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Conserved domains on  [gi|1958648402|ref|XP_038941778|]
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TATA-binding protein-associated factor 172 isoform X2 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 12113717)

DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA, similar to TATA-binding protein-associated factor MOT1 (Modifier of transcription 1)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1007 8.51e-163

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 496.67  E-value: 8.51e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  458 EELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 537
Cdd:COG0553    211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  538 qraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 617
Cdd:COG0553    282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  618 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 697
Cdd:COG0553    352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  698 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 777
Cdd:COG0553    432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  778 AALSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkNTTEKLAVQNsslhdiqhaPKLSALKQLLldcglgn 857
Cdd:COG0553    487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL--------EEGAELSGRS---------AKLEALLELL------- 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  858 gtssesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 937
Cdd:COG0553    543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  938 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1007
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
1-278 4.16e-68

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


:

Pssm-ID: 463447  Cd Length: 445  Bit Score: 235.60  E-value: 4.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402    1 MQNECKQFISSLADAHIEVGNRVNN-------------NVLTIDQANDLVTTLFNEVTSTFDLNPQVL--QQLDSKRHQV 65
Cdd:pfam12054  199 LRTQCQQLLNTFRDVGKVSQSKLPKlavvvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   66 QMTVAETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQYIAKLLQQCTTR-TPCPNS 144
Cdd:pfam12054  279 QAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPND 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  145 KVIKNLCSSLCVDPYLTPCVtcpvptqsgqenskgsnsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgpipkaikaq 224
Cdd:pfam12054  359 KIVKNLCTFLCVDTSETPEF-----------------------HPNAKLTDGILTLRKEEDKADHADA------------ 403
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958648402  225 iadlpagssgnilVELDEGQKPYLVQRRGAEFALTTVVKHFGAEMALKLPHLWD 278
Cdd:pfam12054  404 -------------AKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWE 444
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1007 8.51e-163

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 496.67  E-value: 8.51e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  458 EELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 537
Cdd:COG0553    211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  538 qraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 617
Cdd:COG0553    282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  618 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 697
Cdd:COG0553    352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  698 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 777
Cdd:COG0553    432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  778 AALSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkNTTEKLAVQNsslhdiqhaPKLSALKQLLldcglgn 857
Cdd:COG0553    487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL--------EEGAELSGRS---------AKLEALLELL------- 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  858 gtssesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 937
Cdd:COG0553    543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  938 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1007
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
493-730 9.67e-158

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: 466.06  E-value: 9.67e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 652
Cdd:cd17999     75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648402  653 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 730
Cdd:cd17999    155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
486-1041 2.81e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 295.56  E-value: 2.81e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  486 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRAqeyarsklaecMPLPSLVVCPPTLT 565
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  566 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 637
Cdd:PLN03142   232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  638 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 717
Cdd:PLN03142   305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  718 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDetvssaALSEETEKPKLkatghVFQ 797
Cdd:PLN03142   374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLD------VVNAGGERKRL-----LNI 437
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  798 ALQyLRKLCNHPALV--LTPQHPEFknTTEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGTSSESgtesvvaqhRIL 875
Cdd:PLN03142   438 AMQ-LRKCCNHPYLFqgAEPGPPYT--TGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVL 491
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  876 IFCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHD 954
Cdd:PLN03142   492 IFSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSD 568
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  955 WNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDLFTLDkd 1030
Cdd:PLN03142   569 WNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQgrlaEQKTV---NKDELLQMVRYG-- 643
                          570
                   ....*....|.
gi 1958648402 1031 gkAEKADSSTS 1041
Cdd:PLN03142   644 --AEMVFSSKD 652
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
496-812 6.19e-69

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: 232.57  E-value: 6.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  496 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAGDHCQRAQeyarsklaecMPLPSLVVCPPTLTGHWVDEVGK 574
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLLYLKHVDKN----------WGGPTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  575 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 651
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  652 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 731
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  732 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDETVSSaalseetEKPKLKATGhVFQALQYLRKLCNHPAL 811
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLNAIKTG-------EGGREIKAS-LLNILMRLRKICNHPGL 288

                   .
gi 1958648402  812 V 812
Cdd:pfam00176  289 I 289
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
1-278 4.16e-68

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


Pssm-ID: 463447  Cd Length: 445  Bit Score: 235.60  E-value: 4.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402    1 MQNECKQFISSLADAHIEVGNRVNN-------------NVLTIDQANDLVTTLFNEVTSTFDLNPQVL--QQLDSKRHQV 65
Cdd:pfam12054  199 LRTQCQQLLNTFRDVGKVSQSKLPKlavvvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   66 QMTVAETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQYIAKLLQQCTTR-TPCPNS 144
Cdd:pfam12054  279 QAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPND 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  145 KVIKNLCSSLCVDPYLTPCVtcpvptqsgqenskgsnsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgpipkaikaq 224
Cdd:pfam12054  359 KIVKNLCTFLCVDTSETPEF-----------------------HPNAKLTDGILTLRKEEDKADHADA------------ 403
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958648402  225 iadlpagssgnilVELDEGQKPYLVQRRGAEFALTTVVKHFGAEMALKLPHLWD 278
Cdd:pfam12054  404 -------------AKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWE 444
DEXDc smart00487
DEAD-like helicases superfamily;
492-686 3.67e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.41  E-value: 3.67e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   492 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhcqrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 570
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   571 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 645
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1958648402   646 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 686
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-1007 8.51e-163

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 496.67  E-value: 8.51e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  458 EELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 537
Cdd:COG0553    211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  538 qraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 617
Cdd:COG0553    282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  618 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 697
Cdd:COG0553    352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  698 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 777
Cdd:COG0553    432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  778 AALSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkNTTEKLAVQNsslhdiqhaPKLSALKQLLldcglgn 857
Cdd:COG0553    487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL--------EEGAELSGRS---------AKLEALLELL------- 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  858 gtssesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 937
Cdd:COG0553    543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  938 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1007
Cdd:COG0553    613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
493-730 9.67e-158

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: 466.06  E-value: 9.67e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 652
Cdd:cd17999     75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648402  653 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 730
Cdd:cd17999    155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
489-732 7.78e-85

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: 273.29  E-value: 7.78e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  489 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhCQRAQEYarsklaecMPLPSLVVCPPTLTGHW 568
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALL----LSRKEEG--------RKGPSLVVAPTSLIYNW 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  569 VDEVGKFCSReyLNPLHYTGPPTERiRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVK 648
Cdd:cd18012     69 EEEAAKFAPE--LKVLVIHGTKRKR-EKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  649 QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARsssreqeagvlAMDALHRQVLPFLL 728
Cdd:cd18012    146 ALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFIL 214

                   ....
gi 1958648402  729 RRMK 732
Cdd:cd18012    215 RRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
486-1041 2.81e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 295.56  E-value: 2.81e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  486 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRAqeyarsklaecMPLPSLVVCPPTLT 565
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  566 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 637
Cdd:PLN03142   232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  638 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 717
Cdd:PLN03142   305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  718 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDetvssaALSEETEKPKLkatghVFQ 797
Cdd:PLN03142   374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLD------VVNAGGERKRL-----LNI 437
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  798 ALQyLRKLCNHPALV--LTPQHPEFknTTEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGTSSESgtesvvaqhRIL 875
Cdd:PLN03142   438 AMQ-LRKCCNHPYLFqgAEPGPPYT--TGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVL 491
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  876 IFCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHD 954
Cdd:PLN03142   492 IFSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSD 568
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  955 WNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDLFTLDkd 1030
Cdd:PLN03142   569 WNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQgrlaEQKTV---NKDELLQMVRYG-- 643
                          570
                   ....*....|.
gi 1958648402 1031 gkAEKADSSTS 1041
Cdd:PLN03142   644 --AEMVFSSKD 652
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
496-812 6.19e-69

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: 232.57  E-value: 6.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  496 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAGDHCQRAQeyarsklaecMPLPSLVVCPPTLTGHWVDEVGK 574
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLLYLKHVDKN----------WGGPTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  575 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 651
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  652 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 731
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  732 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDETVSSaalseetEKPKLKATGhVFQALQYLRKLCNHPAL 811
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLNAIKTG-------EGGREIKAS-LLNILMRLRKICNHPGL 288

                   .
gi 1958648402  812 V 812
Cdd:pfam00176  289 I 289
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
1-278 4.16e-68

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


Pssm-ID: 463447  Cd Length: 445  Bit Score: 235.60  E-value: 4.16e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402    1 MQNECKQFISSLADAHIEVGNRVNN-------------NVLTIDQANDLVTTLFNEVTSTFDLNPQVL--QQLDSKRHQV 65
Cdd:pfam12054  199 LRTQCQQLLNTFRDVGKVSQSKLPKlavvvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   66 QMTVAETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQYIAKLLQQCTTR-TPCPNS 144
Cdd:pfam12054  279 QAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPND 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  145 KVIKNLCSSLCVDPYLTPCVtcpvptqsgqenskgsnsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgpipkaikaq 224
Cdd:pfam12054  359 KIVKNLCTFLCVDTSETPEF-----------------------HPNAKLTDGILTLRKEEDKADHADA------------ 403
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958648402  225 iadlpagssgnilVELDEGQKPYLVQRRGAEFALTTVVKHFGAEMALKLPHLWD 278
Cdd:pfam12054  404 -------------AKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWE 444
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
493-682 1.13e-65

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: 218.97  E-value: 1.13e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRAQeyarsklaecmPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE-----------RGPVLVVCPLSVLENWEREF 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTERIRLQHQ--VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQL 650
Cdd:cd17919     70 EKWTPD--LRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKAL 147
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958648402  651 TANYRIILSGTPIQNNVLELWSLFDFLMPGFL 682
Cdd:cd17919    148 RAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
493-730 5.11e-60

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: 205.30  E-value: 5.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHcqraqeyaRSKLAEcmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF--------DSGLIK----SVLVVMPTSLIPHWVKEF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLNpLHYTGPPTERIRLQHQVKR-HNLIVASYDVVRNDIDFF-----RNIKFNYCILDEGHVIKNGKTKLSKA 646
Cdd:cd18001     69 AKWTPGLRVK-VFHGTSKKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  647 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPG-FLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLP 725
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                   ....*
gi 1958648402  726 FLLRR 730
Cdd:cd18001    228 YFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
833-982 7.13e-54

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: 183.83  E-value: 7.13e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  833 SLHDIQHAPKLSALKQLLLDCGLGNgtssesgtesvvaqHRILIFCQLKSMLDIVEHDLLKPHlpsVTYLRLDGSIPPGQ 912
Cdd:cd18793      3 PKIEEVVSGKLEALLELLEELREPG--------------EKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKE 65
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  913 RHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLI 982
Cdd:cd18793     66 RQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
493-732 5.00e-52

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: 182.59  E-value: 5.00e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhCQRAQEyarsklaecMPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA---HLRERG---------VWGPFLVIAPLSTLPNWVNEF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTERIRLQHQVKRHN-------LIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSK 645
Cdd:cd18009     72 ARFTPS--VPVLLYHGTKEERERLRKKIMKREgtlqdfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  646 AVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQEAGVLAMdaLHRQV 723
Cdd:cd18009    150 ELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNaaDISNLSEEREQNIVHM--LHAIL 227

                   ....*....
gi 1958648402  724 LPFLLRRMK 732
Cdd:cd18009    228 KPFLLRRLK 236
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
493-730 9.52e-50

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: 176.42  E-value: 9.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILA---------GDHCQRAQEYARSKLAECMPLPSLVVCPPT 563
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrRDRENNRPRFKKKPPASSAKKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  564 LTGHWVDEVGKFcsrEYLNPLHYTGPPTERIrLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 641
Cdd:cd18005     81 VLYNWKDELDTW---GHFEVGVYHGSRKDDE-LEGRLKagRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  642 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHR 721
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                   ....*....
gi 1958648402  722 QVLPFLLRR 730
Cdd:cd18005    237 KLSKFFLRR 245
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
493-730 2.28e-49

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: 175.17  E-value: 2.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICILAGDHCQRaqEYARSKLAECmplpsLVVCPPTLTGH 567
Cdd:cd18004      1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQG--PYGKPTAKKA-----LIVCPSSLVGN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  568 WVDEVGKFCSREYLNPLHYTG--PPTERIRLQHQV-KRHNLIVASYDVVRNDID-FFRNIKFNYCILDEGHVIKNGKTKL 643
Cdd:cd18004     74 WKAEFDKWLGLRRIKVVTADGnaKDVKASLDFFSSaSTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  644 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 723
Cdd:cd18004    154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                   ....*..
gi 1958648402  724 LPFLLRR 730
Cdd:cd18004    234 SRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
493-682 3.34e-49

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: 172.89  E-value: 3.34e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCqrAQEYARsklaecmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH--SKLGLG---------PSLIVCPATVLKQWVKEF 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLNPLHYTGPPT-----------ERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 641
Cdd:cd18000     70 HRWWPPFRVVVLHSSGSGTgseeklgsierKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958648402  642 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFL 682
Cdd:cd18000    150 EITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
493-730 1.06e-47

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: 170.55  E-value: 1.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLaflnkykLH--GILCDDMGLGKTLQSICILAGDHCQRAQEY----ARSKLAECMPLPS--LVVCPPTL 564
Cdd:cd18008      1 LLPYQKQGLAWM-------LPrgGILADEMGLGKTIQALALILATRPQDPKIPeeleENSSDPKKLYLSKttLIVVPLSL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  565 TGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFF----------------RNIKFNYC 628
Cdd:cd18008     74 LSQWKDEIEKHTKPGSLKVYVYHGS--KRIKSIEELSDYDIVITTYGTLASEFPKNkkgggrdskekeasplHRIRWYRV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  629 ILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDArsssre 708
Cdd:cd18008    152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK------ 225
                          250       260
                   ....*....|....*....|..
gi 1958648402  709 qeagvlAMDALHRQVLPFLLRR 730
Cdd:cd18008    226 ------ALERLQALLKPILLRR 241
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
493-730 2.63e-45

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: 162.91  E-value: 2.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRaQEYArsklaecmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK-GNWG----------PHLIVVPTSVMLNWEMEF 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTERIRlqhqvKRH--------NLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 644
Cdd:cd18003     70 KRWCPG--FKILTYYGSAKERKL-----KRQgwmkpnsfHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRW 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  645 KAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIlasrDARSSSREQEAGVLaMDALHRQVL 724
Cdd:cd18003    143 QTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL----TAMSEGSQEENEEL-VRRLHKVLR 217

                   ....*.
gi 1958648402  725 PFLLRR 730
Cdd:cd18003    218 PFLLRR 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
493-679 7.17e-45

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: 160.24  E-value: 7.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqRAQEYARsklaecmPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA-----YLKEIGI-------PGPHLVVVPSSTLDNWLREF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTERIRLQHQVKR----HNLIVASYDVV---RNDIDFFRNIKFNYCILDEGHVIKNGKTKLSK 645
Cdd:cd17998     69 KRWCPS--LKVEPYYGSQEERKHLRYDILKgledFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYR 146
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958648402  646 AVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 679
Cdd:cd17998    147 HLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
493-730 2.59e-41

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: 151.50  E-value: 2.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraqeyarsKLAECMPL--PSLVVCPPTLTGHWVD 570
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLA-------------HLAEEHNIwgPFLVIAPASTLHNWQQ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  571 EVGKFCSReyLNPLHYTGPPTERIRLQHQVKRHNL---------IVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 641
Cdd:cd18002     68 EISRFVPQ--FKVLPYWGNPKDRKVLRKFWDRKNLytrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  642 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEagvlaMDALHR 721
Cdd:cd18002    146 SRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHM 220

                   ....*....
gi 1958648402  722 QVLPFLLRR 730
Cdd:cd18002    221 ILKPFMLRR 229
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
490-732 2.78e-41

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: 151.32  E-value: 2.78e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  490 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraqeYArsKLAECMPLPSLVVCPPTLTGHWV 569
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG---------YL--KHYKNINGPHLIIVPKSTLDNWM 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  570 DEVGKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 646
Cdd:cd17997     70 REFKRWCPS--LRVVVLIGDKEERadiIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  647 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilaSRDARSSSREQeagvlAMDALHRQVLPF 726
Cdd:cd17997    148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF------NVNNCDDDNQE-----VVQRLHKVLRPF 216

                   ....*.
gi 1958648402  727 LLRRMK 732
Cdd:cd17997    217 LLRRIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
493-730 2.95e-41

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: 151.25  E-value: 2.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILagdhcqraqEYARSKlaECMPLPSLVVCPPTLTGHWVDE 571
Cdd:cd17995      1 LRDYQLEGVNWLLF-NWYNRRNcILADEMGLGKTIQSIAFL---------EHLYQV--EGIRGPFLVIAPLSTIPNWQRE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 VGKFCSreyLNPLHYTGPPTER-IRLQHQ-------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 637
Cdd:cd17995     69 FETWTD---MNVVVYHGSGESRqIIQQYEmyfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  638 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamd 717
Cdd:cd17995    146 NRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-------DLKTAEQVEK------- 211
                          250
                   ....*....|...
gi 1958648402  718 aLHRQVLPFLLRR 730
Cdd:cd17995    212 -LQALLKPYMLRR 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
493-730 4.18e-41

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: 150.67  E-value: 4.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraqeYARSKLAecMPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW---------YLAGRLK--LLGPFLVLCPLSVLDNWKEEL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTERIRLQHQVK---RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 649
Cdd:cd18006     70 NRFAPD--LSVITYMGDKEKRLDLQQDIKstnRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  650 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTER--QFAARYgkpilasrdarsssREQEAGVLAMDALHRQVLPFL 727
Cdd:cd18006    148 FSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAY--------------SETDDESETVEELHLLLQPFL 213

                   ...
gi 1958648402  728 LRR 730
Cdd:cd18006    214 LRR 216
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
490-732 5.86e-41

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: 150.60  E-value: 5.86e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  490 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraqeYarskLAECMPL--PSLVVCP-PTLTG 566
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLIT---------Y----LMEKKKNngPYLVIVPlSTLSN 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  567 hWVDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 644
Cdd:cd17996     68 -WVSEFEKWAPS--VSKIVYKGTPDVRKKLQSQIRagKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLT 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  645 KAVKQ-LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 723
Cdd:cd17996    145 QTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVL 224

                   ....*....
gi 1958648402  724 LPFLLRRMK 732
Cdd:cd17996    225 RPFLLRRLK 233
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
492-730 1.37e-40

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: 149.04  E-value: 1.37e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  492 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdHCQRAQEyarsklaecMPLPSLVVCPPTLTGHWVDE 571
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS--YLFHSQQ---------QYGPFLVVVPLSTMPAWQRE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 VGKFCSReyLNPLHYTGPPTER--IR----LQHQVKR--HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKL 643
Cdd:cd17993     70 FAKWAPD--MNVIVYLGDIKSRdtIReyefYFSQTKKlkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  644 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarsssrEQEAGVlamDALHRQV 723
Cdd:cd17993    148 YEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDE-------------EQEKGI---ADLHKEL 211

                   ....*..
gi 1958648402  724 LPFLLRR 730
Cdd:cd17993    212 EPFILRR 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
491-742 2.50e-36

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: 137.87  E-value: 2.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  491 AELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqrAQEYARSklaecMPLPSLVVCPPTLTGHWVD 570
Cdd:cd18064     14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLG------YMKHYRN-----IPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  571 EVGKFCSReyLNPLHYTGPPTERIRLQHQV---KRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAV 647
Cdd:cd18064     83 EFKRWVPT--LRAVCLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  648 KQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFL 727
Cdd:cd18064    161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTNNCLGDQK----LVERLHMVLRPFL 228
                          250
                   ....*....|....*
gi 1958648402  728 LRRMKEDVLQDLPPK 742
Cdd:cd18064    229 LRRIKADVEKSLPPK 243
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
493-730 1.96e-33

