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Conserved domains on  [gi|1154592370|gb|KSI33706|]
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helicase [Pseudomonas aeruginosa]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
16-638 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 604.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  16 DDLPRLRQQGWFIDIRADFAYDLTPIDAWYAEVEEADDRQWFELELGIQVAGQRVSLLPALTELIRRSPALLDPRALARH 95
Cdd:COG0553    64 LAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  96 ADEEQLVLRLELNPPLRVALPFGRLKPVLAALSDFYLGDPEPQRKLRLGAPDAARLADLDELPLAWEGGDNLRDFAR--R 173
Cdd:COG0553   144 ALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDafR 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 174 LRSFQARPATPPQGLRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLI 253
Cdd:COG0553   224 LRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLV 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 254 PNWLDEAERFAPDLRVLALHGAGRR-RDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAR 332
Cdd:COG0553   303 GNWQRELAKFAPGLRVLVLDGTRERaKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKhGDEARLSHLAARLRPFLLRRTKEQVASEL 412
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEK-GDEEALERLRRLLRPFLLRRTKEDVLKDL 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 413 PPKSEFTQFVELSEAQRELYETVRlaldRKVREEIARRGLARSRIVILEALLKLRQVCCDTRLLqrqeDGARSGRALSSG 492
Cdd:COG0553   462 PEKTEETLYVELTPEQRALYEAVL----EYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAELSGRSA 533
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 493 KLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGK-VPVFLISLKAGGV 569
Cdd:COG0553   534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGE 613
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 570 GLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLIARGTVEEKIQHLQQEKAALADGLFS 638
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
16-638 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 604.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  16 DDLPRLRQQGWFIDIRADFAYDLTPIDAWYAEVEEADDRQWFELELGIQVAGQRVSLLPALTELIRRSPALLDPRALARH 95
Cdd:COG0553    64 LAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  96 ADEEQLVLRLELNPPLRVALPFGRLKPVLAALSDFYLGDPEPQRKLRLGAPDAARLADLDELPLAWEGGDNLRDFAR--R 173
Cdd:COG0553   144 ALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDafR 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 174 LRSFQARPATPPQGLRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLI 253
Cdd:COG0553   224 LRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLV 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 254 PNWLDEAERFAPDLRVLALHGAGRR-RDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAR 332
Cdd:COG0553   303 GNWQRELAKFAPGLRVLVLDGTRERaKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKhGDEARLSHLAARLRPFLLRRTKEQVASEL 412
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEK-GDEEALERLRRLLRPFLLRRTKEDVLKDL 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 413 PPKSEFTQFVELSEAQRELYETVRlaldRKVREEIARRGLARSRIVILEALLKLRQVCCDTRLLqrqeDGARSGRALSSG 492
Cdd:COG0553   462 PEKTEETLYVELTPEQRALYEAVL----EYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAELSGRSA 533
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 493 KLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGK-VPVFLISLKAGGV 569
Cdd:COG0553   534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGE 613
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 570 GLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLIARGTVEEKIQHLQQEKAALADGLFS 638
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
188-405 3.18e-109

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: 328.37  E-value: 3.18e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 188 LRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLIPNWLDEAERFAPDL 267
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR-KGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGAGRRRDFAR-IDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTP 346
Cdd:cd18012    80 KVLVIHGTKRKREKLRaLEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 347 LENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSHLAARLRPFLLRRTK 405
Cdd:cd18012   160 IENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
180-632 2.06e-85

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 289.01  E-value: 2.06e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  180 RPATPPQGLRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDE 259
Cdd:PLN03142   158 RLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNE 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  260 AERFAPDLRVLALHGAGRRRDFARID-----EHDLVLTTYALLPRDAAELgkRRFH--LLILDEAQNIKNATTKAAVAAR 332
Cdd:PLN03142   238 IRRFCPVLRAVKFHGNPEERAHQREEllvagKFDVCVTSFEMAIKEKTAL--KRFSwrYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRtpIEKHGDEAR-LSHLAARLRPFLLRRTKEQVASE 411
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ--ISGENDQQEvVQQLHKVLRPFLLRRLKSDVEKG 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  412 LPPKSEFTQFVELSEAQRELYetvRLALDRKVreEIARRGLARSRIviLEALLKLRQVCCDTRLLQRQEDGA--RSGRAL 489
Cdd:PLN03142   394 LPPKKETILKVGMSQMQKQYY---KALLQKDL--DVVNAGGERKRL--LNIAMQLRKCCNHPYLFQGAEPGPpyTTGEHL 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  490 --SSGKLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQ---SGKVpVFLI 562
Cdd:PLN03142   467 veNSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTggEDRDASIDAFNkpgSEKF-VFLL 545
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  563 SLKAGGVGLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLIARGTVEEKIQHLQQEKAAL 632
Cdd:PLN03142   546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
195-476 6.09e-76

