd:cd18069    146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
566-815 7.25e-12

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: 67.01  E-value: 7.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekersepvTWLSKNDSsvfTSSGTLIVCPASL 645
Cdd:cd18063     27 YQLQGLEWMVSLYNNN-LNGILADEMGLGKTIQTIALI------------------TYLMEHKR---LNGPYLIIVPLST 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSnRLRIYlYHGPNRSRHAKV----LSTYDIVITTYSLLAKEipttkqegevpganlsvegtSAPLLQ 721
Cdd:cd18063     85 LSNWTYEFDKWAPS-VVKIS-YKGTPAMRRSLVpqlrSGKFNVLLTTYEYIIKD--------------------KHILAK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  722 VVWARIILDEAHNVKNPRVQ-TSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-----FSLWKS 789
Cdd:cd18063    143 IRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGE 222
                          250       260
                   ....*....|....*....|....*....
gi 1907152327  790 QVD---NGSMKGGERLSILTKSLLLRRTK 815
Cdd:cd18063    223 RVDlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
566-813 1.45e-11

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: 65.44  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLL--WRESQKpqgGILADDMGLGKTLTMIALILTkknqqkskekersepvTWLsKNDSSVFtssgtLIVCPA 643
Cdd:cd18059      4 YQLEGVNWLLfnWYNTRN---CILADEMGLGKTIQSITFLYE----------------IYL-KGIHGPF-----LVIAPL 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  644 SLIHHWKNEVEkrvTSNRLRIYLYHGPNRSRhaKVLSTYDI------------------VITTYSLLAKEIPTtkqegev 705
Cdd:cd18059     59 STIPNWEREFR---TWTELNVVVYHGSQASR--RTIQLYEMyfkdpqgrvikgsykfhaIITTFEMILTDCPE------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  706 pganlsvegtsapLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFS 785
Cdd:cd18059    127 -------------LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSET 193
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907152327  786 LWKSQVdnGSMKGGE---RLSILTKSLLLRR 813
Cdd:cd18059    194 TFMQEF--GDLKTEEqvqKLQAILKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
566-815 1.95e-11

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: 65.45  E-value: 1.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqkskekersepvTWLSKNDSsvfTSSGTLIVCPASL 645
Cdd:cd18062     27 YQIKGLEWLVSLYNNN-LNGILADEMGLGKTIQTIALI------------------TYLMEHKR---INGPFLIIVPLST 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRVTSnrLRIYLYHGPNRSRHAKV----LSTYDIVITTYSLLAKEipttkqegevpganlsvegtSAPLLQ 721
Cdd:cd18062     85 LSNWVYEFDKWAPS--VVKVSYKGSPAARRAFVpqlrSGKFNVLLTTYEYIIKD--------------------KQILAK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  722 VVWARIILDEAHNVKNPRVQ-TSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL------RCSPFDE-----FSLWKS 789
Cdd:cd18062    143 IRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGE 222
                          250       260
                   ....*....|....*....|....*....
gi 1907152327  790 QVD---NGSMKGGERLSILTKSLLLRRTK 815
Cdd:cd18062    223 KVDlneEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
565-789 1.03e-10

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: 62.07  E-value: 1.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  565 LH--QKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALI--LTKKNQQKSkekersePVtwlskndssvftssgtLIV 640
Cdd:cd17994      1 LHpyQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLysLYKEGHSKG-------PF----------------LVS 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  641 CPASLIHHWKNEVEkrVTSNRLRIYLYHGPNrsrhakvlstydIVITTYSLLAKEipttkqegevpganlsvegtSAPLL 720
Cdd:cd17994     57 APLSTIINWEREFE--MWAPDFYVVTYVGDH------------VLLTSYELISID--------------------QAILG 102
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152327  721 QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLrcSPfDEFSLWKS 789
Cdd:cd17994    103 SIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFL--TP-ERFNNLQG 168
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
566-776 1.13e-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: 62.75  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwresQKPQGGILADdMGLGKTLTMIALIltkknqQKSKEKERSEPVtwlskndssvftssgtLIVCPASL 645
Cdd:cd18013      4 YQKVAINFII----EHPYCGLFLD-MGLGKTVTTLTAL------SDLQLDDFTRRV----------------LVIAPLRV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHH-WKNEVEKRVTSNRLRIYLYHGPNRSRHAKVLSTYDIVITTYSLLAKEIptTKQEGEVPganlsvegtsapllqvvW 724
Cdd:cd18013     57 ARStWPDEVEKWNHLRNLTVSVAVGTERQRSKAANTPADLYVINRENLKWLV--NKSGDPWP-----------------F 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907152327  725 ARIILDEAHNVKNPRVQTSIAVCKLQAQARWAV--TGTPIQNNLLDMYSLMKFL 776
Cdd:cd18013    118 DMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIglTGTPSPNGLMDLWAQIALL 171
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
577-777 1.95e-10