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: 129.51  E-value: 1.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICIL-----AGDHCQRAQEYArsklaecmplpsLVVCPP 562
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMwtllrQSPQCKPEIDKA------------IVVSPS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  563 TLTGHWVDEVGKFCSREyLNPLHYTGPPTERIRLQ---------HQVKRHNLIVaSYDVVRNDIDFFRNIKFNYCILDEG 633
Cdd:cd18067     69 SLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKlvqwasqqgRRVSTPVLII-SYETFRLHVEVLQKGEVGLVICDEG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  634 HVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGV 713
Cdd:cd18067    147 HRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGE 226
                          250
                   ....*....|....*..
gi 1958648402  714 LAMDALHRQVLPFLLRR 730
Cdd:cd18067    227 EKLQELISIVNRCIIRR 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
489-732 3.43e-33

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: 129.03  E-value: 3.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  489 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqRAQEYARsklaecMPLPSLVVCPPTLTGHW 568
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------LNGPYLIIVPLSTLSNW 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  569 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 646
Cdd:cd18063     89 TYEFDKWAPS--VVKISYKGTPAMRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  647 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPiLASRDARSSSREQEAgVLAMDALHRQVLP 725
Cdd:cd18063    167 LNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP-FAMTGERVDLNEEET-ILIIRRLHKVLRP 244

                   ....*..
gi 1958648402  726 FLLRRMK 732
Cdd:cd18063    245 FLLRRLK 251
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
493-677 1.27e-32

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: 127.21  E-value: 1.27e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHG-ILCDDMGLGKTLQSIC-ILAGDHCQRAQEYAR--------SKLAECMpLPS---LVV 559
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIAlILAQKNTQNRKEEEKekalteweSKKDSTL-VPSagtLVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  560 CPPTLTGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFFRN---------IKFNYCIL 630
Cdd:cd18072     80 CPASLVHQWKNEVESRVASNKLRVCLYHGP--NRERIGEVLRDYDIVITTYSLVAKEIPTYKEesrssplfrIAWARIIL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958648402  631 DEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFL 677
Cdd:cd18072    158 DEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
515-710 1.48e-32

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


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 126.64  E-value: 1.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  515 ILCDDMGLGKTLQSICILagdhcqraQEYARSKLAECMPLpslVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERI 594
Cdd:cd18007     30 ILAHTMGLGKTLQVITFL--------HTYLAAAPRRSRPL---VLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  595 RLQHQV------KRHNLIVASYDVVRNDI-----------DFFRNIKFNYC---ILDEGHVIKNGKTKLSKAVKQLTANY 654
Cdd:cd18007     99 ADARLRkinkwhKEGGVLLIGYELFRNLAsnattdprlkqEFIAALLDPGPdllVLDEGHRLKNEKSQLSKALSKVKTKR 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958648402  655 RIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQE 710
Cdd:cd18007    179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVR 234
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
493-730 2.65e-32

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: 125.73  E-value: 2.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLH-----GILCDDMGLGKTLQSICILAGDHCQraQEYARSKLAEcmplPSLVVCPPTLTGH 567
Cdd:cd18066      1 LRPHQREGIEFLYECVMGMRVnerfgAILADEMGLGKTLQCISLIWTLLRQ--GPYGGKPVIK----RALIVTPGSLVKN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  568 WVDEVGKFCSREylnplhytgppteRIRL-----QHQVKR------HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 636
Cdd:cd18066     75 WKKEFQKWLGSE-------------RIKVftvdqDHKVEEfiasplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  637 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAM 716
Cdd:cd18066    142 KNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARA 221
                          250
                   ....*....|....
gi 1958648402  717 DALHRQVLPFLLRR 730
Cdd:cd18066    222 AELTRLTGLFILRR 235
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
489-732 5.38e-32

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: 125.54  E-value: 5.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  489 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqRAQEYARsklaecMPLPSLVVCPPTLTGHW 568
Cdd:cd18062     20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------INGPFLIIVPLSTLSNW 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  569 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 646
Cdd:cd18062     89 VYEFDKWAPS--VVKVSYKGSPAARRAFVPQLRsgKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  647 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASrdARSSSREQEAGVLAMDALHRQVLP 725
Cdd:cd18062    167 LNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GEKVDLNEEETILIIRRLHKVLRP 244

                   ....*..
gi 1958648402  726 FLLRRMK 732
Cdd:cd18062    245 FLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
493-732 1.06e-31

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: 123.97  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraqeyaRSKLAECMPLPSLVVCPPTLTGHWVDEV 572
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLG-----------YLKHYRNIPGPHMVLVPKSTLHNWMNEF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 649
Cdd:cd18065     85 KRWVPS--LRAVCLIGDKDARaafIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  650 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFLLR 729
Cdd:cd18065    163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVLKPFLLR 230

                   ...
gi 1958648402  730 RMK 732
Cdd:cd18065    231 RIK 233
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
493-710 1.46e-31

