NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50310019|ref|XP_455023|]
View 

uncharacterized protein KLLA0_E23717g [Kluyveromyces lactis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1182-1794 9.19e-164

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 516.70  E-value: 9.19e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1182 DRQGVVELLYHLSIQLESDILPYVVFLIVPLLGRMSDSNEDIRKLATTTFASIIKLVPLEAGIAAPVGLSEELLRGREKE 1261
Cdd:COG0553  134 LLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELEL 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1262 RDFIQQM---MDPSKAKPFKLPVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqylrsedyk 1338
Cdd:COG0553  214 LAEAAVDafrLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLE---------- 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1339 ktQSEKTRPLPSLIICPPSLTGHWEQEFQQYSPTLNVLVYAGgPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYN 1418
Cdd:COG0553  284 --LKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWD 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1419 YCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIassrnsktss 1498
Cdd:COG0553  361 LVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------- 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1499 keQEAGALALEALHKQVLPFMLRRLKEEVLSDLPPKIIQDYYCELSDLQKQLYNDFVKKqknvVEKDIENTAEVENKQHI 1578
Cdd:COG0553  431 --EKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLI 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1579 FQALQYMRKLCNHPSLVLNSSHPQfqqvqsylsqtgmdlhdIGHAPKLEALKTLLLECgigiqdvekksnknpsidnVIS 1658
Cdd:COG0553  505 LAALTRLRQICSHPALLLEEGAEL-----------------SGRSAKLEALLELLEEL-------------------LAE 548
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1659 QHRVLIFCQLKDMLDMVENDLLKKHLPSVTfmrLDGSVDSRDRQKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIF 1738
Cdd:COG0553  549 GEKVLVFSQFTDTLDLLEERLEERGIEYAY---LHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIH 625
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 50310019 1739 VEHDWNPMNDLQAMDRAHRLGQKKVVNVYRIITKGTLEEKIMGLQKFKMNIASTIV 1794
Cdd:COG0553  626 YDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
636-1073 2.33e-153

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: 479.05  E-value: 2.33e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    636 VNSKGQEKSIDFVFSKYLTSILHLLITPIGEqgknyAMDIQHITKPSSSYLINLERKRSNATANSSNVTATY-----SHR 710
Cdd:pfam12054    6 LRSLKPPEALLHAFCPHLSPWLTLLMTPIGV-----PMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSpgrqgSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    711 VNIDSPMLAGDVTLIGLDIIYNTRVKAAKTLGLTLSFFQESTLRSFFENVLASCLDLPYSTPRMLVAIVLSSFCTNWKEN 790
Cdd:pfam12054   81 HNVDKPMIGGDVTLVGMDVVIRTRIAAAKALGLLLSYWPEESPLDFFTKLLLPYLNSPSALQRLLAAIIIEEWAKNCKKE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    791 QqhNPVPAFMSTLFSSTFLGFLTGATTLPVFRELTPILKALRTQCQSLMTTFVDVGMLPPQRVPAIAIIVKGEPEAGPEA 870
Cdd:pfam12054  161 K--SSSVSTLPETLSEKLLEILENPSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKLAVVVQGEPEAGPGA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    871 FSIQTAEKVQTEFYAKLFSLLPNAQKILAQKPLEDARYRVSLAIESAKESERERQLEVLSSYASAVMLIDGLPNKLNPLI 950
Cdd:pfam12054  239 FSIEQAEKLVGEDYDKLKKSLSPKQKLLALQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPII 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    951 RSLMDNVKSEKHTILQQTSGDSIVNLISELVSAQKHNVANKIVKNLCGFICVDTSEVPEF--DGTNTTVITTLVKEAASL 1028
Cdd:pfam12054  319 KPLMDSIKKEENEELQQRSADALAHLIDLCVDRGKPGPNDKIVKNLCTFLCVDTSETPEFhpNAKLTDGILTLRKEEDKA 398
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 50310019   1029 SLQEDSEMKKMTESARIKRKGGMHTLMKLLIKFQEKTLEVVPQLK 1073
Cdd:pfam12054  399 DHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLW 443
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1182-1794 9.19e-164

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 516.70  E-value: 9.19e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1182 DRQGVVELLYHLSIQLESDILPYVVFLIVPLLGRMSDSNEDIRKLATTTFASIIKLVPLEAGIAAPVGLSEELLRGREKE 1261
Cdd:COG0553  134 LLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELEL 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1262 RDFIQQM---MDPSKAKPFKLPVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqylrsedyk 1338
Cdd:COG0553  214 LAEAAVDafrLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLE---------- 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1339 ktQSEKTRPLPSLIICPPSLTGHWEQEFQQYSPTLNVLVYAGgPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYN 1418
Cdd:COG0553  284 --LKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWD 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1419 YCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIassrnsktss 1498
Cdd:COG0553  361 LVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------- 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1499 keQEAGALALEALHKQVLPFMLRRLKEEVLSDLPPKIIQDYYCELSDLQKQLYNDFVKKqknvVEKDIENTAEVENKQHI 1578
Cdd:COG0553  431 --EKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLI 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1579 FQALQYMRKLCNHPSLVLNSSHPQfqqvqsylsqtgmdlhdIGHAPKLEALKTLLLECgigiqdvekksnknpsidnVIS 1658
Cdd:COG0553  505 LAALTRLRQICSHPALLLEEGAEL-----------------SGRSAKLEALLELLEEL-------------------LAE 548
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1659 QHRVLIFCQLKDMLDMVENDLLKKHLPSVTfmrLDGSVDSRDRQKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIF 1738
Cdd:COG0553  549 GEKVLVFSQFTDTLDLLEERLEERGIEYAY---LHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIH 625
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 50310019 1739 VEHDWNPMNDLQAMDRAHRLGQKKVVNVYRIITKGTLEEKIMGLQKFKMNIASTIV 1794
Cdd:COG0553  626 YDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
636-1073 2.33e-153

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: 479.05  E-value: 2.33e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    636 VNSKGQEKSIDFVFSKYLTSILHLLITPIGEqgknyAMDIQHITKPSSSYLINLERKRSNATANSSNVTATY-----SHR 710
Cdd:pfam12054    6 LRSLKPPEALLHAFCPHLSPWLTLLMTPIGV-----PMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSpgrqgSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    711 VNIDSPMLAGDVTLIGLDIIYNTRVKAAKTLGLTLSFFQESTLRSFFENVLASCLDLPYSTPRMLVAIVLSSFCTNWKEN 790
Cdd:pfam12054   81 HNVDKPMIGGDVTLVGMDVVIRTRIAAAKALGLLLSYWPEESPLDFFTKLLLPYLNSPSALQRLLAAIIIEEWAKNCKKE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    791 QqhNPVPAFMSTLFSSTFLGFLTGATTLPVFRELTPILKALRTQCQSLMTTFVDVGMLPPQRVPAIAIIVKGEPEAGPEA 870
Cdd:pfam12054  161 K--SSSVSTLPETLSEKLLEILENPSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKLAVVVQGEPEAGPGA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    871 FSIQTAEKVQTEFYAKLFSLLPNAQKILAQKPLEDARYRVSLAIESAKESERERQLEVLSSYASAVMLIDGLPNKLNPLI 950
Cdd:pfam12054  239 FSIEQAEKLVGEDYDKLKKSLSPKQKLLALQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPII 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    951 RSLMDNVKSEKHTILQQTSGDSIVNLISELVSAQKHNVANKIVKNLCGFICVDTSEVPEF--DGTNTTVITTLVKEAASL 1028
Cdd:pfam12054  319 KPLMDSIKKEENEELQQRSADALAHLIDLCVDRGKPGPNDKIVKNLCTFLCVDTSETPEFhpNAKLTDGILTLRKEEDKA 398
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 50310019   1029 SLQEDSEMKKMTESARIKRKGGMHTLMKLLIKFQEKTLEVVPQLK 1073
Cdd:pfam12054  399 DHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLW 443
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1287-1522 6.34e-139