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 244.90  E-value: 6.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 195 YQLEGLSWMQTL-RELDSGGVLADDMGLGKTLQSLA---HVLLE-KQAGRldtPALVVMPTSLIPNWLDEAERFA--PDL 267
Cdd:pfam00176   1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISlllYLKHVdKNWGG---PTLIVVPLSLLHNWMNEFERWVspPAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGAGR-----RRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:pfam00176  78 RVVVLHGNKRpqerwKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSHLAARLRPFLLRRTKEQVASELPPKSEFTQFV 422
Cdd:pfam00176 158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 423 ELSEAQRELYETVRLA--LDRKVREEIARRGLARsrivILEALLKLRQVCCDTRLL 476
Cdd:pfam00176 238 RLSKLQRKLYQTFLLKkdLNAIKTGEGGREIKAS----LLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
191-364 1.50e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.80  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  191 ELRPYQLEGLSWMqtlRELDSGGVLADDMGLGKTLQSLAHvLLEKQAGRLDTPALVVMPT-SLIPNWLDEAERFAPDL-- 267
Cdd:smart00487   8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  268 -RVLALHGAGRRRDFARI--DEHDLVLTTYALLPRDAAE--LGKRRFHLLILDEAQNIKNATTK---AAVAARELAARHR 339
Cdd:smart00487  84 kVVGLYGGDSKREQLRKLesGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGFGdqlEKLLKLLPKNVQL 163
                          170       180
                   ....*....|....*....|....*...
gi 1154592370  340 LCLTGTPLENH---LGELWSLFHFLMPG 364
Cdd:smart00487 164 LLLSATPPEEIenlLELFLNDPVFIDVG 191
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
16-638 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 604.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  16 DDLPRLRQQGWFIDIRADFAYDLTPIDAWYAEVEEADDRQWFELELGIQVAGQRVSLLPALTELIRRSPALLDPRALARH 95
Cdd:COG0553    64 LAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  96 ADEEQLVLRLELNPPLRVALPFGRLKPVLAALSDFYLGDPEPQRKLRLGAPDAARLADLDELPLAWEGGDNLRDFAR--R 173
Cdd:COG0553   144 ALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDafR 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 174 LRSFQARPATPPQGLRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLI 253
Cdd:COG0553   224 LRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLIVAPTSLV 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 254 PNWLDEAERFAPDLRVLALHGAGRR-RDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAR 332
Cdd:COG0553   303 GNWQRELAKFAPGLRVLVLDGTRERaKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVR 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKhGDEARLSHLAARLRPFLLRRTKEQVASEL 412
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEK-GDEEALERLRRLLRPFLLRRTKEDVLKDL 461
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 413 PPKSEFTQFVELSEAQRELYETVRlaldRKVREEIARRGLARSRIVILEALLKLRQVCCDTRLLqrqeDGARSGRALSSG 492
Cdd:COG0553   462 PEKTEETLYVELTPEQRALYEAVL----EYLRRELEGAEGIRRRGLILAALTRLRQICSHPALL----LEEGAELSGRSA 533
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 493 KLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGK-VPVFLISLKAGGV 569
Cdd:COG0553   534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGE 613
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 570 GLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLIARGTVEEKIQHLQQEKAALADGLFS 638
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
188-405 3.18e-109

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: 328.37  E-value: 3.18e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 188 LRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLIPNWLDEAERFAPDL 267
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR-KGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGAGRRRDFAR-IDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTP 346
Cdd:cd18012    80 KVLVIHGTKRKREKLRaLEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 347 LENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSHLAARLRPFLLRRTK 405
Cdd:cd18012   160 IENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
180-632 2.06e-85

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 289.01  E-value: 2.06e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  180 RPATPPQGLRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDE 259
Cdd:PLN03142   158 RLLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNE 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  260 AERFAPDLRVLALHGAGRRRDFARID-----EHDLVLTTYALLPRDAAELgkRRFH--LLILDEAQNIKNATTKAAVAAR 332
Cdd:PLN03142   238 IRRFCPVLRAVKFHGNPEERAHQREEllvagKFDVCVTSFEMAIKEKTAL--KRFSwrYIIIDEAHRIKNENSLLSKTMR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRtpIEKHGDEAR-LSHLAARLRPFLLRRTKEQVASE 411
Cdd:PLN03142   316 LFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ--ISGENDQQEvVQQLHKVLRPFLLRRLKSDVEKG 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  412 LPPKSEFTQFVELSEAQRELYetvRLALDRKVreEIARRGLARSRIviLEALLKLRQVCCDTRLLQRQEDGA--RSGRAL 489
Cdd:PLN03142   394 LPPKKETILKVGMSQMQKQYY---KALLQKDL--DVVNAGGERKRL--LNIAMQLRKCCNHPYLFQGAEPGPpyTTGEHL 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  490 --SSGKLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQ---SGKVpVFLI 562
Cdd:PLN03142   467 veNSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTggEDRDASIDAFNkpgSEKF-VFLL 545
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  563 SLKAGGVGLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLIARGTVEEKIQHLQQEKAAL 632
Cdd:PLN03142   546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
195-476 6.09e-76

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 244.90  E-value: 6.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 195 YQLEGLSWMQTL-RELDSGGVLADDMGLGKTLQSLA---HVLLE-KQAGRldtPALVVMPTSLIPNWLDEAERFA--PDL 267
Cdd:pfam00176   1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISlllYLKHVdKNWGG---PTLIVVPLSLLHNWMNEFERWVspPAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGAGR-----RRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:pfam00176  78 RVVVLHGNKRpqerwKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWIL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSHLAARLRPFLLRRTKEQVASELPPKSEFTQFV 422
Cdd:pfam00176 158 TGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 423 ELSEAQRELYETVRLA--LDRKVREEIARRGLARsrivILEALLKLRQVCCDTRLL 476
Cdd:pfam00176 238 RLSKLQRKLYQTFLLKkdLNAIKTGEGGREIKAS----LLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
192-366 6.19e-63

