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Conserved domains on  [gi|2217271652|ref|XP_047288113|]
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transcription termination factor 2 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
570-819 8.01e-146

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: 437.68  E-value: 8.01e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 647
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILaDDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  648 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 727
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  728 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 807
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 2217271652  808 LSILTKSLLLRR 819
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1141 5.16e-124

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 5.16e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGIL-DDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 637
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLaDDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  638 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 716
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  717 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 792
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  793 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 872
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  873 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 952
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  953 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1031
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652 1032 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1111
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 2217271652 1112 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1141
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
zf-GRF super family cl46396
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-39 8.07e-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: 8.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217271652    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
147-378 1.92e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 2217271652  375 TLDL 378
Cdd:PTZ00108  1385 EDDD 1388
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
570-819 8.01e-146

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: 437.68  E-value: 8.01e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 647
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILaDDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  648 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 727
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  728 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 807
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 2217271652  808 LSILTKSLLLRR 819
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1141 5.16e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 5.16e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGIL-DDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 637
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLaDDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  638 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 716
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  717 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 792
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  793 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 872
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  873 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 952
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  953 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1031
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652 1032 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1111
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 2217271652 1112 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1141
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
573-932 1.14e-71

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: 240.66  E-value: 1.14e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdFTSHGTLIICPASL 651
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILaDEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSNKLRVYLYHGPNRDSRA-----RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLL 726
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN-----GS 801
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  802 KKGGERLSILTKSLLLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYNVFFarsrsalqsylkrHESRGNQsgr 881
Cdd:pfam00176  201 KKGVSRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-------------LKKDLNA--- 258
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217271652  882 spnnpfsrVALEFGSEEPRHSeaadsprsstvhILSQLLRLRQCCCHLSLL 932
Cdd:pfam00176  259 --------IKTGEGGREIKAS------------LLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
989-1116 5.72e-52

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: 178.44  E-value: 5.72e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  989 STKISSLLAELEAIQRNSasQKSVIVSQWTNMLKVVALHLKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLL 1068
Cdd:cd18793     10 SGKLEALLELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217271652 1069 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVVIHRFV 1116
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
563-1132 7.75e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 157.65  E-value: 7.75e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  563 PAGLKVPLLLHQKQALAWLLwRESQKPQGGIL-DDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkdDSCDFTS- 640
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLI-RLYENGINGILaDEMGLGKTLQTISL------------------LGYLH--EYRGITGp 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  641 HgtLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRAR------VLSTYDIVITTYSLVAKEiptnkqeaeipga 714
Cdd:PLN03142   222 H--MVVAPKSTLGNWMNEIRRFCPV--LRAVKFHG-NPEERAHqreellVAGKFDVCVTSFEMAIKE------------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  715 nlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFN 791
Cdd:PLN03142   284 -------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFD 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  792 LWRSQvdNGSKKGGERLSILTKSL---LLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYnvffarsRSALQSY 868
Cdd:PLN03142   357 EWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------KALLQKD 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  869 LKrhesrgnqsgrspnnpfsrvALEFGSEEPRhseaadsprsstvhILSQLLRLRQCCCHLSLLKSAL-DPMELKGEGLV 947
Cdd:PLN03142   422 LD--------------------VVNAGGERKR--------------LLNIAMQLRKCCNHPYLFQGAEpGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  948 lsleeqlsaltlselrdsEPSStvslngtffKMELFEgmrestkisSLLAELEaiQRNSasqKSVIVSQWTNMLKVVALH 1027
Cdd:PLN03142   468 ------------------ENSG---------KMVLLD---------KLLPKLK--ERDS---RVLIFSQMTRLLDILEDY 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652 1028 LKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQ 1106
Cdd:PLN03142   507 LMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQ 586
                          570       580
                   ....*....|....*....|....*.
gi 2217271652 1107 QKDVVIHRFVCEGTVEEKILQLQEKK 1132
Cdd:PLN03142   587 KKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXDc smart00487
DEAD-like helicases superfamily;
569-797 3.14e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 3.14e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652   569 PLLLHQKQALAWLLWREsqkpQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscdftshgTLIIC 647
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILaAPTGSGKTLAALLPALEALKRGKGGR----------------------VLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652   648 P-ASLIHHWKNEVEKRVNSNKLR-VYLYHGPNRDSRARVLST--YDIVITTYSLVAKEIPTNKqeaeipganlnvegtst 723
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDK----------------- 124
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217271652   724 pLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACA-RWAVTGTPIQNNLLDMYSLLK-FLRCSPFDEFNLWRSQV 797
Cdd:smart00487  125 -LSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
991-1105 5.64e-19

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: 83.41  E-value: 5.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  991 KISSLLAELEAIQRNsasqKSVIVSQWTNMLKVVALhLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAG 1070
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217271652 1071 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1105
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1024-1105 2.36e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.94  E-value: 2.36e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  1024 VALHLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYR 1103
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 2217271652  1104 VG 1105
Cdd:smart00490   81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
560-767 9.83e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.19  E-value: 9.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  560 AEDPAGLKVPLLLHQKQAL-AWLLWRESQKPQGGILDDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdf 638
Cdd:COG1061     71 GDEASGTSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  639 tshgTLIICP-ASLIHHWKNEVEKrvnsnKLRVYLYHGPNRDSrarvlsTYDIVITTYSLVAKEIPTNKqeaeipganln 717
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKDS------DAPITVATYQSLARRAHLDE----------- 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217271652  718 vegtstplLRIAWARIILDEAHNVKNPRVQTSIAvcKLQACARWAVTGTP 767
Cdd:COG1061    184 --------LGDRFGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-39 8.07e-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: 8.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217271652    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
147-378 1.92e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 2217271652  375 TLDL 378
Cdd:PTZ00108  1385 EDDD 1388
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
570-819 8.01e-146

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: 437.68  E-value: 8.01e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 647
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILaDDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  648 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 727
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  728 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 807
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 2217271652  808 LSILTKSLLLRR 819
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1141 5.16e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 396.90  E-value: 5.16e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGIL-DDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 637
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLaDDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  638 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 716
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  717 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 792
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  793 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 872
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  873 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 952
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  953 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1031
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652 1032 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1111
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 2217271652 1112 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1141
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
570-819 1.85e-100

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: 317.69  E-value: 1.85e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWResqkpqGGIL-DDMGLGKTLTMIALILTQKNQEKKEEKEKSTaltwLSKDDSCDFTSHGTLIICP 648
Cdd:cd18008      1 LLPYQKQGLAWMLPR------GGILaDEMGLGKTIQALALILATRPQDPKIPEELEE----NSSDPKKLYLSKTTLIVVP 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQeaeiPGANLNVEGTSTPLLRI 728
Cdd:cd18008     71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPKNKK----GGGRDSKEKEASPLHRI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  729 AWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQV----DNGSKKG 804
Cdd:cd18008    147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDIskpfSKNDRKA 226
                          250
                   ....*....|....*
gi 2217271652  805 GERLSILTKSLLLRR 819
Cdd:cd18008    227 LERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
573-932 1.14e-71

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: 240.66  E-value: 1.14e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdFTSHGTLIICPASL 651
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILaDEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSNKLRVYLYHGPNRDSRA-----RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLL 726
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN-----GS 801
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  802 KKGGERLSILTKSLLLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYNVFFarsrsalqsylkrHESRGNQsgr 881
Cdd:pfam00176  201 KKGVSRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-------------LKKDLNA--- 258
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217271652  882 spnnpfsrVALEFGSEEPRHSeaadsprsstvhILSQLLRLRQCCCHLSLL 932
Cdd:pfam00176  259 --------IKTGEGGREIKAS------------LLNILMRLRKICNHPGLI 289
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
570-819 5.03e-62

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: 211.56  E-value: 5.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRE-----------------------SQK--PQ---GGIL-DDMGLGKTLTMIALILTQKnqekkee 620
Cdd:cd18071      1 LLPHQKQALAWMVSREnsqdlppfweeavglflntitnfSQKkrPElvrGGILaDDMGLGKTLTTISLILANF------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  621 kekstaltwlskddscdftshgTLIICPASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAK 700
Cdd:cd18071     74 ----------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLAS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  701 EiptnkqeaeipganlnvEGT--STPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSL 778
Cdd:cd18071    132 D-----------------FGAkgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2217271652  779 LKFLRCSPFDEFNLWRS----QVDNGSKKGGERLSILTKSLLLRR 819
Cdd:cd18071    195 LSFLHLKPFSNPEYWRRliqrPLTMGDPTGLKRLQVLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
570-818 1.17e-53

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: 188.32  E-value: 1.17e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWResqkpqGGIL-DDMGLGKTLTMIALILTQKNQEKKeekekSTALTWLSKDDSC---------DFT 639
Cdd:cd18070      1 LLPYQRRAVNWMLVP------GGILaDEMGLGKTVEVLALILLHPRPDND-----LDAADDDSDEMVCcpdclvaetPVS 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  640 SHGTLIICPASLIHHWKNEVEKRVNSNkLRVYLYHGPNRDS-----RARVLSTYDIVITTYSLVAKEIptnkQEAEIPGA 714
Cdd:cd18070     70 SKATLIVCPSAILAQWLDEINRHVPSS-LKVLTYQGVKKDGalaspAPEILAEYDIVVTTYDVLRTEL----HYAEANRS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  715 NL------NVEGTSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD 788
Cdd:cd18070    145 NRrrrrqkRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2217271652  789 EFNLWRSQVDN--GSKKGGERLSILTKSLLLR 818
Cdd:cd18070    225 DSDWWARVLIRpqGRNKAREPLAALLKELLWR 256
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
989-1116 5.72e-52

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: 178.44  E-value: 5.72e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  989 STKISSLLAELEAIQRNSasQKSVIVSQWTNMLKVVALHLKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLL 1068
Cdd:cd18793     10 SGKLEALLELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217271652 1069 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVVIHRFV 1116
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
570-794 3.17e-51

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: 178.53  E-value: 3.17e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRESQKPqGGIL-DDMGLGKTLTMIALILTQKNQekkeekekstaltwlsKDDSCDFtshgtLIICP 648
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGP-GGILaDEMGLGKTLQAIAFLAYLLKE----------------GKERGPV-----LVVCP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSnkLRVYLYHGPNRDSRAR----VLSTYDIVITTYSLVAKEIPTnkqeaeipganlnvegtstp 724
Cdd:cd17919     59 LSVLENWEREFEKWTPD--LRVVVYHGSQRERAQIrakeKLDKFDVVLTTYETLRRDKAS-------------------- 116
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  725 LLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCsPFdefnLWR 794
Cdd:cd17919    117 LRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP-PF----LLR 181
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
574-821 5.75e-48

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: 170.44  E-value: 5.75e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  574 QKQALAWLlWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdftSHGTLIICPASLI 652
Cdd:cd18012      9 QKEGFNWL-SFLRHYGLGGILaDDMGLGKTLQTLALLLSRKEEGR----------------------KGPSLVVAPTSLI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRvnSNKLRVYLYHGPNRDSRA-RVLSTYDIVITTYSLVAKEIptnkqEAeipganlnvegtstpLLRIAWA 731
Cdd:cd18012     66 YNWEEEAAKF--APELKVLVIHGTKRKREKlRALEDYDLVITSYGLLRRDI-----EL---------------LKEVKFH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  732 RIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLrcSP-----FDEFN-LWRSQVDNGSKKGG 805
Cdd:cd18012    124 YLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPgllgsYKRFKkRFAKPIEKDGDEEA 201
                          250
                   ....*....|....*..
gi 2217271652  806 -ERLSILTKSLLLRRTK 821
Cdd:cd18012    202 lEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
563-1132 7.75e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 157.65  E-value: 7.75e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  563 PAGLKVPLLLHQKQALAWLLwRESQKPQGGIL-DDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkdDSCDFTS- 640
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLI-RLYENGINGILaDEMGLGKTLQTISL------------------LGYLH--EYRGITGp 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  641 HgtLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRAR------VLSTYDIVITTYSLVAKEiptnkqeaeipga 714
Cdd:PLN03142   222 H--MVVAPKSTLGNWMNEIRRFCPV--LRAVKFHG-NPEERAHqreellVAGKFDVCVTSFEMAIKE------------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  715 nlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFN 791
Cdd:PLN03142   284 -------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFD 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  792 LWRSQvdNGSKKGGERLSILTKSL---LLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYnvffarsRSALQSY 868
Cdd:PLN03142   357 EWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------KALLQKD 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  869 LKrhesrgnqsgrspnnpfsrvALEFGSEEPRhseaadsprsstvhILSQLLRLRQCCCHLSLLKSAL-DPMELKGEGLV 947
Cdd:PLN03142   422 LD--------------------VVNAGGERKR--------------LLNIAMQLRKCCNHPYLFQGAEpGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  948 lsleeqlsaltlselrdsEPSStvslngtffKMELFEgmrestkisSLLAELEaiQRNSasqKSVIVSQWTNMLKVVALH 1027
Cdd:PLN03142   468 ------------------ENSG---------KMVLLD---------KLLPKLK--ERDS---RVLIFSQMTRLLDILEDY 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652 1028 LKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQ 1106
Cdd:PLN03142   507 LMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQ 586
                          570       580
                   ....*....|....*....|....*.
gi 2217271652 1107 QKDVVIHRFVCEGTVEEKILQLQEKK 1132
Cdd:PLN03142   587 KKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
573-782 2.52e-31

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: 123.23  E-value: 2.52e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALIltqknqekkeekekstALTWLSKDDSCDFTSHGTLIICPASLI 652
Cdd:cd17999      4 YQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL----------------ASDHHKRANSFNSENLPSLVVCPPTLV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSNKLRVYLYHGPNRDSRARV--LSTYDIVITTYSLVAKEIPTnkqeaeipganlnvegtstpLLRIAW 730
Cdd:cd17999     68 GHWVAEIKKYFPNAFLKPLAYVGPPQERRRLReqGEKHNVIVASYDVLRNDIEV--------------------LTKIEW 127
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217271652  731 ARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 782
Cdd:cd17999    128 NYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
573-782 2.84e-30

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: 120.17  E-value: 2.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLlWRESQKPQGGIL-DDMGLGKTLTMIALIltqknqekkEEKEKSTALtwlskddscdftsHGTLIICPASL 651
Cdd:cd18001      4 HQREGVAWL-WSLHDGGKGGILaDDMGLGKTVQICAFL---------SGMFDSGLI-------------KSVLVVMPTSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSnkLRVYLYHGPNRDSRAR----VLSTYDIVITTYSLVakeipTNKQEAeipganLNVEGTSTpllr 727
Cdd:cd18001     61 IPHWVKEFAKWTPG--LRVKVFHGTSKKERERnlerIQRGGGVLLTTYGMV-----LSNTEQ------LSADDHDE---- 123
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217271652  728 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 782
Cdd:cd18001    124 FKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
570-833 7.44e-30

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: 119.41  E-value: 7.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWReSQKPQGGIL-DDMGLGKTLTMIALILT-------------QKNQEKKEEKEKSTALTWLskdds 635
Cdd:cd18005      1 LRDYQREGVEFMYDL-YKNGRGGILgDDMGLGKTVQVIAFLAAvlgktgtrrdrenNRPRFKKKPPASSAKKPVL----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  636 cdftshgtlIICPASLIHHWKNEVEKRvnsNKLRVYLYHGPNRD----SRARvLSTYDIVITTYSLVAKEIPTnkqeaei 711
Cdd:cd18005     75 ---------IVAPLSVLYNWKDELDTW---GHFEVGVYHGSRKDdeleGRLK-AGRLEVVVTTYDTLRRCIDS------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  712 pganlnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFN 791
Cdd:cd18005    135 -------------LNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRS 201
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2217271652  792 LWRSQVDNGSKKGGERLSILTKSLLLRRTKDQLDSTGRPLVI 833
Cdd:cd18005    202 QFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFL 243
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
573-781 2.60e-29

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: 115.88  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKpQGGIL-DDMGLGKTLTMIALIltqknqekkeekekstaltwlskdDSCDFTSHG---TLIICP 648
Cdd:cd18000      4 YQQTGVQWLWELHCQR-VGGILgDEMGLGKTIQIIAFL------------------------AALHHSKLGlgpSLIVCP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEK----------------RVNSNKLRVYLYHGPNRDsraRVLSTYDIVITTYSLVAKEiptnkqeaeip 712
Cdd:cd18000     59 ATVLKQWVKEFHRwwppfrvvvlhssgsgTGSEEKLGSIERKSQLIR---KVVGDGGILITTYEGFRKH----------- 124
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217271652  713 ganlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKF 781
Cdd:cd18000    125 ---------KDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDF 184
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
573-819 1.09e-27

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: 112.76  E-value: 1.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWL----LWRESQKPQGGIL-DDMGLGKTLTMIALILTQKNQekkeekekstaltwlSKDDSCdfTSHGTLIIC 647
Cdd:cd18004      4 HQREGVQFLydclTGRRGYGGGGAILaDEMGLGKTLQAIALVWTLLKQ---------------GPYGKP--TAKKALIVC 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  648 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVL-----STYDIVITTYSLVAKEiptnkqeaeipgANLNVEGTS 722
Cdd:cd18004     67 PSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKASLDffssaSTYPVLIISYETLRRH------------AEKLSKKIS 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  723 TPLLriawariILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSK 802
Cdd:cd18004    135 IDLL-------ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIL 207
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2217271652  803 KGGER----------------LSILTKSLLLRR 819
Cdd:cd18004    208 RSRDPdaseedkelgaersqeLSELTSRFILRR 240
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
573-821 4.51e-26

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: 107.41  E-value: 4.51e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLwreSQKPQG--GIL-DDMGLGKTLTMIALI--LTQ-KNQEKkeekekstaltwlskddscdftSHgtLII 646
Cdd:cd17997      7 YQIRGLNWLI---SLFENGinGILaDEMGLGKTLQTISLLgyLKHyKNING----------------------PH--LII 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  647 CPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVLST------YDIVITTYSLVAKEiptnkqeaeipganlnveg 720
Cdd:cd17997     60 VPKSTLDNWMREFKRWCPS--LRVVVLIG-DKEERADIIRDvllpgkFDVCITSYEMVIKE------------------- 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  721 tSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLW--RS 795
Cdd:cd17997    118 -KTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFtssEDFDEWfnVN 196
                          250       260
                   ....*....|....*....|....*.
gi 2217271652  796 QVDNGSKKGGERLSILTKSLLLRRTK 821
Cdd:cd17997    197 NCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
573-819 1.96e-25

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: 105.90  E-value: 1.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkddsCDFTSHGT-LIICPASL 651
Cdd:cd18003      4 YQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIAL------------------LAHLA----CEKGNWGPhLIVVPTSV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSNKLRVYlYHGPNRDSRARV----LSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLLR 727
Cdd:cd18003     62 MLNWEMEFKRWCPGFKILTY-YGSAKERKLKRQgwmkPNSFHVCITSYQLVVQD--------------------HQVFKR 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  728 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVDNGSKKG 804
Cdd:cd18003    121 KKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFqshQEFKEWFSNPLTAMSEG 200
                          250       260
                   ....*....|....*....|...
gi 2217271652  805 GE--------RLSILTKSLLLRR 819
Cdd:cd18003    201 SQeeneelvrRLHKVLRPFLLRR 223
DEXDc smart00487
DEAD-like helicases superfamily;
569-797 3.14e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 3.14e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652   569 PLLLHQKQALAWLLWREsqkpQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscdftshgTLIIC 647
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILaAPTGSGKTLAALLPALEALKRGKGGR----------------------VLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652   648 P-ASLIHHWKNEVEKRVNSNKLR-VYLYHGPNRDSRARVLST--YDIVITTYSLVAKEIPTNKqeaeipganlnvegtst 723
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDK----------------- 124
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217271652   724 pLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACA-RWAVTGTPIQNNLLDMYSLLK-FLRCSPFDEFNLWRSQV 797
Cdd:smart00487  125 -LSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
570-821 1.27e-20

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: 92.06  E-value: 1.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWL--LWresQKPQGGIL-DDMGLGKTLTMIALIltqknqekkeekekstALTWLSKDDScdftshGTLII 646
Cdd:cd18009      4 MRPYQLEGMEWLrmLW---ENGINGILaDEMGLGKTIQTIALL----------------AHLRERGVWG------PFLVI 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  647 CPASLIHHWKNEVEKRVNSnkLRVYLYHGPN---------RDSRARVLSTYDIVITTYslvakEIPTNKQEAeipganln 717
Cdd:cd18009     59 APLSTLPNWVNEFARFTPS--VPVLLYHGTKeererlrkkIMKREGTLQDFPVVVTSY-----EIAMRDRKA-------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  718 vegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD---EFNLW- 793
Cdd:cd18009    124 -------LQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDdlsSFESWf 196
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2217271652  794 -----RSQVDNGSKKGGERLSILTKSL-------LLRRTK 821
Cdd:cd18009    197 dfsslSDNAADISNLSEEREQNIVHMLhailkpfLLRRLK 236
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
569-821 1.56e-20

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 92.00  E-value: 1.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  569 PLLLHQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIICP 648
Cdd:cd18065     15 TLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPH---------------------MVLVP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVL------STYDIVITTYSLVAKEIPTNKqeaeipganlnvegts 722
Cdd:cd18065     74 KSTLHNWMNEFKRWVPS--LRAVCLIG-DKDARAAFIrdvmmpGEWDVCVTSYEMVIKEKSVFK---------------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  723 tpllRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVDN 799
Cdd:cd18065    135 ----KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaDDFDSWFDTKNC 210
                          250       260
                   ....*....|....*....|...
gi 2217271652  800 -GSKKGGERLSILTKSLLLRRTK 821
Cdd:cd18065    211 lGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
574-819 1.65e-20

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: 91.54  E-value: 1.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  574 QKQALAWLL--WRESQkpqGGIL-DDMGLGKTLTMIALIltqknqekkeekekstaltwlskdDSCdFTSHGT----LII 646
Cdd:cd17995      5 QLEGVNWLLfnWYNRR---NCILaDEMGLGKTIQSIAFL------------------------EHL-YQVEGIrgpfLVI 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  647 CPASLIHHWKNEVEKRVNsnkLRVYLYHGpNRDSRARVLS-----------------TYDIVITTYSLVAKEIPTnkqea 709
Cdd:cd17995     57 APLSTIPNWQREFETWTD---MNVVVYHG-SGESRQIIQQyemyfkdaqgrkkkgvyKFDVLITTYEMVIADAEE----- 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  710 eipganlnvegtstpLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACArwAVTGTPIQNNLLDMYSLLKFLRCSPF 787
Cdd:cd17995    128 ---------------LRKIPWRVVVVDEAHRLKNRnsKLLQGLKKLTLEHKL--LLTGTPLQNNTEELWSLLNFLEPEKF 190
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2217271652  788 DefNLWRSQVDNGSKKGGE---RLSILTKSLLLRR 819
Cdd:cd17995    191 P--SSEEFLEEFGDLKTAEqveKLQALLKPYMLRR 223
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
570-783 1.65e-20

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: 91.97  E-value: 1.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLlWR-------ESQKPQGGIL-DDMGLGKTLTMIALILTqknqekkeekekstaltWLSKDDscdFTSH 641
Cdd:cd18007      1 LKPHQVEGVRFL-WSnlvgtdvGSDEGGGCILaHTMGLGKTLQVITFLHT-----------------YLAAAP---RRSR 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  642 gTLIICPASLIHHWKNEVEK----RVNSNKLRVYLYHGPNRDSRARVLSTY----DIVITTYS----LVAKEIPTNKQEA 709
Cdd:cd18007     60 -PLVLCPASTLYNWEDEFKKwlppDLRPLLVLVSLSASKRADARLRKINKWhkegGVLLIGYElfrnLASNATTDPRLKQ 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217271652  710 EIPGANLnVEGTSTpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 783
Cdd:cd18007    139 EFIAALL-DPGPDL---------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFAR 202
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
573-819 7.71e-20