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: 430.62  E-value: 6.34e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRSEDYKktqsekTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFN------SENLPSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPT--LNVLVYAGGPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLINS 1444
Cdd:cd17999   75 KKYFPNafLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310019 1445 NHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQVLPFMLRR 1522
Cdd:cd17999  155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1280-1780 1.47e-91

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 322.52  E-value: 1.47e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1280 PVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsEDYKKTQSektrplPSLIICPPSLT 1359
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLG---YL--HEYRGITG------PHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1360 GHWEQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTA---DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLA 1436
Cdd:PLN03142  232 GNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAgkfDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1437 KAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiASSRNsktssKEQEagalALEALHKQVL 1516
Cdd:PLN03142  312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ---ISGEN-----DQQE----VVQQLHKVLR 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1517 PFMLRRLKEEVLSDLPPKIIQDYYCELSDLQKQLYndfvkkqKNVVEKDIE--NTAEvENKQHIFQALQyMRKLCNHPSL 1594
Cdd:PLN03142  380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY-------KALLQKDLDvvNAGG-ERKRLLNIAMQ-LRKCCNHPYL 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1595 vlnsshpqFQQVQSYLSQTGMDlHDIGHAPKLEALKTLLLECGigiqdvEKKSnknpsidnvisqhRVLIFCQLKDMLDM 1674
Cdd:PLN03142  451 --------FQGAEPGPPYTTGE-HLVENSGKMVLLDKLLPKLK------ERDS-------------RVLIFSQMTRLLDI 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1675 VENDLLKKHLPsvtFMRLDGSVDSRDRQKVVRKFNEDPSID-CLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMD 1753
Cdd:PLN03142  503 LEDYLMYRGYQ---YCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQD 579
                         490       500
                  ....*....|....*....|....*..
gi 50310019  1754 RAHRLGQKKVVNVYRIITKGTLEEKIM 1780
Cdd:PLN03142  580 RAHRIGQKKEVQVFRFCTEYTIEEKVI 606
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1290-1595 2.92e-79

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: 263.78  E-value: 2.92e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1290 YQQDGVNWLAFL-NKYHLHGILCDDMGLGKTLQTICIIAsdqYLRSEDykktqseKTRPLPSLIICPPSLTGHWEQEFQQ 1368
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL---YLKHVD-------KNWGGPTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1369 Y--SPTLNVLVYAGGPSVRYPL---QGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLIN 1443
Cdd:pfam00176   71 WvsPPALRVVVLHGNKRPQERWkndPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1444 SNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKeqeagalaleaLHKQVLPFMLRRL 1523
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50310019   1524 KEEVLSDLPPKIIQDYYCELSDLQKQLYNDFVKKqknvVEKDIENTAEVENKQH--IFQALQYMRKLCNHPSLV 1595
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLK----KDLNAIKTGEGGREIKasLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
1286-1482 2.99e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.18  E-value: 2.99e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    1286 TLRKYQQDGVNWLAFLNKyhlHGILCDDMGLGKTLQTICIIAsdQYLRSEDYKKTqsektrplpsLIICP-PSLTGHWEQ 1364
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL--EALKRGKGGRV----------LVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    1365 EFQQYSP--TLNVLVYAGGPSVRYPLQGQV-PTADIVVTSYDVARNDV--DFLKKYDYNYCVLDEGHIIKNS--QSKLAK 1437
Cdd:smart00487   73 ELKKLGPslGLKVVGLYGGDSKREQLRKLEsGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 50310019    1438 AVKLINSN-HRLVLTGTP---IQNNVVELWSLFDFLMPGFLGTEKMFQE 1482
Cdd:smart00487  153 LLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1182-1794 9.19e-164

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 516.70  E-value: 9.19e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1182 DRQGVVELLYHLSIQLESDILPYVVFLIVPLLGRMSDSNEDIRKLATTTFASIIKLVPLEAGIAAPVGLSEELLRGREKE 1261
Cdd:COG0553  134 LLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELEL 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1262 RDFIQQM---MDPSKAKPFKLPVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqylrsedyk 1338
Cdd:COG0553  214 LAEAAVDafrLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLE---------- 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1339 ktQSEKTRPLPSLIICPPSLTGHWEQEFQQYSPTLNVLVYAGgPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYN 1418
Cdd:COG0553  284 --LKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDG-TRERAKGANPFEDADLVITSYGLLRRDIELLAAVDWD 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1419 YCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIassrnsktss 1498
Cdd:COG0553  361 LVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI---------- 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1499 keQEAGALALEALHKQVLPFMLRRLKEEVLSDLPPKIIQDYYCELSDLQKQLYNDFVKKqknvVEKDIENTAEVENKQHI 1578
Cdd:COG0553  431 --EKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEY----LRRELEGAEGIRRRGLI 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1579 FQALQYMRKLCNHPSLVLNSSHPQfqqvqsylsqtgmdlhdIGHAPKLEALKTLLLECgigiqdvekksnknpsidnVIS 1658
Cdd:COG0553  505 LAALTRLRQICSHPALLLEEGAEL-----------------SGRSAKLEALLELLEEL-------------------LAE 548
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1659 QHRVLIFCQLKDMLDMVENDLLKKHLPSVTfmrLDGSVDSRDRQKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIF 1738
Cdd:COG0553  549 GEKVLVFSQFTDTLDLLEERLEERGIEYAY---LHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIH 625
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 50310019 1739 VEHDWNPMNDLQAMDRAHRLGQKKVVNVYRIITKGTLEEKIMGLQKFKMNIASTIV 1794
Cdd:COG0553  626 YDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
636-1073 2.33e-153

