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Conserved domains on  [gi|334185970|ref|NP_001190085|]
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ROOT GROWTH DEFECTIVE 3 [Arabidopsis thaliana]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1378-1996 5.38e-148

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 476.25  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1378 GRQGAGMLIGLLVQGLGVELVPYSPLLVVPLLRCMSDVDSSVRQSVTRSFAALVPMLPLARGVPPPVGLSKDLSSNAEDA 1457
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1458 KFLEQLLDNSHIDDYKLCT----------ELKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAE 1527
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRlrealeslpaGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1528 RRGStdeldvfPSIIVCPSTLVGHWAFEIEKYidLSLLSVLQYVGSAqDRVSLREQFNNHNVIITSYDVVRKDVDYLTQF 1607
Cdd:COG0553   288 GLAR-------PVLIVAPTSLVGNWQRELAKF--APGLRVLVLDGTR-ERAKGANPFEDADLVITSYGLLRRDIELLAAV 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1608 SWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPlLAARDPK 1687
Cdd:COG0553   358 DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-IEKGDEE 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1688 csakdaeagvlAMEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQLKLYEQFSgSSAKQEIssiikvdgsads 1767
Cdd:COG0553   437 -----------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL-EYLRREL------------ 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1768 gnADVAPTKASTHVFQALQYLLKLCSHPLLVLGDKVTEPVasdlaamingcsdiitelhkvqHSPKLVALQEILEEcgig 1847
Cdd:COG0553   493 --EGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSG----------------------RSAKLEALLELLEE---- 544
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1848 sdasssdgtLSVGQHRVLIFAQHKALLDIIEKDLFQAHmksVTYMRLDGSVVPEKRFEIVKAFNSDPTIDVLLLTTHVGG 1927
Cdd:COG0553   545 ---------LLAEGEKVLVFSQFTDTLDLLEERLEERG---IEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1928 LGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVI 1996
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
813-1270 7.10e-103

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: 338.06  E-value: 7.10e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   813 VWRLLVQC--PVDDLEDTAKFYMASWIELAATPYGSTLDATKMFWPVAPPRKSHFKAAakmkavkleneaSSILGFDYAR 890
Cdd:pfam12054    1 VWEALLRSlkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRK------------SKKKEEPPPS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   891 SSASLEKQEDASARSTKIIVGSDMEMS----VTRTRVVTASALGIFASRLREGS-MQFVVDPLSSTLTSMSGVQRQVGSI 965
Cdd:pfam12054   69 DIPSPGRQGSSSHNVDKPMIGGDVTLVgmdvVIRTRIAAAKALGLLLSYWPEESpLDFFTKLLLPYLNSPSALQRLLAAI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   966 VLISWFRETKCKAPSdgsgSLPGFPSPLKKWLLDLLACadPAFPTkdiflPYAELSRTYTKMRNEASQLLHTVETcHCFD 1045
Cdd:pfam12054  149 IIEEWAKNCKKEKSS----SVSTLPETLSEKLLEILEN--PSRPP-----YYRELVPYLTRLRTQCQQLLNTFRD-VGKV 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1046 KLLSTNKLNVESVTADETIDFASTLDLWNKesAGNESLEK-----------QVFEDVESSRQQLLSTAGYLKCVQSNLHI 1114
Cdd:pfam12054  217 SQSKLPKLAVVVQGEPEAGPGAFSIEQAEK--LVGEDYDKlkkslspkqklLALQQLEDRRRRVQAAIEEAKEAKEQRDV 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1115 TVTSLVAAAVVWMSEFPARLNPIILPLMASIKREQEQILQQIAAEALAELIAYCVDR-KPSPNDKLIKNICSLTCMDPSE 1193
Cdd:pfam12054  295 RVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSE 374
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970  1194 TPQASIISSM-DIVddmdfLSSRSNtgKQKAKVVLASGEDRSKVEGFITRRGSELALKHLSLKFGGSLFDKLPKLWEC 1270
Cdd:pfam12054  375 TPEFHPNAKLtDGI-----LTLRKE--EDKADHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1378-1996 5.38e-148

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 476.25  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1378 GRQGAGMLIGLLVQGLGVELVPYSPLLVVPLLRCMSDVDSSVRQSVTRSFAALVPMLPLARGVPPPVGLSKDLSSNAEDA 1457
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1458 KFLEQLLDNSHIDDYKLCT----------ELKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAE 1527
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRlrealeslpaGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1528 RRGStdeldvfPSIIVCPSTLVGHWAFEIEKYidLSLLSVLQYVGSAqDRVSLREQFNNHNVIITSYDVVRKDVDYLTQF 1607
Cdd:COG0553   288 GLAR-------PVLIVAPTSLVGNWQRELAKF--APGLRVLVLDGTR-ERAKGANPFEDADLVITSYGLLRRDIELLAAV 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1608 SWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPlLAARDPK 1687
Cdd:COG0553   358 DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-IEKGDEE 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1688 csakdaeagvlAMEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQLKLYEQFSgSSAKQEIssiikvdgsads 1767
Cdd:COG0553   437 -----------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL-EYLRREL------------ 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1768 gnADVAPTKASTHVFQALQYLLKLCSHPLLVLGDKVTEPVasdlaamingcsdiitelhkvqHSPKLVALQEILEEcgig 1847
Cdd:COG0553   493 --EGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSG----------------------RSAKLEALLELLEE---- 544
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1848 sdasssdgtLSVGQHRVLIFAQHKALLDIIEKDLFQAHmksVTYMRLDGSVVPEKRFEIVKAFNSDPTIDVLLLTTHVGG 1927
Cdd:COG0553   545 ---------LLAEGEKVLVFSQFTDTLDLLEERLEERG---IEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1928 LGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVI 1996
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1482-1714 2.64e-144

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: 447.18  E-value: 2.64e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdELDVFPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF-NSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSAQDRVSLREQFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLI 1641
Cdd:cd17999    80 NAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185970 1642 LSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMPFLLRR 1714
Cdd:cd17999   160 LSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
813-1270 7.10e-103

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: 338.06  E-value: 7.10e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   813 VWRLLVQC--PVDDLEDTAKFYMASWIELAATPYGSTLDATKMFWPVAPPRKSHFKAAakmkavkleneaSSILGFDYAR 890
Cdd:pfam12054    1 VWEALLRSlkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRK------------SKKKEEPPPS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   891 SSASLEKQEDASARSTKIIVGSDMEMS----VTRTRVVTASALGIFASRLREGS-MQFVVDPLSSTLTSMSGVQRQVGSI 965
Cdd:pfam12054   69 DIPSPGRQGSSSHNVDKPMIGGDVTLVgmdvVIRTRIAAAKALGLLLSYWPEESpLDFFTKLLLPYLNSPSALQRLLAAI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   966 VLISWFRETKCKAPSdgsgSLPGFPSPLKKWLLDLLACadPAFPTkdiflPYAELSRTYTKMRNEASQLLHTVETcHCFD 1045
Cdd:pfam12054  149 IIEEWAKNCKKEKSS----SVSTLPETLSEKLLEILEN--PSRPP-----YYRELVPYLTRLRTQCQQLLNTFRD-VGKV 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1046 KLLSTNKLNVESVTADETIDFASTLDLWNKesAGNESLEK-----------QVFEDVESSRQQLLSTAGYLKCVQSNLHI 1114
Cdd:pfam12054  217 SQSKLPKLAVVVQGEPEAGPGAFSIEQAEK--LVGEDYDKlkkslspkqklLALQQLEDRRRRVQAAIEEAKEAKEQRDV 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1115 TVTSLVAAAVVWMSEFPARLNPIILPLMASIKREQEQILQQIAAEALAELIAYCVDR-KPSPNDKLIKNICSLTCMDPSE 1193
Cdd:pfam12054  295 RVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSE 374
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970  1194 TPQASIISSM-DIVddmdfLSSRSNtgKQKAKVVLASGEDRSKVEGFITRRGSELALKHLSLKFGGSLFDKLPKLWEC 1270
Cdd:pfam12054  375 TPEFHPNAKLtDGI-----LTLRKE--EDKADHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1450-2014 1.43e-79

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 286.70  E-value: 1.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1450 LSSNAEDAKFLEQLLDN-SHIDDYKLCTE---LKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdA 1525
Cdd:PLN03142  134 LTEEEEDEEYLKEEEDGlGGSGGTRLLVQpscIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGY-L 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1526 AERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYIdlSLLSVLQYVGSAQDRVSLREQF---NNHNVIITSYDVVRKDVD 1602
Cdd:PLN03142  213 HEYRGITG-----PHMVVAPKSTLGNWMNEIRRFC--PVLRAVKFHGNPEERAHQREELlvaGKFDVCVTSFEMAIKEKT 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1603 YLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkplla 1682
Cdd:PLN03142  286 ALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----- 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1683 ardpkCSAKDAEAGVLamEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQlklyeqfsgssaKQEISSIIKVD 1762
Cdd:PLN03142  361 -----ISGENDQQEVV--QQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQ------------KQYYKALLQKD 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1763 GSADSGNADVAptKASTHVFQalqyLLKLCSHPLLVLGDKVTEPvasdlaamingcsdIITELHKVQHSPKLVALQEILE 1842
Cdd:PLN03142  422 LDVVNAGGERK--RLLNIAMQ----LRKCCNHPYLFQGAEPGPP--------------YTTGEHLVENSGKMVLLDKLLP 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1843 EcgigsdasssdgtLSVGQHRVLIFAQHKALLDIIEKDLFqahMKSVTYMRLDGSVVPEKRFEIVKAFNSDPTID-VLLL 1921
Cdd:PLN03142  482 K-------------LKERDSRVLIFSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLL 545
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1922 TTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVIN---- 1997
Cdd:PLN03142  546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQqgrl 625
                         570
                  ....*....|....*..
gi 334185970 1998 AENasmKTMNTDQLLDL 2014
Cdd:PLN03142  626 AEQ---KTVNKDELLQM 639
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1485-1798 2.04e-72

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: 244.52  E-value: 2.04e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1485 YQQEGINWLGFLKRFKLH-GILCDDMGLGKTLQASAIVA--SDAAERRGStdeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRgGILADEMGLGKTLQTISLLLylKHVDKNWGG-------PTLIVVPLSLLHNWMNEFERWVS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1562 LSLLSVLQYVGSAQDRVSLRE---QFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQH 1638
Cdd:pfam00176   74 PPALRVVVLHGNKRPQERWKNdpnFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKdaeagvlameaLHKQVMPFLLRRTKEE 1718
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRTKKD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1719 VLSDLPEKIIQDRYCDLSPVQLKLYEQFSGSSAKQEISSIIKVDGSADSgnadvaptkasthVFQALQYLLKLCSHPLLV 1798
Cdd:pfam00176  223 VEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKAS-------------LLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
1481-1670 3.67e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.18  E-value: 3.67e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   1481 QLRRYQQEGINWLGFLKRfklHGILCDDMGLGKTLQASAIVASDAAERRGstdeldvFPSIIVCP-STLVGHWAFEIEKY 1559
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKG-------GRVLVLVPtRELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   1560 IDLSLLSVLQYVGSAQDRVSLREQFNNH-NVIITSYDVVRKDV--DYLTQFSWNYCILDEGHIIKNA--KSKITAAVKQL 1634
Cdd:smart00487   78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLL 157
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 334185970   1635 -KAQHRLILSGTP---IQNNIMELWSLFDFLMPGFLGTER 1670
Cdd:smart00487  158 pKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1378-1996 5.38e-148

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 476.25  E-value: 5.38e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1378 GRQGAGMLIGLLVQGLGVELVPYSPLLVVPLLRCMSDVDSSVRQSVTRSFAALVPMLPLARGVPPPVGLSKDLSSNAEDA 1457
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1458 KFLEQLLDNSHIDDYKLCT----------ELKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAE 1527
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRlrealeslpaGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1528 RRGStdeldvfPSIIVCPSTLVGHWAFEIEKYidLSLLSVLQYVGSAqDRVSLREQFNNHNVIITSYDVVRKDVDYLTQF 1607
Cdd:COG0553   288 GLAR-------PVLIVAPTSLVGNWQRELAKF--APGLRVLVLDGTR-ERAKGANPFEDADLVITSYGLLRRDIELLAAV 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1608 SWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPlLAARDPK 1687
Cdd:COG0553   358 DWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-IEKGDEE 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1688 csakdaeagvlAMEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQLKLYEQFSgSSAKQEIssiikvdgsads 1767
Cdd:COG0553   437 -----------ALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVL-EYLRREL------------ 492
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1768 gnADVAPTKASTHVFQALQYLLKLCSHPLLVLGDKVTEPVasdlaamingcsdiitelhkvqHSPKLVALQEILEEcgig 1847
Cdd:COG0553   493 --EGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSG----------------------RSAKLEALLELLEE---- 544
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1848 sdasssdgtLSVGQHRVLIFAQHKALLDIIEKDLFQAHmksVTYMRLDGSVVPEKRFEIVKAFNSDPTIDVLLLTTHVGG 1927
Cdd:COG0553   545 ---------LLAEGEKVLVFSQFTDTLDLLEERLEERG---IEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGG 612
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1928 LGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVI 1996
Cdd:COG0553   613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1482-1714 2.64e-144

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: 447.18  E-value: 2.64e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdELDVFPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSF-NSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSAQDRVSLREQFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLI 1641
Cdd:cd17999    80 NAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185970 1642 LSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMPFLLRR 1714
Cdd:cd17999   160 LSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
813-1270 7.10e-103