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: 62.60  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  577 RESQKPQG--GILADDMGLGKTLTMIALILTKKNQQKSKEKERsepvtwlskndssvftssgTLIVCPASLIHHWKNEVE 654
Cdd:cd18068     21 KKTKKSPGsgCILAHCMGLGKTLQVVTFLHTVLLCEKLENFSR-------------------VLVVCPLNTVLNWLNEFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  655 KRVT----SNRLRIY---LYHGPNRSRHAKVLSTYD--IVITTYSL---LAKE--IPTTKQEGEV-------PGANLsve 713
Cdd:cd18068     82 KWQEglkdEEKIEVNelaTYKRPQERSYKLQRWQEEggVMIIGYDMyriLAQErnVKSREKLKEIfnkalvdPGPDF--- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152327  714 gtsapllqvvwarIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLR 777
Cdd:cd18068    159 -------------VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
566-813 2.44e-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: 61.99  E-value: 2.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALIltkknQQKSKEKERSEPVtwlskndssvftssgtLIVCPASL 645
Cdd:cd18053     24 YQLNGLNWLA-HSWCKGNSCILADEMGLGKTIQTISFL-----NYLFHEHQLYGPF----------------LLVVPLST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEKRV-------------TSNRLRIYLYHGPNRSRhakvlSTYDIVITTYSLLAKEipttkqegevpganlsv 712
Cdd:cd18053     82 LTSWQREIQTWApqmnavvylgdinSRNMIRTHEWMHPQTKR-----LKFNILLTTYEILLKD----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  713 egtSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVD 792
Cdd:cd18053    140 ---KSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHG 216
                          250       260
                   ....*....|....*....|.
gi 1907152327  793 NGSMKGGERLSILTKSLLLRR 813
Cdd:cd18053    217 KGREYGYASLHKELEPFLLRR 237
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
566-813 3.70e-10

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: 61.17  E-value: 3.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltkknqqksKEKERSEpvtwlskndssvfTSSGTLIVCPASL 645
Cdd:cd18061      4 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFL---------YEILLTG-------------IRGPFLIIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEkrvTSNRLRIYLYHGPNRSRhaKVLSTYDIVITTYSllAKEIPTTKQEGEVPGANLSVEGTSAPLLQVVWA 725
Cdd:cd18061     61 IANWEREFR---TWTDLNVVVYHGSLISR--QMIQQYEMYFRDSQ--GRIIRGAYRFQAIITTFEMILGGCPELNAIDWR 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  726 RIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEFSLWKSQVdnGSMKGGE---RL 802
Cdd:cd18061    134 CVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF--GDLKTEEqvqKL 211
                          250
                   ....*....|.
gi 1907152327  803 SILTKSLLLRR 813
Cdd:cd18061    212 QAILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
566-784 4.20e-10

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: 61.23  E-value: 4.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKKNQQKSKekersepvtwlskndssvftsSGTLIVCPASL 645
Cdd:cd18057      4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTIVFLYSLYKEGHSK---------------------GPYLVSAPLST 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEkrVTSNRLRIYLYHGPNRSRHA---KVLSTYDIVITTysllAKEIPTTKQEGEVpgaNLSVEGTSAPLL-- 720
Cdd:cd18057     62 IINWEREFE--MWAPDFYVVTYTGDKESRSVireNEFSFEDNAIRS----GKKVFRMKKEAQI---KFHVLLTSYELIti 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  721 ------QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFDEF 784
Cdd:cd18057    133 dqailgSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNL 202
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
563-782 3.49e-09

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: 58.48  E-value: 3.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  563 LLLHQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKknqqkSKEKERSEPVtwlskndssvftssgtLIVCP 642
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYSL-----YKEGHTKGPF----------------LVSAP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  643 ASLIHHWKNEVEkrVTSNRLRIYLYHGPNRSR---HAKVLSTYDIVITTysllAKEIPTTKQEGEVPGANLS-----VEG 714
Cdd:cd18055     59 LSTIINWEREFQ--MWAPDFYVVTYTGDKDSRaiiRENEFSFDDNAVKG----GKKAFKMKREAQVKFHVLLtsyelVTI 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152327  715 TSAPLLQVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFLRCSPFD 782
Cdd:cd18055    133 DQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFN 200
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
566-776 1.04e-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: 57.00  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTKKNQQKSKekersepvtwlskndssvftsSGTLIVCPASL 645
Cdd:cd18056      4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTAVFLYSLYKEGHSK---------------------GPFLVSAPLST 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  646 IHHWKNEVEkrVTSNRLRIYLYHGPNRSR---HAKVLSTYDIVITTysllAKEIPTTKQEGEVpgaNLSVEGTSAPLL-- 720
Cdd:cd18056     62 IINWEREFE--MWAPDMYVVTYVGDKDSRaiiRENEFSFEDNAIRG----GKKASRMKKEASV---KFHVLLTSYELIti 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907152327  721 ------QVVWARIILDEAHNVKNPRVQTSIAVCKLQAQARWAVTGTPIQNNLLDMYSLMKFL 776
Cdd:cd18056    133 dmailgSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFL 194
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
553-761 1.07e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.27  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  553 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTKKNQQKskekersepvtwlskndssvf 632
Cdd:COG1061     71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  633 tssgTLIVCP-ASLIHHWKNEVEKrvtsnRLRIYLYHGPNRSRHakvlstYDIVITTYSLLAKeipttkqegevpgaNLS 711
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKDSD------APITVATYQSLAR--------------RAH 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907152327  712 VEgtsapLLQVVWARIILDEAHNVKNPRVQTSIAvcKLQAQARWAVTGTP 761
Cdd:COG1061    181 LD-----ELGDRFGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
566-735 5.74e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.30  E-value: 5.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  566 HQKQALAWLLWRESQKPqgGILADDMGLGKTLTMIALILTKKNQqkskekersepvtwlskndssvftssGTLIVCP-AS 644
Cdd:cd17926      4 YQEEALEAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKEL--------------------------RTLIVVPtDA 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  645 LIHHWKNEVEKRVTSNRLRIylyhgpNRSRHAKVLSTYDIVITTYSLLAKEIPTTKqegevpganlsvEGTSAPLLqvvw 724
Cdd:cd17926     56 LLDQWKERFEDFLGDSSIGL------IGGGKKKDFDDANVVVATYQSLSNLAEEEK------------DLFDQFGL---- 113
                          170
                   ....*....|.
gi 1907152327  725 arIILDEAHNV 735
Cdd:cd17926    114 --LIVDEAHHL 122
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-44 7.28e-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: 43.93  E-value: 7.28e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907152327    4 VKCPeHGDACFLKTGVRDGPNKGKSFYVC---RTNTCGFVQATD 44
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGFFQWAD 43
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
637-749 8.06e-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: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152327  637 TLIVCPASL-IHHWKNEVEKRVTSNRLRIYLYHGPNRSRhakvLSTYDIVITTYSLLAKeipTTKqegevpgANLSVEGT 715
Cdd:cd18029     54 TLVLCTSAVsVEQWRRQFLDWTTIDDEQIGRFTSDKKEI----FPEAGVTVSTYSMLAN---TRK-------RSPESEKF 119
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907152327  716 SAPLLQVVWARIILDEAHNVKNP---RVQTSIAV-CKL 749
Cdd:cd18029    120 MEFITEREWGLIILDEVHVVPAPmfrRVLTLQKAhCKL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH