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Conserved domains on  [gi|1034562578|ref|XP_016858044|]
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transcription termination factor 2 isoform X7 [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 ...
570-820 1.96e-148

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: 444.62  E-value: 1.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 648
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 728
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  729 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 808
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1034562578  809 LSILTKSLLLRR 820
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1142 8.70e-127

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 8.70e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 638
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  639 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 717
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  718 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 793
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  794 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 873
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  874 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 953
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  954 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1032
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578 1033 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1112
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1034562578 1113 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1142
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 8.00e-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: 8.00e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034562578    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
147-378 1.89e-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: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 1034562578  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 ...
570-820 1.96e-148

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: 444.62  E-value: 1.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 648
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 728
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  729 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 808
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1034562578  809 LSILTKSLLLRR 820
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1142 8.70e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 8.70e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 638
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  639 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 717
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  718 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 793
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  794 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 873
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  874 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 953
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  954 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1032
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578 1033 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1112
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1034562578 1113 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1142
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
573-933 4.45e-74

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 247.60  E-value: 4.45e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdFTSHGTLIICPASL 652
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSNKLRVYLYHGPNRDSRA-----RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLL 727
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN-----GS 802
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  803 KKGGERLSILTKSLLLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYNVFFarsrsalqsylkrHESRGNQsgr 882
Cdd:pfam00176  201 KKGVSRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-------------LKKDLNA--- 258
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034562578  883 spnnpfsrVALEFGSEEPRHSeaadsprsstvhILSQLLRLRQCCCHLSLL 933
Cdd:pfam00176  259 --------IKTGEGGREIKAS------------LLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
990-1117 5.67e-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: 5.67e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  990 STKISSLLAELEAIQRNSasQKSVIVSQWTNMLKVVALHLKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLL 1069
Cdd:cd18793     10 SGKLEALLELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034562578 1070 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVVIHRFV 1117
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
563-1133 6.26e-41

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 164.20  E-value: 6.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  563 PAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkdDSCDFTS- 641
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISL------------------LGYLH--EYRGITGp 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  642 HgtLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRAR------VLSTYDIVITTYSLVAKEiptnkqeaeipga 715
Cdd:PLN03142   222 H--MVVAPKSTLGNWMNEIRRFCPV--LRAVKFHG-NPEERAHqreellVAGKFDVCVTSFEMAIKE------------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  716 nlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFN 792
Cdd:PLN03142   284 -------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFD 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  793 LWRSQvdNGSKKGGERLSILTKSL---LLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYnvffarsRSALQSY 869
Cdd:PLN03142   357 EWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------KALLQKD 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  870 LKrhesrgnqsgrspnnpfsrvALEFGSEEPRhseaadsprsstvhILSQLLRLRQCCCHLSLLKSAL-DPMELKGEGLV 948
Cdd:PLN03142   422 LD--------------------VVNAGGERKR--------------LLNIAMQLRKCCNHPYLFQGAEpGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  949 lsleeqlsaltlselrdsEPSStvslngtffKMELFEgmrestkisSLLAELEaiQRNSasqKSVIVSQWTNMLKVVALH 1028
Cdd:PLN03142   468 ------------------ENSG---------KMVLLD---------KLLPKLK--ERDS---RVLIFSQMTRLLDILEDY 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578 1029 LKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQ 1107
Cdd:PLN03142   507 LMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQ 586
                          570       580
                   ....*....|....*....|....*.
gi 1034562578 1108 QKDVVIHRFVCEGTVEEKILQLQEKK 1133
Cdd:PLN03142   587 KKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXDc smart00487
DEAD-like helicases superfamily;
569-798 3.55e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 98.72  E-value: 3.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578   569 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscdftshgTLIIC 648
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGGR----------------------VLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578   649 P-ASLIHHWKNEVEKRVNSNKLR-VYLYHGPNRDSRARVLST--YDIVITTYSLVAKEIPTNKqeaeipganlnvegtst 724
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDK----------------- 124
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034562578   725 pLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACA-RWAVTGTPIQNNLLDMYSLLK-FLRCSPFDEFNLWRSQV 798
Cdd:smart00487  125 -LSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
992-1106 5.65e-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: 5.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  992 KISSLLAELEAIQRNsasqKSVIVSQWTNMLKVVALhLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAG 1071
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034562578 1072 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1106
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1025-1106 2.37e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.94  E-value: 2.37e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  1025 VALHLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYR 1104
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 1034562578  1105 VG 1106
Cdd:smart00490   81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
560-768 2.37e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.11  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  560 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdf 639
Cdd:COG1061     71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  640 tshgTLIICP-ASLIHHWKNEVEKrvnsnKLRVYLYHGPNRDsrarvlSTYDIVITTYSLVAKEIPTNKqeaeipganln 718
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKD------SDAPITVATYQSLARRAHLDE----------- 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034562578  719 vegtstplLRIAWARIILDEAHNVKNPRVQTSIAvcKLQACARWAVTGTP 768
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 8.00e-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: 8.00e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034562578    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
147-378 1.89e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 1034562578  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 ...
570-820 1.96e-148

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: 444.62  E-value: 1.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEKSTALT-WLSKDDSCDFTSHGTLIIC 648
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALTeWESKKDSTLVPSAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEaeipganlnveGTSTPLLR 728
Cdd:cd18072     81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYKEE-----------SRSSPLFR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  729 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGGER 808
Cdd:cd18072    150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGER 229
                          250
                   ....*....|..
gi 1034562578  809 LSILTKSLLLRR 820
Cdd:cd18072    230 LNILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
559-1142 8.70e-127

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 8.70e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  559 VAEDPAGLKVPLLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscd 638
Cdd:COG0553    231 LESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLLELKERGLARP----------------- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  639 ftshgTLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGP-NRDSRARVLSTYDIVITTYSLVAKEIPTnkqeaeipganl 717
Cdd:COG0553    293 -----VLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGTrERAKGANPFEDADLVITSYGLLRRDIEL------------ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  718 nvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL---RCSPFDEFN-L 793
Cdd:COG0553    354 --------LAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLnpgLLGSLKAFReR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  794 WRSQVDNGSKKGGERLSILTKSLLLRRTKDQLdstgrpLVILPQRKFQLHHLKLSEDEETVYNvffarsrsALQSYLKRH 873
Cdd:COG0553    426 FARPIEKGDEEALERLRRLLRPFLLRRTKEDV------LKDLPEKTEETLYVELTPEQRALYE--------AVLEYLRRE 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  874 esrgnqsgrspnnpfsrvalefgseeprhsEAADSPRSSTVHILSQLLRLRQCCCHLSLLksaldpmelkgeglvlsLEE 953
Cdd:COG0553    492 ------------------------------LEGAEGIRRRGLILAALTRLRQICSHPALL-----------------LEE 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  954 QLSaltlSELRDSepsstvslngtffKMELFegmrestkissllaeLEAIQRNSASQKSVIV-SQWTNMLKVVALHLKKH 1032
Cdd:COG0553    525 GAE----LSGRSA-------------KLEAL---------------LELLEELLAEGEKVLVfSQFTDTLDLLEERLEER 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578 1033 GLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVV 1112
Cdd:COG0553    573 GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQ 652
                          570       580       590
                   ....*....|....*....|....*....|
gi 1034562578 1113 IHRFVCEGTVEEKILQLQEKKKDLAKQVLS 1142
Cdd:COG0553    653 VYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
570-820 3.90e-103

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: 325.01  E-value: 3.90e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTQKNQEKKEEKEKSTaltwLSKDDSCDFTSHGTLIICP 649
Cdd:cd18008      1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILATRPQDPKIPEELEE----NSSDPKKLYLSKTTLIVVP 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIPTNKQeaeiPGANLNVEGTSTPLLRI 729
Cdd:cd18008     71 LSLLSQWKDEIEKHTKPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPKNKK----GGGRDSKEKEASPLHRI 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  730 AWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQV----DNGSKKG 805
Cdd:cd18008    147 RWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDIskpfSKNDRKA 226
                          250
                   ....*....|....*
gi 1034562578  806 GERLSILTKSLLLRR 820
Cdd:cd18008    227 LERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
573-933 4.45e-74

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


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 247.60  E-value: 4.45e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdFTSHGTLIICPASL 652
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDK--------------------NWGGPTLIVVPLSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSNKLRVYLYHGPNRDSRA-----RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLL 727
Cdd:pfam00176   61 LHNWMNEFERWVSPPALRVVVLHGNKRPQERwkndpNFLADFDVVITTYETLRKH--------------------KELLK 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN-----GS 802
Cdd:pfam00176  121 KVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGG 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  803 KKGGERLSILTKSLLLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYNVFFarsrsalqsylkrHESRGNQsgr 882
Cdd:pfam00176  201 KKGVSRLHKLLKPFLLRRTKKDVEKS------LPPKVEYILFCRLSKLQRKLYQTFL-------------LKKDLNA--- 258
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034562578  883 spnnpfsrVALEFGSEEPRHSeaadsprsstvhILSQLLRLRQCCCHLSLL 933
Cdd:pfam00176  259 --------IKTGEGGREIKAS------------LLNILMRLRKICNHPGLI 289
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
570-820 2.52e-64

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: 218.11  E-value: 2.52e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRE-----------------------SQK--PQ---GGILADDMGLGKTLTMIALILTQKnqekkee 621
Cdd:cd18071      1 LLPHQKQALAWMVSREnsqdlppfweeavglflntitnfSQKkrPElvrGGILADDMGLGKTLTTISLILANF------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  622 kekstaltwlskddscdftshgTLIICPASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAK 701
Cdd:cd18071     74 ----------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLAS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  702 EiptnkqeaeipganlnvEGT--STPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSL 779
Cdd:cd18071    132 D-----------------FGAkgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSL 194
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034562578  780 LKFLRCSPFDEFNLWRS----QVDNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18071    195 LSFLHLKPFSNPEYWRRliqrPLTMGDPTGLKRLQVLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
570-819 4.44e-56

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 195.26  E-value: 4.44e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWResqkpqGGILADDMGLGKTLTMIALILTQKNQEKKeekekSTALTWLSKDDSC---------DFT 640
Cdd:cd18070      1 LLPYQRRAVNWMLVP------GGILADEMGLGKTVEVLALILLHPRPDND-----LDAADDDSDEMVCcpdclvaetPVS 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  641 SHGTLIICPASLIHHWKNEVEKRVNSNkLRVYLYHGPNRDS-----RARVLSTYDIVITTYSLVAKEIptnkQEAEIPGA 715
Cdd:cd18070     70 SKATLIVCPSAILAQWLDEINRHVPSS-LKVLTYQGVKKDGalaspAPEILAEYDIVVTTYDVLRTEL----HYAEANRS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  716 NL------NVEGTSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD 789
Cdd:cd18070    145 NRrrrrqkRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC 224
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034562578  790 EFNLWRSQVDN--GSKKGGERLSILTKSLLLR 819
Cdd:cd18070    225 DSDWWARVLIRpqGRNKAREPLAALLKELLWR 256
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
570-795 1.09e-53

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: 185.46  E-value: 1.09e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRESQKPqGGILADDMGLGKTLTMIALILTQKNQekkeekekstaltwlsKDDSCDFtshgtLIICP 649
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGP-GGILADEMGLGKTLQAIAFLAYLLKE----------------GKERGPV-----LVVCP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEKRVNSnkLRVYLYHGPNRDSRAR----VLSTYDIVITTYSLVAKEIPTnkqeaeipganlnvegtstp 725
Cdd:cd17919     59 LSVLENWEREFEKWTPD--LRVVVYHGSQRERAQIrakeKLDKFDVVLTTYETLRRDKAS-------------------- 116
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  726 LLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCsPFdefnLWR 795
Cdd:cd17919    117 LRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP-PF----LLR 181
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
990-1117 5.67e-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: 5.67e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  990 STKISSLLAELEAIQRNSasQKSVIVSQWTNMLKVVALHLKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQVMLISLL 1069
Cdd:cd18793     10 SGKLEALLELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTK 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034562578 1070 AGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQQKDVVIHRFV 1117
Cdd:cd18793     88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
574-822 1.61e-50

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: 177.76  E-value: 1.61e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  574 QKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdftSHGTLIICPASLI 653
Cdd:cd18012      9 QKEGFNWL-SFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR----------------------KGPSLVVAPTSLI 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  654 HHWKNEVEKRvnSNKLRVYLYHGPNRDSRA-RVLSTYDIVITTYSLVAKEIptnkqEAeipganlnvegtstpLLRIAWA 732
Cdd:cd18012     66 YNWEEEAAKF--APELKVLVIHGTKRKREKlRALEDYDLVITSYGLLRRDI-----EL---------------LKEVKFH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  733 RIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLrcSP-----FDEFN-LWRSQVDNGSKKGG 806
Cdd:cd18012    124 YLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFL--NPgllgsYKRFKkRFAKPIEKDGDEEA 201
                          250
                   ....*....|....*..
gi 1034562578  807 -ERLSILTKSLLLRRTK 822
Cdd:cd18012    202 lEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
563-1133 6.26e-41

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 164.20  E-value: 6.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  563 PAGLKVPLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkdDSCDFTS- 641
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLI-RLYENGINGILADEMGLGKTLQTISL------------------LGYLH--EYRGITGp 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  642 HgtLIICPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRAR------VLSTYDIVITTYSLVAKEiptnkqeaeipga 715
Cdd:PLN03142   222 H--MVVAPKSTLGNWMNEIRRFCPV--LRAVKFHG-NPEERAHqreellVAGKFDVCVTSFEMAIKE------------- 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  716 nlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFN 792
Cdd:PLN03142   284 -------KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFD 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  793 LWRSQvdNGSKKGGERLSILTKSL---LLRRTKDQLDSTgrplviLPQRKFQLHHLKLSEDEETVYnvffarsRSALQSY 869
Cdd:PLN03142   357 EWFQI--SGENDQQEVVQQLHKVLrpfLLRRLKSDVEKG------LPPKKETILKVGMSQMQKQYY-------KALLQKD 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  870 LKrhesrgnqsgrspnnpfsrvALEFGSEEPRhseaadsprsstvhILSQLLRLRQCCCHLSLLKSAL-DPMELKGEGLV 948
Cdd:PLN03142   422 LD--------------------VVNAGGERKR--------------LLNIAMQLRKCCNHPYLFQGAEpGPPYTTGEHLV 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  949 lsleeqlsaltlselrdsEPSStvslngtffKMELFEgmrestkisSLLAELEaiQRNSasqKSVIVSQWTNMLKVVALH 1028
Cdd:PLN03142   468 ------------------ENSG---------KMVLLD---------KLLPKLK--ERDS---RVLIFSQMTRLLDILEDY 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578 1029 LKKHGLTYATIDGSVNPKQRMDLVEAFNHSRGPQ-VMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVGQ 1107
Cdd:PLN03142   507 LMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQ 586
                          570       580
                   ....*....|....*....|....*.
gi 1034562578 1108 QKDVVIHRFVCEGTVEEKILQLQEKK 1133
Cdd:PLN03142   587 KKEVQVFRFCTEYTIEEKVIERAYKK 612
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
592-783 2.63e-33

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: 128.62  E-value: 2.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  592 GILADDMGLGKTLTMIALIltqknqekkeekekstALTWLSKDDSCDFTSHGTLIICPASLIHHWKNEVEKRVNSNKLRV 671
Cdd:cd17999     22 GILCDDMGLGKTLQTLCIL----------------ASDHHKRANSFNSENLPSLVVCPPTLVGHWVAEIKKYFPNAFLKP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  672 YLYHGPNRDSRARV--LSTYDIVITTYSLVAKEIPTnkqeaeipganlnvegtstpLLRIAWARIILDEAHNVKNPRVQT 749
Cdd:cd17999     86 LAYVGPPQERRRLReqGEKHNVIVASYDVLRNDIEV--------------------LTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034562578  750 SIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 783
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
573-783 1.43e-32

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: 126.72  E-value: 1.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLlWRESQKPQGGILADDMGLGKTLTMIALIltqknqekkEEKEKSTALtwlskddscdftsHGTLIICPASL 652
Cdd:cd18001      4 HQREGVAWL-WSLHDGGKGGILADDMGLGKTVQICAFL---------SGMFDSGLI-------------KSVLVVMPTSL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSnkLRVYLYHGPNRDSRAR----VLSTYDIVITTYSLVakeipTNKQEAeipganLNVEGTSTpllr 728
Cdd:cd18001     61 IPHWVKEFAKWTPG--LRVKVFHGTSKKERERnlerIQRGGGVLLTTYGMV-----LSNTEQ------LSADDHDE---- 123
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034562578  729 IAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 783
Cdd:cd18001    124 FKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
570-834 8.23e-32

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: 124.80  E-value: 8.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWReSQKPQGGILADDMGLGKTLTMIALILT-------------QKNQEKKEEKEKSTALTWLskdds 636
Cdd:cd18005      1 LRDYQREGVEFMYDL-YKNGRGGILGDDMGLGKTVQVIAFLAAvlgktgtrrdrenNRPRFKKKPPASSAKKPVL----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  637 cdftshgtlIICPASLIHHWKNEVEKRvnsNKLRVYLYHGPNRD----SRARvLSTYDIVITTYSLVAKEIPTnkqeaei 712
Cdd:cd18005     75 ---------IVAPLSVLYNWKDELDTW---GHFEVGVYHGSRKDdeleGRLK-AGRLEVVVTTYDTLRRCIDS------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  713 pganlnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFN 792
Cdd:cd18005    135 -------------LNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRS 201
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034562578  793 LWRSQVDNGSKKGGERLSILTKSLLLRRTKDQLDSTGRPLVI 834
Cdd:cd18005    202 QFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFL 243
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
573-782 2.67e-31

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 121.66  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltqknqekkeekekstaltwlskdDSCDFTSHG---TLIICP 649
Cdd:cd18000      4 YQQTGVQWLWELHCQR-VGGILGDEMGLGKTIQIIAFL------------------------AALHHSKLGlgpSLIVCP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEK----------------RVNSNKLRVYLYHGPNRDsraRVLSTYDIVITTYSLVAKEiptnkqeaeip 713
Cdd:cd18000     59 ATVLKQWVKEFHRwwppfrvvvlhssgsgTGSEEKLGSIERKSQLIR---KVVGDGGILITTYEGFRKH----------- 124
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034562578  714 ganlnvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKF 782
Cdd:cd18000    125 ---------KDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDF 184
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
573-820 3.65e-30

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 120.08  E-value: 3.65e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWL----LWRESQKPQGGILADDMGLGKTLTMIALILTQKNQekkeekekstaltwlSKDDSCdfTSHGTLIIC 648
Cdd:cd18004      4 HQREGVQFLydclTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQ---------------GPYGKP--TAKKALIVC 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVL-----STYDIVITTYSLVAKEiptnkqeaeipgANLNVEGTS 723
Cdd:cd18004     67 PSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKASLDffssaSTYPVLIISYETLRRH------------AEKLSKKIS 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  724 TPLLriawariILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSK 803
Cdd:cd18004    135 IDLL-------ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIL 207
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034562578  804 KGGER----------------LSILTKSLLLRR 820
Cdd:cd18004    208 RSRDPdaseedkelgaersqeLSELTSRFILRR 240
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
573-822 1.69e-28

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: 114.73  E-value: 1.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALI--LTQ-KNQEKkeekekstaltwlskddscdftSHgtLII 647
Cdd:cd17997      7 YQIRGLNWLI---SLFENGinGILADEMGLGKTLQTISLLgyLKHyKNING----------------------PH--LII 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  648 CPASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVLST------YDIVITTYSLVAKEiptnkqeaeipganlnveg 721
Cdd:cd17997     60 VPKSTLDNWMREFKRWCPS--LRVVVLIG-DKEERADIIRDvllpgkFDVCITSYEMVIKE------------------- 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  722 tSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLW--RS 796
Cdd:cd17997    118 -KTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFtssEDFDEWfnVN 196
                          250       260
                   ....*....|....*....|....*.
gi 1034562578  797 QVDNGSKKGGERLSILTKSLLLRRTK 822
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 ...
573-820 1.22e-27

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 112.06  E-value: 1.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLSkddsCDFTSHGT-LIICPAS 651
Cdd:cd18003      4 YQHIGLDWLA-TLYEKNLNGILADEMGLGKTIQTIAL------------------LAHLA----CEKGNWGPhLIVVPTS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEKRVNSNKLRVYlYHGPNRDSRARV----LSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLL 727
Cdd:cd18003     61 VMLNWEMEFKRWCPGFKILTY-YGSAKERKLKRQgwmkPNSFHVCITSYQLVVQD--------------------HQVFK 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVDNGSKK 804
Cdd:cd18003    120 RKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFqshQEFKEWFSNPLTAMSE 199
                          250       260
                   ....*....|....*....|....
gi 1034562578  805 GGE--------RLSILTKSLLLRR 820
Cdd:cd18003    200 GSQeeneelvrRLHKVLRPFLLRR 223
DEXDc smart00487
DEAD-like helicases superfamily;
569-798 3.55e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 98.72  E-value: 3.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578   569 PLLLHQKQALAWLLWREsqkpQGGILADDMGLGKTLTMIALILTQKNQEKKEEkekstaltwlskddscdftshgTLIIC 648
Cdd:smart00487    8 PLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEALKRGKGGR----------------------VLVLV 61
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578   649 P-ASLIHHWKNEVEKRVNSNKLR-VYLYHGPNRDSRARVLST--YDIVITTYSLVAKEIPTNKqeaeipganlnvegtst 724
Cdd:smart00487   62 PtRELAEQWAEELKKLGPSLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDK----------------- 124
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034562578   725 pLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACA-RWAVTGTPIQNNLLDMYSLLK-FLRCSPFDEFNLWRSQV 798
Cdd:smart00487  125 -LSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVqLLLLSATPPEEIENLLELFLNdPVFIDVGFTPLEPIEQF 201
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
570-822 5.12e-23

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 99.00  E-value: 5.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALIltqknqekkeekekstALTWLSKDDScdftshGTLII 647
Cdd:cd18009      4 MRPYQLEGMEWLrmLW---ENGINGILADEMGLGKTIQTIALL----------------AHLRERGVWG------PFLVI 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  648 CPASLIHHWKNEVEKRVNSnkLRVYLYHGPN---------RDSRARVLSTYDIVITTYslvakEIPTNKQEAeipganln 718
Cdd:cd18009     59 APLSTLPNWVNEFARFTPS--VPVLLYHGTKeererlrkkIMKREGTLQDFPVVVTSY-----EIAMRDRKA-------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  719 vegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD---EFNLW- 794
Cdd:cd18009    124 -------LQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDdlsSFESWf 196
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1034562578  795 -----RSQVDNGSKKGGERLSILTKSL-------LLRRTK 822
Cdd:cd18009    197 dfsslSDNAADISNLSEEREQNIVHMLhailkpfLLRRLK 236
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
570-784 5.86e-23

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 98.90  E-value: 5.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLlWR-------ESQKPQGGILADDMGLGKTLTMIALILTqknqekkeekekstaltWLSKDDscdFTSH 642
Cdd:cd18007      1 LKPHQVEGVRFL-WSnlvgtdvGSDEGGGCILAHTMGLGKTLQVITFLHT-----------------YLAAAP---RRSR 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  643 gTLIICPASLIHHWKNEVEK----RVNSNKLRVYLYHGPNRDSRARVLSTY----DIVITTYS----LVAKEIPTNKQEA 710
Cdd:cd18007     60 -PLVLCPASTLYNWEDEFKKwlppDLRPLLVLVSLSASKRADARLRKINKWhkegGVLLIGYElfrnLASNATTDPRLKQ 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034562578  711 EIPGANLnVEGTSTpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 784
Cdd:cd18007    139 EFIAALL-DPGPDL---------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFAR 202
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
574-820 6.08e-23

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


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 98.47  E-value: 6.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  574 QKQALAWLL--WRESQkpqGGILADDMGLGKTLTMIALIltqknqekkeekekstaltwlskdDSCdFTSHGT----LII 647
Cdd:cd17995      5 QLEGVNWLLfnWYNRR---NCILADEMGLGKTIQSIAFL------------------------EHL-YQVEGIrgpfLVI 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  648 CPASLIHHWKNEVEKRVNsnkLRVYLYHGpNRDSRARVLS-----------------TYDIVITTYSLVAKEIPTnkqea 710
Cdd:cd17995     57 APLSTIPNWQREFETWTD---MNVVVYHG-SGESRQIIQQyemyfkdaqgrkkkgvyKFDVLITTYEMVIADAEE----- 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  711 eipganlnvegtstpLLRIAWARIILDEAHNVKNP--RVQTSIAVCKLQACArwAVTGTPIQNNLLDMYSLLKFLRCSPF 788
Cdd:cd17995    128 ---------------LRKIPWRVVVVDEAHRLKNRnsKLLQGLKKLTLEHKL--LLTGTPLQNNTEELWSLLNFLEPEKF 190
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034562578  789 DefNLWRSQVDNGSKKGGE---RLSILTKSLLLRR 820
Cdd:cd17995    191 P--SSEEFLEEFGDLKTAEqveKLQALLKPYMLRR 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
573-820 1.01e-21

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: 94.81  E-value: 1.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLL-WRESQkpQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIICPAS 651
Cdd:cd18006      4 YQLEGVNWLLqCRAEQ--HGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPF---------------------LVLCPLS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRA------RVLSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTP 725
Cdd:cd18006     61 VLDNWKEELNRFAPD--LSVITYMG-DKEKRLdlqqdiKSTNRFHVLLTTYEICLKD--------------------ASF 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  726 LLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-----DEFNLWRSQVDN 800
Cdd:cd18006    118 LKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdklDDFIKAYSETDD 197
                          250       260
                   ....*....|....*....|
gi 1034562578  801 GSKKGGERLSILTKsLLLRR 820
Cdd:cd18006    198 ESETVEELHLLLQP-FLLRR 216
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
569-822 1.63e-21

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: 94.70  E-value: 1.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  569 PLLLHQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIIC 648
Cdd:cd18065     15 TLRDYQVRGLNWMI-SLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPH---------------------MVLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVL------STYDIVITTYSLVAKEIPTNKqeaeipganlnvegt 722
Cdd:cd18065     73 PKSTLHNWMNEFKRWVPS--LRAVCLIG-DKDARAAFIrdvmmpGEWDVCVTSYEMVIKEKSVFK--------------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  723 stpllRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVD 799
Cdd:cd18065    135 -----KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaDDFDSWFDTKN 209
                          250       260
                   ....*....|....*....|....
gi 1034562578  800 N-GSKKGGERLSILTKSLLLRRTK 822
Cdd:cd18065    210 ClGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
573-787 1.83e-21

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: 94.53  E-value: 1.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKP----QGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskdDSCDFTSHGTLIIC 648
Cdd:cd18066      4 HQREGIEFLYECVMGMRvnerFGAILADEMGLGKTLQCISLIWTLLRQGP----------------YGGKPVIKRALIVT 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIptnkqeAEIPGANLNVegtstpllr 728
Cdd:cd18066     68 PGSLVKNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSL------DQISKLNFDL--------- 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034562578  729 iawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFlrCSP 787
Cdd:cd18066    133 -----VICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDF--VNP 184
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
573-792 5.99e-21

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 93.20  E-value: 5.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltqknqekkeekeksTALTWLSKDdscdftsHGT-LIICPAS 651
Cdd:cd17996      7 YQLKGLQWMVSLYNNN-LNGILADEMGLGKTIQTISLI---------------TYLMEKKKN-------NGPyLVIVPLS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEKRVNSnkLRVYLYHGPnRDSRARVLST-----YDIVITTYSLVAKEIPTnkqeaeipganlnvegtstpL 726
Cdd:cd17996     64 TLSNWVSEFEKWAPS--VSKIVYKGT-PDVRKKLQSQiragkFNVLLTTYEYIIKDKPL--------------------L 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  727 LRIAWARIILDEAHNVKNprvqtsiAVCKL--------QACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-F 791
Cdd:cd17996    121 SKIKWKYMIIDEGHRMKN-------AQSKLtqtlntyyHARYRLLLTGTPLQNNLPELWALLNFLlpkifkSCKTFEQwF 193

                   .
gi 1034562578  792 N 792
Cdd:cd17996    194 N 194
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
573-788 1.74e-20

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: 90.52  E-value: 1.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALI--LTQKNqekkeekekstaltwlskddscdftSHGT-LIICP 649
Cdd:cd17998      4 YQLIGLNWLNLLYQKK-LSGILADEMGLGKTIQVIAFLayLKEIG-------------------------IPGPhLVVVP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARV-------LSTYDIVITTYSLVAkeipTNKQEAE-IPGANLNVeg 721
Cdd:cd17998     58 SSTLDNWLREFKRWCPS--LKVEPYYG-SQEERKHLrydilkgLEDFDVIVTTYNLAT----SNPDDRSfFKRLKLNY-- 128
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034562578  722 tstpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF 788
Cdd:cd17998    129 ------------VVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
573-820 2.63e-19

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: 88.33  E-value: 2.63e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwreSQKPQG--GILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLSKDdscdftsHGT----LI 646
Cdd:cd18002      4 YQLKGLNWLA---NLYEQGinGILADEMGLGKTVQSIAV------------------LAHLAEE-------HNIwgpfLV 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  647 ICPASLIHHWKNEVEKRVNsnKLRVYLYHGPNRD--------SRARVL---STYDIVITTYSLVAKEIPTnkqeaeipga 715
Cdd:cd18002     56 IAPASTLHNWQQEISRFVP--QFKVLPYWGNPKDrkvlrkfwDRKNLYtrdAPFHVVITSYQLVVQDEKY---------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  716 nlnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFD---EFN 792
Cdd:cd18002    124 ----------FQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDshdEFN 193
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034562578  793 LWRSQ-VDNGSKKGG-------ERLSILTKSLLLRR 820
Cdd:cd18002    194 EWFSKdIESHAENKTglnehqlKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
573-831 4.31e-19

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 88.18  E-value: 4.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKKEEKEkstaltwlskddscdftshgtLIICPASL 652
Cdd:cd18064     19 YQVRGLNWLI-SLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPH---------------------MVLVPKST 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSnkLRVYLYHGpNRDSRARVL------STYDIVITTYSLVAKEIPTNKqeaeipganlnvegtstpl 726
Cdd:cd18064     77 LHNWMAEFKRWVPT--LRAVCLIG-DKDQRAAFVrdvllpGEWDVCVTSYEMLIKEKSVFK------------------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  727 lRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF---DEFNLWRSQVDN-GS 802
Cdd:cd18064    135 -KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFnsaEDFDSWFDTNNClGD 213
                          250       260
                   ....*....|....*....|....*....
gi 1034562578  803 KKGGERLSILTKSLLLRRTKDQLDSTGRP 831
Cdd:cd18064    214 QKLVERLHMVLRPFLLRRIKADVEKSLPP 242
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
992-1106 5.65e-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: 5.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  992 KISSLLAELEAIQRNsasqKSVIVSQWTNMLKVVALhLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAG 1071
Cdd:pfam00271    2 KLEALLELLKKERGG----KVLIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034562578 1072 GVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYRVG 1106
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
574-820 1.13e-18

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: 85.87  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  574 QKQALAWL--LWresQKPQGGILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLSKDdscdFTSHGT-LIICPA 650
Cdd:cd17993      6 QLTGLNWLahSW---CKGNNGILADEMGLGKTVQTISF------------------LSYLFHS----QQQYGPfLVVVPL 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  651 SLIHHWKNEVEKRVNSNKLRVYLyhgPNRDSRArVLSTYD------------IVITTYSLVAKEiptnKQEaeipganln 718
Cdd:cd17993     61 STMPAWQREFAKWAPDMNVIVYL---GDIKSRD-TIREYEfyfsqtkklkfnVLLTTYEIILKD----KAF--------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  719 vegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQV 798
Cdd:cd17993    124 -------LGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEH 196
                          250       260
                   ....*....|....*....|..
gi 1034562578  799 DNGSKKGGERLSILTKSLLLRR 820
Cdd:cd17993    197 DEEQEKGIADLHKELEPFILRR 218
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
570-820 1.01e-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: 83.02  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWREsqkpqGGIL-ADDMGLGKTLTMIALILTQKNQekkeekekstaltW-LskddscdftshgtLII 647
Cdd:cd18010      1 LLPFQREGVCFALRRG-----GRVLiADEMGLGKTVQAIAIAAYYREE-------------WpL-------------LIV 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  648 CPASLIHHWKNEVEKRVNS-NKLRVYLYHGPNRDSRArvlSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPL 726
Cdd:cd18010     50 CPSSLRLTWADEIERWLPSlPPDDIQVIVKSKDGLRD---GDAKVVIVSYDLLRRL--------------------EKQL 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  727 LRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAV--TGTPIQNNLLDMYSLLKFLR---CSPFDEFNLWRSQVDNG 801
Cdd:cd18010    107 LARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVIllSGTPALSRPIELFTQLDALDpklFGRFHDFGRRYCAAKQG 186
                          250       260
                   ....*....|....*....|....*..
gi 1034562578  802 SK----KGGERL----SILTKSLLLRR 820
Cdd:cd18010    187 GFgwdySGSSNLeelhLLLLATIMIRR 213
HELICc smart00490
helicase superfamily c-terminal domain;
1025-1106 2.37e-16

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 74.94  E-value: 2.37e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  1025 VALHLKKHGLTYATIDGSVNPKQRMDLVEAFNhsRGPQVMLISLLAGGVGLNLTGGNHLFLLDMHWNPSLEDQACDRIYR 1104
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 1034562578  1105 VG 1106
Cdd:smart00490   81 AG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
570-783 5.49e-16

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: 78.10  E-value: 5.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLwreSQKPQGGILADDMGLGKTLTMIALILtqknqekkeekekstALTWLSKDDSCdftshgtLIICP 649
Cdd:cd18011      1 PLPHQIDAVLRAL---RKPPVRLLLADEVGLGKTIEAGLIIK---------------ELLLRGDAKRV-------LILCP 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEKRVNSNKLRVY-LYHGPNRDSRARVLSTYDIVITTYSLVakeiptnKQEAEIPGAnlnvegtstpLLR 728
Cdd:cd18011     56 ASLVEQWQDELQDKFGLPFLILDrETAAQLRRLIGNPFEEFPIVIVSLDLL-------KRSEERRGL----------LLS 118
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034562578  729 IAWARIILDEAHNVKN---PRVQTSIAVCKLQACARWAV---TGTPIQNNLLDMYSLLKFL 783
Cdd:cd18011    119 EEWDLVVVDEAHKLRNsggGKETKRYKLGRLLAKRARHVlllTATPHNGKEEDFRALLSLL 179
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
573-820 8.63e-16

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: 77.79  E-value: 8.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALILTQKNQEKKEEKekstaltwlskddscdftshgtLIICPASL 652
Cdd:cd18060      4 YQLEGVNWLLFNWYNR-QNCILADEMGLGKTIQSIAFLQEVYNVGIHGPF----------------------LVIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSNKLrvyLYHGP-------------NRDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeipgan 716
Cdd:cd18060     61 ITNWEREFNTWTEMNTI---VYHGSlasrqmiqqyemyCKDSRGRLIPgayKFDALITTFEMILSDCPE----------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  717 lnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFNLWR 795
Cdd:cd18060    127 ---------LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLK 197
                          250       260
                   ....*....|....*....|....*
gi 1034562578  796 SQVDNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18060    198 DFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
573-820 6.93e-15

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


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 75.43  E-value: 6.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLL--WRESQKPqggILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLskddscdFTSHGT----LI 646
Cdd:cd18054     24 YQLEGLNWLAhsWCKNNSV---ILADEMGLGKTIQTISF------------------LSYL-------FHQHQLygpfLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  647 ICPASLIHHWKNEVEKRVNSNKLRVYLYHGPNRD---------SRARVLStYDIVITTYSLVAKEiptnkqeaeipganl 717
Cdd:cd18054     76 VVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNtireyewihSQTKRLK-FNALITTYEILLKD--------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  718 nvegtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQ 797
Cdd:cd18054    140 -----KTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEED 214
                          250       260
                   ....*....|....*....|...
gi 1034562578  798 VDNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18054    215 HGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
573-820 3.11e-14

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


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 73.15  E-value: 3.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIaliltqknqekkeekekstalTWLSkdDSCDFTSHGT-LIICPAS 651
Cdd:cd18058      4 YQLEGMNWLLFNWYNR-KNCILADEMGLGKTIQSI---------------------TFLS--EIFLMGIRGPfLIIAPLS 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEKRVNSNklrVYLYHGPN-------------RDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeipga 715
Cdd:cd18058     60 TITNWEREFRTWTEMN---AIVYHGSQisrqmiqqyemyyRDEQGNPLSgifKFQVVITTFEMILADCPE---------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  716 nlnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFNLW 794
Cdd:cd18058    127 ----------LKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFpSETTFL 196
                          250       260
                   ....*....|....*....|....*.
gi 1034562578  795 RSQVDNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18058    197 EEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
573-782 7.17e-14

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 72.50  E-value: 7.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLlWR--ESQKPQGG---ILADDMGLGKTLTMIALIltqknqekkeekekstaLTWLSKDDSCDFTSHGTLII 647
Cdd:cd18067      4 HQREGVKFL-YRcvTGRRIRGShgcIMADEMGLGKTLQCITLM-----------------WTLLRQSPQCKPEIDKAIVV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  648 CPASLIHHWKNEVEKRVNSNkLRVYLYHGPNRDSRARVLStydivittyslvakeiptnkQEAEIPGANLnvegtSTPLL 727
Cdd:cd18067     66 SPSSLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKLV--------------------QWASQQGRRV-----STPVL 119
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 RIAW---------------ARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKF 782
Cdd:cd18067    120 IISYetfrlhvevlqkgevGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNF 189
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
573-783 3.27e-12

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: 67.37  E-value: 3.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwresQKPQGGILADdMGLGKTLTMIaliltqknqekkeekeksTALTWLSKDdscDFTSHgTLIICPASL 652
Cdd:cd18013      4 YQKVAINFII----EHPYCGLFLD-MGLGKTVTTL------------------TALSDLQLD---DFTRR-VLVIAPLRV 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHH-WKNEVEKRVNSNKLRVYLYHGPNRDSRARVLSTYDIVITTYSLVAKEIptNKQEAEIPganlnvegtstpllriaW 731
Cdd:cd18013     57 ARStWPDEVEKWNHLRNLTVSVAVGTERQRSKAANTPADLYVINRENLKWLV--NKSGDPWP-----------------F 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034562578  732 ARIILDEAHNVKNPRVQTSIAVCKLQACARWAV--TGTPIQNNLLDMYSLLKFL 783
Cdd:cd18013    118 DMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIglTGTPSPNGLMDLWAQIALL 171
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
573-820 1.04e-11

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 65.82  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLL--WRESQKpqgGILADDMGLGKTLTMIALILTqknqekkeekekstalTWLSKddscdftSHGT-LIICP 649
Cdd:cd18059      4 YQLEGVNWLLfnWYNTRN---CILADEMGLGKTIQSITFLYE----------------IYLKG-------IHGPfLVIAP 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEkrvNSNKLRVYLYHGPN-------------RDSRARVLS---TYDIVITTYSLVAKEIPTnkqeaeip 713
Cdd:cd18059     58 LSTIPNWEREFR---TWTELNVVVYHGSQasrrtiqlyemyfKDPQGRVIKgsyKFHAIITTFEMILTDCPE-------- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  714 ganlnvegtstpLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPF-DEFN 792
Cdd:cd18059    127 ------------LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFpSETT 194
                          250       260
                   ....*....|....*....|....*...
gi 1034562578  793 LWRSQVDNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18059    195 FMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
573-822 1.16e-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: 66.24  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltqknqekkeekekstalTWLSKDDSCDFTshgTLIICPASL 652
Cdd:cd18063     27 YQLQGLEWMVSLYNNN-LNGILADEMGLGKTIQTIALI------------------TYLMEHKRLNGP---YLIIVPLST 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSNKLRVYLYHGPNRDSRARVLST--YDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLLRIA 730
Cdd:cd18063     85 LSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSgkFNVLLTTYEYIIKD--------------------KHILAKIR 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  731 WARIILDEAHNVKNPRVQ-TSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-----FNLWRSQV 798
Cdd:cd18063    145 WKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGERV 224
                          250       260
                   ....*....|....*....|....*..
gi 1034562578  799 DNGSKKG---GERLSILTKSLLLRRTK 822
Cdd:cd18063    225 DLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
573-820 2.25e-11

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: 65.03  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltqknqekkeekeKSTALTWLSKDdscdftshgTLIICPASL 652
Cdd:cd18061      4 YQLEGLNWLLFNWYNR-RNCILADEMGLGKTIQSITFL-------------YEILLTGIRGP---------FLIIAPLST 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSNklrVYLYHGP-------------NRDSRARVLS---TYDIVITTYSLVAkeiptnkqeaeipgan 716
Cdd:cd18061     61 IANWEREFRTWTDLN---VVVYHGSlisrqmiqqyemyFRDSQGRIIRgayRFQAIITTFEMIL---------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  717 lnveGTSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRS 796
Cdd:cd18061    122 ----GGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQ 197
                          250       260
                   ....*....|....*....|....*
gi 1034562578  797 QV-DNGSKKGGERLSILTKSLLLRR 820
Cdd:cd18061    198 EFgDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
573-820 3.04e-11

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


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 64.00  E-value: 3.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDSCD--FtshgtLIICPA 650
Cdd:cd17994      4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYS------------------LYKEGHSKgpF-----LVSAPL 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  651 SLIHHWKNEVEkrVNSNKLRVYLYHGPNrdsrarvlstydIVITTYSLVAKEIPTnkqeaeipganlnvegtstpLLRIA 730
Cdd:cd17994     60 STIINWEREFE--MWAPDFYVVTYVGDH------------VLLTSYELISIDQAI--------------------LGSID 105
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  731 WARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNGSKKGG-ERL 809
Cdd:cd17994    106 WAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQiKKL 185
                          250
                   ....*....|.
gi 1034562578  810 SILTKSLLLRR 820
Cdd:cd17994    186 HDLLGPHMLRR 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
573-822 4.74e-11

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


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 64.30  E-value: 4.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKpQGGILADDMGLGKTLTMIALIltqknqekkeekekstalTWLSKDDSCDFTshgTLIICPASL 652
Cdd:cd18062     27 YQIKGLEWLVSLYNNN-LNGILADEMGLGKTIQTIALI------------------TYLMEHKRINGP---FLIIVPLST 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEKRVNSnkLRVYLYHGPNRDSRARV----LSTYDIVITTYSLVAKEiptnkqeaeipganlnvegtSTPLLR 728
Cdd:cd18062     85 LSNWVYEFDKWAPS--VVKVSYKGSPAARRAFVpqlrSGKFNVLLTTYEYIIKD--------------------KQILAK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  729 IAWARIILDEAHNVKNPRVQ-TSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL------RCSPFDE-----FNLWRS 796
Cdd:cd18062    143 IRWKYMIVDEGHRMKNHHCKlTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLlptifkSCSTFEQwfnapFAMTGE 222
                          250       260
                   ....*....|....*....|....*....
gi 1034562578  797 QVDNGSKKG---GERLSILTKSLLLRRTK 822
Cdd:cd18062    223 KVDLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
584-784 1.12e-10

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 63.37  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  584 RESQKPQG--GILADDMGLGKTLTMIALILTqknqekkeekekstaLTWLSKDDSCDftshGTLIICPASLIHHWKNEVE 661
Cdd:cd18068     21 KKTKKSPGsgCILAHCMGLGKTLQVVTFLHT---------------VLLCEKLENFS----RVLVVCPLNTVLNWLNEFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  662 KRV----NSNKLRVY---LYHGPNRDSRA--RVLSTYDIVITTYSL-----VAKEIPTNKQEAEI-------PGANLnve 720
Cdd:cd18068     82 KWQeglkDEEKIEVNelaTYKRPQERSYKlqRWQEEGGVMIIGYDMyrilaQERNVKSREKLKEIfnkalvdPGPDF--- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034562578  721 gtstpllriawarIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 784
Cdd:cd18068    159 -------------VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
570-820 1.32e-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: 62.72  E-value: 1.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  570 LLLHQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdfTSHGTLIICP 649
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYS------------------LYKEGH---TKGPFLVSAP 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  650 ASLIHHWKNEVEkrVNSNKLRVYLYHGpNRDSRARVLSTYDIVITTYSLVAKEIPTNKQEAEIpgaNLNVEGTSTPLL-- 727
Cdd:cd18055     59 LSTIINWEREFQ--MWAPDFYVVTYTG-DKDSRAIIRENEFSFDDNAVKGGKKAFKMKREAQV---KFHVLLTSYELVti 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 ------RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDNG 801
Cdd:cd18055    133 dqaalgSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADI 212
                          250       260
                   ....*....|....*....|
gi 1034562578  802 SKKGG-ERLSILTKSLLLRR 820
Cdd:cd18055    213 SKEDQiKKLHDLLGPHMLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
591-784 2.20e-10