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 206.65  E-value: 6.19e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARI----DEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTPL 347
Cdd:cd17919    81 YHGSQRERAQIRAkeklDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160
                         170
                  ....*....|....*....
gi 1154592370 348 ENHLGELWSLFHFLMPGWL 366
Cdd:cd17919   161 QNNLEELWALLDFLDPPFL 179
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
491-613 2.75e-61

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: 200.40  E-value: 2.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 491 SGKLAYLLDMLDELIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSG-KVPVFLISLKAG 567
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTssKERQKLVDRFNEDpDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1154592370 568 GVGLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVYRLI 613
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
192-403 4.44e-58

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: 195.65  E-value: 4.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLA-----HVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPD 266
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCilasdHHKRANSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 267 --LRVLALHG--AGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:cd17999    81 afLKPLAYVGppQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPI-----------EKHGDEARLSHLAARLRPFLLRR 403
Cdd:cd17999   161 SGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPIlasrdskasakEQEAGALALEALHKQVLPFLLRR 232
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
192-403 3.88e-52

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: 179.47  E-value: 3.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQS---LAHVLLEKQagrLDTPALVVMPTSLIPNWLDEAERFAPDLR 268
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTialLAHLACEKG---NWGPHLIVVPTSVMLNWEMEFKRWCPGFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 269 VLALHGAGRRRDFARI-----DEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLT 343
Cdd:cd18003    78 ILTYYGSAKERKLKRQgwmkpNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 344 GTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTP----IEKHGDEAR--LSHLAARLRPFLLRR 403
Cdd:cd18003   158 GTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEENEelVRRLHKVLRPFLLRR 223
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
192-403 5.42e-51

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: 176.71  E-value: 5.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMqtlreLDSGGVLADDMGLGKTLQSLAHVLLEKQAG-----------------RLDTPALVVMPTSLIP 254
Cdd:cd18008     1 LLPYQKQGLAWM-----LPRGGILADEMGLGKTIQALALILATRPQDpkipeeleenssdpkklYLSKTTLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 255 NWLDEAERF--APDLRVLALHGAGRRRDFARIDEHDLVLTTYALL----------------PRDAAELGKRRFHLLILDE 316
Cdd:cd18008    76 QWKDEIEKHtkPGSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYRVILDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 317 AQNIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEArLSHLAARL 396
Cdd:cd18008   156 AHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKA-LERLQALL 234

                  ....*..
gi 1154592370 397 RPFLLRR 403
Cdd:cd18008   235 KPILLRR 241
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
192-405 8.40e-51

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 176.04  E-value: 8.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGrLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18009     4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVPVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHG-AGRRRDFAR--------IDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:cd18009    83 YHGtKEERERLRKkimkregtLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLL 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQ--DYRTPIEKHGDEARLSH---------LAARLRPFLLRRTK 405
Cdd:cd18009   163 TGTPLQNNLSELWSLLNFLLPDVFDDLSSFESwfDFSSLSDNAADISNLSEereqnivhmLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
191-405 1.56e-50

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: 174.82  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 191 ELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVL 270
Cdd:cd17997     3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 271 ALHGAGR-RRDFAR----IDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGT 345
Cdd:cd17997    83 VLIGDKEeRADIIRdvllPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGT 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 346 PLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSHLAARLRPFLLRRTK 405
Cdd:cd17997   163 PLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
192-403 1.22e-49

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: 172.94  E-value: 1.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTpALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS-VLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHG---AGRRRDFARI-DEHDLVLTTYALLPRDAAELGKR-----RFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:cd18001    80 FHGtskKERERNLERIqRGGGVLLTTYGMVLSNTEQLSADdhdefKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGW-LGDARQFAQDYRTPIEK-------HGDEARLSHLAARLR----PFLLRR 403
Cdd:cd18001   160 TGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRgrdkdatQGEKALGSEVAENLRqiikPYFLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
192-405 7.45e-46

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 162.54  E-value: 7.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHV--LLEKQagRLDTPALVVMPTSLIPNWLDEAERFAPDLRV 269
Cdd:cd17996     4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLItyLMEKK--KNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 270 LALHG--AGRRRDFARI--DEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAREL-AARHRLCLTG 344
Cdd:cd17996    82 IVYKGtpDVRKKLQSQIraGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYyHARYRLLLTG 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 345 TPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHG--DEARLS---------HLAARLRPFLLRRTK 405
Cdd:cd17996   162 TPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGeqVKIELNeeetlliirRLHKVLRPFLLRRLK 233
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
192-403 1.75e-45

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 161.26  E-value: 1.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLA---HVLlekQAGRLDTPALVVMPTSLIPNWLDEAERFApDLR 268
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAfleHLY---QVEGIRGPFLVIAPLSTIPNWQREFETWT-DMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 269 VLALHGAGRRRDFARIDEH----------------DLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAR 332
Cdd:cd17995    77 VVVYHGSGESRQIIQQYEMyfkdaqgrkkkgvykfDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154592370 333 ELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrtpiekhGD---EARLSHLAARLRPFLLRR 403
Cdd:cd17995   157 KLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF-------GDlktAEQVEKLQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
191-403 1.73e-44

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 158.29  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 191 ELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVL 270
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 271 ALHGAGRRRDFARIDE----------HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRL 340
Cdd:cd17993    81 VYLGDIKSRDTIREYEfyfsqtkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 341 CLTGTPLENHLGELWSLFHFLMPGwlgdarQFaqDYRTPIEKHGDEAR---LSHLAARLRPFLLRR 403
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPG------KF--DIWEEFEEEHDEEQekgIADLHKELEPFILRR 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
192-403 1.17e-43

