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Conserved domains on  [gi|27477070|ref|NP_003963|]
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TATA-binding protein-associated factor 172 [Homo sapiens]

Protein Classification

Mot1 family DEAD/DEAH box helicase( domain architecture ID 13778164)

Mot1 family DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA, similar to Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) that regulates transcription in association with TATA binding protein (TBP); contains a DUF3535 domain

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

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, ...
1231-1780 4.32e-154

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 490.12  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1231 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1310
Cdd:COG0553  211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1311 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1390
Cdd:COG0553  282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1391 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1470
Cdd:COG0553  352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1471 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1550
Cdd:COG0553  432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1551 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1630
Cdd:COG0553  487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1631 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1710
Cdd:COG0553  543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1711 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1780
Cdd:COG0553  613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
586-1051 6.30e-123

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: 394.69  E-value: 6.30e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    586 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 650
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    651 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 729
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    730 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 798
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    799 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 866
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    867 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 945
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    946 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 1025
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 27477070   1026 GAEFALTTIVKHFGGEMAVKLPHLWD 1051
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
HEAT COG1413
HEAT repeat [General function prediction only];
340-454 6.41e-05

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 44.62  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  340 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 408
Cdd:COG1413   28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 27477070  409 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 454
Cdd:COG1413   98 AA----EALGRLGD------PAAVPALLEALKDPDWEVRRAAARAL 133
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1231-1780 4.32e-154

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 490.12  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1231 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1310
Cdd:COG0553  211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1311 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1390
Cdd:COG0553  282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1391 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1470
Cdd:COG0553  352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1471 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1550
Cdd:COG0553  432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1551 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1630
Cdd:COG0553  487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1631 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1710
Cdd:COG0553  543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1711 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1780
Cdd:COG0553  613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1266-1503 4.62e-153

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: 469.14  E-value: 4.62e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1425
Cdd:cd17999   75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477070 1426 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 1503
Cdd:cd17999  155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
586-1051 6.30e-123

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: 394.69  E-value: 6.30e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    586 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 650
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    651 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 729
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    730 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 798
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    799 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 866
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    867 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 945
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    946 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 1025
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 27477070   1026 GAEFALTTIVKHFGGEMAVKLPHLWD 1051
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1259-1797 3.15e-82

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 294.40  E-value: 3.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1259 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLT 1338
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1339 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 1410
Cdd:PLN03142  232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1411 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 1490
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1491 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDETVSSAtlseetEKPKLkatghVFQ 1570
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLDVVNAGG------ERKRL-----LNI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1571 ALQyLRKLCNHPALVLTPQ-HPEFkTTAEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGSTSESgtesvvaqhRILI 1649
Cdd:PLN03142  438 AMQ-LRKCCNHPYLFQGAEpGPPY-TTGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVLI 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1650 FCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHDW 1728
Cdd:PLN03142  493 FSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477070  1729 NPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDL 1797
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQgrlaEQKTV---NKDELLQM 639
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1269-1585 5.57e-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: 234.11  E-value: 5.57e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1269 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAgdHCHRAQEYARSklaecmplPSLVVCPPTLTGHWVDEVGK 1347
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL--YLKHVDKNWGG--------PTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1348 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1424
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1425 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 1504
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1505 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDeTVSSATLSEETEKpklkatgHVFQALQYLRKLCNHPAL 1584
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLN-AIKTGEGGREIKA-------SLLNILMRLRKICNHPGL 288

                   .
gi 27477070   1585 V 1585
Cdd:pfam00176  289 I 289
DEXDc smart00487
DEAD-like helicases superfamily;
1265-1459 8.09e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 8.09e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    1265 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhchrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 1343
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    1344 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 1418
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 27477070    1419 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 1459
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
HEAT COG1413
HEAT repeat [General function prediction only];
340-454 6.41e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 44.62  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  340 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 408
Cdd:COG1413   28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 27477070  409 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 454
Cdd:COG1413   98 AA----EALGRLGD------PAAVPALLEALKDPDWEVRRAAARAL 133
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1231-1780 4.32e-154

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 490.12  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1231 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1310
Cdd:COG0553  211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1311 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1390
Cdd:COG0553  282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1391 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1470
Cdd:COG0553  352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1471 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1550
Cdd:COG0553  432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1551 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1630
Cdd:COG0553  487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1631 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1710
Cdd:COG0553  543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1711 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1780
Cdd:COG0553  613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1266-1503 4.62e-153

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: 469.14  E-value: 4.62e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1425
Cdd:cd17999   75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477070 1426 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 1503
Cdd:cd17999  155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
586-1051 6.30e-123

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: 394.69  E-value: 6.30e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    586 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 650
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    651 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 729
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    730 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 798
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    799 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 866
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    867 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 945
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    946 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 1025
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 27477070   1026 GAEFALTTIVKHFGGEMAVKLPHLWD 1051
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1262-1505 5.98e-84