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: 62.14  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  591 GGILADDMGLGKTLTMIALIltqknqekkeekekstaltwlskDDSCDFTSHGT-LIICPASLIHHWKNEVEK------- 662
Cdd:cd18069     30 GCILAHSMGLGKTLQVISFL-----------------------DVLLRHTGAKTvLAIVPVNTLQNWLSEFNKwlpppea 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  663 --RVNSNKLRVYLYHGPNR--DSRARVLSTYD----IVITTYSLVAKEiptnkqeaeiPGANLnvegtstpllriawarI 734
Cdd:cd18069     87 lpNVRPRPFKVFILNDEHKttAARAKVIEDWVkdggVLLMGYEMFRLR----------PGPDV----------------V 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034562578  735 ILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLR 784
Cdd:cd18069    141 ICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
573-820 1.46e-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: 59.69  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdfTSHGTLIICPASL 652
Cdd:cd18057      4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTIVFLYS------------------LYKEGH---SKGPYLVSAPLST 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  653 IHHWKNEVEkrVNSNKLRVYLYHGpNRDSRARV----LSTYDIVITTyslvAKEIPTNKQEAEIpgaNLNVEGTSTPLL- 727
Cdd:cd18057     62 IINWEREFE--MWAPDFYVVTYTG-DKESRSVIreneFSFEDNAIRS----GKKVFRMKKEAQI---KFHVLLTSYELIt 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  728 -------RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVDN 800
Cdd:cd18057    132 idqailgSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
                          250       260
                   ....*....|....*....|.
gi 1034562578  801 GSKKGG-ERLSILTKSLLLRR 820
Cdd:cd18057    212 ISKEDQiKKLHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
573-820 2.66e-09

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: 58.91  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLwRESQKPQGGILADDMGLGKTLTMIALiltqknqekkeekekstaLTWLskddscdFTSHGT----LIIC 648
Cdd:cd18053     24 YQLNGLNWLA-HSWCKGNSCILADEMGLGKTIQTISF------------------LNYL-------FHEHQLygpfLLVV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  649 PASLIHHWKNEVEKRVNSNKLRVYLYHGPNRD---------SRARVLStYDIVITTYSLVAKEiptnkqeaeipganlnv 719
Cdd:cd18053     78 PLSTLTSWQREIQTWAPQMNAVVYLGDINSRNmirthewmhPQTKRLK-FNILLTTYEILLKD----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  720 egtSTPLLRIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFLRCSPFDEFNLWRSQVD 799
Cdd:cd18053    140 ---KSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHG 216
                          250       260
                   ....*....|....*....|.
gi 1034562578  800 NGSKKGGERLSILTKSLLLRR 820
Cdd:cd18053    217 KGREYGYASLHKELEPFLLRR 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
560-768 2.37e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.11  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  560 AEDPAGLKVPLLLHQKQALAWLLWRESQKPQGGILADDMGLGKTLTMIALILTQKNQEKkeekekstaltwlskddscdf 639
Cdd:COG1061     71 GDEASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKR--------------------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  640 tshgTLIICP-ASLIHHWKNEVEKrvnsnKLRVYLYHGPNRDsrarvlSTYDIVITTYSLVAKEIPTNKqeaeipganln 718
Cdd:COG1061    130 ----VLVLVPrRELLEQWAEELRR-----FLGDPLAGGGKKD------SDAPITVATYQSLARRAHLDE----------- 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034562578  719 vegtstplLRIAWARIILDEAHNVKNPRVQTSIAvcKLQACARWAVTGTP 768
Cdd:COG1061    184 --------LGDRFGLVIIDEAHHAGAPSYRRILE--AFPAAYRLGLTATP 223
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
573-783 4.84e-08

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 55.07  E-value: 4.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPQGgILADDMGLGKTLTMIALILTqknqekkeekekstaltwLSKDDScdftSHGTLII-CPAS 651
Cdd:cd18056      4 YQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTAVFLYS------------------LYKEGH----SKGPFLVsAPLS 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEkrVNSNKLRVYLYHGpNRDSRARV----LSTYDIVITTyslvAKEIPTNKQEAEIpgaNLNVEGTSTPLL 727
Cdd:cd18056     61 TIINWEREFE--MWAPDMYVVTYVG-DKDSRAIIreneFSFEDNAIRG----GKKASRMKKEASV---KFHVLLTSYELI 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034562578  728 --------RIAWARIILDEAHNVKNPRVQTSIAVCKLQACARWAVTGTPIQNNLLDMYSLLKFL 783
Cdd:cd18056    131 tidmailgSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFL 194
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
573-742 1.32e-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: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  573 HQKQALAWLLWRESQKPqgGILADDMGLGKTLTMIALIltqknqekkeekekstaltwlskddsCDFTSHGTLIICP-AS 651
Cdd:cd17926      4 YQEEALEAWLAHKNNRR--GILVLPTGSGKTLTALALI--------------------------AYLKELRTLIVVPtDA 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  652 LIHHWKNEVEKRVNSNKLRvYLYHGPNRDSRARvlstyDIVITTYSLVakeipTNKQEAEIPGANlnvegtstpllriAW 731
Cdd:cd17926     56 LLDQWKERFEDFLGDSSIG-LIGGGKKKDFDDA-----NVVVATYQSL-----SNLAEEEKDLFD-------------QF 111
                          170
                   ....*....|.
gi 1034562578  732 ARIILDEAHNV 742
Cdd:cd17926    112 GLLIVDEAHHL 122
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
4-39 8.00e-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: 8.00e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1034562578    4 VRCPeHGTFCFLKTGVRDGPNKGKSFYVC---RADTCSF 39
Cdd:pfam06839    1 PLCP-CGQRAVLLTVRKTGPNPGRQFYKCpvgREKQCGF 38
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
147-378 1.89e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  147 EEKKADKKQREKGDQLFDQKK--EQKPEMMEKDLSSGLVPKKKQSVVQEKKQEEGAEIQCEAETGGTHKRDFSEIKSQQC 224
Cdd:PTZ00108  1148 EEKEIAKEQRLKSKTKGKASKlrKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  225 QGNELTRPSASSQEKSSGKSQDVQRESEPLREKVTQLL---------PQNVHSHNSISKPQKGGPLNKEYTNW-EAKETK 294
Cdd:PTZ00108  1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLskegkpknaPKRVSAVQYSPPPPSKRPDGESNGGSkPSSPTK 1307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562578  295 AKDGPSIQATQKSLPQGhfqERPETHSVPAPGGPAAQAAPAAPGLSLGEGREAATSSDDEEEDDVVFVSSKPGSPLLFDS 374
Cdd:PTZ00108  1308 KKVKKRLEGSLAALKKK---KKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDEDD 1384

                   ....
gi 1034562578  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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