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: 156.51  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQS---LAHVLLEKQagrLDTPALVVMPTSLIPNWLDEAERFAPDLR 268
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSiavLAHLAEEHN---IWGPFLVIAPASTLHNWQQEISRFVPQFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 269 VLALHGAGRRRDFAR--IDEHDL---------VLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAAR 337
Cdd:cd18002    78 VLPYWGNPKDRKVLRkfWDRKNLytrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 338 HRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHG------DEARLSHLAARLRPFLLRR 403
Cdd:cd18002   158 NRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAenktglNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
190-415 5.05e-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: 152.51  E-value: 5.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 190 AELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRV 269
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 270 LALHG-----AGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTG 344
Cdd:cd18064    94 VCLIGdkdqrAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 345 TPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPiEKHGDEARLSHLAARLRPFLLRRTKEQVASELPPK 415
Cdd:cd18064   174 TPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTN-NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
192-403 7.92e-42

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: 152.15  E-value: 7.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLA--------------------HVLLEKQAGRLDTPALVVMPTS 251
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAflaavlgktgtrrdrennrpRFKKKPPASSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 252 LIPNWLDEAERFApDLRVLALHGAGRRRDFA-RIDE--HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAA 328
Cdd:cd18005    81 VLYNWKDELDTWG-HFEVGVYHGSRKDDELEgRLKAgrLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 329 VAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIE---KHG--------DEARLSHLAARLR 397
Cdd:cd18005   160 QAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKrgqRHTatarelrlGRKRKQELAVKLS 239

                  ....*.
gi 1154592370 398 PFLLRR 403
Cdd:cd18005   240 KFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
192-366 1.46e-39

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: 144.00  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAG-----------RRRDFARID----EHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAA 336
Cdd:cd18000    81 LHSSGsgtgseeklgsIERKSQLIRkvvgDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1154592370 337 RHRLCLTGTPLENHLGELWSLFHFLMPGWL 366
Cdd:cd18000   161 PHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
192-405 1.22e-38

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: 142.85  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHG-----AGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTP 346
Cdd:cd18065    96 LIGdkdarAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 347 LENHLGELWSLFHFLMPGWLGDARQFAQDYRTPiEKHGDEARLSHLAARLRPFLLRRTK 405
Cdd:cd18065   176 LQNNLHELWALLNFLLPDVFNSADDFDSWFDTK-NCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
192-363 1.42e-38

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: 140.98  E-value: 1.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRlDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDEH------DLVLTTYALL---PRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCL 342
Cdd:cd17998    80 YYGSQEERKHLRYDILkgledfDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                         170       180
                  ....*....|....*....|.
gi 1154592370 343 TGTPLENHLGELWSLFHFLMP 363
Cdd:cd17998   160 TGTPLQNNLLELMSLLNFIMP 180
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
192-403 1.21e-37

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: 140.11  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWM--QTLRELDSGG---VLADDMGLGKTLQSLA--HVLLE--KQAGRLDTPALVVMPTSLIPNWLDEAER 262
Cdd:cd18004     1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIAlvWTLLKqgPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 263 FAPDLRVLALHGAGRRRDFARIDEH-------DLVLTTYALLPRDAAELGK-RRFHLLILDEAQNIKNATTKAAVAAREL 334
Cdd:cd18004    81 WLGLRRIKVVTADGNAKDVKASLDFfssastyPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 335 AARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGD-----------EARLSHLAARLRPFLLRR 403
Cdd:cd18004   161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDpdaseedkelgAERSQELSELTSRFILRR 240
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
191-403 1.29e-36

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: 137.06  E-value: 1.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 191 ELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVL 270
Cdd:cd18054    20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 271 ALHGAGRRRDFARidEHDLV------------LTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARH 338
Cdd:cd18054   100 VYIGDLMSRNTIR--EYEWIhsqtkrlkfnalITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNH 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154592370 339 RLCLTGTPLENHLGELWSLFHFLMPgwlgDARQFAQDYRtpiEKHGD--EARLSHLAARLRPFLLRR 403
Cdd:cd18054   178 RLLITGTPLQNSLKELWSLLHFIMP----EKFEFWEDFE---EDHGKgrENGYQSLHKVLEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
192-403 1.71e-36

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: 136.03  E-value: 1.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHG-----AGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTP 346
Cdd:cd18006    81 YMGdkekrLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 347 LENHLGELWSLFHFLMPGWLG--DARQFAQDYRtpiEKHGDEARLSHLAARLRPFLLRR 403
Cdd:cd18006   161 IQNSLQELYALLSFIEPNVFPkdKLDDFIKAYS---ETDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
188-405 4.91e-35

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 133.26  E-value: 4.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 188 LRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDL 267
Cdd:cd18063    20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGA-GRRRDFA---RIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAREL-AARHRLCL 342
Cdd:cd18063   100 VKISYKGTpAMRRSLVpqlRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHyVAPRRILL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSH---------LAARLRPFLLRRTK 405
Cdd:cd18063   180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEeetiliirrLHKVLRPFLLRRLK 251
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
192-403 1.54e-34

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: 129.87  E-value: 1.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGagrrrdfaridEHDLvLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTPLENHL 351
Cdd:cd17994    81 YVG-----------DHVL-LTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 352 GELWSLFHFLMPGWLGDARQFAQDYrTPIEKhgdEARLSHLAARLRPFLLRR 403
Cdd:cd17994   149 EELFHLLNFLTPERFNNLQGFLEEF-ADISK---EDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
188-405 1.69e-34

