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Conserved domains on  [gi|386765298|ref|NP_001246974|]
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uncharacterized protein Dmel_CG10445, isoform D [Drosophila melanogaster]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12785252)

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

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 209-534 2.27e-120

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


The actual alignment was detected with superfamily member cd18072:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 241  Bit Score: 366.03  E-value: 2.27e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILASEETKNRKREEKKKALTlkwtqefnrvyckeirkism 288
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALT-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdEEEEHLSNGRYP 368
Cdd:cd18072   61 --------------------------------------------------------------------EWESKKDSTLVP 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SANTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGiEAFRSYDLVITSYNLVVNELKRYGNT---SPLFAVY 445
Cdd:cd18072   73 SAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIG-EVLRDYDIVITTYSLVAKEIPTYKEEsrsSPLFRIA 151

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNL-NESMLGHRRLN 524
Cdd:cd18072  152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVdNKSRKGGERLN 231

                        330
                 ....*....|
gi 386765298 525 FIIKPLMLRR 534
Cdd:cd18072  232 ILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 113-919 6.92e-83

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 281.73  E-value: 6.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 113 RLEALGEFLDTLRLREDQQEIKIEDNSELVDHTEQPKWSNLYSGLNRYRQKANHTAAQFYQHKSNIIDSLKTLYEPIQPR 192
Cdd:COG0553  146 LLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 193 PAIDDLEKQPALLLVRLLKHQQSCLKWMQFRERQKIsGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwt 272
Cdd:COG0553  226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL---------------------- 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 273 qefnrvyckeirkismfddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepev 352
Cdd:COG0553      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 353 fssdeeEEHLSNGRYPsanTLVVCPMSVMCQWAHEVAsKVAQNaIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLVVNEL 432
Cdd:COG0553  283 ------ELKERGLARP---VLIVAPTSLVGNWQRELA-KFAPG-LRVLVLDGTRERAKGANPFEDADLVITSYGLLRRDI 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 433 KRYGntsplfAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNvPN-FQDLQQWKK 511
Cdd:COG0553  352 ELLA------AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN-PGlLGSLKAFRE 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 512 N-------LNESMLghRRLNFIIKPLMLRRTKQKLqasgdMPALPSLKIELICVQLSKTEMAVYQILSAISKKIFTQFLL 584
Cdd:COG0553  425 RfarpiekGDEEAL--ERLRRLLRPFLLRRTKEDV-----LKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEG 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 585 QREKGNsdlnyyslertpqfiaghmsderyneiyerflkslgynpgekilgiyILVLLLRLRQFCCHPGLmigmlrgalt 664
Cdd:COG0553  498 IRRRGL-----------------------------------------------ILAALTRLRQICSHPAL---------- 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 665 aedvqnvkvdasdvegqlkmdVLAELDKFDEtdseddccdeedstrrdgnfklevikdeikeenvpwdsgddlptassfe 744
Cdd:COG0553  521 ---------------------LLEEGAELSG------------------------------------------------- 530

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 745 dqldsaralkllnpqnpifqfirPSAKLKMVIDKLEELLTGtNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAK 824
Cdd:COG0553  531 -----------------------RSAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 825 EREIVLRDFNANNEKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRI 904
Cdd:COG0553  587 ERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666

                        810
                 ....*....|....*
gi 386765298 905 KSLQDCKLEIAKVVL 919
Cdd:COG0553  667 LELLEEKRALAESVL 681
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 209-534 2.27e-120

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: 366.03  E-value: 2.27e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILASEETKNRKREEKKKALTlkwtqefnrvyckeirkism 288
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALT-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdEEEEHLSNGRYP 368
Cdd:cd18072   61 --------------------------------------------------------------------EWESKKDSTLVP 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SANTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGiEAFRSYDLVITSYNLVVNELKRYGNT---SPLFAVY 445
Cdd:cd18072   73 SAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIG-EVLRDYDIVITTYSLVAKEIPTYKEEsrsSPLFRIA 151

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNL-NESMLGHRRLN 524
Cdd:cd18072  152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVdNKSRKGGERLN 231

                        330
                 ....*....|
gi 386765298 525 FIIKPLMLRR 534
Cdd:cd18072  232 ILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 113-919 6.92e-83

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 281.73  E-value: 6.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 113 RLEALGEFLDTLRLREDQQEIKIEDNSELVDHTEQPKWSNLYSGLNRYRQKANHTAAQFYQHKSNIIDSLKTLYEPIQPR 192
Cdd:COG0553  146 LLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 193 PAIDDLEKQPALLLVRLLKHQQSCLKWMQFRERQKIsGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwt 272
Cdd:COG0553  226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL---------------------- 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 273 qefnrvyckeirkismfddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepev 352
Cdd:COG0553      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 353 fssdeeEEHLSNGRYPsanTLVVCPMSVMCQWAHEVAsKVAQNaIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLVVNEL 432
Cdd:COG0553  283 ------ELKERGLARP---VLIVAPTSLVGNWQRELA-KFAPG-LRVLVLDGTRERAKGANPFEDADLVITSYGLLRRDI 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 433 KRYGntsplfAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNvPN-FQDLQQWKK 511
Cdd:COG0553  352 ELLA------AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN-PGlLGSLKAFRE 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 512 N-------LNESMLghRRLNFIIKPLMLRRTKQKLqasgdMPALPSLKIELICVQLSKTEMAVYQILSAISKKIFTQFLL 584
Cdd:COG0553  425 RfarpiekGDEEAL--ERLRRLLRPFLLRRTKEDV-----LKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEG 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 585 QREKGNsdlnyyslertpqfiaghmsderyneiyerflkslgynpgekilgiyILVLLLRLRQFCCHPGLmigmlrgalt 664
Cdd:COG0553  498 IRRRGL-----------------------------------------------ILAALTRLRQICSHPAL---------- 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 665 aedvqnvkvdasdvegqlkmdVLAELDKFDEtdseddccdeedstrrdgnfklevikdeikeenvpwdsgddlptassfe 744
Cdd:COG0553  521 ---------------------LLEEGAELSG------------------------------------------------- 530

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 745 dqldsaralkllnpqnpifqfirPSAKLKMVIDKLEELLTGtNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAK 824
Cdd:COG0553  531 -----------------------RSAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 825 EREIVLRDFNANNEKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRI 904
Cdd:COG0553  587 ERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666

                        810
                 ....*....|....*
gi 386765298 905 KSLQDCKLEIAKVVL 919
Cdd:COG0553  667 LELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 212-654 3.46e-46

