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Conserved domains on  [gi|767964209|ref|XP_011538630|]
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TATA-binding protein-associated factor 172 isoform X4 [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, ...
1075-1624 6.34e-156

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 492.82  E-value: 6.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1075 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1154
Cdd:COG0553   211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1155 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1234
Cdd:COG0553   282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1235 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1314
Cdd:COG0553   352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1315 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1394
Cdd:COG0553   432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1395 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1474
Cdd:COG0553   487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1475 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1554
Cdd:COG0553   543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1555 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1624
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
430-895 2.42e-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: 2.42e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   430 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 494
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   495 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 573
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   574 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 642
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   643 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 710
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   711 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 789
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   790 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 869
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 767964209   870 GAEFALTTIVKHFGGEMAVKLPHLWD 895
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
HEAT COG1413
HEAT repeat [General function prediction only];
184-298 3.80e-05

HEAT repeat [General function prediction only];


:

Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.00  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  184 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 252
Cdd:COG1413    28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767964209  253 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 298
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, ...
1075-1624 6.34e-156

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 492.82  E-value: 6.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1075 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1154
Cdd:COG0553   211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1155 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1234
Cdd:COG0553   282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1235 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1314
Cdd:COG0553   352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1315 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1394
Cdd:COG0553   432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1395 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1474
Cdd:COG0553   487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1475 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1554
Cdd:COG0553   543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1555 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1624
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1110-1347 7.76e-154

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: 7.76e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1269
Cdd:cd17999    75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964209 1270 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 1347
Cdd:cd17999   155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
430-895 2.42e-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: 2.42e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   430 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 494
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   495 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 573
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   574 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 642
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   643 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 710
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   711 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 789
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   790 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 869
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 767964209   870 GAEFALTTIVKHFGGEMAVKLPHLWD 895
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1103-1641 1.20e-82

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 295.56  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1103 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLT 1182
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1183 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 1254
Cdd:PLN03142  232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1255 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 1334
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1335 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDETVSSAtlseetEKPKLkatghVFQ 1414
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLDVVNAGG------ERKRL-----LNI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1415 ALQyLRKLCNHPALVLTPQ-HPEFkTTAEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGSTSESgtesvvaqhRILI 1493
Cdd:PLN03142  438 AMQ-LRKCCNHPYLFQGAEpGPPY-TTGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVLI 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1494 FCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHDW 1572
Cdd:PLN03142  493 FSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964209 1573 NPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDL 1641
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 ...
1113-1429 5.99e-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: 5.99e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1113 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAgdHCHRAQEYARSklaecmplPSLVVCPPTLTGHWVDEVGK 1191
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL--YLKHVDKNWGG--------PTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1192 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1268
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1269 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 1348
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1349 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDeTVSSATLSEETEKpklkatgHVFQALQYLRKLCNHPAL 1428
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLN-AIKTGEGGREIKA-------SLLNILMRLRKICNHPGL 288

                   .
gi 767964209  1429 V 1429
Cdd:pfam00176  289 I 289
DEXDc smart00487
DEAD-like helicases superfamily;
1109-1303 8.25e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 8.25e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   1109 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhchrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 1187
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   1188 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 1262
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 767964209   1263 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 1303
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
HEAT COG1413
HEAT repeat [General function prediction only];
184-298 3.80e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.00  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  184 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 252
Cdd:COG1413    28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767964209  253 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 298
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, ...
1075-1624 6.34e-156

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 492.82  E-value: 6.34e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1075 AELIQLKAKERHFLEQLldgkKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhc 1154
Cdd:COG0553   211 LELLAEAAVDAFRLRRL----REALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALL----- 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1155 hraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEVGKFCSReyLNPLHYTGPpTERIRLQHQVKRHNLIVASYDVVRNDI 1234
Cdd:COG0553   282 ---LELKERGLAR----PVLIVAPTSLVGNWQRELAKFAPG--LRVLVLDGT-RERAKGANPFEDADLVITSYGLLRRDI 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1235 DFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1314
Cdd:COG0553   352 ELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIE 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1315 ASRDArsssreqeagvlAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEdfaksrakcdvdeTVSS 1394
Cdd:COG0553   432 KGDEE------------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYE-------------AVLE 486
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1395 ATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLtpqhpefkttAEKLAVQNSSlhdiqhaPKLSALKQLLldcglgn 1474
Cdd:COG0553   487 YLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL----------EEGAELSGRS-------AKLEALLELL------- 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1475 gstsesgTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGG 1554
Cdd:COG0553   543 -------EELLAEGEKVLVFSQFTDTLDLLEERLEERGIE---YAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1555 LGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVIS 1624
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1110-1347 7.76e-154

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: 7.76e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYarsklaECMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF------NSENLPSLVVCPPTLVGHWVAEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1269
Cdd:cd17999    75 KKYFPNAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964209 1270 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRR 1347
Cdd:cd17999   155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
430-895 2.42e-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: 2.42e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   430 VWMELLSKA-SVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLE--------------VKARAKEKTGGKVRQGQSQNK 494
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKpsgqpyspperrksKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   495 -EVLQEYIAGADTIMEDPatrdfVVMRARMMAAKLLGALCCCIcdpgvnvvtQEIKPAESLGQLLLFHLNSKSALQRISV 573
Cdd:pfam12054   81 hNVDKPMIGGDVTLVGMD-----VVIRTRIAAAKALGLLLSYW---------PEESPLDFFTKLLLPYLNSPSALQRLLA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   574 ALVICEWAALQK-----ECKAVTLAVQPRLLDIL---SEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNN--- 642
Cdd:pfam12054  147 AIIIEEWAKNCKkekssSVSTLPETLSEKLLEILenpSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKlav 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   643 ----------NVLTIDQASDLVTTVFNEATSSFDLNPQVL--QQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVS 710
Cdd:pfam12054  227 vvqgepeagpGAFSIEQAEKLVGEDYDKLKKSLSPKQKLLalQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVA 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   711 LQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTR-TPCPNSKIIKNLCSSLCVDPYLTPCVtcpvptqs 789
Cdd:pfam12054  307 LKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSETPEF-------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   790 gqenskgstsekdgmHHTVTKHRGIITLYRHQKAAFAITSrrgptpkavkaqiadlpagssgnilVELDEAQKPYLVQRR 869
Cdd:pfam12054  379 ---------------HPNAKLTDGILTLRKEEDKADHADA-------------------------AKFEEEAKEARIQRR 418
                          490       500
                   ....*....|....*....|....*.
gi 767964209   870 GAEFALTTIVKHFGGEMAVKLPHLWD 895
Cdd:pfam12054  419 GAKLALEQLAKKFGASLFEKVPKLWE 444
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1106-1349 3.99e-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: 274.83  E-value: 3.99e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1106 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhCHRAQEYarsklaecMPLPSLVVCPPTLTGHW 1185
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALL----LSRKEEG--------RKGPSLVVAPTSLIYNW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1186 VDEVGKFCSReyLNPLHYTGPPTERiRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVK 1265
Cdd:cd18012    69 EEEAAKFAPE--LKVLVIHGTKRKR-EKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1266 QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARsssreqeagvlAMDALHRQVLPFLL 1345
Cdd:cd18012   146 ALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFIL 214

                  ....
gi 767964209 1346 RRMK 1349
Cdd:cd18012   215 RRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1103-1641 1.20e-82

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 295.56  E-value: 1.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1103 PVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLT 1182
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRG-----------ITGPHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1183 GHWVDEVGKFCSreYLNPLHYTGPPTERirlQHQvkRHNLIVA--------SYDVVRNDIDFFRNIKFNYCILDEGHVIK 1254
Cdd:PLN03142  232 GNWMNEIRRFCP--VLRAVKFHGNPEER---AHQ--REELLVAgkfdvcvtSFEMAIKEKTALKRFSWRYIIIDEAHRIK 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1255 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrdarSSSREQEAGVLAMd 1334
Cdd:PLN03142  305 NENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----------ISGENDQQEVVQQ- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1335 aLHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYedfaKSRAKCDVDETVSSAtlseetEKPKLkatghVFQ 1414
Cdd:PLN03142  374 -LHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY----KALLQKDLDVVNAGG------ERKRL-----LNI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1415 ALQyLRKLCNHPALVLTPQ-HPEFkTTAEKLaVQNSSlhdiqhapklsalKQLLLDCGLGNGSTSESgtesvvaqhRILI 1493
Cdd:PLN03142  438 AMQ-LRKCCNHPYLFQGAEpGPPY-TTGEHL-VENSG-------------KMVLLDKLLPKLKERDS---------RVLI 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1494 FCQLKSMLDIVEHDLLkphLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSID-VLLLTTHVGGLGLNLTGADTVVFVEHDW 1572
Cdd:PLN03142  493 FSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDW 569
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964209 1573 NPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQ----ENSSLqsmGTDQLLDL 1641
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 ...
1113-1429 5.99e-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: 5.99e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1113 YQQDGVNWLAFL-NKYKLHGILCDDMGLGKTLQSICILAgdHCHRAQEYARSklaecmplPSLVVCPPTLTGHWVDEVGK 1191
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL--YLKHVDKNWGG--------PTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1192 FCSREYLNPLHYTGPPTERIRLQHQVKR---HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1268
Cdd:pfam00176   71 WVSPPALRVVVLHGNKRPQERWKNDPNFladFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1269 ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSReqeagvlamdaLHRQVLPFLLRRM 1348
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1349 KEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRakcDVDeTVSSATLSEETEKpklkatgHVFQALQYLRKLCNHPAL 1428
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKK---DLN-AIKTGEGGREIKA-------SLLNILMRLRKICNHPGL 288

                   .
gi 767964209  1429 V 1429
Cdd:pfam00176  289 I 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1110-1299 6.34e-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: 6.34e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQeyarsklaecmPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE-----------RGPVLVVCPLSVLENWEREF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTERIRLQHQ--VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQL 1267
Cdd:cd17919    70 EKWTPD--LRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKAL 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767964209 1268 TANYRIILSGTPIQNNVLELWSLFDFLMPGFL 1299
Cdd:cd17919   148 RAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1110-1347 1.04e-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: 1.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHchraqeyaRSKLAEcmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF--------DSGLIK----SVLVVMPTSLIPHWVKEF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLNpLHYTGPPTERIRLQHQVKR-HNLIVASYDVVRNDIDFF-----RNIKFNYCILDEGHVIKNGKTKLSKA 1263
Cdd:cd18001    69 AKWTPGLRVK-VFHGTSKKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1264 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPG-FLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLP 1342
Cdd:cd18001   148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                  ....*
gi 767964209 1343 FLLRR 1347
Cdd:cd18001   228 YFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1450-1599 1.97e-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: 183.45  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1450 SLHDIQHAPKLSALKQLLLDCGLGNgstsesgtesvvaqHRILIFCQLKSMLDIVEHDLLKPHlpsVTYLRLDGSIPPGQ 1529
Cdd:cd18793     3 PKIEEVVSGKLEALLELLEELREPG--------------EKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKE 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1530 RHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLI 1599
Cdd:cd18793    66 RQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1110-1349 1.66e-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: 1.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeyarsklaeCM-----PLPSLVVCPPTLTGH 1184
Cdd:cd18009     4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA-----------------HLrergvWGPFLVIAPLSTLPN 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1185 WVDEVGKFCSReyLNPLHYTGPPTERIRLQHQVKRHN-------LIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGK 1257
Cdd:cd18009    67 WVNEFARFTPS--VPVLLYHGTKEERERLRKKIMKREgtlqdfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1258 TKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQEAGVLAMda 1335
Cdd:cd18009   145 CRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNaaDISNLSEEREQNIVHM-- 222
                         250
                  ....*....|....
gi 767964209 1336 LHRQVLPFLLRRMK 1349
Cdd:cd18009   223 LHAILKPFLLRRLK 236
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1110-1347 2.08e-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: 2.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILA---------GDHCHRAQEYARSKLAECMPLPSLVVCPPT 1180
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrRDRENNRPRFKKKPPASSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1181 LTGHWVDEVGKFcsrEYLNPLHYTGPPTERIrLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 1258
Cdd:cd18005    81 VLYNWKDELDTW---GHFEVGVYHGSRKDDE-LEGRLKagRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1259 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHR 1338
Cdd:cd18005   157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAV 236

                  ....*....
gi 767964209 1339 QVLPFLLRR 1347
Cdd:cd18005   237 KLSKFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1110-1299 8.73e-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: 8.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHChrAQEYARsklaecmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH--SKLGLG---------PSLIVCPATVLKQWVKEF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLNPLHYTGPPT-----------ERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKT 1258
Cdd:cd18000    70 HRWWPPFRVVVLHSSGSGTgseeklgsierKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767964209 1259 KLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFL 1299
Cdd:cd18000   150 EITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1110-1347 1.42e-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: 173.63  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICILAGdhCHRAQEYARSKLAECmplpsLVVCPPTLTGH 1184
Cdd:cd18004     1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWT--LLKQGPYGKPTAKKA-----LIVCPSSLVGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1185 WVDEVGKFCSREYLNPLHYTGPPTERIRLQHQV---KRHNLIVASYDVVRNDID-FFRNIKFNYCILDEGHVIKNGKTKL 1260
Cdd:cd18004    74 WKAEFDKWLGLRRIKVVTADGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1261 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 1340
Cdd:cd18004   154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                  ....*..
gi 767964209 1341 LPFLLRR 1347
Cdd:cd18004   234 SRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1110-1347 2.07e-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: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLaflnkykLH--GILCDDMGLGKTLQSI-CILAGDHCHRAQEY---ARSKLAECMPLPS--LVVCPPTL 1181
Cdd:cd18008     1 LLPYQKQGLAWM-------LPrgGILADEMGLGKTIQALaLILATRPQDPKIPEeleENSSDPKKLYLSKttLIVVPLSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1182 TGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFF----------------RNIKFNYC 1245
Cdd:cd18008    74 LSQWKDEIEKHTKPGSLKVYVYHGS--KRIKSIEELSDYDIVITTYGTLASEFPKNkkgggrdskekeasplHRIRWYRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1246 ILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDArsssre 1325
Cdd:cd18008   152 ILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK------ 225
                         250       260
                  ....*....|....*....|..
gi 767964209 1326 qeagvlAMDALHRQVLPFLLRR 1347
Cdd:cd18008   226 ------ALERLQALLKPILLRR 241
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1110-1347 5.05e-45

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


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 162.91  E-value: 5.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRaQEYArsklaecmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK-GNWG----------PHLIVVPTSVMLNWEMEF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTERIRlqhqvKRH--------NLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 1261
Cdd:cd18003    70 KRWCPG--FKILTYYGSAKERKL-----KRQgwmkpnsfHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRW 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1262 KAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIlasrDARSSSREQEAGVLaMDALHRQVL 1341
Cdd:cd18003   143 QTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL----TAMSEGSQEENEEL-VRRLHKVLR 217

                  ....*.
gi 767964209 1342 PFLLRR 1347
Cdd:cd18003   218 PFLLRR 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1110-1296 5.30e-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: 5.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcHRAQEyarsklaeCMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA----YLKEI--------GIPGPHLVVVPSSTLDNWLREF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTERIRLQHQVKR----HNLIVASYDVV---RNDIDFFRNIKFNYCILDEGHVIKNGKTKLSK 1262
Cdd:cd17998    69 KRWCPS--LKVEPYYGSQEERKHLRYDILKgledFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYR 146
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767964209 1263 AVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1296
Cdd:cd17998   147 HLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1110-1347 1.61e-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: 1.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhcHRAQEYArsklaecMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLA----HLAEEHN-------IWGPFLVIAPASTLHNWQQEI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTERIRLQHQVKRHNL---------IVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKL 1260
Cdd:cd18002    70 SRFVPQ--FKVLPYWGNPKDRKVLRKFWDRKNLytrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1261 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEagvlaMDALHRQV 1340
Cdd:cd18002   148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHMIL 222

                  ....*..
gi 767964209 1341 LPFLLRR 1347
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; ...
1110-1347 1.81e-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: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILagDHCHraqeyarskLAECMPLPSLVVCPPTLTGHWVDE 1188
Cdd:cd17995     1 LRDYQLEGVNWLLF-NWYNRRNcILADEMGLGKTIQSIAFL--EHLY---------QVEGIRGPFLVIAPLSTIPNWQRE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 VGKFCSreyLNPLHYTGPPTER-IRLQHQ-------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1254
Cdd:cd17995    69 FETWTD---MNVVVYHGSGESRqIIQQYEmyfkdaqgrkkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1255 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamd 1334
Cdd:cd17995   146 NRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-------DLKTAEQVEK------- 211
                         250
                  ....*....|...
gi 767964209 1335 aLHRQVLPFLLRR 1347
Cdd:cd17995   212 -LQALLKPYMLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1107-1349 5.26e-41

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 151.32  E-value: 5.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1107 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYArsKLAECMPLPSLVVCPPTLTGHWV 1186
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG---------YL--KHYKNINGPHLIIVPKSTLDNWM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1187 DEVGKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1263
Cdd:cd17997    70 REFKRWCPS--LRVVVLIGDKEERadiIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1264 VKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilaSRDARSSSREQeagvlAMDALHRQVLPF 1343
Cdd:cd17997   148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF------NVNNCDDDNQE-----VVQRLHKVLRPF 216

                  ....*.
gi 767964209 1344 LLRRMK 1349
Cdd:cd17997   217 LLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1107-1349 7.37e-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: 7.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1107 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYarskLAECMPL--PSLVVCP-PTLTG 1183
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLIT---------Y----LMEKKKNngPYLVIVPlSTLSN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1184 hWVDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLS 1261
Cdd:cd17996    68 -WVSEFEKWAPS--VSKIVYKGTPDVRKKLQSQIRagKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1262 KAVKQ-LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQV 1340
Cdd:cd17996   145 QTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVL 224

                  ....*....
gi 767964209 1341 LPFLLRRMK 1349
Cdd:cd17996   225 RPFLLRRLK 233
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1110-1347 1.09e-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: 149.90  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraqeYARSKLAecMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW---------YLAGRLK--LLGPFLVLCPLSVLDNWKEEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTERIRLQHQVK---RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 1266
Cdd:cd18006    70 NRFAPD--LSVITYMGDKEKRLDLQQDIKstnRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1267 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTER--QFAARYgkpilasrdarsssREQEAGVLAMDALHRQVLPFL 1344
Cdd:cd18006   148 FSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAY--------------SETDDESETVEELHLLLQPFL 213

                  ...
gi 767964209 1345 LRR 1347
Cdd:cd18006   214 LRR 216
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1109-1347 1.88e-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: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1109 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHcHRAQEYArsklaecmplPSLVVCPPTLTGHWVDE 1188
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLF-HSQQQYG----------PFLVVVPLSTMPAWQRE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 VGKFCSReyLNPLHYTGPPTER--IR----LQHQVKR--HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKL 1260
Cdd:cd17993    70 FAKWAPD--MNVIVYLGDIKSRdtIReyefYFSQTKKlkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1261 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarsssrEQEAGVlamDALHRQV 1340
Cdd:cd17993   148 YEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDE-------------EQEKGI---ADLHKEL 211

                  ....*..
gi 767964209 1341 LPFLLRR 1347
Cdd:cd17993   212 EPFILRR 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1108-1359 4.96e-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: 4.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1108 AELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLTGHWVD 1187
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRN-----------IPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1188 EVGKFCSReyLNPLHYTGPPTERIRLQHQV---KRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAV 1264
Cdd:cd18064    83 EFKRWVPT--LRAVCLIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1265 KQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFL 1344
Cdd:cd18064   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTNNCLGDQK----LVERLHMVLRPFL 228
                         250
                  ....*....|....*
gi 767964209 1345 LRRMKEDVLQDLPPK 1359
Cdd:cd18064   229 LRRIKADVEKSLPPK 243
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1106-1349 4.92e-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: 129.41  E-value: 4.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1106 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchRAQEYARsklaecMPLPSLVVCPPTLTGHW 1185
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------LNGPYLIIVPLSTLSNW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1186 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1263
Cdd:cd18063    89 TYEFDKWAPS--VVKISYKGTPAMRRSLVPQLRsgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1264 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPiLASRDARSSSREQEAgVLAMDALHRQVLP 1342
Cdd:cd18063   167 LNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP-FAMTGERVDLNEEET-ILIIRRLHKVLRP 244