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: 479.05  E-value: 2.33e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    636 VNSKGQEKSIDFVFSKYLTSILHLLITPIGEqgknyAMDIQHITKPSSSYLINLERKRSNATANSSNVTATY-----SHR 710
Cdd:pfam12054    6 LRSLKPPEALLHAFCPHLSPWLTLLMTPIGV-----PMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSpgrqgSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    711 VNIDSPMLAGDVTLIGLDIIYNTRVKAAKTLGLTLSFFQESTLRSFFENVLASCLDLPYSTPRMLVAIVLSSFCTNWKEN 790
Cdd:pfam12054   81 HNVDKPMIGGDVTLVGMDVVIRTRIAAAKALGLLLSYWPEESPLDFFTKLLLPYLNSPSALQRLLAAIIIEEWAKNCKKE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    791 QqhNPVPAFMSTLFSSTFLGFLTGATTLPVFRELTPILKALRTQCQSLMTTFVDVGMLPPQRVPAIAIIVKGEPEAGPEA 870
Cdd:pfam12054  161 K--SSSVSTLPETLSEKLLEILENPSRPPYYRELVPYLTRLRTQCQQLLNTFRDVGKVSQSKLPKLAVVVQGEPEAGPGA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    871 FSIQTAEKVQTEFYAKLFSLLPNAQKILAQKPLEDARYRVSLAIESAKESERERQLEVLSSYASAVMLIDGLPNKLNPLI 950
Cdd:pfam12054  239 FSIEQAEKLVGEDYDKLKKSLSPKQKLLALQQLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALVALKGLPKKLNPII 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    951 RSLMDNVKSEKHTILQQTSGDSIVNLISELVSAQKHNVANKIVKNLCGFICVDTSEVPEF--DGTNTTVITTLVKEAASL 1028
Cdd:pfam12054  319 KPLMDSIKKEENEELQQRSADALAHLIDLCVDRGKPGPNDKIVKNLCTFLCVDTSETPEFhpNAKLTDGILTLRKEEDKA 398
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 50310019   1029 SLQEDSEMKKMTESARIKRKGGMHTLMKLLIKFQEKTLEVVPQLK 1073
Cdd:pfam12054  399 DHADAAKFEEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLW 443
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1287-1522 6.34e-139

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: 430.62  E-value: 6.34e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRSEDYKktqsekTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFN------SENLPSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPT--LNVLVYAGGPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLINS 1444
Cdd:cd17999   75 KKYFPNafLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310019 1445 NHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQVLPFMLRR 1522
Cdd:cd17999  155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1283-1524 3.31e-93

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: 300.64  E-value: 3.31e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1283 IKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQylrsedykktqsEKTRPLPSLIICPPSLTGHW 1362
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRK------------EEGRKGPSLVVAPTSLIYNW 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1363 EQEFQQYSPTLNVLVYAGGPSVRyPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLI 1442
Cdd:cd18012   69 EEEAAKFAPELKVLVIHGTKRKR-EKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1443 NSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKtsskeqeagalALEALHKQVLPFMLRR 1522
Cdd:cd18012  148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFILRR 216

                 ..
gi 50310019 1523 LK 1524
Cdd:cd18012  217 LK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1280-1780 1.47e-91

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 322.52  E-value: 1.47e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1280 PVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsEDYKKTQSektrplPSLIICPPSLT 1359
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLG---YL--HEYRGITG------PHMVVAPKSTL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1360 GHWEQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTA---DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLA 1436
Cdd:PLN03142  232 GNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAgkfDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLS 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1437 KAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiASSRNsktssKEQEagalALEALHKQVL 1516
Cdd:PLN03142  312 KTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ---ISGEN-----DQQE----VVQQLHKVLR 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1517 PFMLRRLKEEVLSDLPPKIIQDYYCELSDLQKQLYndfvkkqKNVVEKDIE--NTAEvENKQHIFQALQyMRKLCNHPSL 1594
Cdd:PLN03142  380 PFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYY-------KALLQKDLDvvNAGG-ERKRLLNIAMQ-LRKCCNHPYL 450
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1595 vlnsshpqFQQVQSYLSQTGMDlHDIGHAPKLEALKTLLLECGigiqdvEKKSnknpsidnvisqhRVLIFCQLKDMLDM 1674
Cdd:PLN03142  451 --------FQGAEPGPPYTTGE-HLVENSGKMVLLDKLLPKLK------ERDS-------------RVLIFSQMTRLLDI 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019  1675 VENDLLKKHLPsvtFMRLDGSVDSRDRQKVVRKFNEDPSID-CLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMD 1753
Cdd:PLN03142  503 LEDYLMYRGYQ---YCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQD 579
                         490       500
                  ....*....|....*....|....*..
gi 50310019  1754 RAHRLGQKKVVNVYRIITKGTLEEKIM 1780
Cdd:PLN03142  580 RAHRIGQKKEVQVFRFCTEYTIEEKVI 606
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1290-1595 2.92e-79

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: 263.78  E-value: 2.92e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1290 YQQDGVNWLAFL-NKYHLHGILCDDMGLGKTLQTICIIAsdqYLRSEDykktqseKTRPLPSLIICPPSLTGHWEQEFQQ 1368
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLL---YLKHVD-------KNWGGPTLIVVPLSLLHNWMNEFER 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1369 Y--SPTLNVLVYAGGPSVRYPL---QGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLIN 1443
Cdd:pfam00176   71 WvsPPALRVVVLHGNKRPQERWkndPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1444 SNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKeqeagalaleaLHKQVLPFMLRRL 1523
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSR-----------LHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50310019   1524 KEEVLSDLPPKIIQDYYCELSDLQKQLYNDFVKKqknvVEKDIENTAEVENKQH--IFQALQYMRKLCNHPSLV 1595
Cdd:pfam00176  220 KKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLK----KDLNAIKTGEGGREIKasLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1287-1474 1.33e-70

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: 234.38  E-value: 1.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRSEdykktqseKTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLA---YLLKE--------GKERGPVLVVCPLSVLENWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPLQGQ--VPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLINS 1444
Cdd:cd17919   70 EKWTPDLRVVVYHGSQRERAQIRAKekLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRA 149
                        170       180       190
                 ....*....|....*....|....*....|
gi 50310019 1445 NHRLVLTGTPIQNNVVELWSLFDFLMPGFL 1474
Cdd:cd17919  150 KRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1284-1524 8.04e-61

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: 208.78  E-value: 8.04e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1284 KATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRsedykktqsEKTRPLPSLIICPPSLTGHWE 1363
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA---HLR---------ERGVWGPFLVIAPLSTLPNWV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1364 QEFQQYSPTLNVLVYAGGPSVR-------YPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLA 1436
Cdd:cd18009   69 NEFARFTPSVPVLLYHGTKEERerlrkkiMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1437 KAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiASSRNSKTSSKEQEAGALA---LEALHK 1513
Cdd:cd18009  149 QELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFD---FSSLSDNAADISNLSEEREqniVHMLHA 225
                        250
                 ....*....|.
gi 50310019 1514 QVLPFMLRRLK 1524
Cdd:cd18009  226 ILKPFLLRRLK 236
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1287-1522 4.59e-59

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 203.37  E-value: 4.59e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqYLRSEDYKKtqsektrplpSLIICPPSLTGHWEQEF 1366
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSG--MFDSGLIKS----------VLVVMPTSLIPHWVKEF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGG-PSVRYPLQGQVPTA-DIVVTSYDVARNDVDFLKKYD-----YNYCVLDEGHIIKNSQSKLAKAV 1439
Cdd:cd18001   69 AKWTPGLRVKVFHGTsKKERERNLERIQRGgGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1440 KLINSNHRLVLTGTPIQNNVVELWSLFDFLMPG-FLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQVLPF 1518
Cdd:cd18001  149 REIPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPY 228