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: 167.48  E-value: 3.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  212 HQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwtqefnrvYCKEIRKISMfdd 291
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLL----------------------------YLKHVDKNWG--- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  292 eeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpEPevfssdeeeehlsngrypsan 371
Cdd:pfam00176  50 ---------------------------------------------------------GP--------------------- 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  372 TLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGI----EAFRSYDLVITSYNLVvneLKRYgntSPLFAVYWN 447
Cdd:pfam00176  52 TLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQERWkndpNFLADFDVVITTYETL---RKHK---ELLKKVHWH 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  448 RVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLN------ESMLGHR 521
Cdd:pfam00176 126 RIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpiergGGKKGVS 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  522 RLNFIIKPLMLRRTKQKLQASgdmpaLPSLKIELICVQLSKTEMAVYQilsaiskkiftQFLLQRekgnsdlnyyslert 601
Cdd:pfam00176 206 RLHKLLKPFLLRRTKKDVEKS-----LPPKVEYILFCRLSKLQRKLYQ-----------TFLLKK--------------- 254

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386765298  602 pqfiaghmsdeRYNEIyerfLKSLGYNPGEKilgiYILVLLLRLRQFCCHPGL 654
Cdd:pfam00176 255 -----------DLNAI----KTGEGGREIKA----SLLNILMRLRKICNHPGL 288
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 769-895 3.85e-44

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: 156.10  E-value: 3.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 769 SAKLKMVIDKLEELLTGtNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNANNEKRVLLLSLTA 848
Cdd:cd18793   10 SGKLEALLELLEELREP-GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386765298 849 GGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYM 895
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 373-904 5.94e-19

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 92.56  E-value: 5.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  373 LVVCPMSVMCQWAHEVasKVAQNAIRVLTFHGPNRHEIGIEAFR----SYDLVITSYNLVVNE---LKRYgntsplfavY 445
Cdd:PLN03142  223 MVVAPKSTLGNWMNEI--RRFCPVLRAVKFHGNPEERAHQREELlvagKFDVCVTSFEMAIKEktaLKRF---------S 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQ---WKKNLNESMLGH-- 520
Cdd:PLN03142  292 WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETfdeWFQISGENDQQEvv 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  521 RRLNFIIKPLMLRRTKQKLQASgdmpaLPSLKIELICVQLSktEMavyqilsaisKKIFTQFLLQRekgnsDLnyysler 600
Cdd:PLN03142  372 QQLHKVLRPFLLRRLKSDVEKG-----LPPKKETILKVGMS--QM----------QKQYYKALLQK-----DL------- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  601 tpqfiaghmsdERYNEIYERflkslgynpgEKILGIyilvlLLRLRQFCCHPGLmigmLRGAltaedvqnvkvdasdveg 680
Cdd:PLN03142  423 -----------DVVNAGGER----------KRLLNI-----AMQLRKCCNHPYL----FQGA------------------ 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  681 qlkmdvlaeldkfdetdseddccdeedstrrdgnfklevikdeikEENVPWDSGDDLPTASSfedqldsaralkllnpqn 760
Cdd:PLN03142  455 ---------------------------------------------EPGPPYTTGEHLVENSG------------------ 471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  761 pifqfirpsaklKMVI-DKLEELLTGTNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNA-NNE 838
Cdd:PLN03142  472 ------------KMVLlDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpGSE 539

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298  839 KRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRI 904
Cdd:PLN03142  540 KFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKV 605
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 776-884 1.36e-17

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 79.18  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  776 IDKLEELL-TGTNDKIIVTSQWVSYLAIvRKRLQDLSWETLDFNGQLTAKEREIVLRDFNanNEKRVLLLSLTAGGVGLN 854
Cdd:pfam00271   3 LEALLELLkKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 386765298  855 LNVANHMLIVDLHWNPQLERQAQDRIYRYG 884
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
802-884 9.52e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 9.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298   802 IVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNANneKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIY 881
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNG--KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 386765298   882 RYG 884
Cdd:smart00490  80 RAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
360-486 1.25e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.04  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298   360 EHLSNGRYPSanTLVVCPMSV-MCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRS--YDLVITSYNLVVNELKRyg 436
Cdd:smart00487  47 EALKRGKGGR--VLVLVPTRElAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN-- 122

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386765298   437 ntSPLFAVYWNRVILDEAHIIRNSKTNC-CNSVCQLRAHCH--WALTGTPVQN 486
Cdd:smart00487 123 --DKLSLSNVDLVILDEAHRLLDGGFGDqLEKLLKLLPKNVqlLLLSATPPEE 173
 
Name Accession Description Interval E-value
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 209-534 2.27e-120

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: 366.03  E-value: 2.27e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILASEETKNRKREEKKKALTlkwtqefnrvyckeirkism 288
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEEKEKALT-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdEEEEHLSNGRYP 368
Cdd:cd18072   61 --------------------------------------------------------------------EWESKKDSTLVP 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SANTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGiEAFRSYDLVITSYNLVVNELKRYGNT---SPLFAVY 445
Cdd:cd18072   73 SAGTLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNRERIG-EVLRDYDIVITTYSLVAKEIPTYKEEsrsSPLFRIA 151

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNL-NESMLGHRRLN 524
Cdd:cd18072  152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVdNKSRKGGERLN 231

                        330
                 ....*....|
gi 386765298 525 FIIKPLMLRR 534
Cdd:cd18072  232 ILTKSLLLRR 241
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 113-919 6.92e-83