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: 274.44  E-value: 5.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1262 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhCHRAQEYarsklaecMPLPSLVVCPPTLTGHW 1341
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALL----LSRKEEG--------RKGPSLVVAPTSLIYNW 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1342 VDEVGKFCSReyLNPLHYTGPPTERiRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVK 1421
Cdd:cd18012   69 EEEAAKFAPE--LKVLVIHGTKRKR-EKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1422 QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARsssreqeagvlAMDALHRQVLPFLL 1501
Cdd:cd18012  146 ALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFIL 214

                 ....
gi 27477070 1502 RRMK 1505
Cdd:cd18012  215 RRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1259-1797 3.15e-82

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 294.40  E-value: 3.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1259 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLT 1338
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1339 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 1410
Cdd:PLN03142  232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1411 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 1490
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1491 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDETVSSAtlseetEKPKLkatghVFQ 1570
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLDVVNAGG------ERKRL-----LNI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1571 ALQyLRKLCNHPALVLTPQ-HPEFkTTAEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGSTSESgtesvvaqhRILI 1649
Cdd:PLN03142  438 AMQ-LRKCCNHPYLFQGAEpGPPY-TTGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVLI 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  1650 FCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHDW 1728
Cdd:PLN03142  493 FSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477070  1729 NPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDL 1797
Cdd:PLN03142  570 NPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQgrlaEQKTV---NKDELLQM 639
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1269-1585 5.57e-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: 234.11  E-value: 5.57e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1269 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAgdHCHRAQEYARSklaecmplPSLVVCPPTLTGHWVDEVGK 1347
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL--YLKHVDKNWGG--------PTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1348 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1424
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1425 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 1504
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1505 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDeTVSSATLSEETEKpklkatgHVFQALQYLRKLCNHPAL 1584
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLN-AIKTGEGGREIKA-------SLLNILMRLRKICNHPGL 288

                   .
gi 27477070   1585 V 1585
Cdd:pfam00176  289 I 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1266-1455 7.67e-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: 218.20  E-value: 7.67e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQeyarsklaecmPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE-----------RGPVLVVCPLSVLENWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTERIRLQHQ--VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQL 1423
Cdd:cd17919   70 EKWTPD--LRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKAL 147
                        170       180       190
                 ....*....|....*....|....*....|..
gi 27477070 1424 TANYRIILSGTPIQNNVLELWSLFDFLMPGFL 1455
Cdd:cd17919  148 RAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1266-1503 1.15e-59

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: 1.15e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHchraqeyaRSKLAEcmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF--------DSGLIK----SVLVVMPTSLIPHWVKEF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLNpLHYTGPPTERIRLQHQVKR-HNLIVASYDVVRNDIDFF-----RNIKFNYCILDEGHVIKNGKTKLSKA 1419
Cdd:cd18001   69 AKWTPGLRVK-VFHGTSKKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1420 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPG-FLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLP 1498
Cdd:cd18001  148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                 ....*
gi 27477070 1499 FLLRR 1503
Cdd:cd18001  228 YFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1606-1755 2.50e-53

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: 183.06  E-value: 2.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1606 SLHDIQHAPKLSALKQLLLDCGLGNgstsesgtesvvaqHRILIFCQLKSMLDIVEHDLLKPHlpsVTYLRLDGSIPPGQ 1685
Cdd:cd18793    3 PKIEEVVSGKLEALLELLEELREPG--------------EKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKE 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1686 RHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLI 1755
Cdd:cd18793   66 RQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1266-1505 1.96e-51

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: 181.82  E-value: 1.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeyarsklaeCM-----PLPSLVVCPPTLTGH 1340
Cdd:cd18009    4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA-----------------HLrergvWGPFLVIAPLSTLPN 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1341 WVDEVGKFCSReyLNPLHYTGPPTERIRLQHQVKRHN-------LIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGK 1413
Cdd:cd18009   67 WVNEFARFTPS--VPVLLYHGTKEERERLRKKIMKREgtlqdfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLN 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1414 TKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQEAGVLAMda 1491
Cdd:cd18009  145 CRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNaaDISNLSEEREQNIVHM-- 222
                        250
                 ....*....|....
gi 27477070 1492 LHRQVLPFLLRRMK 1505
Cdd:cd18009  223 LHAILKPFLLRRLK 236
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1266-1503 2.30e-49

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: 176.03  E-value: 2.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILA---------GDHCHRAQEYARSKLAECMPLPSLVVCPPT 1336
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrRDRENNRPRFKKKPPASSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1337 LTGHWVDEVGKFcsrEYLNPLHYTGPPTERIrLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 1414
Cdd:cd18005   81 VLYNWKDELDTW---GHFEVGVYHGSRKDDE-LEGRLKagRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1415 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHR 1494
Cdd:cd18005  157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                 ....*....
gi 27477070 1495 QVLPFLLRR 1503
Cdd:cd18005  237 KLSKFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1266-1455 8.97e-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: 172.51  E-value: 8.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHChrAQEYARsklaecmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH--SKLGLG---------PSLIVCPATVLKQWVKEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLNPLHYTGPPT-----------ERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 1414
Cdd:cd18000   70 HRWWPPFRVVVLHSSGSGTgseeklgsierKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 27477070 1415 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFL 1455
Cdd:cd18000  150 EITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1266-1503 2.01e-48

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: 173.24  E-value: 2.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICILAGdhCHRAQEYARSKLAECmplpsLVVCPPTLTGH 1340
Cdd:cd18004    1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWT--LLKQGPYGKPTAKKA-----LIVCPSSLVGN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1341 WVDEVGKFCSREYLNPLHYTGPPTERIRLQHQV---KRHNLIVASYDVVRNDID-FFRNIKFNYCILDEGHVIKNGKTKL 1416
Cdd:cd18004   74 WKAEFDKWLGLRRIKVVTADGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1417 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 1496
Cdd:cd18004  154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                 ....*..
gi 27477070 1497 LPFLLRR 1503
Cdd:cd18004  234 SRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1266-1503 2.28e-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: 170.16  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLaflnkykLH--GILCDDMGLGKTLQSI-CILAGDHCHRAQEY---ARSKLAECMPLPS--LVVCPPTL 1337
Cdd:cd18008    1 LLPYQKQGLAWM-------LPrgGILADEMGLGKTIQALaLILATRPQDPKIPEeleENSSDPKKLYLSKttLIVVPLSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1338 TGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFF----------------RNIKFNYC 1401
Cdd:cd18008   74 LSQWKDEIEKHTKPGSLKVYVYHGS--KRIKSIEELSDYDIVITTYGTLASEFPKNkkgggrdskekeasplHRIRWYRV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1402 ILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDArsssre 1481
Cdd:cd18008  152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK------ 225
                        250       260
                 ....*....|....*....|..
gi 27477070 1482 qeagvlAMDALHRQVLPFLLRR 1503
Cdd:cd18008  226 ------ALERLQALLKPILLRR 241
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1266-1452 5.50e-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: 161.40  E-value: 5.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcHRAQEyarsklaeCMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA----YLKEI--------GIPGPHLVVVPSSTLDNWLREF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTERIRLQHQVKR----HNLIVASYDVV---RNDIDFFRNIKFNYCILDEGHVIKNGKTKLSK 1418
Cdd:cd17998   69 KRWCPS--LKVEPYYGSQEERKHLRYDILKgledFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYR 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 27477070 1419 AVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1452
Cdd:cd17998  147 HLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1266-1503 5.73e-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: 162.52  E-value: 5.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRaQEYArsklaecmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK-GNWG----------PHLIVVPTSVMLNWEMEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTERIRlqhqvKRH--------NLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 1417
Cdd:cd18003   70 KRWCPG--FKILTYYGSAKERKL-----KRQgwmkpnsfHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRW 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1418 KAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIlasrDARSSSREQEAGVLaMDALHRQVL 1497
Cdd:cd18003  143 QTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL----TAMSEGSQEENEEL-VRRLHKVLR 217

                 ....*.
gi 27477070 1498 PFLLRR 1503
Cdd:cd18003  218 PFLLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1266-1503 1.79e-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: 153.04  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcHRAQEYArsklaecMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLA----HLAEEHN-------IWGPFLVIAPASTLHNWQQEI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTERIRLQHQVKRHNL---------IVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKL 1416
Cdd:cd18002   70 SRFVPQ--FKVLPYWGNPKDRKVLRKFWDRKNLytrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1417 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEagvlaMDALHRQV 1496
Cdd:cd18002  148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHMIL 222

                 ....*..
gi 27477070 1497 LPFLLRR 1503
Cdd:cd18002  223 KPFMLRR 229
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1266-1503 2.15e-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: 152.40  E-value: 2.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILagDHCHraqeyarskLAECMPLPSLVVCPPTLTGHWVDE 1344
Cdd:cd17995    1 LRDYQLEGVNWLLF-NWYNRRNcILADEMGLGKTIQSIAFL--EHLY---------QVEGIRGPFLVIAPLSTIPNWQRE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 VGKFCSreyLNPLHYTGPPTER-IRLQHQ-------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1410
Cdd:cd17995   69 FETWTD---MNVVVYHGSGESRqIIQQYEmyfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1411 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamd 1490
Cdd:cd17995  146 NRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-------DLKTAEQVEK------- 211
                        250
                 ....*....|...
gi 27477070 1491 aLHRQVLPFLLRR 1503
Cdd:cd17995  212 -LQALLKPYMLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1263-1505 6.13e-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: 150.94  E-value: 6.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1263 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYArsKLAECMPLPSLVVCPPTLTGHWV 1342
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG---------YL--KHYKNINGPHLIIVPKSTLDNWM 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1343 DEVGKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1419
Cdd:cd17997   70 REFKRWCPS--LRVVVLIGDKEERadiIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1420 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilaSRDARSSSREQeagvlAMDALHRQVLPF 1499
Cdd:cd17997  148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF------NVNNCDDDNQE-----VVQRLHKVLRPF 216

                 ....*.
gi 27477070 1500 LLRRMK 1505
Cdd:cd17997  217 LLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1263-1505 8.28e-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: 150.98  E-value: 8.28e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1263 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYarskLAECMPL--PSLVVCP-PTLTG 1339
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLIT---------Y----LMEKKKNngPYLVIVPlSTLSN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1340 hWVDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 1417
Cdd:cd17996   68 -WVSEFEKWAPS--VSKIVYKGTPDVRKKLQSQIRagKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1418 KAVKQ-LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 1496
Cdd:cd17996  145 QTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVL 224

                 ....*....
gi 27477070 1497 LPFLLRRMK 1505
Cdd:cd17996  225 RPFLLRRLK 233
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1266-1503 1.06e-40

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: 150.28  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYARSKLAecMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW---------YLAGRLK--LLGPFLVLCPLSVLDNWKEEL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTERIRLQHQVK---RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 1422
Cdd:cd18006   70 NRFAPD--LSVITYMGDKEKRLDLQQDIKstnRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1423 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTER--QFAARYgkpilasrdarsssREQEAGVLAMDALHRQVLPFL 1500
Cdd:cd18006  148 FSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAY--------------SETDDESETVEELHLLLQPFL 213

                 ...
gi 27477070 1501 LRR 1503
Cdd:cd18006  214 LRR 216
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1265-1503 2.09e-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: 149.43  E-value: 2.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1265 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHcHRAQEYArsklaecmplPSLVVCPPTLTGHWVDE 1344
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLF-HSQQQYG----------PFLVVVPLSTMPAWQRE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 VGKFCSReyLNPLHYTGPPTER--IR----LQHQVKR--HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKL 1416
Cdd:cd17993   70 FAKWAPD--MNVIVYLGDIKSRdtIReyefYFSQTKKlkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1417 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarsssrEQEAGVlamDALHRQV 1496
Cdd:cd17993  148 YEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDE-------------EQEKGI---ADLHKEL 211

                 ....*..
gi 27477070 1497 LPFLLRR 1503
Cdd:cd17993  212 EPFILRR 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1264-1515 6.13e-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: 137.49  E-value: 6.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1264 AELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLTGHWVD 1343
Cdd:cd18064   14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRN-----------IPGPHMVLVPKSTLHNWMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1344 EVGKFCSReyLNPLHYTGPPTERIRLQHQV---KRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAV 1420
Cdd:cd18064   83 EFKRWVPT--LRAVCLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1421 KQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFL 1500
Cdd:cd18064  161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTNNCLGDQK----LVERLHMVLRPFL 228
                        250
                 ....*....|....*
gi 27477070 1501 LRRMKEDVLQDLPPK 1515
Cdd:cd18064  229 LRRIKADVEKSLPPK 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1262-1505 5.69e-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: 5.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1262 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchRAQEYARsklaecMPLPSLVVCPPTLTGHW 1341
Cdd:cd18063   20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------LNGPYLIIVPLSTLSNW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1342 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1419
Cdd:cd18063   89 TYEFDKWAPS--VVKISYKGTPAMRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1420 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPiLASRDARSSSREQEAgVLAMDALHRQVLP 1498
Cdd:cd18063  167 LNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP-FAMTGERVDLNEEET-ILIIRRLHKVLRP 244

                 ....*..
gi 27477070 1499 FLLRRMK 1505
Cdd:cd18063  245 FLLRRLK 251
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1266-1503 9.97e-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: 128.36  E-value: 9.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICIL-----AGDHCHRAQEYArsklaecmplpsLVVCPP 1335
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMwtllrQSPQCKPEIDKA------------IVVSPS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1336 TLTGHWVDEVGKFCSREyLNPLHYTGPPTERIRLQ---------HQVKRHNLIVaSYDVVRNDIDFFRNIKFNYCILDEG 1406
Cdd:cd18067   69 SLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKlvqwasqqgRRVSTPVLII-SYETFRLHVEVLQKGEVGLVICDEG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1407 HVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGV 1486
Cdd:cd18067  147 HRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGE 226
                        250
                 ....*....|....*..
gi 27477070 1487 LAMDALHRQVLPFLLRR 1503
Cdd:cd18067  227 EKLQELISIVNRCIIRR 243
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1288-1483 2.83e-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: 2.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1288 ILCDDMGLGKTLQSICILagdhchraQEYARSKLAECMPLpslVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERI 1367
Cdd:cd18007   30 ILAHTMGLGKTLQVITFL--------HTYLAAAPRRSRPL---VLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1368 RLQHQV------KRHNLIVASYDVVRNDI-----------DFFRNIKFNYC---ILDEGHVIKNGKTKLSKAVKQLTANY 1427
Cdd:cd18007   99 ADARLRkinkwhKEGGVLLIGYELFRNLAsnattdprlkqEFIAALLDPGPdllVLDEGHRLKNEKSQLSKALSKVKTKR 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 27477070 1428 RIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQE 1483
Cdd:cd18007  179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVR 234
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1262-1505 1.06e-31

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: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1262 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchRAQEYARsklaecMPLPSLVVCPPTLTGHW 1341
Cdd:cd18062   20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------INGPFLIIVPLSTLSNW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1342 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1419
Cdd:cd18062   89 VYEFDKWAPS--VVKVSYKGSPAARRAFVPQLRsgKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1420 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASrdARSSSREQEAGVLAMDALHRQVLP 1498
Cdd:cd18062  167 LNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GEKVDLNEEETILIIRRLHKVLRP 244

                 ....*..
gi 27477070 1499 FLLRRMK 1505
Cdd:cd18062  245 FLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1266-1505 1.48e-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: 124.36  E-value: 1.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18065   16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRN-----------IPGPHMVLVPKSTLHNWMNEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 1422
Cdd:cd18065   85 KRWVPS--LRAVCLIGDKDARaafIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1423 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFLLR 1502
Cdd:cd18065  163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVLKPFLLR 230

                 ...
gi 27477070 1503 RMK 1505
Cdd:cd18065  231 RIK 233
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1266-1483 1.91e-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: 123.47  E-value: 1.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWlAFLNKYKLhgILCDDMGLGKTLQSICILagdHCHRAqEYarsklaecmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18010    1 LLPFQREGVCF-ALRRGGRV--LIADEMGLGKTVQAIAIA---AYYRE-EW-----------PLLIVCPSSLRLTWADEI 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLNPLHYTGPPTERIR-LQHQVkrhnLIVaSYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1424
Cdd:cd18010   63 ERWLPSLPPDDIQVIVKSKDGLRdGDAKV----VIV-SYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLL 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477070 1425 --ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQE 1483
Cdd:cd18010  138 krAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFgwDYSGSSNLEE 200
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1266-1450 3.60e-31

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: 123.74  E-value: 3.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHG-ILCDDMGLGKTLQSIC-ILAGDHCHRAQEYAR--------SKLAECMpLPS---LVV 1332
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIAlILAQKNTQNRKEEEKekalteweSKKDSTL-VPSagtLVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1333 CPPTLTGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFFRN---------IKFNYCIL 1403
Cdd:cd18072   80 CPASLVHQWKNEVESRVASNKLRVCLYHGP--NRERIGEVLRDYDIVITTYSLVAKEIPTYKEesrssplfrIAWARIIL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 27477070 1404 DEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFL 1450
Cdd:cd18072  158 DEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1263-1503 4.77e-31

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: 123.19  E-value: 4.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1263 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHcHRAQEYArsklaecmplPSLVVCPPTLTGHWV 1342
Cdd:cd18054   18 NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLF-HQHQLYG----------PFLLVVPLSTLTSWQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1343 DE-------------VGKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 1409
Cdd:cd18054   87 REfeiwapeinvvvyIGDLMSRNTIREYEWIHSQTKRLKF-------NALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1410 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarssSREQeagvlAM 1489
Cdd:cd18054  160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-----------GREN-----GY 223
                        250
                 ....*....|....
gi 27477070 1490 DALHRQVLPFLLRR 1503
Cdd:cd18054  224 QSLHKVLEPFLLRR 237
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1266-1503 8.73e-31

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: 122.26  E-value: 8.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLH-----GILCDDMGLGKTLQSICILAGDHCHraQEYARSKLAEcmplPSLVVCPPTLTGH 1340
Cdd:cd18066    1 LRPHQREGIEFLYECVMGMRVnerfgAILADEMGLGKTLQCISLIWTLLRQ--GPYGGKPVIK----RALIVTPGSLVKN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1341 WVDEVGKFCSREylnplhytgppteRIRL-----QHQVKR------HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 1409
Cdd:cd18066   75 WKKEFQKWLGSE-------------RIKVftvdqDHKVEEfiasplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1410 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAM 1489
Cdd:cd18066  142 KNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARA 221
                        250
                 ....*....|....
gi 27477070 1490 DALHRQVLPFLLRR 1503
Cdd:cd18066  222 AELTRLTGLFILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1287-1503 1.37e-29

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: 119.11  E-value: 1.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1287 GILCDDMGLGKTLQSICILAGDhchraqeyarsklaecmplPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPptER 1366
Cdd:cd18071   51 GILADDMGLGKTLTTISLILAN-------------------FTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGG--ER 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1367 IRLQHQVKRHNLIVASYDVVRNDIDF-----FRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVL 1441
Cdd:cd18071  110 NRDPKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477070 1442 ELWSLFDFLMPGFLGTERQFAARYGKPIlasrdarssSREQEAGVLAMDALHRQVlpfLLRR 1503
Cdd:cd18071  190 DLGSLLSFLHLKPFSNPEYWRRLIQRPL---------TMGDPTGLKRLQVLMKQI---TLRR 239
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1265-1503 1.84e-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: 115.53  E-value: 1.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1265 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILaGDHCHRAQEYArsklaecmplPSLVVCPPTLTGHWVDE 1344
Cdd:cd18053   20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL-NYLFHEHQLYG----------PFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 V-------------GKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1411
Cdd:cd18053   89 IqtwapqmnavvylGDINSRNMIRTHEWMHPQTKRLKF-------NILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1412 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilaSRDARSSSreqeagvlamda 1491
Cdd:cd18053  162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GREYGYAS------------ 225
                        250
                 ....*....|..
gi 27477070 1492 LHRQVLPFLLRR 1503
Cdd:cd18053  226 LHKELEPFLLRR 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1266-1452 1.24e-25

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: 1.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNkyklhGILCDDMGLGKTLQSI-CILAgdhcHRAQE------YARSKLAECMPLP---------- 1328
Cdd:cd18070    1 LLPYQRRAVNWMLVPG-----GILADEMGLGKTVEVLaLILL----HPRPDndldaaDDDSDEMVCCPDClvaetpvssk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1329 -SLVVCPPTLTGHWVDEVGKFcSREYLNPLHYTGPPTE---RIRLQHQVKRHNLIVASYDVVRNDIDF---FRN------ 1395
Cdd:cd18070   72 aTLIVCPSAILAQWLDEINRH-VPSSLKVLTYQGVKKDgalASPAPEILAEYDIVVTTYDVLRTELHYaeaNRSnrrrrr 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1396 -------------IKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1452
Cdd:cd18070  151 qkryeappsplvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1287-1481 1.32e-24

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: 104.58  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1287 GILCDDMGLGKTLQSICILagdH----CHRAQEYARSklaecmplpsLVVCPPTLTGHWVDEVGKFcsREYLNPLH---- 1358
Cdd:cd18068   31 CILAHCMGLGKTLQVVTFL---HtvllCEKLENFSRV----------LVVCPLNTVLNWLNEFEKW--QEGLKDEEkiev 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1359 -----YTGPPTERIRLQHQVKRHNLIVASYDVVRNdIDFFRNIKF-----------------NYCILDEGHVIKNGKTKL 1416
Cdd:cd18068   96 nelatYKRPQERSYKLQRWQEEGGVMIIGYDMYRI-LAQERNVKSreklkeifnkalvdpgpDFVVCDEGHILKNEASAV 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477070 1417 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSRE 1481
Cdd:cd18068  175 SKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVD 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1266-1503 1.53e-24

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: 103.98  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------QEVYNVGIHG----PFLVIAPLSTITNWEREF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSreyLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1411
Cdd:cd18060   69 NTWTE---MNTIVYHGSLASRQMIQQYemyckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1412 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamda 1491
Cdd:cd18060  146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLKTEEQVQK-------- 210
                        250
                 ....*....|..
gi 27477070 1492 LHRQVLPFLLRR 1503
Cdd:cd18060  211 LQAILKPMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
1265-1459 8.09e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 8.09e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    1265 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhchrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 1343
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    1344 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 1418
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 27477070    1419 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 1459
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1266-1466 5.87e-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: 99.34  E-value: 5.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILAgdhchraQEYARSklaecMPLPSLVVCPPTLTGHWVDE 1344
Cdd:cd18059    1 LREYQLEGVNWLLF-NWYNTRNcILADEMGLGKTIQSITFLY-------EIYLKG-----IHGPFLVIAPLSTIPNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 vgkFCSREYLNPLHYTGPPTERIRLQ--------------HQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1410
Cdd:cd18059   68 ---FRTWTELNVVVYHGSQASRRTIQlyemyfkdpqgrviKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLK 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 27477070 1411 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1466
Cdd:cd18059  145 NRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG 200
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1266-1466 4.06e-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: 97.03  E-value: 4.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraQEYARSklaecMPLPSLVVCPPTLTGHWVDEv 1345
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-------EIFLMG-----IRGPFLIIAPLSTITNWERE- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1411
Cdd:cd18058   68 --FRTWTEMNAIVYHGSQISRQMIQQYemyyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27477070 1412 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1466
Cdd:cd18058  146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1645-1744 1.91e-21