                  ....*..
gi 767964209 1343 FLLRRMK 1349
Cdd:cd18063   245 FLLRRLK 251
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1110-1347 8.38e-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: 8.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWL----AFLNKYKLHG-ILCDDMGLGKTLQSICIL-----AGDHCHRAQEYArsklaecmplpsLVVCPP 1179
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMwtllrQSPQCKPEIDKA------------IVVSPS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1180 TLTGHWVDEVGKFCSREyLNPLHYTGPPTERIRLQ---------HQVKRHNLIVaSYDVVRNDIDFFRNIKFNYCILDEG 1250
Cdd:cd18067    69 SLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKlvqwasqqgRRVSTPVLII-SYETFRLHVEVLQKGEVGLVICDEG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1251 HVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGV 1330
Cdd:cd18067   147 HRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGE 226
                         250
                  ....*....|....*..
gi 767964209 1331 LAMDALHRQVLPFLLRR 1347
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 ...
1132-1327 2.52e-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: 2.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1132 ILCDDMGLGKTLQSICILagdhchraQEYARSKLAECMPLpslVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERI 1211
Cdd:cd18007    30 ILAHTMGLGKTLQVITFL--------HTYLAAAPRRSRPL---VLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1212 RLQHQV------KRHNLIVASYDVVRNDI-----------DFFRNIKFNYC---ILDEGHVIKNGKTKLSKAVKQLTANY 1271
Cdd:cd18007    99 ADARLRkinkwhKEGGVLLIGYELFRNLAsnattdprlkqEFIAALLDPGPdllVLDEGHRLKNEKSQLSKALSKVKTKR 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964209 1272 RIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQE 1327
Cdd:cd18007   179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVR 234
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1106-1349 9.01e-32

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


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 125.54  E-value: 9.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1106 INAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchRAQEYARsklaecMPLPSLVVCPPTLTGHW 1185
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----YLMEHKR------INGPFLIIVPLSTLSNW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1186 VDEVGKFCSReyLNPLHYTGPPTERIRLQHQVK--RHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKA 1263
Cdd:cd18062    89 VYEFDKWAPS--VVKVSYKGSPAARRAFVPQLRsgKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1264 VK-QLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASrdARSSSREQEAGVLAMDALHRQVLP 1342
Cdd:cd18062   167 LNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GEKVDLNEEETILIIRRLHKVLRP 244

                  ....*..
gi 767964209 1343 FLLRRMK 1349
Cdd:cd18062   245 FLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1110-1349 1.31e-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: 1.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAqeyarsklaecMPLPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRN-----------IPGPHMVLVPKSTLHNWMNEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSReyLNPLHYTGPPTER---IRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQ 1266
Cdd:cd18065    85 KRWVPS--LRAVCLIGDKDARaafIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVRE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1267 LTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrDARSSSREQEagvlAMDALHRQVLPFLLR 1346
Cdd:cd18065   163 FKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVLKPFLLR 230