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 281.73  E-value: 6.92e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 113 RLEALGEFLDTLRLREDQQEIKIEDNSELVDHTEQPKWSNLYSGLNRYRQKANHTAAQFYQHKSNIIDSLKTLYEPIQPR 192
Cdd:COG0553  146 LLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 193 PAIDDLEKQPALLLVRLLKHQQSCLKWMQFRERQKIsGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwt 272
Cdd:COG0553  226 RLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGL-GGLLADDMGLGKTIQALALLL---------------------- 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 273 qefnrvyckeirkismfddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepev 352
Cdd:COG0553      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 353 fssdeeEEHLSNGRYPsanTLVVCPMSVMCQWAHEVAsKVAQNaIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLVVNEL 432
Cdd:COG0553  283 ------ELKERGLARP---VLIVAPTSLVGNWQRELA-KFAPG-LRVLVLDGTRERAKGANPFEDADLVITSYGLLRRDI 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 433 KRYGntsplfAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNvPN-FQDLQQWKK 511
Cdd:COG0553  352 ELLA------AVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLN-PGlLGSLKAFRE 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 512 N-------LNESMLghRRLNFIIKPLMLRRTKQKLqasgdMPALPSLKIELICVQLSKTEMAVYQILSAISKKIFTQFLL 584
Cdd:COG0553  425 RfarpiekGDEEAL--ERLRRLLRPFLLRRTKEDV-----LKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEG 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 585 QREKGNsdlnyyslertpqfiaghmsderyneiyerflkslgynpgekilgiyILVLLLRLRQFCCHPGLmigmlrgalt 664
Cdd:COG0553  498 IRRRGL-----------------------------------------------ILAALTRLRQICSHPAL---------- 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 665 aedvqnvkvdasdvegqlkmdVLAELDKFDEtdseddccdeedstrrdgnfklevikdeikeenvpwdsgddlptassfe 744
Cdd:COG0553  521 ---------------------LLEEGAELSG------------------------------------------------- 530

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 745 dqldsaralkllnpqnpifqfirPSAKLKMVIDKLEELLTGtNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAK 824
Cdd:COG0553  531 -----------------------RSAKLEALLELLEELLAE-GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 825 EREIVLRDFNANNEKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRI 904
Cdd:COG0553  587 ERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKI 666

                        810
                 ....*....|....*
gi 386765298 905 KSLQDCKLEIAKVVL 919
Cdd:COG0553  667 LELLEEKRALAESVL 681
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 209-534 5.12e-62

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: 210.22  E-value: 5.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRerqkisGGILADDMGLGKTLSMIALILASeetknrkreekkkaltlkwtqefnrvyckeirkism 288
Cdd:cd18008    1 LLPYQKQGLAWMLPR------GGILADEMGLGKTIQALALILAT------------------------------------ 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyePPEKRtchvktkkinqfrilddddndagdkavvedeqkdllAKTPEPEVFSSDEEEEHLSNGryp 368
Cdd:cd18008   39 ---------------RPQDP------------------------------------KIPEELEENSSDPKKLYLSKT--- 64

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 sanTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHeIGIEAFRSYDLVITSYNLVVNELKRYGNT---------- 438
Cdd:cd18008   65 ---TLIVVPLSLLSQWKDEIEKHTKPGSLKVYVYHGSKRI-KSIEELSDYDIVITTYGTLASEFPKNKKGggrdskekea 140

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 439 SPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKN-----L 513
Cdd:cd18008  141 SPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDiskpfS 220

                        330       340
                 ....*....|....*....|.
gi 386765298 514 NESMLGHRRLNFIIKPLMLRR 534
Cdd:cd18008  221 KNDRKALERLQALLKPILLRR 241
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 212-654 3.46e-46

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: 167.48  E-value: 3.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  212 HQQSCLKWMQFRERQKISGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwtqefnrvYCKEIRKISMfdd 291
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLL----------------------------YLKHVDKNWG--- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  292 eeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpEPevfssdeeeehlsngrypsan 371
Cdd:pfam00176  50 ---------------------------------------------------------GP--------------------- 51

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  372 TLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGI----EAFRSYDLVITSYNLVvneLKRYgntSPLFAVYWN 447
Cdd:pfam00176  52 TLIVVPLSLLHNWMNEFERWVSPPALRVVVLHGNKRPQERWkndpNFLADFDVVITTYETL---RKHK---ELLKKVHWH 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  448 RVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLN------ESMLGHR 521
Cdd:pfam00176 126 RIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpiergGGKKGVS 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  522 RLNFIIKPLMLRRTKQKLQASgdmpaLPSLKIELICVQLSKTEMAVYQilsaiskkiftQFLLQRekgnsdlnyyslert 601
Cdd:pfam00176 206 RLHKLLKPFLLRRTKKDVEKS-----LPPKVEYILFCRLSKLQRKLYQ-----------TFLLKK--------------- 254

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386765298  602 pqfiaghmsdeRYNEIyerfLKSLGYNPGEKilgiYILVLLLRLRQFCCHPGL 654
Cdd:pfam00176 255 -----------DLNAI----KTGEGGREIKA----SLLNILMRLRKICNHPGL 288
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 769-895 3.85e-44

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: 156.10  E-value: 3.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 769 SAKLKMVIDKLEELLTGtNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNANNEKRVLLLSLTA 848
Cdd:cd18793   10 SGKLEALLELLEELREP-GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386765298 849 GGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYM 895
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 213-536 1.13e-33

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: 129.22  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 213 QQSCLKWMQFRERQKIsGGILADDMGLGKTLSMIALILASEEtknrkreekkkaltlkwtqefnrvyckeirkismfdde 292
Cdd:cd18012    9 QKEGFNWLSFLRHYGL-GGILADDMGLGKTLQTLALLLSRKE-------------------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 293 eesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdeeeehlSNGRYPSant 372
Cdd:cd18012   50 ----------------------------------------------------------------------EGRKGPS--- 56

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEvASKVAQnAIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLVVNELKRYGNTSplfavyWNRVILD 452
Cdd:cd18012   57 LVVAPTSLIYNWEEE-AAKFAP-ELKVLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIELLKEVK------FHYLVLD 128

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 453 EAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVN---VPNFQDLQQ-----WKKNLNESMLghRRLN 524
Cdd:cd18012  129 EAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNpglLGSYKRFKKrfakpIEKDGDEEAL--EELK 206

                        330
                 ....*....|..
gi 386765298 525 FIIKPLMLRRTK 536
Cdd:cd18012  207 KLISPFILRRLK 218
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 209-534 4.73e-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: 127.97  E-value: 4.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRER----------------------------QKISGGILADDMGLGKTLSMIALILASEetknrkr 260
Cdd:cd18071    1 LLPHQKQALAWMVSRENsqdlppfweeavglflntitnfsqkkrpELVRGGILADDMGLGKTLTTISLILANF------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 261 eekkkaltlkwtqefnrvyckeirkismfddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeq 340
Cdd:cd18071      --------------------------------------------------------------------------------

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 341 kdllaktpepevfssdeeeehlsngrypsanTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEiGIEAFRSYDL 420
Cdd:cd18071   74 -------------------------------TLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNR-DPKLLSKYDI 121

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 421 VITSYNLVVNElkrYGN--TSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFV 498
Cdd:cd18071  122 VLTTYNTLASD---FGAkgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFL 198