                 ....
gi 50310019 1519 MLRR 1522
Cdd:cd18001  229 FLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1286-1524 1.44e-56

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: 196.44  E-value: 1.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1286 TLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRseDYKKTQSektrplPSLIICPPSLTGHWEQE 1365
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLIT---YLM--EKKKNNG------PYLVIVPLSTLSNWVSE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSPTLNVLVYAGGPSVRYPLQGQVPTA--DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVK-LI 1442
Cdd:cd17996   72 FEKWAPSVSKIVYKGTPDVRKKLQSQIRAGkfNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNtYY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1443 NSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQVLPFMLRR 1522
Cdd:cd17996  152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRR 231

                 ..
gi 50310019 1523 LK 1524
Cdd:cd17996  232 LK 233
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1284-1524 2.93e-54

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: 189.46  E-value: 2.93e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1284 KATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRseDYKKTQSektrplPSLIICPPSLTGHWE 1363
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG---YLK--HYKNING------PHLIIVPKSTLDNWM 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1364 QEFQQYSPTLNVLVYAGGPSVRYP-LQGQVPTA--DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVK 1440
Cdd:cd17997   70 REFKRWCPSLRVVVLIGDKEERADiIRDVLLPGkfDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1441 LINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFakpiassrNSKTSSKEQEAgalALEALHKQVLPFML 1520
Cdd:cd17997  150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF--------NVNNCDDDNQE---VVQRLHKVLRPFLL 218

                 ....
gi 50310019 1521 RRLK 1524
Cdd:cd17997  219 RRIK 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1622-1770 6.06e-53

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 181.91  E-value: 6.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1622 HAPKLEALKTLLLECgigiqdvekksnknpsidnVISQHRVLIFCQLKDMLDMVENDLLKKHlpsVTFMRLDGSVDSRDR 1701
Cdd:cd18793    9 VSGKLEALLELLEEL-------------------REPGEKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKER 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50310019 1702 QKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRAHRLGQKKVVNVYRII 1770
Cdd:cd18793   67 QKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1287-1522 2.06e-52

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: 183.99  E-value: 2.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFlNKYHLHG-ILCDDMGLGKTLQTICIIasdQYLRsedykktQSEKTRPlPSLIICPPSLTGHWEQE 1365
Cdd:cd17995    1 LRDYQLEGVNWLLF-NWYNRRNcILADEMGLGKTIQSIAFL---EHLY-------QVEGIRG-PFLVIAPLSTIPNWQRE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSpTLNVLVYAGGPSVR--------YPLQGQVPTA------DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNS 1431
Cdd:cd17995   69 FETWT-DMNVVVYHGSGESRqiiqqyemYFKDAQGRKKkgvykfDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1432 QSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFakpiassrnSKTSSKEQeagalaLEAL 1511
Cdd:cd17995  148 NSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF---------GDLKTAEQ------VEKL 212
                        250
                 ....*....|.
gi 50310019 1512 HKQVLPFMLRR 1522
Cdd:cd17995  213 QALLKPYMLRR 223
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1287-1522 2.89e-51

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: 180.63  E-value: 2.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsedykktQSEKTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLA---HL--------ACEKGNWGPHLIVVPTSVMLNWEMEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPL-QG--QVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLIN 1443
Cdd:cd18003   70 KRWCPGFKILTYYGSAKERKLKrQGwmKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50310019 1444 SNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIassrnSKTSSKEQEAGALALEALHKQVLPFMLRR 1522
Cdd:cd18003  150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL-----TAMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1286-1522 2.99e-51

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: 180.63  E-value: 2.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1286 TLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRsedykktqseKTRPL--PSLIICPPSLTGHWE 1363
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS---YLF----------HSQQQygPFLVVVPLSTMPAWQ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1364 QEFQQYSPTLNVLVYAGGPSVR--------YPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKL 1435
Cdd:cd17993   68 REFAKWAPDMNVIVYLGDIKSRdtireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1436 AKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERfakpiassrnsktSSKEQEAGalaLEALHKQV 1515
Cdd:cd17993  148 YEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE-------------HDEEQEKG---IADLHKEL 211

                 ....*..
gi 50310019 1516 LPFMLRR 1522
Cdd:cd17993  212 EPFILRR 218
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1287-1474 3.74e-50

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: 176.36  E-value: 3.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYlrsedykktqSEKTRPlPSLIICPPSLTGHWEQEF 1366
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHH----------SKLGLG-PSLIVCPATVLKQWVKEF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLV-YAGGPSVRYP------------LQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQS 1433
Cdd:cd18000   70 HRWWPPFRVVVlHSSGSGTGSEeklgsierksqlIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 50310019 1434 KLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFL 1474
Cdd:cd18000  150 EITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1287-1522 5.65e-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: 177.86  E-value: 5.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLaflnkYHLHGILCDDMGLGKTLQTICIIASDQYLRSEDYKKTQSEKTRPLP------SLIICPPSLTG 1360
Cdd:cd18008    1 LLPYQKQGLAWM-----LPRGGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSDPKKlylsktTLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1361 HWEQEFQQY--SPTLNVLVYAGGPsvRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNY----------------CVL 1422
Cdd:cd18008   76 QWKDEIEKHtkPGSLKVYVYHGSK--RIKSIEELSDYDIVITTYGTLASEFPKNKKGGGRDskekeasplhrirwyrVIL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1423 DEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSktsskeqe 1502
Cdd:cd18008  154 DEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-------- 225
                        250       260
                 ....*....|....*....|
gi 50310019 1503 agalALEALHKQVLPFMLRR 1522
Cdd:cd18008  226 ----ALERLQALLKPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1287-1522 1.35e-49

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 176.80  E-value: 1.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAS---------DQYLRSEDYKKTQSEKTRPLPSLIICPPS 1357
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAvlgktgtrrDRENNRPRFKKKPPASSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1358 LTGHWEQEFQQYSpTLNVLVYAGG-----PSVRYPlQGQVptaDIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQ 1432
Cdd:cd18005   81 VLYNWKDELDTWG-HFEVGVYHGSrkddeLEGRLK-AGRL---EVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1433 SKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALH 1512
Cdd:cd18005  156 SKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELA 235
                        250
                 ....*....|
gi 50310019 1513 KQVLPFMLRR 1522
Cdd:cd18005  236 VKLSKFFLRR 245
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1287-1471 4.75e-48

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: 170.26  E-value: 4.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRsedykktqsEKTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA---YLK---------EIGIPGPHLVVVPSSTLDNWLREF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGG----PSVRYPLQGQVPTADIVVTSYDVA---RNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAV 1439
Cdd:cd17998   69 KRWCPSLKVEPYYGSqeerKHLRYDILKGLEDFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHL 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 50310019 1440 KLINSNHRLVLTGTPIQNNVVELWSLFDFLMP 1471
Cdd:cd17998  149 MTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1287-1522 1.65e-46