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: 123.08  E-value: 1.46e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWlAFLNKYKLhgILCDDMGLGKTLQSICILAgdhcqraqeYARsklAECmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18010      1 LLPFQREGVCF-ALRRGGRV--LIADEMGLGKTVQAIAIAA---------YYR---EEW---PLLIVCPSSLRLTWADEI 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLNPLHYTGPPTERIR-LQHQVkrhnLIVaSYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 651
Cdd:cd18010     63 ERWLPSLPPDDIQVIVKSKDGLRdGDAKV----VIV-SYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLL 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958648402  652 --ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQE 710
Cdd:cd18010    138 krAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFgwDYSGSSNLEE 200
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
490-730 1.49e-30

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: 120.88  E-value: 1.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  490 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCQRaQEYArsklaecmplPSLVVCPPTLTGHWV 569
Cdd:cd18054     18 NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQH-QLYG----------PFLLVVPLSTLTSWQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  570 DE-------------VGKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 636
Cdd:cd18054     87 REfeiwapeinvvvyIGDLMSRNTIREYEWIHSQTKRLKF-------NALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  637 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarssSREQeagvlAM 716
Cdd:cd18054    160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-----------GREN-----GY 223
                          250
                   ....*....|....
gi 1958648402  717 DALHRQVLPFLLRR 730
Cdd:cd18054    224 QSLHKVLEPFLLRR 237
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
514-730 5.28e-30

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: 119.50  E-value: 5.28e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  514 GILCDDMGLGKTLQSICILAGDhcqraqeyarsklaecmplPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPptER 593
Cdd:cd18071     51 GILADDMGLGKTLTTISLILAN-------------------FTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGG--ER 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  594 IRLQHQVKRHNLIVASYDVVRNDIDF-----FRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVL 668
Cdd:cd18071    110 NRDPKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958648402  669 ELWSLFDFLMPGFLGTERQFAARYGKPIlasrdarssSREQEAGVLAMDALHRQVlpfLLRR 730
Cdd:cd18071    190 DLGSLLSFLHLKPFSNPEYWRRLIQRPL---------TMGDPTGLKRLQVLMKQI---TLRR 239
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
492-730 8.82e-28

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: 112.84  E-value: 8.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  492 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILaGDHCQRAQEYArsklaecmplPSLVVCPPTLTGHWVDE 571
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL-NYLFHEHQLYG----------PFLLVVPLSTLTSWQRE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 V-------------GKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 638
Cdd:cd18053     89 IqtwapqmnavvylGDINSRNMIRTHEWMHPQTKRLKF-------NILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  639 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilaSRDARSSSreqeagvlamda 718
Cdd:cd18053    162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GREYGYAS------------ 225
                          250
                   ....*....|..
gi 1958648402  719 LHRQVLPFLLRR 730
Cdd:cd18053    226 LHKELEPFLLRR 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
493-679 6.09e-26

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: 108.20  E-value: 6.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNkyklhGILCDDMGLGKTLQSI-CILAGDHCQRAQE--YARSKLAECMPLP-----------SLV 558
Cdd:cd18070      1 LLPYQRRAVNWMLVPG-----GILADEMGLGKTVEVLaLILLHPRPDNDLDaaDDDSDEMVCCPDClvaetpvsskaTLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  559 VCPPTLTGHWVDEVGKFcSREYLNPLHYTGPPTE---RIRLQHQVKRHNLIVASYDVVRNDIDF---FRN---------- 622
Cdd:cd18070     76 VCPSAILAQWLDEINRH-VPSSLKVLTYQGVKKDgalASPAPEILAEYDIVVTTYDVLRTELHYaeaNRSnrrrrrqkry 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958648402  623 ---------IKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 679
Cdd:cd18070    155 eappsplvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
514-708 4.15e-25

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: 105.36  E-value: 4.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  514 GILCDDMGLGKTLQSICILagdH----CQRAQEYARSklaecmplpsLVVCPPTLTGHWVDEVGKFcsREYLNPLH---- 585
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFL---HtvllCEKLENFSRV----------LVVCPLNTVLNWLNEFEKW--QEGLKDEEkiev 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  586 -----YTGPPTERIRLQHQVKRHNLIVASYDVVRNdIDFFRNIKF-----------------NYCILDEGHVIKNGKTKL 643
Cdd:cd18068     96 nelatYKRPQERSYKLQRWQEEGGVMIIGYDMYRI-LAQERNVKSreklkeifnkalvdpgpDFVVCDEGHILKNEASAV 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958648402  644 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSRE 708
Cdd:cd18068    175 SKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVD 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
493-730 5.52e-25

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: 104.37  E-value: 5.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcqraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------QEVYNVGIHG----PFLVIAPLSTITNWEREF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSreyLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 638
Cdd:cd18060     69 NTWTE---MNTIVYHGSLASRQMIQQYemyckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  639 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamda 718
Cdd:cd18060    146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLKTEEQVQK-------- 210
                          250
                   ....*....|..
gi 1958648402  719 LHRQVLPFLLRR 730
Cdd:cd18060    211 LQAILKPMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
492-686 3.67e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.41  E-value: 3.67e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   492 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhcqrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 570
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   571 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 645
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1958648402   646 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 686
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
493-693 2.56e-23