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 386765298 499 NVPNFQDLQQWKKNLNE-----SMLGHRRLNFIIKPLMLRR 534
Cdd:cd18071  199 HLKPFSNPEYWRRLIQRpltmgDPTGLKRLQVLMKQITLRR 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 209-533 1.19e-32

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: 127.46  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMqfrerqKISGGILADDMGLGKTLSMIALILASEETknrkreekkkaltlkwtqefnrvyckEIRKISM 288
Cdd:cd18070    1 LLPYQRRAVNWM------LVPGGILADEMGLGKTVEVLALILLHPRP--------------------------DNDLDAA 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 FDDEEESGKEeeqyEPPEKRTCHVKTKKinqfrilddddndagdkavvedeqkdllaktpepevfssdeeeehlsngryp 368
Cdd:cd18070   49 DDDSDEMVCC----PDCLVAETPVSSKA---------------------------------------------------- 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 sanTLVVCPMSVMCQWAHEVAsKVAQNAIRVLTFHGPNR----HEIGIEAFRSYDLVITSYNLVVNEL------------ 432
Cdd:cd18070   73 ---TLIVCPSAILAQWLDEIN-RHVPSSLKVLTYQGVKKdgalASPAPEILAEYDIVVTTYDVLRTELhyaeanrsnrrr 148

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 433 ----KRYGNTSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQL-RAHChWALTGTPVQNRGVDVFALLRFVNVPNFQDLQ 507
Cdd:cd18070  149 rrqkRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLpRVNR-WCVSGTPIQRGLDDLFGLLSFLGVEPFCDSD 227

                        330       340
                 ....*....|....*....|....*....
gi 386765298 508 QWKKNLNESMLGHRRLNF---IIKPLMLR 533
Cdd:cd18070  228 WWARVLIRPQGRNKAREPlaaLLKELLWR 256
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 209-501 1.85e-30

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: 118.44  E-value: 1.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRErQKISGGILADDMGLGKTLSMIALILaseetknrkreekkkaltlkwtqefnrvyckeirkism 288
Cdd:cd17919    1 LRPYQLEGLNFLLELY-ENGPGGILADEMGLGKTLQAIAFLA-------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdeeeeHLSNGRYP 368
Cdd:cd17919   42 ------------------------------------------------------------------------YLLKEGKE 49

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SANTLVVCPMSVMCQWAHEVaSKVAQNaIRVLTFHGPNRHEIGI---EAFRSYDLVITSYNLVVNELKRygntspLFAVY 445
Cdd:cd17919   50 RGPVLVVCPLSVLENWEREF-EKWTPD-LRVVVYHGSQRERAQIrakEKLDKFDVVLTTYETLRRDKAS------LRKFR 121

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVP 501
Cdd:cd17919  122 WDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPP 177
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 209-503 7.09e-24

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: 101.27  E-value: 7.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRERQKISGgILADDMGLGKTLSMIAlILASeetknrkreekkkaltlkwtqefnrvyckeirkism 288
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHG-ILCDDMGLGKTLQTLC-ILAS------------------------------------ 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtCHVKTKkinqfrilddddndagdkavvedeqkdllaktpepevfsSDEEEEHLsngryP 368
Cdd:cd17999   43 ---------------------DHHKRA---------------------------------------NSFNSENL-----P 57

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SantLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRS-YDLVITSYNLVVNELKRYGNTSplfavyWN 447
Cdd:cd17999   58 S---LVVCPPTLVGHWVAEIKKYFPNAFLKPLAYVGPPQERRRLREQGEkHNVIVASYDVLRNDIEVLTKIE------WN 128

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298 448 RVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVnVPNF 503
Cdd:cd17999  129 YCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFL-MPGY 183
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 373-904 5.94e-19

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 92.56  E-value: 5.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  373 LVVCPMSVMCQWAHEVasKVAQNAIRVLTFHGPNRHEIGIEAFR----SYDLVITSYNLVVNE---LKRYgntsplfavY 445
Cdd:PLN03142  223 MVVAPKSTLGNWMNEI--RRFCPVLRAVKFHGNPEERAHQREELlvagKFDVCVTSFEMAIKEktaLKRF---------S 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQ---WKKNLNESMLGH-- 520
Cdd:PLN03142  292 WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETfdeWFQISGENDQQEvv 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  521 RRLNFIIKPLMLRRTKQKLQASgdmpaLPSLKIELICVQLSktEMavyqilsaisKKIFTQFLLQRekgnsDLnyysler 600
Cdd:PLN03142  372 QQLHKVLRPFLLRRLKSDVEKG-----LPPKKETILKVGMS--QM----------QKQYYKALLQK-----DL------- 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  601 tpqfiaghmsdERYNEIYERflkslgynpgEKILGIyilvlLLRLRQFCCHPGLmigmLRGAltaedvqnvkvdasdveg 680
Cdd:PLN03142  423 -----------DVVNAGGER----------KRLLNI-----AMQLRKCCNHPYL----FQGA------------------ 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  681 qlkmdvlaeldkfdetdseddccdeedstrrdgnfklevikdeikEENVPWDSGDDLPTASSfedqldsaralkllnpqn 760
Cdd:PLN03142  455 ---------------------------------------------EPGPPYTTGEHLVENSG------------------ 471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  761 pifqfirpsaklKMVI-DKLEELLTGTNDKIIVTSQWVSYLAIVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNA-NNE 838
Cdd:PLN03142  472 ------------KMVLlDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpGSE 539

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298  839 KRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIYRYGQTKPTFIYRYMCQDTVEQRI 904
Cdd:PLN03142  540 KFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKV 605
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 776-884 1.36e-17

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 79.18  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298  776 IDKLEELL-TGTNDKIIVTSQWVSYLAIvRKRLQDLSWETLDFNGQLTAKEREIVLRDFNanNEKRVLLLSLTAGGVGLN 854
Cdd:pfam00271   3 LEALLELLkKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVAERGLD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 386765298  855 LNVANHMLIVDLHWNPQLERQAQDRIYRYG 884
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 209-539 7.03e-17

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: 81.27  E-value: 7.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMqFRERQKISGGILADDMGLGKTLSMIALILAseetknrkreekkkaltlkwtqefnrVYckeirkism 288
Cdd:cd18005    1 LRDYQREGVEFM-YDLYKNGRGGILGDDMGLGKTVQVIAFLAA--------------------------VL--------- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppeKRTCHVKTKKINQFRILddddndagdkavvedeqkdllaktpepevfssdeEEEHLSNGRYP 368
Cdd:cd18005   45 ------------------GKTGTRRDRENNRPRFK----------------------------------KKPPASSAKKP 72

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SantLVVCPMSVMCQWAHEVaSKVAQnaIRVLTFHGPNRHEIGIEAFRS--YDLVITSYNLVVNELKRygntspLFAVYW 446
Cdd:cd18005   73 V---LIVAPLSVLYNWKDEL-DTWGH--FEVGVYHGSRKDDELEGRLKAgrLEVVVTTYDTLRRCIDS------LNSINW 140

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 447 NRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESMLGHRRLNFI 526
Cdd:cd18005  141 SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTAT 220

                        330
                 ....*....|....
gi 386765298 527 IKPLML-RRTKQKL 539
Cdd:cd18005  221 ARELRLgRKRKQEL 234
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 373-536 2.75e-16

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: 78.90  E-value: 2.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVasKVAQNAIRVLTFHGPN--RHEIGIEAF--RSYDLVITSYNLVVNE---LKRYGntsplfavy 445
Cdd:cd17997   57 LIIVPKSTLDNWMREF--KRWCPSLRVVVLIGDKeeRADIIRDVLlpGKFDVCITSYEMVIKEktvLKKFN--------- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVnVPNF----QDLQQWKKNLNESMLGH- 520
Cdd:cd17997  126 WRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFL-LPDVftssEDFDEWFNVNNCDDDNQe 204

                        170
                 ....*....|....*...
gi 386765298 521 --RRLNFIIKPLMLRRTK 536
Cdd:cd17997  205 vvQRLHKVLRPFLLRRIK 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 209-501 4.56e-16

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: 77.36  E-value: 4.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 209 LLKHQQSCLKWMQFRERQKiSGGILADDMGLGKTLSMIALILAseetknrkreekkkaltLKWTQEFNRvyckeirkism 288
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQR-VGGILGDEMGLGKTIQIIAFLAA-----------------LHHSKLGLG----------- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 289 fddeeesgkeeeqyeppekrtchvktkkinqfrilddddndagdkavvedeqkdllaktpepevfssdeeeehlsngryP 368
Cdd:cd18000   52 -------------------------------------------------------------------------------P 52

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 369 SantLVVCPMSVMCQW---AHEVASKVaqnaiRVLTFH------GPNRHEIGIEAFRS--------YDLVITSYNLVvNE 431
Cdd:cd18000   53 S---LIVCPATVLKQWvkeFHRWWPPF-----RVVVLHssgsgtGSEEKLGSIERKSQlirkvvgdGGILITTYEGF-RK 123

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 432 LKRYgntspLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVP 501
Cdd:cd18000  124 HKDL-----LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFPP 188
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 373-534 8.13e-16

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: 77.54  E-value: 8.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQnaIRVLTFHGPNRHEIGIEAF----------RSYDLVITSYNLVVNELKRYGNtsplf 442
Cdd:cd18002   54 LVIAPASTLHNWQQEISRFVPQ--FKVLPYWGNPKDRKVLRKFwdrknlytrdAPFHVVITSYQLVVQDEKYFQR----- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 443 aVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVnVPNFQD----LQQW--------- 509
Cdd:cd18002  127 -VKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFI-MPTLFDshdeFNEWfskdiesha 204

                        170       180
                 ....*....|....*....|....*..
gi 386765298 510 --KKNLNESMLghRRLNFIIKPLMLRR 534
Cdd:cd18002  205 enKTGLNEHQL--KRLHMILKPFMLRR 229
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 372-498 4.90e-15

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: 75.49  E-value: 4.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 372 TLVVCPMSVMCQWAHEVASKVAqnAIRVLTFHGPNRHEigieafRSYDL---------VITSYNLVVNelkrygNTSPLF 442
Cdd:cd18001   52 VLVVMPTSLIPHWVKEFAKWTP--GLRVKVFHGTSKKE------RERNLeriqrgggvLLTTYGMVLS------NTEQLS 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765298 443 AVY-----WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFV 498
Cdd:cd18001  118 ADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFA 178
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 360-534 5.08e-15

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: 75.79  E-value: 5.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 360 EHLSNGRYPSANTLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRS----YDLVITSYNLVVNELKRY 435
Cdd:cd18004   50 KQGPYGKPTAKKALIVCPSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKASLDFFSsastYPVLIISYETLRRHAEKL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 436 GNTSPLfavywNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKK---- 511
Cdd:cd18004  130 SKKISI-----DLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKvfee 204

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 386765298 512 ----------NLNESMLGHRR---LNFIIKPLMLRR 534
Cdd:cd18004  205 pilrsrdpdaSEEDKELGAERsqeLSELTSRFILRR 240
HELICc smart00490
helicase superfamily c-terminal domain;
802-884 9.52e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 9.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298   802 IVRKRLQDLSWETLDFNGQLTAKEREIVLRDFNANneKRVLLLSLTAGGVGLNLNVANHMLIVDLHWNPQLERQAQDRIY 881
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNG--KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 386765298   882 RYG 884
Cdd:smart00490  80 RAG 82
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 373-534 7.67e-14

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: 71.61  E-value: 7.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWahEVASKVAQNAIRVLTFHGP--NRHEIGIEAFR--SYDLVITSYNLVVNELKRYGNtsplfaVYWNR 448
Cdd:cd18003   54 LIVVPTSVMLNW--EMEFKRWCPGFKILTYYGSakERKLKRQGWMKpnSFHVCITSYQLVVQDHQVFKR------KKWKY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVnVPN----FQDLQQW-----------KKNL 513
Cdd:cd18003  126 LILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFL-MPHifqsHQEFKEWfsnpltamsegSQEE 204

                        170       180
                 ....*....|....*....|.
gi 386765298 514 NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18003  205 NEELV--RRLHKVLRPFLLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 373-536 2.93e-13

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: 70.49  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQnaIRVLTFHGP-----------NRHEIGIEAFrsyDLVITSYNLVVNELKRygntspL 441
Cdd:cd18009   56 LVIAPLSTLPNWVNEFARFTPS--VPVLLYHGTkeererlrkkiMKREGTLQDF---PVVVTSYEIAMRDRKA------L 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 442 FAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDL---QQW--------- 509
Cdd:cd18009  125 QHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLssfESWfdfsslsdn 204

                        170       180       190
                 ....*....|....*....|....*....|..
gi 386765298 510 ---KKNLNESMLGH--RRLNFIIKPLMLRRTK 536
Cdd:cd18009  205 aadISNLSEEREQNivHMLHAILKPFLLRRLK 236
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 373-534 8.12e-13

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: 68.81  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNAIrvlTFHGP-------------NRHEIGIEAFRSY--DLVITSYNLVVNELkrygn 437
Cdd:cd17995   54 LVIAPLSTIPNWQREFETWTDMNVV---VYHGSgesrqiiqqyemyFKDAQGRKKKGVYkfDVLITTYEMVIADA----- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 438 tSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESM 517
Cdd:cd17995  126 -EELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLK 204

                        170
                 ....*....|....*....
gi 386765298 518 LGH--RRLNFIIKPLMLRR 534
Cdd:cd17995  205 TAEqvEKLQALLKPYMLRR 223
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 373-534 8.71e-12

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: 65.85  E-value: 8.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNAIrvlTFHGPNRHEIGIEAFRSY---------------DLVITSYNLVVNELKRygn 437
Cdd:cd18060   53 LVIAPLSTITNWEREFNTWTEMNTI---VYHGSLASRQMIQQYEMYckdsrgrlipgaykfDALITTFEMILSDCPE--- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 438 tspLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESM 517
Cdd:cd18060  127 ---LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLK 203

                        170
                 ....*....|....*....
gi 386765298 518 LGH--RRLNFIIKPLMLRR 534
Cdd:cd18060  204 TEEqvQKLQAILKPMMLRR 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 373-534 1.24e-10

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: 62.07  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVaSKVAQNaIRVLTFHG--PNRHEI--GIEAFRSYDLVITSYNLVVNElkrygnTSPLFAVYWNR 448
Cdd:cd18006   54 LVLCPLSVLDNWKEEL-NRFAPD-LSVITYMGdkEKRLDLqqDIKSTNRFHVLLTTYEICLKD------ASFLKSFPWAS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNF------QDLQQWKKNLNESMLgHRR 522
Cdd:cd18006  126 LVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkdkldDFIKAYSETDDESET-VEE 204

                        170
                 ....*....|..
gi 386765298 523 LNFIIKPLMLRR 534
Cdd:cd18006  205 LHLLLQPFLLRR 216
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 373-496 1.31e-10

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: 62.22  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVaskvaqnaIRVLtfHGPNRHEIGI-----EAFRSYD--LVITSYNLVVNELKRygntspLFAVY 445
Cdd:cd18010   47 LIVCPSSLRLTWADEI--------ERWL--PSLPPDDIQVivkskDGLRDGDakVVIVSYDLLRRLEKQ------LLARK 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386765298 446 WNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWA--LTGTPVQNRGVDVFALLR 496
Cdd:cd18010  111 FKVVICDESHYLKNSKAKRTKAALPLLKRAKRVilLSGTPALSRPIELFTQLD 163
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 361-503 2.12e-10

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: 61.92  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 361 HLSNGRYPSANT-LVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIG---IEAFRSYD-----LVItSYNLVVNE 431
Cdd:cd18007   48 HTYLAAAPRRSRpLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSASKRAdarLRKINKWHkeggvLLI-GYELFRNL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 432 LKRYGNTSPLFAVYW--------NRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVnVPNF 503
Cdd:cd18007  127 ASNATTDPRLKQEFIaalldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA-RPKY 205
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 373-534 3.22e-10

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: 60.77  E-value: 3.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRSYDLVITSYNLvvneLKRYGNTSPLF-AVYWNRVIL 451
Cdd:cd18011   51 LILCPASLVEQWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEEFPIVIVSLDL----LKRSEERRGLLlSEEWDLVVV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 452 DEAHIIRNS---KTNCCNSVCQLRAHCHWA---LTGTPVQNRGVDVFALLRFVNvPNFqdlqqwkKNLNESMLGHRRLNF 525
Cdd:cd18011  127 DEAHKLRNSgggKETKRYKLGRLLAKRARHvllLTATPHNGKEEDFRALLSLLD-PGR-------FAVLGRFLRLDGLRE 198


                 ....*....
gi 386765298 526 IIKPLMLRR 534
Cdd:cd18011  199 VLAKVLLRR 207
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 373-536 3.68e-10

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: 61.23  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVAsKVAQnAIRVLTFHGP--NRHEI-GIEAFRSYDLVITSYNLVVNElkrygnTSPLFAVYWNRV 449
Cdd:cd17996   57 LVIVPLSTLSNWVSEFE-KWAP-SVSKIVYKGTpdVRKKLqSQIRAGKFNVLLTTYEYIIKD------KPLLSKIKWKYM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 450 ILDEAHIIRNSKtncCNSVCQLRAHCHWA----LTGTPVQNRGVDVFALLRFVnVPNF----QDLQQW------------ 509
Cdd:cd17996  129 IIDEGHRMKNAQ---SKLTQTLNTYYHARyrllLTGTPLQNNLPELWALLNFL-LPKIfkscKTFEQWfntpfantgeqv 204

                        170       180
                 ....*....|....*....|....*....
gi 386765298 510 KKNLN--ESMLGHRRLNFIIKPLMLRRTK 536
Cdd:cd17996  205 KIELNeeETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 372-521 6.79e-10

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: 60.24  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 372 TLVVCPMSVMCQWAHEVASKVAQNAIRVLTFHGPNRheigIEAFRS---YDLVITSYNLVVNELKRYGNtsplfaVYWNR 448
Cdd:cd18066   63 ALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHK----VEEFIAsplYSVLIISYEMLLRSLDQISK------LNFDL 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESMLGHR 521
Cdd:cd18066  133 VICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSR 205
DEXDc smart00487
DEAD-like helicases superfamily;
360-486 1.25e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.04  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298   360 EHLSNGRYPSanTLVVCPMSV-MCQWAHEVASKVAQNAIRVLTFHGPNRHEIGIEAFRS--YDLVITSYNLVVNELKRyg 436
Cdd:smart00487  47 EALKRGKGGR--VLVLVPTRElAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN-- 122

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386765298   437 ntSPLFAVYWNRVILDEAHIIRNSKTNC-CNSVCQLRAHCH--WALTGTPVQN 486
Cdd:smart00487 123 --DKLSLSNVDLVILDEAHRLLDGGFGDqLEKLLKLLPKNVqlLLLSATPPEE 173
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 373-534 1.57e-09

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: 59.29  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNAIrvlTFHGPN-------------RHEIG--IEAFRSYDLVITSYNLVVN---ELKR 434
Cdd:cd18058   53 LIIAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemyyRDEQGnpLSGIFKFQVVITTFEMILAdcpELKK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 435 ygntsplfaVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQD----LQQWK 510
Cdd:cd18058  130 ---------INWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSettfLEEFG 200

                        170       180
                 ....*....|....*....|....
gi 386765298 511 KNLNESMLghRRLNFIIKPLMLRR 534
Cdd:cd18058  201 DLKTEEQV--KKLQSILKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 373-536 2.12e-09

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: 59.29  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVaSKVAQNAIRVLTFHGPNRHEIGIEAFRS--YDLVITSYNLVVNElkrygnTSPLFAVYWNRVI 450
Cdd:cd18062   77 LIIVPLSTLSNWVYEF-DKWAPSVVKVSYKGSPAARRAFVPQLRSgkFNVLLTTYEYIIKD------KQILAKIRWKYMI 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 451 LDEAHIIRNSKtncCNSVCQLRAHC----HWALTGTPVQNRGVDVFALLRFVNVPNFQD---LQQW----------KKNL 513
Cdd:cd18062  150 VDEGHRMKNHH---CKLTQVLNTHYvaprRLLLTGTPLQNKLPELWALLNFLLPTIFKScstFEQWfnapfamtgeKVDL 226

                        170       180
                 ....*....|....*....|....*
gi 386765298 514 N--ESMLGHRRLNFIIKPLMLRRTK 536
Cdd:cd18062  227 NeeETILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 373-536 2.91e-09

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: 58.49  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAqnAIRVLTFHGPNRHEIG----IEAFRSYDLVITSYNLVVNElkrygnTSPLFAVYWNR 448
Cdd:cd18065   69 MVLVPKSTLHNWMNEFKRWVP--SLRAVCLIGDKDARAAfirdVMMPGEWDVCVTSYEMVIKE------KSVFKKFNWRY 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQ---DLQQWKKNLNesMLGHR---- 521
Cdd:cd18065  141 LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNsadDFDSWFDTKN--CLGDQklve 218

                        170
                 ....*....|....*
gi 386765298 522 RLNFIIKPLMLRRTK 536
Cdd:cd18065  219 RLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 373-498 3.77e-09

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: 57.40  E-value: 3.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAqnAIRVLTFHGPN------RHEIgIEAFRSYDLVITSYNLVVN---ELKRYGNTSPLFA 443
Cdd:cd17998   53 LVVVPSSTLDNWLREFKRWCP--SLKVEPYYGSQeerkhlRYDI-LKGLEDFDVIVTTYNLATSnpdDRSFFKRLKLNYV 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765298 444 VYwnrvilDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFV 498
Cdd:cd17998  130 VY------DEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 373-534 4.89e-09

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: 57.73  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNairVLTFHGPNRHEIGIEAFRSY---------------DLVITSYNLVVNELKRYGN 437
Cdd:cd18059   53 LVIAPLSTIPNWEREFRTWTELN---VVVYHGSQASRRTIQLYEMYfkdpqgrvikgsykfHAIITTFEMILTDCPELRN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 438 tsplfaVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQD----LQQWKKNL 513
Cdd:cd18059  130 ------IPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSettfMQEFGDLK 203

                        170       180
                 ....*....|....*....|.
gi 386765298 514 NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18059  204 TEEQV--QKLQAILKPMMLRR 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 418-542 9.58e-09

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: 56.98  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 418 YDLVITSYNLVVNELKRYGNTSplfavyWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRF 497
Cdd:cd18064  116 WDVCVTSYEMLIKEKSVFKKFN------WRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNF 189

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386765298 498 VNVPNFQ---DLQQWKKNLNesMLGHR----RLNFIIKPLMLRRTKQKLQAS 542
Cdd:cd18064  190 LLPDVFNsaeDFDSWFDTNN--CLGDQklveRLHMVLRPFLLRRIKADVEKS 239
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 364-536 1.12e-08

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: 57.00  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 364 NGRYpsantLVVCPMSVMCQWAHEVaSKVAQNAIRVLTFHGPNRHEIGIEAFRS--YDLVITSYNLVVNElkrygnTSPL 441
Cdd:cd18063   73 NGPY-----LIIVPLSTLSNWTYEF-DKWAPSVVKISYKGTPAMRRSLVPQLRSgkFNVLLTTYEYIIKD------KHIL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 442 FAVYWNRVILDEAHIIRNSKtncCNSVCQLRAHC----HWALTGTPVQNRGVDVFALLRFVNVPNFQD---LQQW----- 509
Cdd:cd18063  141 AKIRWKYMIVDEGHRMKNHH---CKLTQVLNTHYvaprRILLTGTPLQNKLPELWALLNFLLPTIFKScstFEQWfnapf 217

                        170       180       190
                 ....*....|....*....|....*....|....
gi 386765298 510 -----KKNLN--ESMLGHRRLNFIIKPLMLRRTK 536
Cdd:cd18063  218 amtgeRVDLNeeETILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 373-534 1.20e-08

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: 56.21  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVA-------------SKVAQNAIRVLTFHGPNRHEIgieafrSYDLVITSYNLVVNELKRYGNTS 439
Cdd:cd17993   55 LVVVPLSTMPAWQREFAkwapdmnvivylgDIKSRDTIREYEFYFSQTKKL------KFNVLLTTYEIILKDKAFLGSIK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 440 plfavyWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESM-L 518
Cdd:cd17993  129 ------WQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQeK 202

                        170
                 ....*....|....*.
gi 386765298 519 GHRRLNFIIKPLMLRR 534
Cdd:cd17993  203 GIADLHKELEPFILRR 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 344-534 2.07e-08

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: 56.17  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 344 LAKTPEPEVFSSDEEEEHLSNGRYpsantLVVCPMSVMCQWAHE-------------VASKVAQNAIRVLTFHGPNRHEI 410
Cdd:cd18054   50 LGKTIQTISFLSYLFHQHQLYGPF-----LLVVPLSTLTSWQREfeiwapeinvvvyIGDLMSRNTIREYEWIHSQTKRL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 411 gieafrSYDLVITSYNLVVNELKRYGNtsplfaVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVD 490
Cdd:cd18054  125 ------KFNALITTYEILLKDKTVLGS------INWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386765298 491 VFALLRFVNVPNFQDLQQWKKNLNESML-GHRRLNFIIKPLMLRR 534
Cdd:cd18054  193 LWSLLHFIMPEKFEFWEDFEEDHGKGREnGYQSLHKVLEPFLLRR 237
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 373-534 4.09e-08