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: 167.30  E-value: 1.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsedykktQSEKTRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLA---HL--------AEEHNIWGPFLVIAPASTLHNWQQEI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPL-----QGQVPTAD----IVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAK 1437
Cdd:cd18002   70 SRFVPQFKVLPYWGNPKDRKVLrkfwdRKNLYTRDapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1438 AVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEagalaLEALHKQVLP 1517
Cdd:cd18002  150 TLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHMILKP 224

                 ....*
gi 50310019 1518 FMLRR 1522
Cdd:cd18002  225 FMLRR 229
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1287-1522 2.01e-45

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: 164.77  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWL----AFLNKYHLHG-ILCDDMGLGKTLQTICIIASdqYLRSEDYKKTQSEKtrplpSLIICPPSLTGH 1361
Cdd:cd18004    1 LRPHQREGVQFLydclTGRRGYGGGGaILADEMGLGKTLQAIALVWT--LLKQGPYGKPTAKK-----ALIVCPSSLVGN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1362 WEQEFQQYSP--TLNVLVYAGGPSVRY---PLQGQVPTADIVVTSYDVARNDVD-FLKKYDYNYCVLDEGHIIKNSQSKL 1435
Cdd:cd18004   74 WKAEFDKWLGlrRIKVVTADGNAKDVKaslDFFSSASTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1436 AKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQV 1515
Cdd:cd18004  154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                 ....*..
gi 50310019 1516 LPFMLRR 1522
Cdd:cd18004  234 SRFILRR 240
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1287-1522 1.32e-44

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: 161.45  E-value: 1.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsedyKKTQSEktrPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLW---YL-----AGRLKL---LGPFLVLCPLSVLDNWKEEL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPLQGQV---PTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLIN 1443
Cdd:cd18006   70 NRFAPDLSVITYMGDKEKRLDLQQDIkstNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50310019 1444 SNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMfqERFAKpiassrnsktSSKEQEAGALALEALHKQVLPFMLRR 1522
Cdd:cd18006  150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKL--DDFIK----------AYSETDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1287-1534 5.16e-42

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: 155.21  E-value: 5.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRSedykktqsektRPLPSLIICPPSLTGHWEQEF 1366
Cdd:cd18064   16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRN-----------IPGPHMVLVPKSTLHNWMAEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPLQGQVPTA---DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLIN 1443
Cdd:cd18064   85 KRWVPTLRAVCLIGDKDQRAAFVRDVLLPgewDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1444 SNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFakpiaSSRNSKTSSKeqeagalALEALHKQVLPFMLRRL 1523
Cdd:cd18064  165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF-----DTNNCLGDQK-------LVERLHMVLRPFLLRRI 232
                        250
                 ....*....|.
gi 50310019 1524 KEEVLSDLPPK 1534
Cdd:cd18064  233 KADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1280-1524 6.88e-40

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: 148.63  E-value: 6.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1280 PVAIKA-TLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRSedykktqsektRPLPSLIICPPSL 1358
Cdd:cd18065    8 PSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRN-----------IPGPHMVLVPKST 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1359 TGHWEQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTA---DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKL 1435
Cdd:cd18065   77 LHNWMNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPgewDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1436 AKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFakpiassrNSKTSSKEQEagalALEALHKQV 1515
Cdd:cd18065  157 SEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVL 224

                 ....*....
gi 50310019 1516 LPFMLRRLK 1524
Cdd:cd18065  225 KPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1283-1524 4.04e-39

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: 147.13  E-value: 4.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1283 IKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRseDYKKTQSektrplPSLIICPPSLTGHW 1362
Cdd:cd18063   20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT---YLM--EHKRLNG------PYLIIVPLSTLSNW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1363 EQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTA--DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLakaVK 1440
Cdd:cd18063   89 TYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGkfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL---TQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1441 LINSNH----RLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSrNSKTSSKEQEAgALALEALHKQVL 1516
Cdd:cd18063  166 VLNTHYvaprRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT-GERVDLNEEET-ILIIRRLHKVLR 243

                 ....*...
gi 50310019 1517 PFMLRRLK 1524
Cdd:cd18063  244 PFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1283-1524 6.10e-38

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: 143.65  E-value: 6.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1283 IKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLRseDYKKTQSektrplPSLIICPPSLTGHW 1362
Cdd:cd18062   20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT---YLM--EHKRING------PFLIIVPLSTLSNW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1363 EQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTA--DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLakaVK 1440
Cdd:cd18062   89 VYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGkfNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL---TQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1441 LINSNH----RLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSrNSKTSSKEQEAgALALEALHKQVL 1516
Cdd:cd18062  166 VLNTHYvaprRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT-GEKVDLNEEET-ILIIRRLHKVLR 243

                 ....*...
gi 50310019 1517 PFMLRRLK 1524
Cdd:cd18062  244 PFLLRRLK 251
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1287-1522 1.29e-35

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: 136.29  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdqYLrsedYKKTQSEKtrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd18054   21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLS---YL----FHQHQLYG----PFLLVVPLSTLTSWQREF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPL--------QGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKA 1438
Cdd:cd18054   90 EIWAPEINVVVYIGDLMSRNTIreyewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1439 VKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiassrnsktssKEQEAGalaLEALHKQVLPF 1518
Cdd:cd18054  170 LIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-------------KGRENG---YQSLHKVLEPF 233

                 ....
gi 50310019 1519 MLRR 1522
Cdd:cd18054  234 LLRR 237
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1287-1522 1.81e-34

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: 131.94  E-value: 1.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNW-LAFLNKyhlhGILCDDMGLGKTLQTICIIAsdqYLRSEdykktqsektrpLPSLIICPPSLTGHWEQE 1365
Cdd:cd18010    1 LLPFQREGVCFaLRRGGR----VLIADEMGLGKTVQAIAIAA---YYREE------------WPLLIVCPSSLRLTWADE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSPTL---NVLVYAGGPSVRYPLQGQvptadIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLI 1442
Cdd:cd18010   62 IERWLPSLppdDIQVIVKSKDGLRDGDAK-----VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1443 --NSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSskeqeaGALALEALHKQVLP-FM 1519
Cdd:cd18010  137 lkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYS------GSSNLEELHLLLLAtIM 210

                 ...
gi 50310019 1520 LRR 1522
Cdd:cd18010  211 IRR 213
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1308-1522 2.60e-34

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: 132.59  E-value: 2.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1308 GILCDDMGLGKTLQTICIIASDqylrsedykktqsektrplPSLIICPPSLTGHWEQEFQQY--SPTLNVLVYAGGPSVR 1385
Cdd:cd18071   51 GILADDMGLGKTLTTISLILAN-------------------FTLIVCPLSVLSNWETQFEEHvkPGQLKVYTYHGGERNR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1386 YP--LQGQvptaDIVVTSYDVARNDVDF-----LKKYDYNYCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNN 1458
Cdd:cd18071  112 DPklLSKY----DIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50310019 1459 VVELWSLFDFLMPGFLGTEKMFQERFAKPIasSRNSKTSSKEqeagalaLEALHKQVLpfmLRR 1522
Cdd:cd18071  188 PKDLGSLLSFLHLKPFSNPEYWRRLIQRPL--TMGDPTGLKR-------LQVLMKQIT---LRR 239
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1287-1522 4.22e-34