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: 131.71  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 188 LRAELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDL 267
Cdd:cd18062    20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 268 RVLALHGA-GRRRDFA---RIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAAREL-AARHRLCL 342
Cdd:cd18062   100 VKVSYKGSpAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHyVAPRRLLL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154592370 343 TGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDEARLSH---------LAARLRPFLLRRTK 405
Cdd:cd18062   180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEeetiliirrLHKVLRPFLLRRLK 251
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
192-403 6.17e-33

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: 126.81  E-value: 6.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTlRE------------------------------LDSGGVLADDMGLGKTLQSLAHVLLekqagrld 241
Cdd:cd18071     1 LLPHQKQALAWMVS-REnsqdlppfweeavglflntitnfsqkkrpeLVRGGILADDMGLGKTLTTISLILA-------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 242 TPALVVMPTSLIPNWLDE-AERFAP-DLRVLALHGAGRRRDFARIDEHDLVLTTYALLPRD-----AAELGKRRFHLLIL 314
Cdd:cd18071    72 NFTLIVCPLSVLSNWETQfEEHVKPgQLKVYTYHGGERNRDPKLLSKYDIVLTTYNTLASDfgakgDSPLHTINWLRVVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 315 DEAQNIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKhGDEARLSHLAA 394
Cdd:cd18071   152 DEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGLKRLQV 230

                  ....*....
gi 1154592370 395 RLRPFLLRR 403
Cdd:cd18071   231 LMKQITLRR 239
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
191-403 2.28e-31

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: 122.47  E-value: 2.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 191 ELRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVL 270
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 271 ALHGAGRRRDFARIDE----------HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHRL 340
Cdd:cd18053   100 VYLGDINSRNMIRTHEwmhpqtkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRL 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154592370 341 CLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrtpieKHGDEARLSHLAARLRPFLLRR 403
Cdd:cd18053   180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEH-----GKGREYGYASLHKELEPFLLRR 237
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
192-403 5.39e-29

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: 115.66  E-value: 5.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQ-TLRELDSGGVLADDMGLGKTLQSLAHVLLEKQA-------------------GRLDTPA---LVVM 248
Cdd:cd18072     1 LLLHQKQALAWLLwRERQKPRGGILADDMGLGKTLTMIALILAQKNTqnrkeeekekalteweskkDSTLVPSagtLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 249 PTSLIPNWLDEAERFAPD--LRVLALHGAGRRRDFARIDEHDLVLTTYAL----LPRDAAE-----LGKRRFHLLILDEA 317
Cdd:cd18072    81 PASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEVLRDYDIVITTYSLvakeIPTYKEEsrsspLFRIAWARIILDEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 318 QNIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEKHGDeaRLSHLaarLR 397
Cdd:cd18072   161 HNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE--RLNIL---TK 235

                  ....*.
gi 1154592370 398 PFLLRR 403
Cdd:cd18072   236 SLLLRR 241
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
192-403 2.37e-28

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: 113.62  E-value: 2.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDEHD------------------------LVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKA 327
Cdd:cd18057    81 YTGDKESRSVIRENEFSfednairsgkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 328 AVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrTPIEKhgdEARLSHLAARLRPFLLRR 403
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISK---EDQIKKLHDLLGPHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
192-403 4.04e-28

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: 112.45  E-value: 4.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFApDLRVLA 271
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIA-FLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDE----------------HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELA 335
Cdd:cd18060    79 YHGSLASRQMIQQYEmyckdsrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 336 ARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrtpiekhGD---EARLSHLAARLRPFLLRR 403
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
192-402 1.08e-27

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: 112.44  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMqtlreLDSGGVLADDMGLGKTLQSLAHVLLE-KQAGRLDT------------------------PALV 246
Cdd:cd18070     1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALILLHpRPDNDLDAadddsdemvccpdclvaetpvsskATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 247 VMPTSLIPNWLDEAERFAPD-LRVLALHGAgRRRDF------ARIDEHDLVLTTYALLP------RDAAELGKRR----- 308
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSsLKVLTYQGV-KKDGAlaspapEILAEYDIVVTTYDVLRtelhyaEANRSNRRRRrqkry 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 309 -----------FHLLILDEAQNIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLM--PGWLGDARQFAQd 375
Cdd:cd18070   155 eappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGvePFCDSDWWARVL- 233
                         250       260
                  ....*....|....*....|....*..
gi 1154592370 376 yrtpIEKHGDEARLSHLAARLRPFLLR 402
Cdd:cd18070   234 ----IRPQGRNKAREPLAALLKELLWR 256
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
192-403 1.41e-27

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: 111.31  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDEHD------------------------LVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKA 327
Cdd:cd18056    81 YVGDKDSRAIIRENEFSfednairggkkasrmkkeasvkfhVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 328 AVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrTPIEKhgdEARLSHLAARLRPFLLRR 403
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF-ADIAK---EDQIKKLHDMLGPHMLRR 232
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
192-403 3.43e-27

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: 110.64  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWM-----QTLRELDSGGVLADDMGLGKTLQSLAHV--LLEK--QAGRLDTPALVVMPTSLIPNWLDEAER 262
Cdd:cd18067     1 LRPHQREGVKFLyrcvtGRRIRGSHGCIMADEMGLGKTLQCITLMwtLLRQspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 263 F-APDLRVLALHGAGRRRDF-----------ARIDEHDLVLTtYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVA 330
Cdd:cd18067    81 WlGGRLQPLAIDGGSKKEIDrklvqwasqqgRRVSTPVLIIS-YETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 331 ARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPI-----------EKHGDEARLSHLAARLRPF 399
Cdd:cd18067   160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlkgrdadasekERQLGEEKLQELISIVNRC 239

                  ....
gi 1154592370 400 LLRR 403
Cdd:cd18067   240 IIRR 243
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
192-403 3.60e-27

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: 110.10  E-value: 3.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRVLA 271
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDEHD------------------------LVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKA 327
Cdd:cd18055    81 YTGDKDSRAIIRENEFSfddnavkggkkafkmkreaqvkfhVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154592370 328 AVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrTPIEKhgdEARLSHLAARLRPFLLRR 403
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISK---EDQIKKLHDLLGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
192-403 5.06e-27

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: 109.36  E-value: 5.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPNWLDEAeRFAPDLRVLA 271
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIT-FLSEIFLMGIRGPFLIIAPLSTITNWEREF-RTWTEMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFAR----------------IDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELA 335
Cdd:cd18058    79 YHGSQISRQMIQqyemyyrdeqgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 336 ARHRLCLTGTPLENHLGELWSLFHFLMPGwlgdarQFAQDyRTPIEKHGD---EARLSHLAARLRPFLLRR 403
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPS------QFPSE-TTFLEEFGDlktEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
192-403 7.43e-27

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: 108.97  E-value: 7.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPNWLDEAeRFAPDLRVLA 271
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSIT-FLYEIYLKGIHGPFLVIAPLSTIPNWEREF-RTWTELNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDE----------------HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELA 335
Cdd:cd18059    79 YHGSQASRRTIQLYEmyfkdpqgrvikgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 336 ARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrtpiekhGD---EARLSHLAARLRPFLLRR 403
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
192-403 3.92e-26

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: 107.24  E-value: 3.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGL-----SWMQTLRELDSGGVLADDMGLGKTLQSLAHV-LLEKQAGRLDTP----ALVVMPTSLIPNWLDEAE 261
Cdd:cd18066     1 LRPHQREGIeflyeCVMGMRVNERFGAILADEMGLGKTLQCISLIwTLLRQGPYGGKPvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 262 RF--APDLRVLALHGAGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELAARHR 339
Cdd:cd18066    81 KWlgSERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154592370 340 LCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPI-----------EKHGDEARLSHLAARLRPFLLRR 403
Cdd:cd18066   161 IILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIvrsreptatpeEKKLGEARAAELTRLTGLFILRR 235
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
192-376 4.10e-25

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: 103.82  E-value: 4.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMqtlreLDSGG--VLADDMGLGKTLQSLAHVLlekqAGRLDTPALVVMPTSLIPNWLDEAERFAPDLRV 269
Cdd:cd18010     1 LLPFQREGVCFA-----LRRGGrvLIADEMGLGKTVQAIAIAA----YYREEWPLLIVCPSSLRLTWADEIERWLPSLPP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 270 LALHGAGRRRDFARIDEHDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTK--AAVAARELAARHRLCLTGTPL 347
Cdd:cd18010    72 DDIQVIVKSKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKrtKAALPLLKRAKRVILLSGTPA 151
                         170       180
                  ....*....|....*....|....*....
gi 1154592370 348 ENHLGELWSLFHFLMPGWLGDARQFAQDY 376
Cdd:cd18010   152 LSRPIELFTQLDALDPKLFGRFHDFGRRY 180
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
492-602 4.92e-25

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: 99.98  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 492 GKLAYLLDMLDEliAEGRRVLLFSQFTSMLAlIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGKVPVfLISLKAGGV 569
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLsqEEREEILEDFRKGKIDV-LVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1154592370 570 GLNLTAADTVIHYDPWWNPAVENQASDRAYRIG 602
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
192-381 1.20e-24

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: 103.14  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWM-----QTLRELDSGG--VLADDMGLGKTLQSLA--HVLLeKQAGRLDTPaLVVMPTSLIPNWLDEAER 262
Cdd:cd18007     1 LKPHQVEGVRFLwsnlvGTDVGSDEGGgcILAHTMGLGKTLQVITflHTYL-AAAPRRSRP-LVLCPASTLYNWEDEFKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 263 FAPD--LRVLALHGAGRRRDF-ARID-------EHDLVLTTYALLPRDA--AELGKRRFH------------LLILDEAQ 318
Cdd:cd18007    79 WLPPdlRPLLVLVSLSASKRAdARLRkinkwhkEGGVLLIGYELFRNLAsnATTDPRLKQefiaalldpgpdLLVLDEGH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154592370 319 NIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIE 381
Cdd:cd18007   159 RLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE 221
DEXDc smart00487
DEAD-like helicases superfamily;
191-364 1.50e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.80  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  191 ELRPYQLEGLSWMqtlRELDSGGVLADDMGLGKTLQSLAHvLLEKQAGRLDTPALVVMPT-SLIPNWLDEAERFAPDL-- 267
Cdd:smart00487   8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  268 -RVLALHGAGRRRDFARI--DEHDLVLTTYALLPRDAAE--LGKRRFHLLILDEAQNIKNATTK---AAVAARELAARHR 339
Cdd:smart00487  84 kVVGLYGGDSKREQLRKLesGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGFGdqlEKLLKLLPKNVQL 163
                          170       180
                   ....*....|....*....|....*...
gi 1154592370  340 LCLTGTPLENH---LGELWSLFHFLMPG 364
Cdd:smart00487 164 LLLSATPPEEIenlLELFLNDPVFIDVG 191
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
192-403 2.02e-23

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: 98.92  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWMQTLRELDSGGVLADDMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPNWLDEAeRFAPDLRVLA 271
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT-FLYEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 272 LHGAGRRRDFARIDE----------------HDLVLTTYALLPRDAAELGKRRFHLLILDEAQNIKNATTKAAVAARELA 335
Cdd:cd18061    79 YHGSLISRQMIQQYEmyfrdsqgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 336 ARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYrtpiekhGD---EARLSHLAARLRPFLLRR 403
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
192-381 2.20e-19

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: 87.56  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWM-----QTLRELDS----GGVLADDMGLGKTLQSLAHVLLEKQAGRLDTpALVVMPTSLIPNWLDEAER 262
Cdd:cd18069     1 LKPHQIGGIRFLydniiESLERYKGssgfGCILAHSMGLGKTLQVISFLDVLLRHTGAKT-VLAIVPVNTLQNWLSEFNK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 263 FAPDLRVLALHGAGRRRDFARIDEHDLVLTTYALLPRDAAE-----LGKRRFHL------LILDEAQNIKNATTKAAVAA 331
Cdd:cd18069    80 WLPPPEALPNVRPRPFKVFILNDEHKTTAARAKVIEDWVKDggvllMGYEMFRLrpgpdvVICDEGHRIKNCHASTSQAL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1154592370 332 RELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIE 381
Cdd:cd18069   160 KNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
HELICc smart00490
helicase superfamily c-terminal domain;
524-602 6.18e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.49  E-value: 6.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370  524 IEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGKVpVFLISLKAGGVGLNLTAADTVIHYDPWWNPAVENQASDRAYRI 601
Cdd:smart00490   3 LAELLKELGIKVARLHGGLsqEEREEILDKFNNGKI-KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 1154592370  602 G 602
Cdd:smart00490  82 G 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
192-382 1.73e-18

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: 85.32  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWM-----QTLRELD----SGGVLADDMGLGKTLQ--SLAH-VLLEKQAGRLDTpALVVMPTSLIPNWLDE 259
Cdd:cd18068     1 LKPHQVDGVQFMwdcccESLKKTKkspgSGCILAHCMGLGKTLQvvTFLHtVLLCEKLENFSR-VLVVCPLNTVLNWLNE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 260 AERFAPDLRVLALHGAGRRRDFARIDEHDLVLT--------------TYALLPRDAAELGKRRFH-------------LL 312
Cdd:cd18068    80 FEKWQEGLKDEEKIEVNELATYKRPQERSYKLQrwqeeggvmiigydMYRILAQERNVKSREKLKeifnkalvdpgpdFV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 313 ILDEAQNIKNATTKAAVAARELAARHRLCLTGTPLENHLGELWSLFHFLMPGWLGDARQFAQDYRTPIEK 382
Cdd:cd18068   160 VCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQN 229
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
192-364 1.54e-15

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 75.79  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLswmqtLRELDSGGV---LADDMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPNWLDE-AERFA-PD 266
Cdd:cd18011     1 PLPHQIDAV-----LRALRKPPVrllLADEVGLGKTIEAGL-IIKELLLRGDAKRVLILCPASLVEQWQDElQDKFGlPF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 267 LRVLALHGAGRRRDFARI-DEHDLVLTTYALLPRD---AAELGKRRFHLLILDEAQNIKNATTKAAVAAREL------AA 336
Cdd:cd18011    75 LILDRETAAQLRRLIGNPfEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRA 154
                         170       180
                  ....*....|....*....|....*...
gi 1154592370 337 RHRLCLTGTPLENHLGELWSLFHFLMPG 364
Cdd:cd18011   155 RHVLLLTATPHNGKEEDFRALLSLLDPG 182
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
147-584 2.55e-10

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.51  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 147 DAARLADLDELPLAWEGGDNLRDFARRLRSFQARPATPPqglraELRPYQLEGL-SWMQTLRELDSGGVLADDMGLGKTL 225
Cdd:COG1061    41 AIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSF-----ELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 226 --QSLAHVLLEKQagrldtPALVVMPT-SLIPNWLDEAERFAPDlrvlALHGAGRRRDFARIdehdlVLTTYALLPRDAA 302
Cdd:COG1061   116 laLALAAELLRGK------RVLVLVPRrELLEQWAEELRRFLGD----PLAGGGKKDSDAPI-----TVATYQSLARRAH 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 303 -ELGKRRFHLLILDEAQNIknATTKAAVAARELAARHRLCLTGTPlenhlgelwslfhflmpgwlgdarqfaqdYRTPiE 381
Cdd:COG1061   181 lDELGDRFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATP-----------------------------FRSD-G 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 382 KHGDEARLSHLAARLRPfllrrtKEQVASE-LPPKSEFTQFVELSEAQRElYEtvrlALDRKVREEIARRGLARSRIVil 460
Cdd:COG1061   229 REILLFLFDGIVYEYSL------KEAIEDGyLAPPEYYGIRVDLTDERAE-YD----ALSERLREALAADAERKDKIL-- 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 461 eallklrqvccdTRLLQRqedgarsgralssgklaylldmldelIAEGRRVLLFSQFTSMLALIEDALRQRGVDYVLLTG 540
Cdd:COG1061   296 ------------RELLRE--------------------------HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTG 337
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1154592370 541 ET--RDRRAPVQRFQSGKVPVfLISLKAGGVGLNLTAADTVIHYDP 584
Cdd:COG1061   338 DTpkKEREEILEAFRDGELRI-LVTVDVLNEGVDVPRLDVAILLRP 382
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
192-361 2.90e-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: 60.44  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGLSWmqtLRELDSGGVLADdMGLGKTLQSLAhVLLEKQAGRLDTPALVVMPTSLIPN-WLDEAERFA--PDLR 268
Cdd:cd18013     1 PHPYQKVAINF---IIEHPYCGLFLD-MGLGKTVTTLT-ALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNhlRNLT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 269 VLALHGAGRRRDFARIDEHDLVLTTYALLPRDAAELGKR-RFHLLILDEAQNIKNATTKAAVAARELAARHR--LCLTGT 345
Cdd:cd18013    76 VSVAVGTERQRSKAANTPADLYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKrlIGLTGT 155
                         170
                  ....*....|....*.
gi 1154592370 346 PLENHLGELWSLFHFL 361
Cdd:cd18013   156 PSPNGLMDLWAQIALL 171
ResIII pfam04851
Type III restriction enzyme, res subunit;
191-346 1.57e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.22  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 191 ELRPYQLEGL-SWMQTLRELDSGGVLADDMGLGKTLQSLAHVLLEKQAGRLDtPALVVMPT-SLIPNWLDEAERFAPDLR 268
Cdd:pfam04851   3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPRkDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 269 VLALHGAGRRRDFARIDEhDLVLTTY----ALLPRDAAELGKRRFHLLILDEA--------QNIKNATTKAavaarelaa 336
Cdd:pfam04851  82 EIGEIISGDKKDESVDDN-KIVVTTIqslyKALELASLELLPDFFDVIIIDEAhrsgassyRNILEYFKPA--------- 151
                         170
                  ....*....|
gi 1154592370 337 rHRLCLTGTP 346
Cdd:pfam04851 152 -FLLGLTATP 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
192-346 3.18e-08

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 53.08  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 192 LRPYQLEGL-SWMQTLRelDSGGVLADDMGLGKTLQSLAhvLLEKqagRLDTPALVVMPT-SLIPNWLDEAERFAPDLRV 269
Cdd:cd17926     1 LRPYQEEALeAWLAHKN--NRRGILVLPTGSGKTLTALA--LIAY---LKELRTLIVVPTdALLDQWKERFEDFLGDSSI 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154592370 270 LALhGAGRRRDFARIdehDLVLTTYALLPRDAAE--LGKRRFHLLILDEAQNIknATTKAAVAARELAARHRLCLTGTP 346
Cdd:cd17926    74 GLI-GGGKKKDFDDA---NVVVATYQSLSNLAEEekDLFDQFGLLIVDEAHHL--PAKTFSEILKELNAKYRLGLTATP 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
560-610 1.94e-07

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: 48.85  E-value: 1.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1154592370 560 FLISLKAGGVGLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKPVFVY 610
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
437-631 7.54e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 52.42  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 437 LALDRKVREEIARRGLARSR-IVILEALLKLRQ---------VCCDTRLLQRQEDGARS--------------------G 486
Cdd:COG1111   246 LALQKKLQRRIREDDSEGYRaISILAEALKLRHalelletqgVEALLRYLERLEEEARSsggskaskrlvsdprfrkamR 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 487 RALSSG----KLAYLLDMLDELIAE--GRRVLLFSQFTSMLALIEDALRQRGVDYVLLTGE-TRD---------RRAPVQ 550
Cdd:COG1111   326 LAEEADiehpKLSKLREILKEQLGTnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaSKEgdkgltqkeQIEILE 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 551 RFQSGKVPVfLISLKAGGVGLNLTAADTVIHYDPWWNPAVENQASDRAYRIGQDKpvfVYRLIARGTVEEKIQH--LQQE 628
Cdd:COG1111   406 RFRAGEFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR---VVVLIAKGTRDEAYYWssRRKE 481

                  ...
gi 1154592370 629 KAA 631
Cdd:COG1111   482 KKM 484
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
211-320 3.18e-06

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: 47.40  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 211 SGGVLADDMGLGKTLQSL--AHVLLEKQAGRldtpALVVMPT-SLIPNWLDE-AERFAPDLRVLALHGA--GRRRDFARI 284
Cdd:cd00046     2 ENVLITAPTGSGKTLAALlaALLLLLKKGKK----VLVLVPTkALALQTAERlRELFGPGIRVAVLVGGssAEEREKNKL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1154592370 285 DEHDLVLTTYALLPRD---AAELGKRRFHLLILDEAQNI 320
Cdd:cd00046    78 GDADIIIATPDMLLNLllrEDRLFLKDLKLIIVDEAHAL 116
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
493-584 7.48e-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: 37.10  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154592370 493 KLAYLLDMLDELIAEGRrVLLFSQFTSMLALIEDALRQRGVDYVLLTGET--RDRRAPVQRFQSGKVPVfLIslkAGGV- 569
Cdd:cd18787    13 KKLLLLLLLLEKLKPGK-AIIFVNTKKRVDRLAELLEELGIKVAALHGDLsqEERERALKKFRSGKVRV-LV---ATDVa 87
                          90
                  ....*....|....*..
gi 1154592370 570 --GLNLTAADTVIHYDP 584
Cdd:cd18787    88 arGLDIPGVDHVINYDL 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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