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: 55.01  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASkvaQNAIRVLTFHGPNRHEIGIEAFRSY---------------DLVITSYNLVVnelkryGN 437
Cdd:cd18061   53 LIIAPLSTIANWEREFRT---WTDLNVVVYHGSLISRQMIQQYEMYfrdsqgriirgayrfQAIITTFEMIL------GG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 438 TSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQD----LQQWKKNL 513
Cdd:cd18061  124 CPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSestfMQEFGDLK 203

                        170       180
                 ....*....|....*....|.
gi 386765298 514 NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18061  204 TEEQV--QKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 344-534 6.39e-07

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: 51.60  E-value: 6.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 344 LAKTPEPEVFSSDEEEEHLSNGRYpsantLVVCPMSVMCQWAHE-------------VASKVAQNAIRVLTFH------- 403
Cdd:cd18056   30 LGKTVQTAVFLYSLYKEGHSKGPF-----LVSAPLSTIINWEREfemwapdmyvvtyVGDKDSRAIIRENEFSfednair 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 404 -GPNRHEIGIEAFRSYDLVITSYNLVVNELKRYGntsplfAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGT 482
Cdd:cd18056  105 gGKKASRMKKEASVKFHVLLTSYELITIDMAILG------SIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGT 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298 483 PVQNRGVDVFALLRFVNVPNFQDLQQWKKNL----NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18056  179 PLQNNLEELFHLLNFLTPERFHNLEGFLEEFadiaKEDQI--KKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 344-534 1.36e-06

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: 50.45  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 344 LAKTPEPEVFSSDEEEEHLSNGRYpsantLVVCPMSVMCQWAHE-------------VASKVAQNAIRVLTFH------- 403
Cdd:cd18057   30 LGKTVQTIVFLYSLYKEGHSKGPY-----LVSAPLSTIINWEREfemwapdfyvvtyTGDKESRSVIRENEFSfednair 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 404 -GPNRHEIGIEAFRSYDLVITSYNLVVNELKRYGntsplfAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGT 482
Cdd:cd18057  105 sGKKVFRMKKEAQIKFHVLLTSYELITIDQAILG------SIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGT 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298 483 PVQNRGVDVFALLRFVNVPNFQDLQQWKKNL----NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18057  179 PLQNNLEELFHLLNFLTPERFNNLEGFLEEFadisKEDQI--KKLHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 373-534 3.18e-06

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: 49.28  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQ-------------NAIRVLTFHGPNRHEIgieafrSYDLVITSYNLVVNELKRYGNTS 439
Cdd:cd18053   74 LLVVPLSTLTSWQREIQTWAPQmnavvylgdinsrNMIRTHEWMHPQTKRL------KFNILLTTYEILLKDKSFLGGLN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 440 plfavyWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESM-L 518
Cdd:cd18053  148 ------WAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGReY 221

                        170
                 ....*....|....*.
gi 386765298 519 GHRRLNFIIKPLMLRR 534
Cdd:cd18053  222 GYASLHKELEPFLLRR 237
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 373-521 1.95e-05

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: 47.08  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVASKVAQNaIRVLTFHGPNRHEIGIEAFRSYD---------LVITSYN---LVVNELKRYGntsp 440
Cdd:cd18067   63 IVVSPSSLVKNWANELGKWLGGR-LQPLAIDGGSKKEIDRKLVQWASqqgrrvstpVLIISYEtfrLHVEVLQKGE---- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 441 lfavyWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNLNESMLGH 520
Cdd:cd18067  138 -----VGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKG 212


                 .
gi 386765298 521 R 521
Cdd:cd18067  213 R 213
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 344-534 7.45e-05

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: 45.39  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 344 LAKTPEPEVFSSDEEEEHLSNGRYpsantLVVCPMSVMCQWAHE-------------VASKVAQNAIRVLTFH------- 403
Cdd:cd18055   30 LGKTIQTIVFLYSLYKEGHTKGPF-----LVSAPLSTIINWEREfqmwapdfyvvtyTGDKDSRAIIRENEFSfddnavk 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 404 -GPNRHEIGIEAFRSYDLVITSYNLVVNElkrygnTSPLFAVYWNRVILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGT 482
Cdd:cd18055  105 gGKKAFKMKREAQVKFHVLLTSYELVTID------QAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGT 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 386765298 483 PVQNRGVDVFALLRFVNVPNFQDLQQWKKNL----NESMLghRRLNFIIKPLMLRR 534
Cdd:cd18055  179 PLQNNLEELFHLLNFLTPERFNNLEGFLEEFadisKEDQI--KKLHDLLGPHMLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 373-534 7.60e-05

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: 44.74  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 373 LVVCPMSVMCQWAHEVasKVAQNAIRVLTFHGPNrheigieafrsydLVITSYNLVVNElkrygnTSPLFAVYWNRVILD 452
Cdd:cd17994   54 LVSAPLSTIINWEREF--EMWAPDFYVVTYVGDH-------------VLLTSYELISID------QAILGSIDWAVLVVD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 453 EAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNVPNFQDLQQWKKNL----NESMLghRRLNFIIK 528
Cdd:cd17994  113 EAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFadisKEDQI--KKLHDLLG 190


                 ....*.
gi 386765298 529 PLMLRR 534
Cdd:cd17994  191 PHMLRR 196
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 449-503 4.62e-04

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: 42.88  E-value: 4.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFVNvPNF 503
Cdd:cd18069  140 VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR-PDF 193
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 449-498 4.52e-03

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: 39.87  E-value: 4.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386765298 449 VILDEAHIIRNSKTNCCNSVCQLRAHCHWALTGTPVQNRGVDVFALLRFV 498
Cdd:cd18068  159 VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFV 208
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
 371-484 6.74e-03

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 38.44  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765298 371 NTLVVCP--MSVMcQWAHEVASKVAQNAIRVLTFHGPNRheigiEAFRSYDLVITSYNLVVNELKRYGNT----SPLFAV 444
Cdd:cd18029   53 STLVLCTsaVSVE-QWRRQFLDWTTIDDEQIGRFTSDKK-----EIFPEAGVTVSTYSMLANTRKRSPESekfmEFITER 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 386765298 445 YWNRVILDEAHII-----RNSKTnccnsvcQLRAHCHWALTGTPV 484
Cdd:cd18029  127 EWGLIILDEVHVVpapmfRRVLT-------LQKAHCKLGLTATLV 164
 
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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