                  ...
gi 767964209 1347 RMK 1349
Cdd:cd18065   231 RIK 233
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1110-1327 1.73e-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: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWlAFLNKYKLhgILCDDMGLGKTLQSICILagdHCHRAqEYarsklaecmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18010     1 LLPFQREGVCF-ALRRGGRV--LIADEMGLGKTVQAIAIA---AYYRE-EW-----------PLLIVCPSSLRLTWADEI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLNPLHYTGPPTERIR-LQHQVkrhnLIVaSYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLT 1268
Cdd:cd18010    63 ERWLPSLPPDDIQVIVKSKDGLRdGDAKV----VIV-SYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLL 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964209 1269 --ANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASR--DARSSSREQE 1327
Cdd:cd18010   138 krAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFgwDYSGSSNLEE 200
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1110-1294 2.64e-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: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHG-ILCDDMGLGKTLQSIC-ILAGDHCHRAQEYAR--------SKLAECMpLPS---LVV 1176
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIAlILAQKNTQNRKEEEKekalteweSKKDSTL-VPSagtLVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1177 CPPTLTGHWVDEVGKFCSREYLNPLHYTGPptERIRLQHQVKRHNLIVASYDVVRNDIDFFRN---------IKFNYCIL 1247
Cdd:cd18072    80 CPASLVHQWKNEVESRVASNKLRVCLYHGP--NRERIGEVLRDYDIVITTYSLVAKEIPTYKEesrssplfrIAWARIIL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767964209 1248 DEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFL 1294
Cdd:cd18072   158 DEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1107-1347 4.32e-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: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1107 NAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHcHRAQEYArsklaecmplPSLVVCPPTLTGHWV 1186
Cdd:cd18054    18 NLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLF-HQHQLYG----------PFLLVVPLSTLTSWQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1187 DE-------------VGKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 1253
Cdd:cd18054    87 REfeiwapeinvvvyIGDLMSRNTIREYEWIHSQTKRLKF-------NALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1254 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilasrdarssSREQeagvlAM 1333
Cdd:cd18054   160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK-----------GREN-----GY 223
                         250
                  ....*....|....
gi 767964209 1334 DALHRQVLPFLLRR 1347
Cdd:cd18054   224 QSLHKVLEPFLLRR 237
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1110-1347 6.23e-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: 122.65  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLH-----GILCDDMGLGKTLQSICILAGDHCHraQEYARSKLAEcmplPSLVVCPPTLTGH 1184
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMRVnerfgAILADEMGLGKTLQCISLIWTLLRQ--GPYGGKPVIK----RALIVTPGSLVKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1185 WVDEVGKFCSREylnplhytgppteRIRL-----QHQVKR------HNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVI 1253
Cdd:cd18066    75 WKKEFQKWLGSE-------------RIKVftvdqDHKVEEfiasplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1254 KNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAM 1333
Cdd:cd18066   142 KNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARA 221
                         250
                  ....*....|....
gi 767964209 1334 DALHRQVLPFLLRR 1347
Cdd:cd18066   222 AELTRLTGLFILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1131-1347 1.03e-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: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1131 GILCDDMGLGKTLQSICILAGDhchraqeyarsklaecmplPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPptER 1210
Cdd:cd18071    51 GILADDMGLGKTLTTISLILAN-------------------FTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGG--ER 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1211 IRLQHQVKRHNLIVASYDVVRNDIDF-----FRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVL 1285
Cdd:cd18071   110 NRDPKLLSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964209 1286 ELWSLFDFLMPGFLGTERQFAARYGKPIlasrdarssSREQEAGVLAMDALHRQVlpfLLRR 1347
Cdd:cd18071   190 DLGSLLSFLHLKPFSNPEYWRRLIQRPL---------TMGDPTGLKRLQVLMKQI---TLRR 239
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1109-1347 1.63e-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: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1109 ELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILaGDHCHRAQEYArsklaecmplPSLVVCPPTLTGHWVDE 1188
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL-NYLFHEHQLYG----------PFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 V-------------GKFCSREYLNPLHYTGPPTERIRLqhqvkrhNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1255
Cdd:cd18053    89 IqtwapqmnavvylGDINSRNMIRTHEWMHPQTKRLKF-------NILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1256 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKpilaSRDARSSSreqeagvlamda 1335
Cdd:cd18053   162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GREYGYAS------------ 225
                         250
                  ....*....|..
gi 767964209 1336 LHRQVLPFLLRR 1347
Cdd:cd18053   226 LHKELEPFLLRR 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1110-1296 1.01e-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: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNkyklhGILCDDMGLGKTLQSI-CILAgdhcHRAQE------YARSKLAECMPLP---------- 1172
Cdd:cd18070     1 LLPYQRRAVNWMLVPG-----GILADEMGLGKTVEVLaLILL----HPRPDndldaaDDDSDEMVCCPDClvaetpvssk 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1173 -SLVVCPPTLTGHWVDEVGKFcSREYLNPLHYTGPPTE---RIRLQHQVKRHNLIVASYDVVRNDIDF---FRN------ 1239
Cdd:cd18070    72 aTLIVCPSAILAQWLDEINRH-VPSSLKVLTYQGVKKDgalASPAPEILAEYDIVVTTYDVLRTELHYaeaNRSnrrrrr 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1240 -------------IKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1296
Cdd:cd18070   151 qkryeappsplvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1131-1325 1.20e-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: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1131 GILCDDMGLGKTLQSICILagdH----CHRAQEYARSklaecmplpsLVVCPPTLTGHWVDEVGKFcsREYLNPLH---- 1202
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFL---HtvllCEKLENFSRV----------LVVCPLNTVLNWLNEFEKW--QEGLKDEEkiev 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1203 -----YTGPPTERIRLQHQVKRHNLIVASYDVVRNdIDFFRNIKF-----------------NYCILDEGHVIKNGKTKL 1260
Cdd:cd18068    96 nelatYKRPQERSYKLQRWQEEGGVMIIGYDMYRI-LAQERNVKSreklkeifnkalvdpgpDFVVCDEGHILKNEASAV 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964209 1261 SKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSRE 1325
Cdd:cd18068   175 SKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVD 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1110-1347 1.34e-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: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL--------QEVYNVGIHG----PFLVIAPLSTITNWEREF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSreyLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1255
Cdd:cd18060    69 NTWTE---MNTIVYHGSLASRQMIQQYemyckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1256 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGkpilasrDARSSSREQEagvlamda 1335
Cdd:cd18060   146 RNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLKTEEQVQK-------- 210
                         250
                  ....*....|..
gi 767964209 1336 LHRQVLPFLLRR 1347
Cdd:cd18060   211 LQAILKPMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
1109-1303 8.25e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 8.25e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   1109 ELRKYQQDGVNWLAFLNKyklHGILCDDMGLGKTLQsicilagdhchrAQEYARSKLAECMPLPSLVVCP-PTLTGHWVD 1187
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA------------ALLPALEALKRGKGGRVLVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   1188 EVGKFCSREYLNPLHYTGPPTERIRLQHQVKRH-NLIVASYDVVRNDI--DFFRNIKFNYCILDEGHVIKNG--KTKLSK 1262
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 767964209   1263 AVKQL-TANYRIILSGTP---IQNNVLELWSLFDFLMPGFLGTER 1303
Cdd:smart00487  153 LLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1110-1310 5.08e-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: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFlNKYKLHG-ILCDDMGLGKTLQSICILAgdhchraQEYARSklaecMPLPSLVVCPPTLTGHWVDE 1188
Cdd:cd18059     1 LREYQLEGVNWLLF-NWYNTRNcILADEMGLGKTIQSITFLY-------EIYLKG-----IHGPFLVIAPLSTIPNWERE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 vgkFCSREYLNPLHYTGPPTERIRLQ--------------HQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1254
Cdd:cd18059    68 ---FRTWTELNVVVYHGSQASRRTIQlyemyfkdpqgrviKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLK 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964209 1255 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1310
Cdd:cd18059   145 NRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG 200
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1110-1310 3.45e-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: 3.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAgdhchraQEYARSklaecMPLPSLVVCPPTLTGHWVDEv 1189
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-------EIFLMG-----IRGPFLIIAPLSTITNWERE- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1255
Cdd:cd18058    68 --FRTWTEMNAIVYHGSQISRQMIQQYemyyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767964209 1256 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1310
Cdd:cd18058   146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1489-1588 1.60e-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: 1.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  1489 HRILIFCQLKSMLDIvehDLLKpHLPSVTYLRLDGSIPPGQRHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFV 1568
Cdd:pfam00271   16 GKVLIFSQTKKTLEA---ELLL-EKEGIKVARLHGDLSQEEREEILEDFRKG-KIDVLV-ATDVAERGLDLPDVDLVINY 89
                           90       100
                   ....*....|....*....|
gi 767964209  1569 EHDWNPMRDLQAMDRAHRIG 1588
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1132-1314 8.30e-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: 8.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1132 ILCDDMGLGKTLQSICILagdhchraqeyarSKLAECMPLPS-LVVCPPTLTGHWVDEVGKFCSREYLNPLhyTGPPTER 1210
Cdd:cd18069    32 ILAHSMGLGKTLQVISFL-------------DVLLRHTGAKTvLAIVPVNTLQNWLSEFNKWLPPPEALPN--VRPRPFK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1211 IRLQHQVkrHNLIVASYDVVRN----------DIDFFRNIKF-NYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTP 1279
Cdd:cd18069    97 VFILNDE--HKTTAARAKVIEDwvkdggvllmGYEMFRLRPGpDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYP 174
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767964209 1280 IQNNVLELWSLFDFLMPGFLGTERQFAARYGKPIL 1314
Cdd:cd18069   175 LQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1110-1310 1.87e-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: 91.99  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraQEYARSKLAEcmplPSLVVCPPTLTGHWVDEv 1189
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL--------YEILLTGIRG----PFLIIAPLSTIANWERE- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 gkFCSREYLNPLHYTGPPTERIRLQHQ--------------VKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKN 1255
Cdd:cd18061    68 --FRTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKN 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767964209 1256 GKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYG 1310
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; ...
1110-1347 2.36e-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: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 1189
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHSKG-PFLVSAPLSTIINWEREF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLnpLHYTGppterirlqhqvkrHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTA 1269
Cdd:cd17994    70 EMWAPDFYV--VTYVG--------------DHVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKI 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964209 1270 NYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQeagvlaMDALHRQVLPFLLRR 1347
Cdd:cd17994   134 GYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF---------ADISKEDQ------IKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1110-1347 1.52e-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: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhchraqeYARSKLAECMPlPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFL----------YSLYKEGHTKG-PFLVSAPLSTIINWEREF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKFCSREYLnpLHYTGPPTER-----------------------IRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCI 1246
Cdd:cd18055    70 QMWAPDFYV--VTYTGDKDSRaiirenefsfddnavkggkkafkMKREAQVKFH-VLLTSYELVTIDQAALGSIRWACLV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1247 LDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQ 1326
Cdd:cd18055   147 VDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ 217
                         250       260
                  ....*....|....*....|.
gi 767964209 1327 eagvlaMDALHRQVLPFLLRR 1347
Cdd:cd18055   218 ------IKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1110-1347 4.57e-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: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdhcHRAQEYARSKlaecmpLPSLVVCPPTLTGHWVDE- 1188
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFL-----YSLYKEGHSK------GPYLVSAPLSTIINWEREf 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 ------------VGKFCSREYLNPLHY--------TGPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILD 1248
Cdd:cd18057    70 emwapdfyvvtyTGDKESRSVIRENEFsfednairSGKKVFRMKKEAQIKFH-VLLTSYELITIDQAILGSIEWACLVVD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1249 EGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYgkpilasrdARSSSREQea 1328
Cdd:cd18057   149 EAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ-- 217
                         250
                  ....*....|....*....
gi 767964209 1329 gvlaMDALHRQVLPFLLRR 1347
Cdd:cd18057   218 ----IKKLHDLLGPHMLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
1502-1588 9.55e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.56  E-value: 9.55e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209   1502 DIVEHDLLKPHLPsvtYLRLDGSIPPGQRHSIVSRFNNDPSidVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAM 1581
Cdd:smart00490    1 EELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75

                    ....*..
gi 767964209   1582 DRAHRIG 1588
Cdd:smart00490   76 GRAGRAG 82
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1110-1296 1.54e-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: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILagdHCHRAQEYARSKLAECMPLPSLV-------VCPPTLt 1182
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFL---YSLYKEGHSKGPFLVSAPLSTIInwerefeMWAPDM- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1183 gHWVDEVGKFCSREYLNPLHYT--------GPPTERIRLQHQVKRHnLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIK 1254
Cdd:cd18056    77 -YVVTYVGDKDSRAIIRENEFSfednairgGKKASRMKKEASVKFH-VLLTSYELITIDMAILGSIDWACLIVDEAHRLK 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767964209 1255 NGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMP 1296
Cdd:cd18056   155 NNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1110-1298 2.99e-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: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVnwLAFLNKYKLHGILCDDMGLGKTLQSICIlagdhchrAQEYARSKLAEcmplPSLVVCPPTLTGHWVDEV 1189
Cdd:cd18011     1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLI--------IKELLLRGDAK----RVLILCPASLVEQWQDEL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1190 GKfcsREYLNPLHYTGPPTERIRLQHQV--KRHNLIVASYDVVRNDI---DFFRNIKFNYCILDEGHVIKNG----KTKL 1260
Cdd:cd18011    67 QD---KFGLPFLILDRETAAQLRRLIGNpfEEFPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEAHKLRNSgggkETKR 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767964209 1261 SKAVKQLTAN--YRIILSGTPIQNNVLELWSLFDFLMPGF 1298
Cdd:cd18011   144 YKLGRLLAKRarHVLLLTATPHNGKEEDFRALLSLLDPGR 183
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1110-1279 1.06e-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: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGV-NWLAFLNKYklHGILCDDMGLGKTLQSICILAgdhchraqeyarsklaECMPLPSLVVCPPT-LTGHWVD 1187
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNR--RGILVLPTGSGKTLTALALIA----------------YLKELRTLIVVPTDaLLDQWKE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1188 EVGKFCSREYLNPLhyTGPPTERIRLQhqvkrhNLIVASYDVVRNDI----DFFRniKFNYCILDEGHVIkNGKTkLSKA 1263
Cdd:cd17926    63 RFEDFLGDSSIGLI--GGGKKKDFDDA------NVVVATYQSLSNLAeeekDLFD--QFGLLIVDEAHHL-PAKT-FSEI 130
                         170
                  ....*....|....*.
gi 767964209 1264 VKQLTANYRIILSGTP 1279
Cdd:cd17926   131 LKELNAKYRLGLTATP 146
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1110-1313 2.03e-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: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1110 LRKYQQDGVNwlaFLNKYKLHGILCDdMGLGKTLQSICILAGDHchraqeyarsklAECMPLPSLVVCPPTLTGH-WVDE 1188
Cdd:cd18013     1 PHPYQKVAIN---FIIEHPYCGLFLD-MGLGKTVTTLTALSDLQ------------LDDFTRRVLVIAPLRVARStWPDE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1189 VGKFcsrEYLNPLHY---TGPPTERIRLQHqvKRHNLIVASYDVVrNDIDFFRNIKFNY--CILDEGHVIKNGKTKLSKA 1263
Cdd:cd18013    65 VEKW---NHLRNLTVsvaVGTERQRSKAAN--TPADLYVINRENL-KWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKA 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964209 1264 VKQL--TANYRIILSGTPIQNNVLELWSLFDFLMPGflgtER------QFAARYGKPI 1313
Cdd:cd18013   139 LRKVrpVIKRLIGLTGTPSPNGLMDLWAQIALLDQG----ERlgrsitAYRERWFDPD 192
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
1435-1606 5.11e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.82  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1435 PEFKTtaeklAVQNSSLHDIQHaPKLSALKQLLldcglgnGSTSESGTESvvaqhRILIFCQLKSMLD-IVEHdLLKPHL 1513
Cdd:COG1111   318 PRFRK-----AMRLAEEADIEH-PKLSKLREIL-------KEQLGTNPDS-----RIIVFTQYRDTAEmIVEF-LSEPGI 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1514 PSVTYLrldgsippGQ-------------RHSIVSRFNNDpSIDVLLlTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQA 1580
Cdd:COG1111   379 KAGRFV--------GQaskegdkgltqkeQIEILERFRAG-EFNVLV-ATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQR 448
                         170       180
                  ....*....|....*....|....*.
gi 767964209 1581 MDRAHRIGQKRVVnVyrLITRGTLEE 1606
Cdd:COG1111   449 KGRTGRKREGRVV-V--LIAKGTRDE 471
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1109-1279 7.07e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 50.79  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1109 ELRKYQQDGVN-WLAFLNKYKLHGILCDDMGLGKTLqsicILAGDhchrAQEYARSKLAecmplpsLVVCP-PTLTGHWV 1186
Cdd:COG1061    80 ELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV----LALAL----AAELLRGKRV-------LVLVPrRELLEQWA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209 1187 DEVgkfcsREYLNPLHYTGPPTERirlqhqvkRHNLIVASYDVVRND--IDFFRNiKFNYCILDEGHVIknGKTKLSKAV 1264
Cdd:COG1061   145 EEL-----RRFLGDPLAGGGKKDS--------DAPITVATYQSLARRahLDELGD-RFGLVIIDEAHHA--GAPSYRRIL 208
                         170
                  ....*....|....*
gi 767964209 1265 KQLTANYRIILSGTP 1279
Cdd:COG1061   209 EAFPAAYRLGLTATP 223
HEAT COG1413
HEAT repeat [General function prediction only];
184-298 3.80e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.00  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  184 EDLVIRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHG 252
Cdd:COG1413    28 EDPDVRAAAARALGRLGD---PRAVPAllealkdpdpeVRAAAAEALG-------RIGDPEAVPALIAALKDEDPEVRRA 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767964209  253 GLlgikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 298
Cdd:COG1413    98 AA----EALGRLGD------PAAVPALLEALKDPDWEVRRAAARAL 133
HEAT COG1413
HEAT repeat [General function prediction only];
188-298 4.78e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 41.92  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964209  188 IRLLCVFALDRFGDfvsDEVVAP-----------VRETCAQTLGvvlkhmnETGVHKTVDVLLKLLTQEQWEVRHGGLlg 256
Cdd:COG1413     1 VRRAAARALGRLGD---PAAVPAliaaladedpdVRAAAARALG-------RLGDPRAVPALLEALKDPDPEVRAAAA-- 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767964209  257 ikYALAVRQDvintllPKVLTRIIEGLQDLDDDVRAVAAASL 298
Cdd:COG1413    69 --EALGRIGD------PEAVPALIAALKDEDPEVRRAAAEAL 102
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1546-1590 2.92e-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: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767964209 1546 LLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQK 1590
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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