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: 132.21  E-value: 4.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWL----AFLNKYHLHG-ILCDDMGLGKTLQTICIIASdqYLRsedykktQSEKTRPL--PSLIICPPSLT 1359
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWT--LLR-------QSPQCKPEidKAIVVSPSSLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1360 GHWEQEFQQY-SPTLNVLVYAGGPS--------VRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKN 1430
Cdd:cd18067   72 KNWANELGKWlGGRLQPLAIDGGSKkeidrklvQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1431 SQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEA 1510
Cdd:cd18067  152 SDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQE 231
                        250
                 ....*....|..
gi 50310019 1511 LHKQVLPFMLRR 1522
Cdd:cd18067  232 LISIVNRCIIRR 243
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1271-1522 4.84e-34

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: 131.71  E-value: 4.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1271 PSKAKPFKLPVAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIasdQYLRSEDYKKTqsektrplPS 1350
Cdd:cd18053    5 ALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL---NYLFHEHQLYG--------PF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1351 LIICPPSLTGHWEQEFQQYSPTLNVLVYAGGPSVRYPL--------QGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVL 1422
Cdd:cd18053   74 LLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRNMIrthewmhpQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1423 DEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKpiasSRNSKTSSkeqe 1502
Cdd:cd18053  154 DEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGK----GREYGYAS---- 225
                        250       260
                 ....*....|....*....|
gi 50310019 1503 agalaleaLHKQVLPFMLRR 1522
Cdd:cd18053  226 --------LHKELEPFLLRR 237
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1309-1488 1.22e-33

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: 130.49  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1309 ILCDDMGLGKTLQTICIIASdqYLRsedYKKTQSektRPlpsLIICPPSLTGHWEQEFQQYSP--TLNVLVYAGGPSVRY 1386
Cdd:cd18007   30 ILAHTMGLGKTLQVITFLHT--YLA---AAPRRS---RP---LVLCPASTLYNWEDEFKKWLPpdLRPLLVLVSLSASKR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1387 PLQGQVPTAD------IVVTSYD-----------VARNDVDFLKKYDYNYC---VLDEGHIIKNSQSKLAKAVKLINSNH 1446
Cdd:cd18007   99 ADARLRKINKwhkeggVLLIGYElfrnlasnattDPRLKQEFIAALLDPGPdllVLDEGHRLKNEKSQLSKALSKVKTKR 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 50310019 1447 RLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPI 1488
Cdd:cd18007  179 RILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPI 220
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1287-1522 3.12e-33

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: 127.94  E-value: 3.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqyLRSEDYKKTqsektrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS---LYKEGHSKG--------PFLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGpsvryplqgqvptaDIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAVKLINSNH 1446
Cdd:cd17994   70 EMWAPDFYVVTYVGD--------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGY 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310019 1447 RLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKpiassrnsktSSKEQEagalaLEALHKQVLPFMLRR 1522
Cdd:cd17994  136 KLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD----------ISKEDQ-----IKKLHDLLGPHMLRR 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1287-1522 2.49e-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: 126.88  E-value: 2.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWL--AFLNKYHLHG---ILCDDMGLGKTLQTICIIASdqYLRSEDYKktqsekTRPL--PSLIICPPSLT 1359
Cdd:cd18066    1 LRPHQREGIEFLyeCVMGMRVNERfgaILADEMGLGKTLQCISLIWT--LLRQGPYG------GKPVikRALIVTPGSLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1360 GHWEQEFQQYSPTLNVLVYAGGPSVRYPLQGQVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQSKLAKAV 1439
Cdd:cd18066   73 KNWKKEFQKWLGSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1440 KLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKEQEAGALALEALHKQVLPFM 1519
Cdd:cd18066  153 TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFI 232

                 ...
gi 50310019 1520 LRR 1522
Cdd:cd18066  233 LRR 235
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1287-1522 2.40e-31

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: 123.61  E-value: 2.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFlNKYHLHG-ILCDDMGLGKTLQTICIIaSDQYLRSEDYkktqsektrplPSLIICPPSLTGHWEQE 1365
Cdd:cd18058    1 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSITFL-SEIFLMGIRG-----------PFLIIAPLSTITNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSpTLNVLVYAGGPSVRY---------------PLQGqVPTADIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKN 1430
Cdd:cd18058   68 FRTWT-EMNAIVYHGSQISRQmiqqyemyyrdeqgnPLSG-IFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1431 SQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiassrnsKTSSKEQeagalaLEA 1510
Cdd:cd18058  146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG---------DLKTEEQ------VKK 210
                        250
                 ....*....|..
gi 50310019 1511 LHKQVLPFMLRR 1522
Cdd:cd18058  211 LQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1287-1522 4.48e-30

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: 119.77  E-value: 4.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFlNKYHLHG-ILCDDMGLGKTLQTICIIasdqylrSEDYKKTQSEktrplPSLIICPPSLTGHWEQE 1365
Cdd:cd18060    1 LREYQLEGVNWLLF-NWYNRQNcILADEMGLGKTIQSIAFL-------QEVYNVGIHG-----PFLVIAPLSTITNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSpTLNVLVYAGGPSVRYPLQGQ-----------VPTA---DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNS 1431
Cdd:cd18060   68 FNTWT-EMNTIVYHGSLASRQMIQQYemyckdsrgrlIPGAykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1432 QSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiassrNSKTSSKEQEagalaLEAL 1511
Cdd:cd18060  147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLKTEEQVQK-----LQAI 214
                        250
                 ....*....|.
gi 50310019 1512 HKqvlPFMLRR 1522
Cdd:cd18060  215 LK---PMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1287-1522 1.21e-29

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: 118.60  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFlNKYHLHG-ILCDDMGLGKTLQTICIIaSDQYLRSEDYkktqsektrplPSLIICPPSLTGHWEQE 1365
Cdd:cd18059    1 LREYQLEGVNWLLF-NWYNTRNcILADEMGLGKTIQSITFL-YEIYLKGIHG-----------PFLVIAPLSTIPNWERE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYSpTLNVLVYAGGPSVRYPLQ----------GQVPTADI----VVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNS 1431
Cdd:cd18059   68 FRTWT-ELNVVVYHGSQASRRTIQlyemyfkdpqGRVIKGSYkfhaIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1432 QSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiassrNSKTSSKEQEagalaLEAL 1511
Cdd:cd18059  147 NCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-------DLKTEEQVQK-----LQAI 214
                        250
                 ....*....|.
gi 50310019 1512 HKqvlPFMLRR 1522
Cdd:cd18059  215 LK---PMMLRR 222
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1287-1471 1.67e-29