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: 99.72  E-value: 2.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILAGDHCQRAQEyarsklaecmplPSLVVCPPTLTGHWVDE 571
Cdd:cd18059      1 LREYQLEGVNWLLF-NWYNTRNcILADEMGLGKTIQSITFLYEIYLKGIHG------------PFLVIAPLSTIPNWERE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 vgkFCSREYLNPLHYTGPPTERIRLQ--------------HQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 637
Cdd:cd18059     68 ---FRTWTELNVVVYHGSQASRRTIQlyemyfkdpqgrviKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLK 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958648402  638 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 693
Cdd:cd18059    145 NRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG 200
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
493-693 1.61e-22

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: 97.42  E-value: 1.61e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcqraQEYARSklaecMPLPSLVVCPPTLTGHWVDEv 572
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-------EIFLMG-----IRGPFLIIAPLSTITNWERE- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 638
Cdd:cd18058     68 --FRTWTEMNAIVYHGSQISRQMIQQYemyyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958648402  639 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 693
Cdd:cd18058    146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
872-971 8.71e-22

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: 91.12  E-value: 8.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  872 HRILIFCQLKSMLDIvehDLLKpHLPSVTYLRLDGSIPPGQRHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFV 951
Cdd:pfam00271   16 GKVLIFSQTKKTLEA---ELLL-EKEGIKVARLHGDLSQEEREEILEDFRKG-KIDVLV-ATDVAERGLDLPDVDLVINY 89
                           90       100
                   ....*....|....*....|
gi 1958648402  952 EHDWNPMRDLQAMDRAHRIG 971
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
515-697 4.97e-21

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: 92.96  E-value: 4.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  515 ILCDDMGLGKTLQSICILagdhcqraqeyarSKLAECMPLPS-LVVCPPTLTGHWVDEVGKFCSREYLNPLhyTGPPTER 593
Cdd:cd18069     32 ILAHSMGLGKTLQVISFL-------------DVLLRHTGAKTvLAIVPVNTLQNWLSEFNKWLPPPEALPN--VRPRPFK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  594 IRLQHQVkrHNLIVASYDVVRN----------DIDFFRNIKF-NYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTP 662
Cdd:cd18069     97 VFILNDE--HKTTAARAKVIEDwvkdggvllmGYEMFRLRPGpDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYP 174
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958648402  663 IQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 697
Cdd:cd18069    175 LQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
493-693 8.58e-21

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: 92.38  E-value: 8.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcqraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEv 572
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL--------YEILLTGIRG----PFLIIAPLSTIANWERE- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 638
Cdd:cd18061     68 --FRTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKN 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958648402  639 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 693
Cdd:cd18061    146 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG 200
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
493-730 1.23e-20

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: 90.96  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcqraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 572
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHSKG-PFLVSAPLSTIINWEREF 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLnpLHYTGppterirlqhqvkrHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 652
Cdd:cd17994     70 EMWAPDFYV--VTYVG--------------DHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKI 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648402  653 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQeagvlaMDALHRQVLPFLLRR 730
Cdd:cd17994    134 GYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF---------ADISKEDQ------IKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
493-730 9.06e-19

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: 86.60  E-value: 9.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcqraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 572
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHTKG-PFLVSAPLSTIINWEREF 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKFCSREYLnpLHYTGPPTER-----------------------IRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCI 629
Cdd:cd18055     70 QMWAPDFYV--VTYTGDKDSRaiirenefsfddnavkggkkafkMKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  630 LDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQ 709
Cdd:cd18055    147 VDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ 217
                          250       260
                   ....*....|....*....|.
gi 1958648402  710 eagvlaMDALHRQVLPFLLRR 730
Cdd:cd18055    218 ------IKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
493-730 2.81e-18

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: 85.12  E-value: 2.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcqraqeYARSKLAECMPlPSLVVCPPTLTGHWVDE- 571
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFL----------YSLYKEGHSKG-PYLVSAPLSTIINWEREf 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 ------------VGKFCSREYLNPLHY--------TGPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILD 631
Cdd:cd18057     70 emwapdfyvvtyTGDKESRSVIRENEFsfednairSGKKVFRMKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  632 EGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQea 711
Cdd:cd18057    149 EAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ-- 217
                          250
                   ....*....|....*....
gi 1958648402  712 gvlaMDALHRQVLPFLLRR 730
Cdd:cd18057    218 ----IKKLHDLLGPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
885-971 4.99e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.56  E-value: 4.99e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402   885 DIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSidVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAM 964
Cdd:smart00490    1 EELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75

                    ....*..
gi 1958648402   965 DRAHRIG 971
Cdd:smart00490   76 GRAGRAG 82
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
493-679 7.27e-18

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: 83.96  E-value: 7.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdHCQRAQEYARSKLAECMPLPSLV-------VCPPTLt 565
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFL---YSLYKEGHSKGPFLVSAPLSTIInwerefeMWAPDM- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  566 gHWVDEVGKFCSREYLNPLHYT--------GPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 637
Cdd:cd18056     77 -YVVTYVGDKDSRAIIRENEFSfednairgGKKASRMKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLK 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958648402  638 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 679
Cdd:cd18056    155 NNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
493-681 1.26e-15

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: 76.94  E-value: 1.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVnwLAFLNKYKLHGILCDDMGLGKTLQSICIlagdhcqrAQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 572
Cdd:cd18011      1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLI--------IKELLLRGDAK----RVLILCPASLVEQWQDEL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  573 GKfcsREYLNPLHYTGPPTERIRLQHQV--KRHNLIVASYDVVRNDI---DFFRNIKFNYCILDEGHVIKNG----KTKL 643
Cdd:cd18011     67 QD---KFGLPFLILDRETAAQLRRLIGNpfEEFPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEAHKLRNSgggkETKR 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958648402  644 SKAVKQLTAN--YRIILSGTPIQNNVLELWSLFDFLMPGF 681
Cdd:cd18011    144 YKLGRLLAKRarHVLLLTATPHNGKEEDFRALLSLLDPGR 183
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
493-662 6.56e-09

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: 55.77  E-value: 6.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGV-NWLAFLNKYklHGILCDDMGLGKTLQSICILAgdhcqraqeyarsklaECMPLPSLVVCPPT-LTGHWVD 570
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNR--RGILVLPTGSGKTLTALALIA----------------YLKELRTLIVVPTDaLLDQWKE 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  571 EVGKFCSREYLNPLhyTGPPTERIRLQhqvkrhNLIVASYDVVRNDI----DFFRniKFNYCILDEGHVIkNGKTkLSKA 646
Cdd:cd17926     63 RFEDFLGDSSIGLI--GGGKKKDFDDA------NVVVATYQSLSNLAeeekDLFD--QFGLLIVDEAHHL-PAKT-FSEI 130
                          170
                   ....*....|....*.
gi 1958648402  647 VKQLTANYRIILSGTP 662
Cdd:cd17926    131 LKELNAKYRLGLTATP 146
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
493-696 1.23e-08

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: 56.59  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  493 LRKYQQDGVNwlaFLNKYKLHGILCDdMGLGKTLQSICILAGDHcqraqeyarsklAECMPLPSLVVCPPTLTGH-WVDE 571
Cdd:cd18013      1 PHPYQKVAIN---FIIEHPYCGLFLD-MGLGKTVTTLTALSDLQ------------LDDFTRRVLVIAPLRVARStWPDE 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  572 VGKFcsrEYLNPLHY---TGPPTERIRLQHqvKRHNLIVASYDVVrNDIDFFRNIKFNY--CILDEGHVIKNGKTKLSKA 646
Cdd:cd18013     65 VEKW---NHLRNLTVsvaVGTERQRSKAAN--TPADLYVINRENL-KWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKA 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958648402  647 VKQL--TANYRIILSGTPIQNNVLELWSLFDFLMPGflgtER------QFAARYGKPI 696
Cdd:cd18013    139 LRKVrpVIKRLIGLTGTPSPNGLMDLWAQIALLDQG----ERlgrsitAYRERWFDPD 192
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
828-1065 1.51e-08

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 58.97  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  828 AVQNSSLHDIQHaPKLSALKQLLLDCGLGNGTSsesgtesvvaqhRILIFCQLKSMLD-IVEHdLLKPHLPSVTYLrldg 906
Cdd:COG1111    323 AMRLAEEADIEH-PKLSKLREILKEQLGTNPDS------------RIIVFTQYRDTAEmIVEF-LSEPGIKAGRFV---- 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  907 sippGQ-------------RHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQK 973
Cdd:COG1111    385 ----GQaskegdkgltqkeQIEILERFRAG-EFNVLV-ATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREG 458
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  974 RVVnVyrLITRGTLEEKI--MGLQKFK------MNIANTVISQENSSLQSMGTDQLLDLFT---LDKDGKAEKADSSTSG 1042
Cdd:COG1111    459 RVV-V--LIAKGTRDEAYywSSRRKEKkmksilKKLKKLLDKQEKEKLKESAQATLDEFESikeLAEDEINEKDLDEIES 535
                          250       260
                   ....*....|....*....|....*..
gi 1958648402 1043 KASMKSV----LENLSDLWDAEQYDSE 1065
Cdd:COG1111    536 SENGAHVdwrePVLLQVIVSTLAESLE 562
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
492-662 4.17e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 50.79  E-value: 4.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  492 ELRKYQQDGVN-WLAFLNKYKLHGILCDDMGLGKTLqsicILAGDhcqrAQEYARSKLAecmplpsLVVCP-PTLTGHWV 569
Cdd:COG1061     80 ELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV----LALAL----AAELLRGKRV-------LVLVPrRELLEQWA 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958648402  570 DEVgkfcsREYLNPLHYTGPPTERirlqhqvkRHNLIVASYDVVRND--IDFFRNiKFNYCILDEGHVIknGKTKLSKAV 647
Cdd:COG1061    145 EEL-----RRFLGDPLAGGGKKDS--------DAPITVATYQSLARRahLDELGD-RFGLVIIDEAHHA--GAPSYRRIL 208
                          170
                   ....*....|....*
gi 1958648402  648 KQLTANYRIILSGTP 662
Cdd:COG1061    209 EAFPAAYRLGLTATP 223
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
929-973 1.84e-03

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 38.07  E-value: 1.84e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958648402  929 LLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQK 973
Cdd:cd18785     25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
 
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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