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: 89.42  E-value: 7.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLL-WRESQkpQGGIL-DDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIICPAS 650
Cdd:cd18006      4 YQLEGVNWLLqCRAEQ--HGCILgDEMGLGKTCQTISLLWYLAGRLKLLGPF---------------------LVLCPLS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  651 LIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRA------RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTP 724
Cdd:cd18006     61 VLDNWKEELNRFAPD--LSVITYMG-DKEKRLdlqqdiKSTNRFHVLLTTYEICLKD--------------------ASF 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  725 LLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-----DEFNLWRSQVDN 799
Cdd:cd18006    118 LKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdklDDFIKAYSETDD 197
                          250       260
                   ....*....|....*....|
gi 2217271652  800 GSKKGGErLSILTKSLLLRR 819
Cdd:cd18006    198 ESETVEE-LHLLLQPFLLRR 216
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
573-786 2.56e-19

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: 88.36  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKP----QGGIL-DDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskdDSCDFTSHGTLIIC 647
Cdd:cd18066      4 HQREGIEFLYECVMGMRvnerFGAILaDEMGLGKTLQCISLIWTLLRQGP----------------YGGKPVIKRALIVT 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  648 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIptnkqeAEIPGANLNVegtstpllr 727
Cdd:cd18066     68 PGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSL------DQISKLNFDL--------- 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217271652  728 iawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFlrCSP 786
Cdd:cd18066    133 -----VICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF--VNP 184
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
573-791 4.79e-19

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: 87.42  E-value: 4.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALIltqknqekkeekeksTALTWLSKDdscdftsHGT-LIICPASL 651
Cdd:cd17996      7 YQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLI---------------TYLMEKKKN-------NGPyLVIVPLST 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSnkLRVYLYHGPnRDSRARVLST-----YDIVITTYSLVAKEIPTnkqeaeipganlnvegtstpLL 726
Cdd:cd17996     65 LSNWVSEFEKWAPS--VSKIVYKGT-PDVRKKLQSQiragkFNVLLTTYEYIIKDKPL--------------------LS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 RIAWARIILDEAHNVKNprvqtsiAVCKL--------QACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-FN 791
Cdd:cd17996    122 KIKWKYMIIDEGHRMKN-------AQSKLtqtlntyyHARYRLLLTGTPLQNNLPELWALLNFLlpkifkSCKTFEQwFN 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
991-1105 5.64e-19

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: 83.41  E-value: 5.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  991 KISSLLAELEAIQRNsasqKSVIVSQWTNMLKVVALhLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAG 1070
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217271652 1071 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1105
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
573-787 1.36e-18

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: 84.74  E-value: 1.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALI--LTQKNqekkeekekstaltwlskddscdftSHGT-LIICPA 649
Cdd:cd17998      4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLayLKEIG-------------------------IPGPhLVVVPS 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  650 SLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARV-------LSTYDIVITTYSLVAkeipTNKQEAE-IPGANLNVegt 721
Cdd:cd17998     59 STLDNWLREFKRWCPS--LKVEPYYG-SQEERKHLrydilkgLEDFDVIVTTYNLAT----SNPDDRSfFKRLKLNY--- 128
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217271652  722 stpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF 787
Cdd:cd17998    129 -----------VVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
573-830 3.44e-18

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: 85.49  E-value: 3.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIICPASLI 652
Cdd:cd18064     19 YQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPH---------------------MVLVPKSTL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVL------STYDIVITTYSLVAKEIPTNKqeaeipganlnvegtstpll 726
Cdd:cd18064     78 HNWMAEFKRWVPT--LRAVCLIG-DKDQRAAFVrdvllpGEWDVCVTSYEMLIKEKSVFK-------------------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVDN-GSK 802
Cdd:cd18064    135 KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaEDFDSWFDTNNClGDQ 214
                          250       260
                   ....*....|....*....|....*...
gi 2217271652  803 KGGERLSILTKSLLLRRTKDQLDSTGRP 830
Cdd:cd18064    215 KLVERLHMVLRPFLLRRIKADVEKSLPP 242
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
573-819 8.65e-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: 83.71  E-value: 8.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALiltqknqekkeekekstaLTWLSKDdscdftsHGT----LIICP 648
Cdd:cd18002      4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAV------------------LAHLAEE-------HNIwgpfLVIAP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNsnKLRVYLYHGPNRD--------SRARVL---STYDIVITTYSLVAKEIPTnkqeaeipganln 717
Cdd:cd18002     59 ASTLHNWQQEISRFVP--QFKVLPYWGNPKDrkvlrkfwDRKNLYtrdAPFHVVITSYQLVVQDEKY------------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  718 vegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD---EFNLWR 794
Cdd:cd18002    124 -------FQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDshdEFNEWF 196
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2217271652  795 SQ-VDNGSKKGG-------ERLSILTKSLLLRR 819
Cdd:cd18002    197 SKdIESHAENKTglnehqlKRLHMILKPFMLRR 229
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
570-819 7.59e-17

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: 80.71  E-value: 7.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWREsqkpqGGIL--DDMGLGKTLTMIALILTQKNQekkeekekstaltW-LskddscdftshgtLII 646
Cdd:cd18010      1 LLPFQREGVCFALRRG-----GRVLiaDEMGLGKTVQAIAIAAYYREE-------------WpL-------------LIV 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  647 CPASLIHHWKNEVEKRVNS-NKLRVYLYHGPNRDSRArvlSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPL 725
Cdd:cd18010     50 CPSSLRLTWADEIERWLPSlPPDDIQVIVKSKDGLRD---GDAKVVIVSYDLLRRL--------------------EKQL 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  726 LRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAV--TGTPIQNNLLDMYSLLKFLR---CSPFDEFNLWRSQVDNG 800
Cdd:cd18010    107 LARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVIllSGTPALSRPIELFTQLDALDpklFGRFHDFGRRYCAAKQG 186
                          250       260
                   ....*....|....*....|....*..
gi 2217271652  801 SK----KGGERL----SILTKSLLLRR 819
Cdd:cd18010    187 GFgwdySGSSNLeelhLLLLATIMIRR 213
HELICc smart00490
helicase superfamily c-terminal domain;
1024-1105 2.36e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.94  E-value: 2.36e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  1024 VALHLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYR 1103
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 2217271652  1104 VG 1105
Cdd:smart00490   81 AG 82
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
574-819 3.05e-16

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: 78.94  E-value: 3.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  574 QKQALAWL--LWresQKPQGGIL-DDMGLGKTLTMIALiltqknqekkeekekstaLTWLSKDdscdFTSHGT-LIICPA 649
Cdd:cd17993      6 QLTGLNWLahSW---CKGNNGILaDEMGLGKTVQTISF------------------LSYLFHS----QQQYGPfLVVVPL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  650 SLIHHWKNEVEKRVNSNKLRVYLyhgPNRDSRArVLSTYD------------IVITTYSLVAKEiptnKQEaeipganln 717
Cdd:cd17993     61 STMPAWQREFAKWAPDMNVIVYL---GDIKSRD-TIREYEfyfsqtkklkfnVLLTTYEIILKD----KAF--------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  718 vegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQV 797
Cdd:cd17993    124 -------LGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEH 196
                          250       260
                   ....*....|....*....|..
gi 2217271652  798 DNGSKKGGERLSILTKSLLLRR 819
Cdd:cd17993    197 DEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
573-819 3.90e-14

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


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 72.78  E-value: 3.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTQKNQEKKEEKekstaltwlskddscdftshgtLIICPASLI 652
Cdd:cd18060      4 YQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPF----------------------LVIAPLSTI 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSNKLrvyLYHGP-------------NRDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeipganl 716
Cdd:cd18060     62 TNWEREFNTWTEMNTI---VYHGSlasrqmiqqyemyCKDSRGRLIPgayKFDALITTFEMILSDCPE------------ 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  717 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFNLWRS 795
Cdd:cd18060    127 --------LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLKD 198
                          250       260
                   ....*....|....*....|....
gi 2217271652  796 QVDNGSKKGGERLSILTKSLLLRR 819
Cdd:cd18060    199 FGDLKTEEQVQKLQAILKPMMLRR 222
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
570-782 1.86e-13

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: 70.40  E-value: 1.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLwreSQKPQGGIL-DDMGLGKTLTMIALILtqknqekkeekekstALTWLSKDDSCdftshgtLIICP 648
Cdd:cd18011      1 PLPHQIDAVLRAL---RKPPVRLLLaDEVGLGKTIEAGLIIK---------------ELLLRGDAKRV-------LILCP 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSNKLRVY-LYHGPNRDSRARVLSTYDIVITTYSLVakeiptnKQEAEIPGAnlnvegtstpLLR 727
Cdd:cd18011     56 ASLVEQWQDELQDKFGLPFLILDrETAAQLRRLIGNPFEEFPIVIVSLDLL-------KRSEERRGL----------LLS 118
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217271652  728 IAWARIILDEAHNVKN---PRVQTSIAVCKLQACARWAV---TGTPIQNNLLDMYSLLKFL 782
Cdd:cd18011    119 EEWDLVVVDEAHKLRNsggGKETKRYKLGRLLAKRARHVlllTATPHNGKEEDFRALLSLL 179
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
573-819 3.40e-13

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: 70.07  E-value: 3.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIaliltqknqekkeekekstalTWLSKDDSCDFtsHGT-LIICPASL 651
Cdd:cd18058      4 YQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---------------------TFLSEIFLMGI--RGPfLIIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEKRVNSNklrVYLYHGPN-------------RDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeipgan 715
Cdd:cd18058     61 ITNWEREFRTWTEMN---AIVYHGSQisrqmiqqyemyyRDEQGNPLSgifKFQVVITTFEMILADCPE----------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  716 lnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFNLWR 794
Cdd:cd18058    127 ---------LKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFpSETTFLE 197
                          250       260
                   ....*....|....*....|....*
gi 2217271652  795 SQVDNGSKKGGERLSILTKSLLLRR 819
Cdd:cd18058    198 EFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
573-819 5.17e-13

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: 70.03  E-value: 5.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALiltqknqekkeekekstaLTWLskddscdFTSHGT----LIICP 648
Cdd:cd18054     24 YQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISF------------------LSYL-------FHQHQLygpfLLVVP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSNKLRVYLYHGPNRD---------SRARVLStYDIVITTYSLVAKEiptnkqeaeipganlnve 719
Cdd:cd18054     79 LSTLTSWQREFEIWAPEINVVVYIGDLMSRNtireyewihSQTKRLK-FNALITTYEILLKD------------------ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  720 gtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN 799
Cdd:cd18054    140 --KTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK 217
                          250       260
                   ....*....|....*....|
gi 2217271652  800 GSKKGGERLSILTKSLLLRR 819
Cdd:cd18054    218 GRENGYQSLHKVLEPFLLRR 237
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
573-782 7.00e-13

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 69.30  E-value: 7.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLwresQKPQGGILDDMGLGKTLTMIaliltqknqekkeekeksTALTWLSKDdscDFTSHgTLIICPASLI 652
Cdd:cd18013      4 YQKVAINFII----EHPYCGLFLDMGLGKTVTTL------------------TALSDLQLD---DFTRR-VLVIAPLRVA 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HH-WKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIptNKQEAEIPganlnvegtstpllriaWA 731
Cdd:cd18013     58 RStWPDEVEKWNHLRNLTVSVAVGTERQRSKAANTPADLYVINRENLKWLV--NKSGDPWP-----------------FD 118
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217271652  732 RIILDEAHNVKNPRVQTSIAVCKLQACARWAV--TGTPIQNNLLDMYSLLKFL 782
Cdd:cd18013    119 MVVIDELSSFKSPRSKRFKALRKVRPVIKRLIglTGTPSPNGLMDLWAQIALL 171
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
573-781 7.79e-12

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: 66.72  E-value: 7.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLlWR--ESQKPQGG----ILDDMGLGKTLTMIALILTqknqekkeekekstaltWLSKDDSCDFTSHGTLII 646
Cdd:cd18067      4 HQREGVKFL-YRcvTGRRIRGShgciMADEMGLGKTLQCITLMWT-----------------LLRQSPQCKPEIDKAIVV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  647 CPASLIHHWKNEVEKRVNSNKLRVYLyHGPNRDSRARVLStydivittyslvakeiptnkQEAEIPGANLnvegtSTPLL 726
Cdd:cd18067     66 SPSSLVKNWANELGKWLGGRLQPLAI-DGGSKKEIDRKLV--------------------QWASQQGRRV-----STPVL 119
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 RIAW---------------ARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKF 781
Cdd:cd18067    120 IISYetfrlhvevlqkgevGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNF 189
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
573-821 4.72e-11

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 64.31  E-value: 4.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALIltqknqekkeekekstalTWLSKDDSCDFTshgTLIICPASLI 652
Cdd:cd18063     27 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALI------------------TYLMEHKRLNGP---YLIIVPLSTL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLST--YDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLLRIAW 730
Cdd:cd18063     86 SNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSgkFNVLLTTYEYIIKD--------------------KHILAKIRW 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  731 ARIILDEAHNVKNPRVQ-TSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-----FNLWRSQVD 798
Cdd:cd18063    146 KYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGERVD 225
                          250       260
                   ....*....|....*....|....*.
gi 2217271652  799 NGSKKG---GERLSILTKSLLLRRTK 821
Cdd:cd18063    226 LNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
573-819 1.31e-10

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: 62.74  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTqknqekkeekekstalTWLSKddscdftSHGT-LIICPASL 651
Cdd:cd18059      4 YQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYE----------------IYLKG-------IHGPfLVIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEkrvNSNKLRVYLYHGPN-------------RDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeipgan 715
Cdd:cd18059     61 IPNWEREFR---TWTELNVVVYHGSQasrrtiqlyemyfKDPQGRVIKgsyKFHAIITTFEMILTDCPE----------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  716 lnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFNLWR 794
Cdd:cd18059    127 ---------LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFpSETTFMQ 197
                          250       260
                   ....*....|....*....|....*
gi 2217271652  795 SQVDNGSKKGGERLSILTKSLLLRR 819
Cdd:cd18059    198 EFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
573-821 2.08e-10

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 62.37  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALIltqknqekkeekekstalTWLSKDDSCDFTshgTLIICPASLI 652
Cdd:cd18062     27 YQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALI------------------TYLMEHKRINGP---FLIIVPLSTL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSnkLRVYLYHGPNRDSRARV----LSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLLRI 728
Cdd:cd18062     86 SNWVYEFDKWAPS--VVKVSYKGSPAARRAFVpqlrSGKFNVLLTTYEYIIKD--------------------KQILAKI 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  729 AWARIILDEAHNVKNPRVQ-TSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-----FNLWRSQ 796
Cdd:cd18062    144 RWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGEK 223
                          250       260
                   ....*....|....*....|....*...
gi 2217271652  797 VDNGSKKG---GERLSILTKSLLLRRTK 821
Cdd:cd18062    224 VDLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
573-819 2.29e-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: 61.95  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALIltqknqekkeekeKSTALTWLSKDdscdftshgTLIICPASLI 652
Cdd:cd18061      4 YQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-------------YEILLTGIRGP---------FLIIAPLSTI 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEKRVNSNklrVYLYHGP-------------NRDSRARVLS---TYDIVITTYSLVAkeiptnkqeaeipganl 716
Cdd:cd18061     62 ANWEREFRTWTDLN---VVVYHGSlisrqmiqqyemyFRDSQGRIIRgayRFQAIITTFEMIL----------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  717 nveGTSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQ 796
Cdd:cd18061    122 ---GGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQE 198
                          250       260
                   ....*....|....*....|....
gi 2217271652  797 V-DNGSKKGGERLSILTKSLLLRR 819
Cdd:cd18061    199 FgDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
570-819 6.29e-10

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: 60.80  E-value: 6.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  570 LLLHQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdfTSHGTLIICPA 649
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS------------------LYKEGH---TKGPFLVSAPL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  650 SLIHHWKNEVEkrVNSNKLRVYLYHGpNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEAEIpgaNLNVEGTSTPLL--- 726
Cdd:cd18055     60 STIINWEREFQ--MWAPDFYVVTYTG-DKDSRAIIRENEFSFDDNAVKGGKKAFKMKREAQV---KFHVLLTSYELVtid 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 -----RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGS 801
Cdd:cd18055    134 qaalgSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADIS 213
                          250
                   ....*....|....*....
gi 2217271652  802 KKGG-ERLSILTKSLLLRR 819
Cdd:cd18055    214 KEDQiKKLHDLLGPHMLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
573-819 6.38e-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: 60.15  E-value: 6.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDSCD--FtshgtLIICPAS 650
Cdd:cd17994      4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS------------------LYKEGHSKgpF-----LVSAPLS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  651 LIHHWKNEVEkrVNSNKLRVYLYHGPNrdsrarvlstydIVITTYSLVAKEIPTnkqeaeipganlnvegtstpLLRIAW 730
Cdd:cd17994     61 TIINWEREFE--MWAPDFYVVTYVGDH------------VLLTSYELISIDQAI--------------------LGSIDW 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  731 ARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGG-ERLS 809
Cdd:cd17994    107 AVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQiKKLH 186
                          250
                   ....*....|
gi 2217271652  810 ILTKSLLLRR 819
Cdd:cd17994    187 DLLGPHMLRR 196
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
573-819 5.51e-09

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


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 58.15  E-value: 5.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdfTSHGTLIICPASLI 652
Cdd:cd18057      4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYS------------------LYKEGH---SKGPYLVSAPLSTI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  653 HHWKNEVEkrVNSNKLRVYLYHGpNRDSRARV----LSTYDIVITTyslvAKEIPTNKQEAEIpgaNLNVEGTSTPLL-- 726
Cdd:cd18057     63 INWEREFE--MWAPDFYVVTYTG-DKESRSVIreneFSFEDNAIRS----GKKVFRMKKEAQI---KFHVLLTSYELIti 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  727 ------RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNG 800
Cdd:cd18057    133 dqailgSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADI 212
                          250       260
                   ....*....|....*....|
gi 2217271652  801 SKKGG-ERLSILTKSLLLRR 819
Cdd:cd18057    213 SKEDQiKKLHDLLGPHMLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
584-783 1.05e-08

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: 57.21  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  584 RESQKPQG--GILDD-MGLGKTLTMIALILTqknqekkeekekstaLTWLSKDDSCDftshGTLIICPASLIHHWKNEVE 660
Cdd:cd18068     21 KKTKKSPGsgCILAHcMGLGKTLQVVTFLHT---------------VLLCEKLENFS----RVLVVCPLNTVLNWLNEFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  661 KRV----NSNKLRVY---LYHGPNRDSRA--RVLSTYDIVITTYSL-----VAKEIPTNKQEAEI-------PGANLnve 719
Cdd:cd18068     82 KWQeglkDEEKIEVNelaTYKRPQERSYKlqRWQEEGGVMIIGYDMyrilaQERNVKSREKLKEIfnkalvdPGPDF--- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217271652  720 gtstpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 783
Cdd:cd18068    159 -------------VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
597-783 3.49e-08

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: 55.59  E-value: 3.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  597 MGLGKTLTMIALIltqknqekkeekekstaltwlskDDSCDFTSHGT-LIICPASLIHHWKNEVEK---------RVNSN 666
Cdd:cd18069     37 MGLGKTLQVISFL-----------------------DVLLRHTGAKTvLAIVPVNTLQNWLSEFNKwlpppealpNVRPR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  667 KLRVYLYHGPNR--DSRARVLSTYD----IVITTYSLVAKEiptnkqeaeiPGANLnvegtstpllriawarIILDEAHN 740
Cdd:cd18069     94 PFKVFILNDEHKttAARAKVIEDWVkdggVLLMGYEMFRLR----------PGPDV----------------VICDEGHR 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2217271652  741 VKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 783
Cdd:cd18069    148 IKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
573-819 5.65e-08

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: 55.06  E-value: 5.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALiltqknqekkeekekstaLTWLskddscdFTSHGT----LIICP 648
Cdd:cd18053     24 YQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISF------------------LNYL-------FHEHQLygpfLLVVP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  649 ASLIHHWKNEVEKRVNSNKLRVYLYHGPNRD---------SRARVLStYDIVITTYSLVAKEiptnkqeaeipganlnve 719
Cdd:cd18053     79 LSTLTSWQREIQTWAPQMNAVVYLGDINSRNmirthewmhPQTKRLK-FNILLTTYEILLKD------------------ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  720 gtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN 799
Cdd:cd18053    140 --KSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK 217
                          250       260
                   ....*....|....*....|
gi 2217271652  800 GSKKGGERLSILTKSLLLRR 819
Cdd:cd18053    218 GREYGYASLHKELEPFLLRR 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
560-767 9.83e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 56.19  E-value: 9.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  560 AEDPAGLKVPLLLHQKQAL-AWLLWRESQKPQGGILDDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdf 638
Cdd:COG1061     71 GDEASGTSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  639 tshgTLIICP-ASLIHHWKNEVEKrvnsnKLRVYLYHGPNRDSrarvlsTYDIVITTYSLVAKEIPTNKqeaeipganln 717
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKDS------DAPITVATYQSLARRAHLDE----------- 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217271652  718 vegtstplLRIAWARIILDEAHNVKNPRVQTSIAvcKLQACARWAVTGTP 767
Cdd:COG1061    184 --------LGDRFGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
573-782 1.80e-07

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: 53.53  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPQGGILDDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdftSHGTLII-CPASL 651
Cdd:cd18056      4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYS------------------LYKEGH----SKGPFLVsAPLST 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  652 IHHWKNEVEkrVNSNKLRVYLYHGpNRDSRARV----LSTYDIVITTyslvAKEIPTNKQEAEIpgaNLNVEGTSTPLL- 726
Cdd:cd18056     62 IINWEREFE--MWAPDMYVVTYVG-DKDSRAIIreneFSFEDNAIRG----GKKASRMKKEASV---KFHVLLTSYELIt 131
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217271652  727 -------RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 782
Cdd:cd18056    132 idmailgSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFL 194
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
573-741 1.38e-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: 49.23  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  573 HQKQALAWLLWRESQKPqgGILDdM--GLGKTLTMIALIltqknqekkeekekstaltwlskddsCDFTSHGTLIICP-A 649
Cdd:cd17926      4 YQEEALEAWLAHKNNRR--GILV-LptGSGKTLTALALI--------------------------AYLKELRTLIVVPtD 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  650 SLIHHWKNEVEKRVNSNKLRvYLYHGPNRDSRARvlstyDIVITTYSLVakeipTNKQEAEIPGANlnvegtstpllriA 729
Cdd:cd17926     55 ALLDQWKERFEDFLGDSSIG-LIGGGKKKDFDDA-----NVVVATYQSL-----SNLAEEEKDLFD-------------Q 110
                          170
                   ....*....|..
gi 2217271652  730 WARIILDEAHNV 741
Cdd:cd17926    111 FGLLIVDEAHHL 122
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-39 8.07e-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: 8.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217271652    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
147-378 1.92e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271652  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 2217271652  375 TLDL 378
Cdd:PTZ00108  1385 EDDD 1388
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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