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: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070   1645 HRILIFCQLKSMLDIvehDLLKpHLPSVTYLRLDGSIPPGQRHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFV 1724
Cdd:pfam00271   16 GKVLIFSQTKKTLEA---ELLL-EKEGIKVARLHGDLSQEEREEILEDFRKG-KIDVLV-ATDVAERGLDLPDVDLVINY 89
                           90       100
                   ....*....|....*....|
gi 27477070   1725 EHDWNPMRDLQAMDRAHRIG 1744
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1288-1470 9.14e-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: 9.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1288 ILCDDMGLGKTLQSICILagdhchraqeyarSKLAECMPLPS-LVVCPPTLTGHWVDEVGKFCSREYLNPLhyTGPPTER 1366
Cdd:cd18069   32 ILAHSMGLGKTLQVISFL-------------DVLLRHTGAKTvLAIVPVNTLQNWLSEFNKWLPPPEALPN--VRPRPFK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1367 IRLQHQVkrHNLIVASYDVVRN----------DIDFFRNIKF-NYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTP 1435
Cdd:cd18069   97 VFILNDE--HKTTAARAKVIEDwvkdggvllmGYEMFRLRPGpDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYP 174
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 27477070 1436 IQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1470
Cdd:cd18069  175 LQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1266-1466 2.52e-20

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: 91.61  E-value: 2.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEv 1345
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL--------YEILLTGIRG----PFLIIAPLSTIANWERE- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1411
Cdd:cd18061   68 --FRTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKN 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27477070 1412 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1466
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; ...
1266-1503 2.57e-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: 2.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 1345
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHSKG-PFLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLnpLHYTGppterirlqhqvkrHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1425
Cdd:cd17994   70 EMWAPDFYV--VTYVG--------------DHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKI 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477070 1426 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQeagvlaMDALHRQVLPFLLRR 1503
Cdd:cd17994  134 GYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF---------ADISKEDQ------IKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1266-1503 1.84e-18

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: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHTKG-PFLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKFCSREYLnpLHYTGPPTER-----------------------IRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCI 1402
Cdd:cd18055   70 QMWAPDFYV--VTYTGDKDSRaiirenefsfddnavkggkkafkMKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1403 LDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQ 1482
Cdd:cd18055  147 VDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ 217
                        250       260
                 ....*....|....*....|.
gi 27477070 1483 eagvlaMDALHRQVLPFLLRR 1503
Cdd:cd18055  218 ------IKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1266-1503 5.13e-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: 5.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcHRAQEYARSKlaecmpLPSLVVCPPTLTGHWVDE- 1344
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFL-----YSLYKEGHSK------GPYLVSAPLSTIINWEREf 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 ------------VGKFCSREYLNPLHY--------TGPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILD 1404
Cdd:cd18057   70 emwapdfyvvtyTGDKESRSVIRENEFsfednairSGKKVFRMKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1405 EGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQea 1484
Cdd:cd18057  149 EAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ-- 217
                        250
                 ....*....|....*....
gi 27477070 1485 gvlaMDALHRQVLPFLLRR 1503
Cdd:cd18057  218 ----IKKLHDLLGPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
1658-1744 1.15e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.18  E-value: 1.15e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070    1658 DIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSidVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAM 1737
Cdd:smart00490    1 EELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75

                    ....*..
gi 27477070    1738 DRAHRIG 1744
Cdd:smart00490   76 GRAGRAG 82
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1266-1452 1.90e-17

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: 83.58  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdHCHRAQEYARSKLAECMPLPSLV-------VCPPTLt 1338
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFL---YSLYKEGHSKGPFLVSAPLSTIInwerefeMWAPDM- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1339 gHWVDEVGKFCSREYLNPLHYT--------GPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1410
Cdd:cd18056   77 -YVVTYVGDKDSRAIIRENEFSfednairgGKKASRMKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLK 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 27477070 1411 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1452
Cdd:cd18056  155 NNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1266-1454 4.09e-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: 76.17  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVnwLAFLNKYKLHGILCDDMGLGKTLQSICIlagdhchrAQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 1345
Cdd:cd18011    1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLI--------IKELLLRGDAK----RVLILCPASLVEQWQDEL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1346 GKfcsREYLNPLHYTGPPTERIRLQHQV--KRHNLIVASYDVVRNDI---DFFRNIKFNYCILDEGHVIKNG----KTKL 1416
Cdd:cd18011   67 QD---KFGLPFLILDRETAAQLRRLIGNpfEEFPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEAHKLRNSgggkETKR 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 27477070 1417 SKAVKQLTAN--YRIILSGTPIQNNVLELWSLFDFLMPGF 1454
Cdd:cd18011  144 YKLGRLLAKRarHVLLLTATPHNGKEEDFRALLSLLDPGR 183
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1266-1435 1.17e-08

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: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGV-NWLAFLNKYklHGILCDDMGLGKTLQSICILAgdhchraqeyarsklaECMPLPSLVVCPPT-LTGHWVD 1343
Cdd:cd17926    1 LRPYQEEALeAWLAHKNNR--RGILVLPTGSGKTLTALALIA----------------YLKELRTLIVVPTDaLLDQWKE 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1344 EVGKFCSREYLNPLhyTGPPTERIRLQhqvkrhNLIVASYDVVRNDI----DFFRniKFNYCILDEGHVIkNGKTkLSKA 1419
Cdd:cd17926   63 RFEDFLGDSSIGLI--GGGKKKDFDDA------NVVVATYQSLSNLAeeekDLFD--QFGLLIVDEAHHL-PAKT-FSEI 130
                        170
                 ....*....|....*.
gi 27477070 1420 VKQLTANYRIILSGTP 1435
Cdd:cd17926  131 LKELNAKYRLGLTATP 146
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1266-1469 2.24e-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: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1266 LRKYQQDGVNwlaFLNKYKLHGILCDdMGLGKTLQSICILAGDHchraqeyarsklAECMPLPSLVVCPPTLTGH-WVDE 1344
Cdd:cd18013    1 PHPYQKVAIN---FIIEHPYCGLFLD-MGLGKTVTTLTALSDLQ------------LDDFTRRVLVIAPLRVARStWPDE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1345 VGKFcsrEYLNPLHY---TGPPTERIRLQHqvKRHNLIVASYDVVrNDIDFFRNIKFNY--CILDEGHVIKNGKTKLSKA 1419
Cdd:cd18013   65 VEKW---NHLRNLTVsvaVGTERQRSKAAN--TPADLYVINRENL-KWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKA 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 27477070 1420 VKQL--TANYRIILSGTPIQNNVLELWSLFDFLMPGflgtER------QFAARYGKPI 1469
Cdd:cd18013  139 LRKVrpVIKRLIGLTGTPSPNGLMDLWAQIALLDQG----ERlgrsitAYRERWFDPD 192
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
1601-1762 7.94e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.43  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1601 AVQNSSLHDIQHaPKLSALKQLLldcglgnGSTSESGTESvvaqhRILIFCQLKSMLD-IVEHdLLKPHLPSVTYLrldg 1679
Cdd:COG1111  323 AMRLAEEADIEH-PKLSKLREIL-------KEQLGTNPDS-----RIIVFTQYRDTAEmIVEF-LSEPGIKAGRFV---- 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1680 sippGQ-------------RHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQK 1746
Cdd:COG1111  385 ----GQaskegdkgltqkeQIEILERFRAG-EFNVLV-ATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREG 458
                        170
                 ....*....|....*.
gi 27477070 1747 RVVnVyrLITRGTLEE 1762
Cdd:COG1111  459 RVV-V--LIAKGTRDE 471
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1265-1435 1.19e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 50.02  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1265 ELRKYQQDGVN-WLAFLNKYKLHGILCDDMGLGKTLqsicILAGDhchrAQEYARSKLAecmplpsLVVCP-PTLTGHWV 1342
Cdd:COG1061   80 ELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV----LALAL----AAELLRGKRV-------LVLVPrRELLEQWA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070 1343 DEVgkfcsREYLNPLHYTGPPTERirlqhqvkRHNLIVASYDVVRND--IDFFRNiKFNYCILDEGHVIknGKTKLSKAV 1420
Cdd:COG1061  145 EEL-----RRFLGDPLAGGGKKDS--------DAPITVATYQSLARRahLDELGD-RFGLVIIDEAHHA--GAPSYRRIL 208
                        170
                 ....*....|....*
gi 27477070 1421 KQLTANYRIILSGTP 1435
Cdd:COG1061  209 EAFPAAYRLGLTATP 223
HEAT COG1413
HEAT repeat [General function prediction only];
340-454 6.41e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 44.62  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  340 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 408
Cdd:COG1413   28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 27477070  409 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 454
Cdd:COG1413   98 AA----EALGRLGD------PAAVPALLEALKDPDWEVRRAAARAL 133
HEAT COG1413
HEAT repeat [General function prediction only];
344-454 8.21e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 41.54  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477070  344 IRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHGGLlg 412
Cdd:COG1413    1 VRRAAARALGRLGD---PAAVPAliaaladedpdVRAAAARALG-------RLGDPRAVPALLEALKDPDPEVRAAAA-- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 27477070  413 ikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 454
Cdd:COG1413   69 --EALGRIGD------PEAVPALIAALKDEDPEVRRAAAEAL 102
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1702-1746 3.19e-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: 3.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 27477070 1702 LLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQK 1746
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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