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: 119.37  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNkyhlhGILCDDMGLGKTLQTICIIAS---------DQYL--RSEDYKKTQSEKTRPL---PSLI 1352
Cdd:cd18070    1 LLPYQRRAVNWMLVPG-----GILADEMGLGKTVEVLALILLhprpdndldAADDdsDEMVCCPDCLVAETPVsskATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1353 ICPPSLTGHWEQEFQQ-YSPTLNVLVYAGGPSVRYpLQGQVP----TADIVVTSYDVARNDVDF------------LKKY 1415
Cdd:cd18070   76 VCPSAILAQWLDEINRhVPSSLKVLTYQGVKKDGA-LASPAPeilaEYDIVVTTYDVLRTELHYaeanrsnrrrrrQKRY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310019 1416 ----------DYNYCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMP 1471
Cdd:cd18070  155 eappsplvlvEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1287-1522 1.18e-28

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: 116.26  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASdqyLRSEDYKKTqsektrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS---LYKEGHTKG--------PFLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVR---------------------YPLQGQVPTA-DIVVTSYDVARNDVDFLKKYDYNYCVLDE 1424
Cdd:cd18055   70 QMWAPDFYVVTYTGDKDSRaiirenefsfddnavkggkkaFKMKREAQVKfHVLLTSYELVTIDQAALGSIRWACLVVDE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1425 GHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKpiassrnsktSSKEQEag 1504
Cdd:cd18055  150 AHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD----------ISKEDQ-- 217
                        250
                 ....*....|....*...
gi 50310019 1505 alaLEALHKQVLPFMLRR 1522
Cdd:cd18055  218 ---IKKLHDLLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1287-1522 1.56e-27

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: 112.41  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIasdqylrsEDYKKTQSEKtrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL--------YEILLTGIRG----PFLIIAPLSTIANWEREF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSpTLNVLVYAGGPSVRYPLQ----------GQVPTA----DIVVTSYDVARNDVDFLKKYDYNYCVLDEGHIIKNSQ 1432
Cdd:cd18061   69 RTWT-DLNVVVYHGSLISRQMIQqyemyfrdsqGRIIRGayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1433 SKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAkpiassrNSKTSSKEQEagalaLEALH 1512
Cdd:cd18061  148 CKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-------DLKTEEQVQK-----LQAIL 215
                        250
                 ....*....|
gi 50310019 1513 KqvlPFMLRR 1522
Cdd:cd18061  216 K---PMMLRR 222
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1287-1469 3.65e-27

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: 112.19  E-value: 3.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFL-NKYHLHGILCDDMGLGKTLQTICIIASDQYLR-----------SEDYKKTQSEKTRPLPSLIIC 1354
Cdd:cd18072    1 LLLHQKQALAWLLWReRQKPRGGILADDMGLGKTLTMIALILAQKNTQnrkeeekekalTEWESKKDSTLVPSAGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1355 PPSLTGHWEQEFQQY--SPTLNVLVYAGgPSvRYPLQGQVPTADIVVTSYDVARNDVDFLKKYD---------YNYCVLD 1423
Cdd:cd18072   81 PASLVHQWKNEVESRvaSNKLRVCLYHG-PN-RERIGEVLRDYDIVITTYSLVAKEIPTYKEESrssplfriaWARIILD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 50310019 1424 EGHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFL 1469
Cdd:cd18072  159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1287-1522 1.06e-26

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: 110.54  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDqylrsedYKKTQSEKtrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSL-------YKEGHSKG----PFLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPL-QGQVPTAD---------------------IVVTSYDVARNDVDFLKKYDYNYCVLDE 1424
Cdd:cd18056   70 EMWAPDMYVVTYVGDKDSRAIIrENEFSFEDnairggkkasrmkkeasvkfhVLLTSYELITIDMAILGSIDWACLIVDE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1425 GHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKpiassrnsktSSKEQEag 1504
Cdd:cd18056  150 AHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD----------IAKEDQ-- 217
                        250
                 ....*....|....*...
gi 50310019 1505 alaLEALHKQVLPFMLRR 1522
Cdd:cd18056  218 ---IKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1287-1522 5.19e-26

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: 108.61  E-value: 5.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDqylrsedYKKTQSEKtrplPSLIICPPSLTGHWEQEF 1366
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSL-------YKEGHSKG----PYLVSAPLSTIINWEREF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPL-QGQVPTAD---------------------IVVTSYDVARNDVDFLKKYDYNYCVLDE 1424
Cdd:cd18057   70 EMWAPDFYVVTYTGDKESRSVIrENEFSFEDnairsgkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLVVDE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1425 GHIIKNSQSKLAKAVKLINSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKpiassrnsktSSKEQEag 1504
Cdd:cd18057  150 AHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD----------ISKEDQ-- 217
                        250
                 ....*....|....*...
gi 50310019 1505 alaLEALHKQVLPFMLRR 1522
Cdd:cd18057  218 ---IKKLHDLLGPHMLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1309-1488 2.70e-25

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: 106.05  E-value: 2.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1309 ILCDDMGLGKTLQTICIIasDQYLRSEDYKKTqsektrplpsLIICPPSLTGHWEQEFQQYSPTlnvlvYAGGPSVR--- 1385
Cdd:cd18069   32 ILAHSMGLGKTLQVISFL--DVLLRHTGAKTV----------LAIVPVNTLQNWLSEFNKWLPP-----PEALPNVRprp 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1386 ---YPLQGQVPTADI---VVTSYDvARNDVdFLKKYDY-------NYCVLDEGHIIKNSQSKLAKAVKLINSNHRLVLTG 1452
Cdd:cd18069   95 fkvFILNDEHKTTAArakVIEDWV-KDGGV-LLMGYEMfrlrpgpDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTG 172
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 50310019 1453 TPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPI 1488
Cdd:cd18069  173 YPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI 208
DEXDc smart00487
DEAD-like helicases superfamily;
1286-1482 2.99e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.18  E-value: 2.99e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    1286 TLRKYQQDGVNWLAFLNKyhlHGILCDDMGLGKTLQTICIIAsdQYLRSEDYKKTqsektrplpsLIICP-PSLTGHWEQ 1364
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL--EALKRGKGGRV----------LVLVPtRELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    1365 EFQQYSP--TLNVLVYAGGPSVRYPLQGQV-PTADIVVTSYDVARNDV--DFLKKYDYNYCVLDEGHIIKNS--QSKLAK 1437
Cdd:smart00487   73 ELKKLGPslGLKVVGLYGGDSKREQLRKLEsGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGgfGDQLEK 152
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 50310019    1438 AVKLINSN-HRLVLTGTP---IQNNVVELWSLFDFLMPGFLGTEKMFQE 1482
Cdd:smart00487  153 LLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1308-1500 4.62e-24

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 103.04  E-value: 4.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1308 GILCDDMGLGKTLQTICIIASdqYLRSEDYKKTQSektrplpSLIICPPSLTGHWEQEFQQYSPTLN---------VLVY 1378
Cdd:cd18068   31 CILAHCMGLGKTLQVVTFLHT--VLLCEKLENFSR-------VLVVCPLNTVLNWLNEFEKWQEGLKdeekievneLATY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1379 AGGPSVRYPLQGQVPTADIVVTSYDVARN-----DVDFLKKY--DYN---------YCVLDEGHIIKNSQSKLAKAVKLI 1442
Cdd:cd18068  102 KRPQERSYKLQRWQEEGGVMIIGYDMYRIlaqerNVKSREKLkeIFNkalvdpgpdFVVCDEGHILKNEASAVSKAMNSI 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50310019 1443 NSNHRLVLTGTPIQNNVVELWSLFDFLMPGFLGTEKMFQERFAKPIASSRNSKTSSKE 1500
Cdd:cd18068  182 RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVD 239
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1660-1759 4.30e-23