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: 338.06  E-value: 7.10e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   813 VWRLLVQC--PVDDLEDTAKFYMASWIELAATPYGSTLDATKMFWPVAPPRKSHFKAAakmkavkleneaSSILGFDYAR 890
Cdd:pfam12054    1 VWEALLRSlkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRK------------SKKKEEPPPS 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   891 SSASLEKQEDASARSTKIIVGSDMEMS----VTRTRVVTASALGIFASRLREGS-MQFVVDPLSSTLTSMSGVQRQVGSI 965
Cdd:pfam12054   69 DIPSPGRQGSSSHNVDKPMIGGDVTLVgmdvVIRTRIAAAKALGLLLSYWPEESpLDFFTKLLLPYLNSPSALQRLLAAI 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   966 VLISWFRETKCKAPSdgsgSLPGFPSPLKKWLLDLLACadPAFPTkdiflPYAELSRTYTKMRNEASQLLHTVETcHCFD 1045
Cdd:pfam12054  149 IIEEWAKNCKKEKSS----SVSTLPETLSEKLLEILEN--PSRPP-----YYRELVPYLTRLRTQCQQLLNTFRD-VGKV 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1046 KLLSTNKLNVESVTADETIDFASTLDLWNKesAGNESLEK-----------QVFEDVESSRQQLLSTAGYLKCVQSNLHI 1114
Cdd:pfam12054  217 SQSKLPKLAVVVQGEPEAGPGAFSIEQAEK--LVGEDYDKlkkslspkqklLALQQLEDRRRRVQAAIEEAKEAKEQRDV 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1115 TVTSLVAAAVVWMSEFPARLNPIILPLMASIKREQEQILQQIAAEALAELIAYCVDR-KPSPNDKLIKNICSLTCMDPSE 1193
Cdd:pfam12054  295 RVLAAAAGALVALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRgKPGPNDKIVKNLCTFLCVDTSE 374
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970  1194 TPQASIISSM-DIVddmdfLSSRSNtgKQKAKVVLASGEDRSKVEGFITRRGSELALKHLSLKFGGSLFDKLPKLWEC 1270
Cdd:pfam12054  375 TPEFHPNAKLtDGI-----LTLRKE--EDKADHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1478-1716 5.67e-82

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: 268.66  E-value: 5.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1478 LKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGStdeldvfPSIIVCPSTLVGHWAFEIE 1557
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKG-------PSLVVAPTSLIYNWEEEAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1558 KYIDLslLSVLQYVGSAQDRVSLReQFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQ 1637
Cdd:cd18012    74 KFAPE--LKVLVIHGTKRKREKLR-ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKAD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1638 HRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKcsakdaeagvlAMEALHKQVMPFLLRRTK 1716
Cdd:cd18012   151 HRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1450-2014 1.43e-79

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 286.70  E-value: 1.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1450 LSSNAEDAKFLEQLLDN-SHIDDYKLCTE---LKVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdA 1525
Cdd:PLN03142  134 LTEEEEDEEYLKEEEDGlGGSGGTRLLVQpscIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGY-L 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1526 AERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYIdlSLLSVLQYVGSAQDRVSLREQF---NNHNVIITSYDVVRKDVD 1602
Cdd:PLN03142  213 HEYRGITG-----PHMVVAPKSTLGNWMNEIRRFC--PVLRAVKFHGNPEERAHQREELlvaGKFDVCVTSFEMAIKEKT 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1603 YLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkplla 1682
Cdd:PLN03142  286 ALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ----- 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1683 ardpkCSAKDAEAGVLamEALHKQVMPFLLRRTKEEVLSDLPEKIIQDRYCDLSPVQlklyeqfsgssaKQEISSIIKVD 1762
Cdd:PLN03142  361 -----ISGENDQQEVV--QQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQ------------KQYYKALLQKD 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1763 GSADSGNADVAptKASTHVFQalqyLLKLCSHPLLVLGDKVTEPvasdlaamingcsdIITELHKVQHSPKLVALQEILE 1842
Cdd:PLN03142  422 LDVVNAGGERK--RLLNIAMQ----LRKCCNHPYLFQGAEPGPP--------------YTTGEHLVENSGKMVLLDKLLP 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1843 EcgigsdasssdgtLSVGQHRVLIFAQHKALLDIIEKDLFqahMKSVTYMRLDGSVVPEKRFEIVKAFNSDPTID-VLLL 1921
Cdd:PLN03142  482 K-------------LKERDSRVLIFSQMTRLLDILEDYLM---YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLL 545
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1922 TTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLIMRGTLEEKVMSLQKFKVSVANTVIN---- 1997
Cdd:PLN03142  546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQqgrl 625
                         570
                  ....*....|....*..
gi 334185970 1998 AENasmKTMNTDQLLDL 2014
Cdd:PLN03142  626 AEQ---KTVNKDELLQM 639
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1485-1798 2.04e-72

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: 244.52  E-value: 2.04e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1485 YQQEGINWLGFLKRFKLH-GILCDDMGLGKTLQASAIVA--SDAAERRGStdeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRgGILADEMGLGKTLQTISLLLylKHVDKNWGG-------PTLIVVPLSLLHNWMNEFERWVS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1562 LSLLSVLQYVGSAQDRVSLRE---QFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQH 1638
Cdd:pfam00176   74 PPALRVVVLHGNKRPQERWKNdpnFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKdaeagvlameaLHKQVMPFLLRRTKEE 1718
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRTKKD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1719 VLSDLPEKIIQDRYCDLSPVQLKLYEQFSGSSAKQEISSIIKVDGSADSgnadvaptkasthVFQALQYLLKLCSHPLLV 1798
Cdd:pfam00176  223 VEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGREIKAS-------------LLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1482-1666 1.00e-63

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: 215.12  E-value: 1.00e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRgstdelDVFPSIIVCPSTLVGHWAFEIEKYid 1561
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGK------ERGPVLVVCPLSVLENWEREFEKW-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSAQDRVSLREQ--FNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHR 1639
Cdd:cd17919    73 TPDLRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRR 152
                         170       180
                  ....*....|....*....|....*..
gi 334185970 1640 LILSGTPIQNNIMELWSLFDFLMPGFL 1666
Cdd:cd17919   153 LLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1482-1714 3.64e-56

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: 195.28  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLgflkrFKLH-----GILCDDMGLGKTLQASAIVASDAaeRRGSTDEldvfpSIIVCPSTLVGHWAFEI 1556
Cdd:cd18001     1 LYPHQREGVAWL-----WSLHdggkgGILADDMGLGKTVQICAFLSGMF--DSGLIKS-----VLVVMPTSLIPHWVKEF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1557 EKYIdlSLLSVLQYVGSAQD--RVSLREQFNNHNVIITSYDVVRKDVDYLT-----QFSWNYCILDEGHIIKNAKSKITA 1629
Cdd:cd18001    69 AKWT--PGLRVKVFHGTSKKerERNLERIQRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1630 AVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPG-FLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVM 1708
Cdd:cd18001   147 SLREIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIK 226

                  ....*.
gi 334185970 1709 PFLLRR 1714
Cdd:cd18001   227 PYFLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1482-1666 4.35e-54

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: 187.92  E-value: 4.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLG------PSLIVCPATVLKQWVKEFHRWWP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVL----------QYVGSAQDRVSLREQFNN-HNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAA 1630
Cdd:cd18000    75 PFRVVVLhssgsgtgseEKLGSIERKSQLIRKVVGdGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLA 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 334185970 1631 VKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFL 1666
Cdd:cd18000   155 CKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1482-1714 8.50e-54

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: 188.33  E-value: 8.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRgstdelDVFPSIIVCPSTLVGHWAFEIEKYid 1561
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKG------NWGPHLIVVPTSVMLNWEMEFKRW-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSAQDRVSLREQFNNHN---VIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQH 1638
Cdd:cd18003    73 CPGFKILTYYGSAKERKLKRQGWMKPNsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334185970 1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPkcSAKDAEAGVlamEALHKQVMPFLLRR 1714
Cdd:cd18003   153 RLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEG--SQEENEELV---RRLHKVLRPFLLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1479-1716 8.78e-53

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: 185.67  E-value: 8.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1479 KVQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdaaerrgsTDELDVF-PSIIVCPSTLVGHWAFEIE 1557
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAH--------LRERGVWgPFLVIAPLSTLPNWVNEFA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1558 KYidLSLLSVLQYVGSAQDRVSLREQFNNHN-------VIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAA 1630
Cdd:cd18009    73 RF--TPSVPVLLYHGTKEERERLRKKIMKREgtlqdfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1631 VKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAAR--DPKCSAKDAEAGVLAMeaLHKQVM 1708
Cdd:cd18009   151 LKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNaaDISNLSEEREQNIVHM--LHAILK 228

                  ....*...
gi 334185970 1709 PFLLRRTK 1716
Cdd:cd18009   229 PFLLRRLK 236
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1830-1972 8.35e-52

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 178.82  E-value: 8.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1830 HSPKLVALQEILEECGIGsdasssdgtlsvgQHRVLIFAQHKALLDIIEKDLFQAHmksVTYMRLDGSVVPEKRFEIVKA 1909
Cdd:cd18793     9 VSGKLEALLELLEELREP-------------GEKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKERQKLVDR 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334185970 1910 FNSDPTIDVLLLTTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVNVHRLI 1972
Cdd:cd18793    73 FNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1482-1714 3.81e-51

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: 181.33  E-value: 3.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLgflkrFK-LHG---------ILCDDMGLGKTLQASAIVAsdAAERRGSTDELDVFPSIIVCPSTLVGH 1551
Cdd:cd18004     1 LRPHQREGVQFL-----YDcLTGrrgyggggaILADEMGLGKTLQAIALVW--TLLKQGPYGKPTAKKALIVCPSSLVGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1552 WAFEIEKYIDLSLLSVLQYVGSAQDRVSLREQFNN---HNVIITSYDVVRKDVDYLTQ-FSWNYCILDEGHIIKNAKSKI 1627
Cdd:cd18004    74 WKAEFDKWLGLRRIKVVTADGNAKDVKASLDFFSSastYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1628 TAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQV 1707
Cdd:cd18004   154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                  ....*..
gi 334185970 1708 MPFLLRR 1714
Cdd:cd18004   234 SRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1482-1714 8.27e-50

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: 177.48  E-value: 8.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLgfLKRfklHGILCDDMGLGKTLQASAIVASDAAERRGSTDELDVFPS-----------IIVCPSTLVG 1550
Cdd:cd18008     1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSdpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1551 HWAFEIEKYIDLSLLSVLQYVGSaqDRVSLREQFNNHNVIITSYDVVRKDVDY----------------LTQFSWNYCIL 1614
Cdd:cd18008    76 QWKDEIEKHTKPGSLKVYVYHGS--KRIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskekeaspLHRIRWYRVIL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1615 DEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGtERQFQASYGKPLLAARDPKcsakdae 1694
Cdd:cd18008   154 DEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFG-DYPWFNSDISKPFSKNDRK------- 225
                         250       260
                  ....*....|....*....|
gi 334185970 1695 agvlAMEALHKQVMPFLLRR 1714
Cdd:cd18008   226 ----ALERLQALLKPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1482-1714 4.39e-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: 175.65  E-value: 4.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVAS---------DAAERR-----GSTDELDVFPSIIVCPST 1547
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAvlgktgtrrDRENNRprfkkKPPASSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1548 LVGHWAFEIEKYidlSLLSVLQYVGSAQDRV-SLREQFNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSK 1626
Cdd:cd18005    81 VLYNWKDELDTW---GHFEVGVYHGSRKDDElEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1627 ITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQ 1706
Cdd:cd18005   158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVK 237

                  ....*...
gi 334185970 1707 VMPFLLRR 1714
Cdd:cd18005   238 LSKFFLRR 245
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1481-1716 5.05e-46

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: 166.39  E-value: 5.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1481 QLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdAAERRGstdelDVFPSIIVCP-STLVGhWAFEIEKY 1559
Cdd:cd17996     3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITY-LMEKKK-----NNGPYLVIVPlSTLSN-WVSEFEKW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 idLSLLSVLQYVGSAQDRVSLREQF--NNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQ-LKA 1636
Cdd:cd17996    76 --APSVSKIVYKGTPDVRKKLQSQIraGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1637 QHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMPFLLRRTK 1716
Cdd:cd17996   154 RYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1481-1716 5.93e-46

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: 165.57  E-value: 5.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1481 QLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdAAERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYi 1560
Cdd:cd17997     3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGY-LKHYKNING-----PHLIIVPKSTLDNWMREFKRW- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 dLSLLSVLQYVGSAQDR------VSLREQFNnhnVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQL 1634
Cdd:cd17997    76 -CPSLRVVVLIGDKEERadiirdVLLPGKFD---VCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1635 KAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFqasygkpllaarDPKCSAKDAEAGVLAM-EALHKQVMPFLLR 1713
Cdd:cd17997   152 NSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDF------------DEWFNVNNCDDDNQEVvQRLHKVLRPFLLR 219

                  ...
gi 334185970 1714 RTK 1716
Cdd:cd17997   220 RIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1482-1714 7.53e-45

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: 162.42  E-value: 7.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVA--SDAAERRGstdeldvfPSIIVCPSTLVGHWAFEIEKY 1559
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEhlYQVEGIRG--------PFLVIAPLSTIPNWQREFETW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 IDLSllsVLQYVGS--AQDRVSLREQFNNH------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKS 1625
Cdd:cd17995    73 TDMN---VVVYHGSgeSRQIIQQYEMYFKDaqgrkkkgvykfDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1626 KITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKpllaardpkcsAKDAEagvlAMEALHK 1705
Cdd:cd17995   150 KLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGD-----------LKTAE----QVEKLQA 214

                  ....*....
gi 334185970 1706 QVMPFLLRR 1714
Cdd:cd17995   215 LLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1481-1714 4.92e-44

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: 159.83  E-value: 4.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1481 QLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYi 1560
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYG------PFLVVVPLSTMPAWQREFAKW- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 dLSLLSVLQYVGSAQDRVSLRE-QFNNH-------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVK 1632
Cdd:cd17993    74 -APDMNVIVYLGDIKSRDTIREyEFYFSqtkklkfNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1633 QLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkpllaardpkcsaKDAEAGVlamEALHKQVMPFLL 1712
Cdd:cd17993   153 EFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHD-------------EEQEKGI---ADLHKELEPFIL 216

                  ..
gi 334185970 1713 RR 1714
Cdd:cd17993   217 RR 218
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1482-1663 5.14e-42

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: 152.92  E-value: 5.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdaAERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAY--LKEIGIPG-----PHLVVVPSSTLDNWLREFKRWC- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVSLR----EQFNNHNVIITSYDVV---RKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQL 1634
Cdd:cd17998    73 -PSLKVEPYYGSQEERKHLRydilKGLEDFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTI 151
                         170       180
                  ....*....|....*....|....*....
gi 334185970 1635 KAQHRLILSGTPIQNNIMELWSLFDFLMP 1663
Cdd:cd17998   152 NANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1482-1714 5.61e-42

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: 154.13  E-value: 5.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLgFLKRFKLHG-ILCDDMGLGKTLQASAIVASdAAERRGstdelDVFPSIIVCPSTLVGHWAFEIEKYI 1560
Cdd:cd18006     1 LRPYQLEGVNWL-LQCRAEQHGcILGDEMGLGKTCQTISLLWY-LAGRLK-----LLGPFLVLCPLSVLDNWKEELNRFA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 dlSLLSVLQYVGSAQDRVSLREQ---FNNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQ 1637
Cdd:cd18006    74 --PDLSVITYMGDKEKRLDLQQDiksTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVD 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1638 HRLILSGTPIQNNIMELWSLFDFLMPGFLGTER--QFQASYgkpllaardpkcsaKDAEAGVLAMEALHKQVMPFLLRR 1714
Cdd:cd18006   152 FRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAY--------------SETDDESETVEELHLLLQPFLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1482-1714 2.32e-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: 152.66  E-value: 2.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASdAAERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAH-LAEEHNIWG-----PFLVIAPASTLHNWQQEISRFV- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVSLREQFNNHN---------VIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVK 1632
Cdd:cd18002    74 -PQFKVLPYWGNPKDRKVLRKFWDRKNlytrdapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1633 QLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEagvlaMEALHKQVMPFLL 1712
Cdd:cd18002   153 SFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHMILKPFML 227

                  ..
gi 334185970 1713 RR 1714
Cdd:cd18002   228 RR 229
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1482-1714 1.94e-37

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: 141.84  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWL----GFLKRFKLHG-ILCDDMGLGKTLQASAIVASdaAERRGSTDELDVFPSIIVCPSTLVGHWAFEI 1556
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWT--LLRQSPQCKPEIDKAIVVSPSSLVKNWANEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1557 EKYIDLSLLSVLQYVGSAQDRVSLREQFNNHN-------VIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITA 1629
Cdd:cd18067    79 GKWLGGRLQPLAIDGGSKKEIDRKLVQWASQQgrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1630 AVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMP 1709
Cdd:cd18067   159 ALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNR 238

                  ....*
gi 334185970 1710 FLLRR 1714
Cdd:cd18067   239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1482-1676 3.42e-37

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: 140.03  E-value: 3.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINwlgFLKRFKLHGILCDDMGLGKTLQASAIVASDAAErrgstdeldvFPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd18010     1 LLPFQREGVC---FALRRGGRVLIADEMGLGKTVQAIAIAAYYREE----------WPLLIVCPSSLRLTWADEIERWLP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSAQDRVSLReqfnNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQL--KAQHR 1639
Cdd:cd18010    68 SLPPDDIQVIVKSKDGLRDG----DAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRV 143
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 334185970 1640 LILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASY 1676
Cdd:cd18010   144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRY 180
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1481-1726 9.89e-37

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: 139.80  E-value: 9.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1481 QLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYI 1560
Cdd:cd18064    15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPG------PHMVLVPKSTLHNWMAEFKRWV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 DlSLLSVLqYVGSAQDRVSLREQF---NNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQ 1637
Cdd:cd18064    89 P-TLRAVC-LIGDKDQRAAFVRDVllpGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1638 HRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYgkpllaarDPKCSAKDAEagvlAMEALHKQVMPFLLRRTKE 1717
Cdd:cd18064   167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTNNCLGDQK----LVERLHMVLRPFLLRRIKA 234

                  ....*....
gi 334185970 1718 EVLSDLPEK 1726
Cdd:cd18064   235 DVEKSLPPK 243
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1481-1716 5.09e-36

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: 138.25  E-value: 5.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1481 QLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYI 1560
Cdd:cd18062    23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRING------PFLIIVPLSTLSNWVYEFDKWA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 DlSLLSVlQYVGSAQDRVSLREQFNN--HNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVK-QLKAQ 1637
Cdd:cd18062    97 P-SVVKV-SYKGSPAARRAFVPQLRSgkFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAP 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1638 HRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPlLAARDPKCSAKDAEAgVLAMEALHKQVMPFLLRRTK 1716
Cdd:cd18062   175 RRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP-FAMTGEKVDLNEEET-ILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1482-1716 1.28e-35

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: 137.12  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd18063    24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNG------PYLIIVPLSTLSNWTYEFDKWAP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVlQYVGSAQDRVSLREQFNN--HNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVK-QLKAQH 1638
Cdd:cd18063    98 -SVVKI-SYKGTPAMRRSLVPQLRSgkFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970 1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPlLAARDPKCSAKDAEAgVLAMEALHKQVMPFLLRRTK 1716
Cdd:cd18063   176 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAP-FAMTGERVDLNEEET-ILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1482-1716 4.47e-35

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: 134.76  E-value: 4.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPG------PHMVLVPKSTLHNWMNEFKRWV- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVS-LREQF--NNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQH 1638
Cdd:cd18065    89 -PSLRAVCLIGDKDARAAfIRDVMmpGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970 1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYgkpllaarDPKCSAKDAEagvlAMEALHKQVMPFLLRRTK 1716
Cdd:cd18065   168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVLKPFLLRRIK 233
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1482-1661 1.08e-33

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: 131.06  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHG-ILCDDMGLGKTLQASAIV--ASDAAERRGSTDEL-----------DVFPS---IIVC 1544
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALIlaQKNTQNRKEEEKEKalteweskkdsTLVPSagtLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1545 PSTLVGHWAFEIEKYIDLSLLSVLQYVGSAQDRVSlrEQFNNHNVIITSYDVVRKD---------VDYLTQFSWNYCILD 1615
Cdd:cd18072    81 PASLVHQWKNEVESRVASNKLRVCLYHGPNRERIG--EVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILD 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 334185970 1616 EGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFL 1661
Cdd:cd18072   159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1482-1714 1.18e-32

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 128.04  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWL-----GFLKRFKLHGILCDDMGLGKTLQASAIVASdaAERRGSTDELDVFP-SIIVCPSTLVGHWAFE 1555
Cdd:cd18066     1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWT--LLRQGPYGGKPVIKrALIVTPGSLVKNWKKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1556 IEKYIDLSLLSVlqYVGSAQDRVslrEQFNN---HNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVK 1632
Cdd:cd18066    79 FQKWLGSERIKV--FTVDQDHKV---EEFIAsplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1633 QLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKDAEAGVLAMEALHKQVMPFLL 1712
Cdd:cd18066   154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFIL 233

                  ..
gi 334185970 1713 RR 1714
Cdd:cd18066   234 RR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1503-1714 1.81e-32

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: 127.59  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1503 GILCDDMGLGKTLQASAIVASDaaerrgstdeldvfPSIIVCPSTLVGHWAFEIEKYIDLSLLSVLQYVGSAQDR-VSLr 1581
Cdd:cd18071    51 GILADDMGLGKTLTTISLILAN--------------FTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRdPKL- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1582 eqFNNHNVIITSYDVVRKDVDY-----LTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWS 1656
Cdd:cd18071   116 --LSKYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334185970 1657 LFDFLMPGFLGTERQFQASYGKPLlaardpkcsAKDAEAGVLAMEALHKQVmpfLLRR 1714
Cdd:cd18071   194 LLSFLHLKPFSNPEYWRRLIQRPL---------TMGDPTGLKRLQVLMKQI---TLRR 239
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1480-1714 1.84e-32

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: 127.43  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1480 VQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKY 1559
Cdd:cd18054    19 LELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYG------PFLLVVPLSTLTSWQREFEIW 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 IdlSLLSVLQYVGSAQDRVSLREQFNNH--------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAV 1631
Cdd:cd18054    93 A--PEINVVVYIGDLMSRNTIREYEWIHsqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1632 KQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKpllaARDPkcsakdaeagvlAMEALHKQVMPFL 1711
Cdd:cd18054   171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGK----GREN------------GYQSLHKVLEPFL 234

                  ...
gi 334185970 1712 LRR 1714
Cdd:cd18054   235 LRR 237
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1482-1692 6.17e-30

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: 120.09  E-value: 6.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWL------GFLKRFKLHG-ILCDDMGLGKTLQA-SAIVASDAAERRGSTdeldvfpSIIVCPSTLVGHWA 1553
Cdd:cd18007     1 LKPHQVEGVRFLwsnlvgTDVGSDEGGGcILAHTMGLGKTLQViTFLHTYLAAAPRRSR-------PLVLCPASTLYNWE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1554 FEIEK-----YIDLSLLSVLQYVGSAQDRVS-LREQFNNHNVIITSYDVVRKDVDYLTQFSWNYC--------------I 1613
Cdd:cd18007    74 DEFKKwlppdLRPLLVLVSLSASKRADARLRkINKWHKEGGVLLIGYELFRNLASNATTDPRLKQefiaalldpgpdllV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1614 LDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLLAARDPKCSAKD 1692
Cdd:cd18007   154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEED 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1480-1714 1.69e-29

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: 119.00  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1480 VQLRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKY 1559
Cdd:cd18053    19 LELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYG------PFLLVVPLSTLTSWQREIQTW 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 IdlSLLSVLQYVGSAQDRVSLREQFNNH--------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAV 1631
Cdd:cd18053    93 A--PQMNAVVYLGDINSRNMIRTHEWMHpqtkrlkfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1632 KQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKpllaARDpkcsakdaeagvLAMEALHKQVMPFL 1711
Cdd:cd18053   171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GRE------------YGYASLHKELEPFL 234

                  ...
gi 334185970 1712 LRR 1714
Cdd:cd18053   235 LRR 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1482-1663 4.37e-28

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: 115.52  E-value: 4.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKrfklhGILCDDMGLGKTLQASAIVASDaaeRRGSTDELDVF----------------------P 1539
Cdd:cd18070     1 LLPYQRRAVNWMLVPG-----GILADEMGLGKTVEVLALILLH---PRPDNDLDAADddsdemvccpdclvaetpvsskA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1540 SIIVCPSTLVGHWAFEIEKYIDLSLlSVLQYVGSAQDRV---SLREQFNNHNVIITSYDVVRKDVDY------------- 1603
Cdd:cd18070    73 TLIVCPSAILAQWLDEINRHVPSSL-KVLTYQGVKKDGAlasPAPEILAEYDIVVTTYDVLRTELHYaeanrsnrrrrrq 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334185970 1604 ---------LTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMP 1663
Cdd:cd18070   152 kryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1482-1714 1.52e-26

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: 109.76  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASD-AAERRGstdeldvfPSIIVCPSTLVGHWAFEIEKYI 1560
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVyNVGIHG--------PFLVIAPLSTITNWEREFNTWT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1561 DLSllsVLQYVGSAQDRvSLREQFNNH---------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKS 1625
Cdd:cd18060    73 EMN---TIVYHGSLASR-QMIQQYEMYckdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1626 KITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkpllaarDPKcsakdAEAGVLAMEALHK 1705
Cdd:cd18060   149 KLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLK-----TEEQVQKLQAILK 216

                  ....*....
gi 334185970 1706 qvmPFLLRR 1714
Cdd:cd18060   217 ---PMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1482-1714 2.80e-25

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: 106.28  E-value: 2.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVAsdaaerrgstdelDVF------PSIIVCPSTLVGHWAFE 1555
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-------------EIFlmgirgPFLIIAPLSTITNWERE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1556 IEKYIDLSllsVLQYVGSAQDRVSLR--------EQFN------NHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIK 1621
Cdd:cd18058    68 FRTWTEMN---AIVYHGSQISRQMIQqyemyyrdEQGNplsgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1622 NAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkpllaarDPKcsakdAEAGVLAME 1701
Cdd:cd18058   145 NRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG-------DLK-----TEEQVKKLQ 212
                         250
                  ....*....|...
gi 334185970 1702 ALHKqvmPFLLRR 1714
Cdd:cd18058   213 SILK---PMMLRR 222
DEXDc smart00487
DEAD-like helicases superfamily;
1481-1670 3.67e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.18  E-value: 3.67e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   1481 QLRRYQQEGINWLGFLKRfklHGILCDDMGLGKTLQASAIVASDAAERRGstdeldvFPSIIVCP-STLVGHWAFEIEKY 1559
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKG-------GRVLVLVPtRELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   1560 IDLSLLSVLQYVGSAQDRVSLREQFNNH-NVIITSYDVVRKDV--DYLTQFSWNYCILDEGHIIKNA--KSKITAAVKQL 1634
Cdd:smart00487   78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLL 157
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 334185970   1635 -KAQHRLILSGTP---IQNNIMELWSLFDFLMPGFLGTER 1670
Cdd:smart00487  158 pKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1482-1663 3.71e-24

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: 102.13  E-value: 3.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAE--RRGstdeldvfPSIIVCPSTLVGHWAFEIEKY 1559
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghSKG--------PFLVSAPLSTIINWEREFEMW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 IdlSLLSVLQYVGSaqdrvslreqfnnhNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQHR 1639
Cdd:cd17994    73 A--PDFYVVTYVGD--------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYK 136
                         170       180
                  ....*....|....*....|....
gi 334185970 1640 LILSGTPIQNNIMELWSLFDFLMP 1663
Cdd:cd17994   137 LLLTGTPLQNNLEELFHLLNFLTP 160
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1482-1677 6.60e-24

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: 102.03  E-value: 6.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGStdeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHG-------PFLVIAPLSTIPNWEREFRTWTE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSllsVLQYVGSAQDR--VSLREQF------------NNHNVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSKI 1627
Cdd:cd18059    74 LN---VVVYHGSQASRrtIQLYEMYfkdpqgrvikgsYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 334185970 1628 TAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYG 1677
Cdd:cd18059   151 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG 200
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1482-1714 3.18e-23

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: 100.52  E-value: 3.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKG------PFLVSAPLSTIINWEREFEMWA- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVSLREQ---FNNH-------------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHI 1619
Cdd:cd18056    74 -PDMYVVTYVGDKDSRAIIRENefsFEDNairggkkasrmkkeasvkfHVLLTSYELITIDMAILGSIDWACLIVDEAHR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1620 IKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKplLAARDpkcsakdaeagvlA 1699
Cdd:cd18056   153 LKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD--IAKED-------------Q 217
                         250
                  ....*....|....*
gi 334185970 1700 MEALHKQVMPFLLRR 1714
Cdd:cd18056   218 IKKLHDMLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1482-1714 2.09e-22

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: 97.77  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQAsaIVASDAAERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKYID 1561
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS--ITFLYEILLTGIRG-----PFLIIAPLSTIANWEREFRTWTD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSllsVLQYVGSAQDRVSLrEQFNNH---------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHIIKNAKSK 1626
Cdd:cd18061    74 LN---VVVYHGSLISRQMI-QQYEMYfrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1627 ITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGkpllaarDPKcsakdAEAGVLAMEALHKq 1706
Cdd:cd18061   150 LLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-------DLK-----TEEQVQKLQAILK- 216

                  ....*...
gi 334185970 1707 vmPFLLRR 1714
Cdd:cd18061   217 --PMMLRR 222
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1503-1680 1.05e-21

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: 96.50  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1503 GILCDDMGLGKTLQASAIVASD-AAERRGSTDELdvfpsIIVCPSTLVGHWAFEIEKYI----DLSLLSV--LQYVGSAQ 1575
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVlLCEKLENFSRV-----LVVCPLNTVLNWLNEFEKWQeglkDEEKIEVneLATYKRPQ 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1576 DRV-SLREQFNNHNVIITSYDVVR-----KDV-----------DYLTQFSWNYCILDEGHIIKNAKSKITAAVKQLKAQH 1638
Cdd:cd18068   106 ERSyKLQRWQEEGGVMIIGYDMYRilaqeRNVksreklkeifnKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKR 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 334185970 1639 RLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPL 1680
Cdd:cd18068   186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPI 227
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1496-1681 3.39e-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: 94.50  E-value: 3.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1496 LKRFK----LHGILCDDMGLGKTLQAsaIVASDAAERRGSTDELdvfpsIIVCPSTLVGHWAFEIEKYI----DLSLLSV 1567
Cdd:cd18069    20 LERYKgssgFGCILAHSMGLGKTLQV--ISFLDVLLRHTGAKTV-----LAIVPVNTLQNWLSEFNKWLpppeALPNVRP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1568 LQY--------VGSAQDRVSLREQFNNHN-VIITSYDVVR----KDVdyltqfswnyCILDEGHIIKNAKSKITAAVKQL 1634
Cdd:cd18069    93 RPFkvfilndeHKTTAARAKVIEDWVKDGgVLLMGYEMFRlrpgPDV----------VICDEGHRIKNCHASTSQALKNI 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 334185970 1635 KAQHRLILSGTPIQNNIMELWSLFDFLMPGFLGTERQFQASYGKPLL 1681
Cdd:cd18069   163 RSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1482-1663 4.34e-21

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: 94.31  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQAsaIVASDAAERRGSTDEldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQT--IVFLYSLYKEGHTKG----PFLVSAPLSTIINWEREFQMWA- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVSLREQ---FNNH-------------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHI 1619
Cdd:cd18055    74 -PDFYVVTYTGDKDSRAIIRENefsFDDNavkggkkafkmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEAHR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334185970 1620 IKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMP 1663
Cdd:cd18055   153 LKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1482-1663 8.15e-21

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: 93.59  E-value: 8.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINWLGFLKRFKLHGILCDDMGLGKTLQASAIVASDAAERRGSTdeldvfPSIIVCPSTLVGHWAFEIEKYId 1561
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKG------PYLVSAPLSTIINWEREFEMWA- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 lSLLSVLQYVGSAQDRVSLREQ---FNNH-------------------NVIITSYDVVRKDVDYLTQFSWNYCILDEGHI 1619
Cdd:cd18057    74 -PDFYVVTYTGDKESRSVIRENefsFEDNairsgkkvfrmkkeaqikfHVLLTSYELITIDQAILGSIEWACLVVDEAHR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334185970 1620 IKNAKSKITAAVKQLKAQHRLILSGTPIQNNIMELWSLFDFLMP 1663
Cdd:cd18057   153 LKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1482-1665 5.69e-18

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: 84.65  E-value: 5.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGInwLGFLKRFKLHGILCDDMGLGKTLQASAIVAsdAAERRGSTDeldvfPSIIVCPSTLVGHWAFEIEKyiD 1561
Cdd:cd18011     1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLIIK--ELLLRGDAK-----RVLILCPASLVEQWQDELQD--K 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1562 LSLLSVLQYVGSA-QDRVSLREQFNNHNVIITSYDVVRKDVDYLTQFS---WNYCILDEGHIIKNA----KSKITAAVKQ 1633
Cdd:cd18011    70 FGLPFLILDRETAaQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLseeWDLVVVDEAHKLRNSgggkETKRYKLGRL 149
                         170       180       190
                  ....*....|....*....|....*....|....
gi 334185970 1634 L--KAQHRLILSGTPIQNNIMELWSLFDFLMPGF 1665
Cdd:cd18011   150 LakRARHVLLLTATPHNGKEEDFRALLSLLDPGR 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1862-1961 3.53e-17

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: 79.18  E-value: 3.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970  1862 HRVLIFAQHKALLDiiEKDLFQAhmKSVTYMRLDGSVVPEKRFEIVKAFNsDPTIDVLLlTTHVGGLGLNLTSADTLVFM 1941
Cdd:pfam00271   16 GKVLIFSQTKKTLE--AELLLEK--EGIKVARLHGDLSQEEREEILEDFR-KGKIDVLV-ATDVAERGLDLPDVDLVINY 89
                           90       100
                   ....*....|....*....|
gi 334185970  1942 EHDWNPMRDHQAMDRAHRLG 1961
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1875-1961 3.60e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 72.24  E-value: 3.60e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970   1875 DIIEKDLfqaHMKSVTYMRLDGSVVPEKRFEIVKAFNSDPTidVLLLTTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAM 1954
Cdd:smart00490    1 EELAELL---KELGIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75

                    ....*..
gi 334185970   1955 DRAHRLG 1961
Cdd:smart00490   76 GRAGRAG 82
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1482-1646 7.97e-10

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: 59.24  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGI-NWLGFLKrfKLHGILCDDMGLGKTLQASAIVAsdaaerrgstdELDVFPSIIVCPST-LVGHWAfeiEKY 1559
Cdd:cd17926     1 LRPYQEEALeAWLAHKN--NRRGILVLPTGSGKTLTALALIA-----------YLKELRTLIVVPTDaLLDQWK---ERF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1560 IDLSLLSVLQYVGSaqdrvSLREQFNNHNVIITSYDVVR---KDVDYLTQFsWNYCILDEGHIIkNAKSkITAAVKQLKA 1636
Cdd:cd17926    65 EDFLGDSSIGLIGG-----GKKKDFDDANVVVATYQSLSnlaEEEKDLFDQ-FGLLIVDEAHHL-PAKT-FSEILKELNA 136
                         170
                  ....*....|
gi 334185970 1637 QHRLILSGTP 1646
Cdd:cd17926   137 KYRLGLTATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1477-1646 5.71e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.19  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1477 ELKVQLRRYQQEGIN-WLGFLKRFKLHGILCDDMGLGKTlqasaIVASDAAERrgstdELDVFPSIIVCPST-LVGHWAF 1554
Cdd:COG1061    76 GTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKT-----VLALALAAE-----LLRGKRVLVLVPRReLLEQWAE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1555 EIEKYIDLSLlsvlqyvgsaqdrVSLREQFNNHNVIITSYDVVRKDVDY-LTQFSWNYCILDEGHiikNAKSKI-TAAVK 1632
Cdd:COG1061   146 ELRRFLGDPL-------------AGGGKKDSDAPITVATYQSLARRAHLdELGDRFGLVIIDEAH---HAGAPSyRRILE 209
                         170
                  ....*....|....
gi 334185970 1633 QLKAQHRLILSGTP 1646
Cdd:COG1061   210 AFPAAYRLGLTATP 223
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1482-1661 7.72e-09

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: 58.13  E-value: 7.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1482 LRRYQQEGINwlgFLKRFKLHGILCDdMGLGKT---LQASAIVASDAAERrgstdeldvfPSIIVCPSTLVGH-WAFEIE 1557
Cdd:cd18013     1 PHPYQKVAIN---FIIEHPYCGLFLD-MGLGKTvttLTALSDLQLDDFTR----------RVLVIAPLRVARStWPDEVE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1558 KYIDLSLLSVLQYVGSAQDRVSLREqfNNHNVIITSYDVVRKDVDYLT-QFSWNYCILDEGHIIKNAKSKITAAVKQLKA 1636
Cdd:cd18013    67 KWNHLRNLTVSVAVGTERQRSKAAN--TPADLYVINRENLKWLVNKSGdPWPFDMVVIDELSSFKSPRSKRFKALRKVRP 144
                         170       180
                  ....*....|....*....|....*..
gi 334185970 1637 Q-HRLI-LSGTPIQNNIMELWSLFDFL 1661
Cdd:cd18013   145 ViKRLIgLTGTPSPNGLMDLWAQIALL 171
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
1822-1988 6.86e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.82  E-value: 6.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1822 ITELHKVQHsPKLVALQEILEEcGIGSDASSsdgtlsvgqhRVLIFAQHKALLDIIEKDLFQAHMKSVTYM---RLDGS- 1897
Cdd:COG1111   326 LAEEADIEH-PKLSKLREILKE-QLGTNPDS----------RIIVFTQYRDTAEMIVEFLSEPGIKAGRFVgqaSKEGDk 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1898 -VVPEKRFEIVKAFnSDPTIDVLLlTTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQKRVVnVhrLIMRGT 1976
Cdd:COG1111   394 gLTQKEQIEILERF-RAGEFNVLV-ATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVV-V--LIAKGT 468
                         170
                  ....*....|....
gi 334185970 1977 LEEKV--MSLQKFK 1988
Cdd:COG1111   469 RDEAYywSSRRKEK 482
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
1477-1645 1.79e-04

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 44.21  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1477 ELK--VQLRRYQQEGINWLgFLKRFKLHGILCDDMGLGKTLqaSAIVAsdAAERRGSTdeldvfpsIIVCPSTL-VGHWA 1553
Cdd:cd18029     2 DLKpsTQLRPYQEKALSKM-FGNGRARSGVIVLPCGAGKTL--VGITA--ACTIKKST--------LVLCTSAVsVEQWR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1554 FEIEKYIDLSLLSVLQYVGSAqdrvslREQFNNHNVIITSYDVVR----------KDVDYLTQFSWNYCILDEGHIIKNA 1623
Cdd:cd18029    69 RQFLDWTTIDDEQIGRFTSDK------KEIFPEAGVTVSTYSMLAntrkrspeseKFMEFITEREWGLIILDEVHVVPAP 142
                         170       180
                  ....*....|....*....|..
gi 334185970 1624 KSKITAavKQLKAQHRLILSGT 1645
Cdd:cd18029   143 MFRRVL--TLQKAHCKLGLTAT 162
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
1502-1620 2.55e-04

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 43.16  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334185970 1502 HGILCDDMGLGKTLQASAIVASDAAERRgstdeldvFPSIIVCP-STLVGHWAFEIEKYIDLSLlsvlqYVGSAQDRVSL 1580
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKKG--------KKVLVLVPtKALALQTAERLRELFGPGI-----RVAVLVGGSSA 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 334185970 1581 REQFNNHN----VIITSYDVVRKDVDYLTQFS---WNYCILDEGHII 1620
Cdd:cd00046    70 EEREKNKLgdadIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAL 116
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1919-1972 4.80e-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: 37.68  E-value: 4.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 334185970 1919 LLLTTHVGGLGLNLTSADTLVFMEHDWNPMRDHQAMDRAHRLGQkRVVNVHRLI 1972
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
 
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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