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: 95.74  E-value: 4.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019   1660 HRVLIFCQLKDMLDMvenDLLKKHLpSVTFMRLDGSVDSRDRQKVVRKFNEDPSIdcLLLTTKVGGLGLNLTGADTVIFV 1739
Cdd:pfam00271   16 GKVLIFSQTKKTLEA---ELLLEKE-GIKVARLHGDLSQEEREEILEDFRKGKID--VLVATDVAERGLDLPDVDLVINY 89
                           90       100
                   ....*....|....*....|
gi 50310019   1740 EHDWNPMNDLQAMDRAHRLG 1759
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1678-1759 7.93e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 7.93e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019    1678 DLLKKHLPS--VTFMRLDGSVDSRDRQKVVRKFNEDPSidCLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRA 1755
Cdd:smart00490    1 EELAELLKElgIKVARLHGGLSQEEREEILDKFNNGKI--KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 50310019    1756 HRLG 1759
Cdd:smart00490   79 GRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1287-1473 8.97e-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: 83.88  E-value: 8.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVnwLAFLNKYHLHGILCDDMGLGKTLQTICIIAsdQYLRSEDYKKTqsektrplpsLIICPPSLTGHWEQEF 1366
Cdd:cd18011    1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEAGLIIK--ELLLRGDAKRV----------LILCPASLVEQWQDEL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1367 QQYSPTLNVLVYAGGPSVRYPLQGQVPTA-DIVVTSYDVAR---NDVDFLKKYDYNYCVLDEGHIIKNSQ----SKLAKA 1438
Cdd:cd18011   67 QDKFGLPFLILDRETAAQLRRLIGNPFEEfPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGggkeTKRYKL 146
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 50310019 1439 VKLINSN--HRLVLTGTPIQNNVVELWSLFDFLMPGF 1473
Cdd:cd18011  147 GRLLAKRarHVLLLTATPHNGKEEDFRALLSLLDPGR 183
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1287-1488 6.76e-10

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: 61.21  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1287 LRKYQQDGVNWLaflnKYHLHGILCDDMGLGKTLQTICIIasdQYLRSEDYKKtqsektrplPSLIICPPSLTGH-WEQE 1365
Cdd:cd18013    1 PHPYQKVAINFI----IEHPYCGLFLDMGLGKTVTTLTAL---SDLQLDDFTR---------RVLVIAPLRVARStWPDE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1366 FQQYS--PTLNVLVYAGGPSVRYP-LQGQvptADIVVTSYDVARNDVD-FLKKYDYNYCVLDEGHIIKNSQSK----LAK 1437
Cdd:cd18013   65 VEKWNhlRNLTVSVAVGTERQRSKaANTP---ADLYVINRENLKWLVNkSGDPWPFDMVVIDELSSFKSPRSKrfkaLRK 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 50310019 1438 AVKLINsnhRLV-LTGTPIQNNVVELWSLFDFLMPG-FLG-TEKMFQERFAKPI 1488
Cdd:cd18013  142 VRPVIK---RLIgLTGTPSPNGLMDLWAQIALLDQGeRLGrSITAYRERWFDPD 192
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
1571-1862 5.27e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 58.20  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1571 EVENKQHIFQALQYMRKLCNHPSLVLNS-------SHPQFQQVQSYLSQTGMDlhdigHaPKLEALKTLllecgigiqdV 1643
Cdd:COG1111  281 ELLETQGVEALLRYLERLEEEARSSGGSkaskrlvSDPRFRKAMRLAEEADIE-----H-PKLSKLREI----------L 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1644 EKKSNKNPSidnvisqHRVLIFCQLKDMLDMVENDLLKKHLPSVTFM------RLDGSVDsRDRQKVVRKF-NEDPSIdc 1716
Cdd:COG1111  345 KEQLGTNPD-------SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVgqaskeGDKGLTQ-KEQIEILERFrAGEFNV-- 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1717 lLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRAHRLGQKKVVnVYriITKGTLEEKIMGLQKFKMNIASTIVNQ 1796
Cdd:COG1111  415 -LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVV-VL--IAKGTRDEAYYWSSRRKEKKMKSILKK 490
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310019 1797 QNAGLGSMNTHQL-------LDLFDADNIPSQEKVEKKKTVEDVANESGLTgKAKEAVGELKELWDSSQYEEE 1862
Cdd:COG1111  491 LKKLLDKQEKEKLkesaqatLDEFESIKELAEDEINEKDLDEIESSENGAH-VDWREPVLLQVIVSTLAESLE 562
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1286-1454 1.46e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 53.10  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1286 TLRKYQQDGVN-WLAFLNKYHLHGILCDDMGLGKTlqticIIASdqylrsEDYKKTQsektRPLPSLIICP-PSLTGHWE 1363
Cdd:COG1061   80 ELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKT-----VLAL------ALAAELL----RGKRVLVLVPrRELLEQWA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1364 QEFQQYSPtlnvLVYAGGPSVRyplqgqvPTADIVVTSYDVARNDVDFLK-KYDYNYCVLDEGHiikNSQSK-LAKAVKL 1441
Cdd:COG1061  145 EELRRFLG----DPLAGGGKKD-------SDAPITVATYQSLARRAHLDElGDRFGLVIIDEAH---HAGAPsYRRILEA 210
                        170
                 ....*....|...
gi 50310019 1442 INSNHRLVLTGTP 1454
Cdd:COG1061  211 FPAAYRLGLTATP 223
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
1307-1453 6.08e-05

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: 45.09  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1307 HGILCDDMGLGKTLQTICIIAsdqylrsedykktQSEKTRPLPSLIICP-PSLTGHWEQEFQQY-SPTLNVLVYAGGPSV 1384
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAAL-------------LLLLKKGKKVLVLVPtKALALQTAERLRELfGPGIRVAVLVGGSSA 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310019 1385 RYPLQGQVPTADIVVTSYDVARNDVDFLKKY---DYNYCVLDEGHII-KNSQSKLAKA---VKLINSNHRLV-LTGT 1453
Cdd:cd00046   70 EEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlIDSRGALILDlavRKAGLKNAQVIlLSAT 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1717-1764 5.87e-04

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: 40.38  E-value: 5.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 50310019 1717 LLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRAHRLGQKKVV 1764
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
1644-1737 1.16e-03

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 40.95  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310019 1644 EKKSNKNPSIDNVISQHRVLIFCQLKDMLDMVENDLLKKHLPSVTfmrLDGSVDSRDRQKVVRKFNEDPSidCLLLTTKV 1723
Cdd:cd18787   12 EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAA---LHGDLSQEERERALKKFRSGKV--RVLVATDV 86
                         90
                 ....*....|....
gi 50310019 1724 GGLGLNLTGADTVI 1737
Cdd:cd18787   87 AARGLDIPGVDHVI 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH