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Conserved domains on  [gi|62234443|ref|NP_080850|]
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chromatin-remodeling ATPase INO80 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13849880)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
520-748 4.06e-166

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: 499.34  E-value: 4.06e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd18002   81 YWGNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRR 748
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
300-832 8.66e-88

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 301.76  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  300 SARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMRE 379
Cdd:COG0553   15 LLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  380 AKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAEN 459
Cdd:COG0553   95 ALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  460 AYHIHQARTRSFDEDAKE-----SRAAALRAADKSGSGFGESYSLANPSIRAGEDIPQ--PTIFNGKLKGYQLKGMNWLA 532
Cdd:COG0553  175 LLLLGLLLALALLALLELallaaEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKATLRPYQLEGAAWLL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  533 NLYEQGINGILADEMGLGKTVQSIALLAHLAERENIwGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRR 612
Cdd:COG0553  255 FLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  613 FwsqktlytqdAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAE 692
Cdd:COG0553  334 F----------EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEE 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  693 LWALLHFIMPTLFDSHEEFNEWFSKDIESHaenksaiDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILTYCQLTSR 772
Cdd:COG0553  404 LWSLLDFLNPGLLGSLKAFRERFARPIEKG-------DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  773 QKLLYQALKnkisieDLLQSSMGSTQQAQNTTSSLMnLVMQFRKVCNHPELF----ERQETWSP 832
Cdd:COG0553  477 QRALYEAVL------EYLRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLleegAELSGRSA 533
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1093-1228 8.32e-63

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: 210.03  E-value: 8.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1093 IPGKESlITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDI 1172
Cdd:cd18793    1 LPPKIE-EVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443 1173 FVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLI 1228
Cdd:cd18793   80 RVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
 
Name Accession Description Interval E-value
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
520-748 4.06e-166

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: 499.34  E-value: 4.06e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd18002   81 YWGNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRR 748
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
300-832 8.66e-88

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 301.76  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  300 SARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMRE 379
Cdd:COG0553   15 LLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  380 AKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAEN 459
Cdd:COG0553   95 ALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  460 AYHIHQARTRSFDEDAKE-----SRAAALRAADKSGSGFGESYSLANPSIRAGEDIPQ--PTIFNGKLKGYQLKGMNWLA 532
Cdd:COG0553  175 LLLLGLLLALALLALLELallaaEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKATLRPYQLEGAAWLL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  533 NLYEQGINGILADEMGLGKTVQSIALLAHLAERENIwGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRR 612
Cdd:COG0553  255 FLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  613 FwsqktlytqdAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAE 692
Cdd:COG0553  334 F----------EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEE 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  693 LWALLHFIMPTLFDSHEEFNEWFSKDIESHaenksaiDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILTYCQLTSR 772
Cdd:COG0553  404 LWSLLDFLNPGLLGSLKAFRERFARPIEKG-------DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  773 QKLLYQALKnkisieDLLQSSMGSTQQAQNTTSSLMnLVMQFRKVCNHPELF----ERQETWSP 832
Cdd:COG0553  477 QRALYEAVL------EYLRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLleegAELSGRSA 533
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
523-824 5.06e-87

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: 285.73  E-value: 5.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    523 YQLKGMNWLANLYEQ-GINGILADEMGLGKTVQSIALLAHLAERENIWG-PFLIISPASTLNNWHQEFTRFV--PKFKVL 598
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    599 PYWGNPHDRKVIRRFwsQKTLYTQDapfhVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNR 678
Cdd:pfam00176   81 VLHGNKRPQERWKND--PNFLADFD----VVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    679 LLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAidenqlSRLHMILKPFMLRRIKKDVENELS 758
Cdd:pfam00176  155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGV------SRLHKLLKPFLLRRTKKDVEKSLP 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443    759 DKIEILTYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTqqaqnTTSSLMNLVMQFRKVCNHPELF 824
Cdd:pfam00176  229 PKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGRE-----IKASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
351-833 7.76e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 298.64  E-value: 7.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   351 KYEKVEKEHRKRAEKEALEQRKLDE----EMREAKRQQRKLNFLITQTELYAHFMSRKRdmghdgiqeeilrkledSSTQ 426
Cdd:PLN03142   59 KREKARLKELKKQKKQEIQKILEQQnaaiDADMNNKGKGRLKYLLQQTEIFAHFAKGDQ-----------------SASA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   427 RQIDIGGGVVVNITQEDYDsnhfkAQALKNAENAYHIHQArTRSFdedakesraaalraadksgsgfgesyslanpsira 506
Cdd:PLN03142  122 KKAKGRGRHASKLTEEEED-----EEYLKEEEDGLGGSGG-TRLL----------------------------------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   507 gediPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQ 586
Cdd:PLN03142  161 ----VQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   587 EFTRFVPKFKVLPYWGNPHDRKvirrfwSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERA------HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkdIESHAENKSAIdenqlSRLHMILKPFML 746
Cdd:PLN03142  311 SKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ--ISGENDQQEVV-----QQLHKVLRPFLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   747 RRIKKDVENELSDKIEILTYCQLTSRQKLLYQALKNKisieDLLQSSMGSTQqaqnttSSLMNLVMQFRKVCNHPELFER 826
Cdd:PLN03142  384 RRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK----DLDVVNAGGER------KRLLNIAMQLRKCCNHPYLFQG 453

                  ....*..
gi 62234443   827 QETWSPF 833
Cdd:PLN03142  454 AEPGPPY 460
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
275-404 8.29e-68

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 224.34  E-value: 8.29e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    275 LNARRRKVWLSIVKKELPKANKQKSSARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEK 354
Cdd:pfam13892    1 YDEKRRKIWKNIAKKDIPKVYRAKQQNHQARLANCKKVAQLCAREARRKASRTQKTMKDPQLRAKRLMREMLLFWKKNEK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 62234443    355 VEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRK 404
Cdd:pfam13892   81 EERELRKRAEKEALEQAKKEEELREAKRQQRKLNFLITQTELYSHFMGKK 130
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1093-1228 8.32e-63

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: 210.03  E-value: 8.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1093 IPGKESlITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDI 1172
Cdd:cd18793    1 LPPKIE-EVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443 1173 FVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLI 1228
Cdd:cd18793   80 RVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1097-1255 7.12e-55

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 209.66  E-value: 7.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  1097 ESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRN-DIFVF 1175
Cdd:PLN03142  464 EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGsEKFVF 543
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  1176 LLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRMVISGG 1255
Cdd:PLN03142  544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1091-1253 1.13e-54

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 204.30  E-value: 1.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1091 IRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRN 1170
Cdd:COG0553  520 LLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1171 DIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRM 1250
Cdd:COG0553  600 EAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAES 679

                 ...
gi 62234443 1251 VIS 1253
Cdd:COG0553  680 VLG 682
DEXDc smart00487
DEAD-like helicases superfamily;
516-702 1.59e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.43  E-value: 1.59e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443     516 FNGKLKGYQLKGMNWLANLYEqgiNGILADEMGLGKT-VQSIALLAHLaeRENIWGPFLIISPASTL-NNWHQEFTRFVP 593
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443     594 KF--KVLPYWGNPHDRKVIRRFWSQKTlytqdapfHVVITSYQLVVQDVK--YFQRVKWQYMVLDEAQALKSSS-SVRWK 668
Cdd:smart00487   80 SLglKVVGLYGGDSKREQLRKLESGKT--------DILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfGDQLE 151
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 62234443     669 ILLQF--QCRNRLLLTGTP---IQNTMAELWALLHFIMP 702
Cdd:smart00487  152 KLLKLlpKNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1104-1217 8.72e-27

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: 106.14  E-value: 8.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   1104 GKLYALDVLLTrlKSQGHRVLIYSQMTRMIDLlEEYMVYRKHTYMRLDGSSKISERRDMVADFqtRNDIFVFLLSTRAGG 1183
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 62234443   1184 LGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLG 1217
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1134-1217 9.50e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 9.50e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    1134 DLLEEYMVYRKHTYMRLDGSSKISERRDMVADFqtRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRA 1213
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 62234443    1214 HRLG 1217
Cdd:smart00490   79 GRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
451-685 1.66e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 62.35  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  451 AQALKNAENAYHIHQARTRSFDEDAKESRAAALRAADKSGSGFGESYSLANPS-IRAGEDIPQPTIFNGKLKGYQLKGMN 529
Cdd:COG1061   11 ADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAeAEALEAGDEASGTSFELRPYQQEALE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  530 -WLANLYEQGINGILADEMGLGKTVqsiaLLAHLAERENIWGPFLIISPASTLNN-WHQEFTRFVPKFkvlpywGNPHDR 607
Cdd:COG1061   91 aLLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDP------LAGGGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  608 KvirrfwsqktlytqDAPFHVVITSYQLVVQD--VKYFQRvKWQYMVLDEAQALkSSSSVRwKILLQFQCRNRLLLTGTP 685
Cdd:COG1061  161 K--------------DSDAPITVATYQSLARRahLDELGD-RFGLVIIDEAHHA-GAPSYR-RILEAFPAAYRLGLTATP 223
eNOPS_SF cd12931
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ...
349-385 1.71e-03

NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore.


Pssm-ID: 240579 [Multi-domain]  Cd Length: 90  Bit Score: 39.15  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 62234443  349 WKKYEKVEKEHRKRAEKEALEQR-KLDEEMREAKRQQR 385
Cdd:cd12931   53 WKALYELEKQQREQLEKELKEAReKLEAEMEAARYEHQ 90
 
Name Accession Description Interval E-value
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
520-748 4.06e-166

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: 499.34  E-value: 4.06e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd18002   81 YWGNPKDRKVLRKFWDRKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRR 748
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
520-748 5.73e-104

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: 330.85  E-value: 5.73e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFWSQKtlytqDApFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd18003   81 YYGSAKERKLKRQGWMKP-----NS-FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRR 748
Cdd:cd18003  155 LLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
517-750 1.29e-89

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: 290.83  E-value: 1.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  517 NGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAEReNIWGPFLIISPASTLNNWHQEFTRFVPKFK 596
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  597 VLPYWGNPHDRKVIRRFWSQKTLYTQDAPfhVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCR 676
Cdd:cd18009   80 VLLYHGTKEERERLRKKIMKREGTLQDFP--VVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSD 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  677 NRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWF-----SKDIESHAENKSAIDENQLSRLHMILKPFMLRRIK 750
Cdd:cd18009  158 NRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfsslSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
300-832 8.66e-88

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 301.76  E-value: 8.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  300 SARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMRE 379
Cdd:COG0553   15 LLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  380 AKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAEN 459
Cdd:COG0553   95 ALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  460 AYHIHQARTRSFDEDAKE-----SRAAALRAADKSGSGFGESYSLANPSIRAGEDIPQ--PTIFNGKLKGYQLKGMNWLA 532
Cdd:COG0553  175 LLLLGLLLALALLALLELallaaEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKATLRPYQLEGAAWLL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  533 NLYEQGINGILADEMGLGKTVQSIALLAHLAERENIwGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRR 612
Cdd:COG0553  255 FLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  613 FwsqktlytqdAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAE 692
Cdd:COG0553  334 F----------EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEE 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  693 LWALLHFIMPTLFDSHEEFNEWFSKDIESHaenksaiDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILTYCQLTSR 772
Cdd:COG0553  404 LWSLLDFLNPGLLGSLKAFRERFARPIEKG-------DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPE 476
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  773 QKLLYQALKnkisieDLLQSSMGSTQQAQNTTSSLMnLVMQFRKVCNHPELF----ERQETWSP 832
Cdd:COG0553  477 QRALYEAVL------EYLRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLleegAELSGRSA 533
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
523-824 5.06e-87

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: 285.73  E-value: 5.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    523 YQLKGMNWLANLYEQ-GINGILADEMGLGKTVQSIALLAHLAERENIWG-PFLIISPASTLNNWHQEFTRFV--PKFKVL 598
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    599 PYWGNPHDRKVIRRFwsQKTLYTQDapfhVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNR 678
Cdd:pfam00176   81 VLHGNKRPQERWKND--PNFLADFD----VVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    679 LLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAidenqlSRLHMILKPFMLRRIKKDVENELS 758
Cdd:pfam00176  155 WILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGV------SRLHKLLKPFLLRRTKKDVEKSLP 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443    759 DKIEILTYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTqqaqnTTSSLMNLVMQFRKVCNHPELF 824
Cdd:pfam00176  229 PKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGGRE-----IKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
517-750 1.75e-86

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: 281.52  E-value: 1.75e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  517 NGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFK 596
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  597 VLPYWGNPHDRK-VIRRfwsqktlYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQC 675
Cdd:cd17997   81 VVVLIGDKEERAdIIRD-------VLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNS 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62234443  676 RNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIEShAENKSAIDenqlsRLHMILKPFMLRRIK 750
Cdd:cd17997  154 RNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCD-DDNQEVVQ-----RLHKVLRPFLLRRIK 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
351-833 7.76e-84

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 298.64  E-value: 7.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   351 KYEKVEKEHRKRAEKEALEQRKLDE----EMREAKRQQRKLNFLITQTELYAHFMSRKRdmghdgiqeeilrkledSSTQ 426
Cdd:PLN03142   59 KREKARLKELKKQKKQEIQKILEQQnaaiDADMNNKGKGRLKYLLQQTEIFAHFAKGDQ-----------------SASA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   427 RQIDIGGGVVVNITQEDYDsnhfkAQALKNAENAYHIHQArTRSFdedakesraaalraadksgsgfgesyslanpsira 506
Cdd:PLN03142  122 KKAKGRGRHASKLTEEEED-----EEYLKEEEDGLGGSGG-TRLL----------------------------------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   507 gediPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQ 586
Cdd:PLN03142  161 ----VQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   587 EFTRFVPKFKVLPYWGNPHDRKvirrfwSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERA------HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkdIESHAENKSAIdenqlSRLHMILKPFML 746
Cdd:PLN03142  311 SKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ--ISGENDQQEVV-----QQLHKVLRPFLL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   747 RRIKKDVENELSDKIEILTYCQLTSRQKLLYQALKNKisieDLLQSSMGSTQqaqnttSSLMNLVMQFRKVCNHPELFER 826
Cdd:PLN03142  384 RRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK----DLDVVNAGGER------KRLLNIAMQLRKCCNHPYLFQG 453

                  ....*..
gi 62234443   827 QETWSPF 833
Cdd:PLN03142  454 AEPGPPY 460
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
520-702 2.09e-78

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: 256.72  E-value: 2.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFWSQKtlytqdaPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd17919   81 YHGSQRERAQIRAKEKLD-------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRL 153
                        170       180
                 ....*....|....*....|...
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMP 702
Cdd:cd17919  154 LLTGTPLQNNLEELWALLDFLDP 176
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
517-750 2.32e-76

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: 253.06  E-value: 2.32e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  517 NGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFK 596
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  597 VLPYWGNPHDRKVIrrfwsQKTLYTQDapFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQC- 675
Cdd:cd17996   81 KIVYKGTPDVRKKL-----QSQIRAGK--FNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHa 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  676 RNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSK--DIESHAENKSAIDENQL---SRLHMILKPFMLRRIK 750
Cdd:cd17996  154 RYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTpfANTGEQVKIELNEEETLliiRRLHKVLRPFLLRRLK 233
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
519-748 1.14e-72

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: 241.88  E-value: 1.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  519 KLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVL 598
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  599 PYWGNPHDRKVIRRF-WSQKTlyTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRN 677
Cdd:cd17993   81 VYLGDIKSRDTIREYeFYFSQ--TKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62234443  678 RLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDieshaenksaiDENQLSRLHMILKPFMLRR 748
Cdd:cd17993  159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEE-----------QEKGIADLHKELEPFILRR 218
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
516-750 1.54e-72

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: 241.32  E-value: 1.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  516 FNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAErENIWGPFLIISPASTLNNWHQEFTRFVPKF 595
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  596 KVLPYWGNPHDRKVIRRFwsqktlytqdAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQC 675
Cdd:cd18012   80 KVLVIHGTKRKREKLRAL----------EDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62234443  676 RNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAenksaiDENQLSRLHMILKPFMLRRIK 750
Cdd:cd18012  150 DHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDG------DEEALEELKKLISPFILRRLK 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
520-748 6.58e-70

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: 234.06  E-value: 6.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPkFKVLP 599
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIR-RFWSQKTLYTQDAP----FHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQ 674
Cdd:cd17995   80 YHGSGESRQIIQqYEMYFKDAQGRKKKgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  675 CRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIESHAenksaidenQLSRLHMILKPFMLRR 748
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-DLKTAE---------QVEKLQALLKPYMLRR 223
DBINO pfam13892
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ...
275-404 8.29e-68

DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.


Pssm-ID: 464024 [Multi-domain]  Cd Length: 134  Bit Score: 224.34  E-value: 8.29e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    275 LNARRRKVWLSIVKKELPKANKQKSSARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEK 354
Cdd:pfam13892    1 YDEKRRKIWKNIAKKDIPKVYRAKQQNHQARLANCKKVAQLCAREARRKASRTQKTMKDPQLRAKRLMREMLLFWKKNEK 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 62234443    355 VEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRK 404
Cdd:pfam13892   81 EERELRKRAEKEALEQAKKEEELREAKRQQRKLNFLITQTELYSHFMGKK 130
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
520-748 2.33e-65

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: 220.77  E-value: 2.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIrrfwsQKTLYTqDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd18006   81 YMGDKEKRLDL-----QQDIKS-TNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFdSHEEFNEWFSKDIESHAENKSAidenqlSRLHMILKPFMLRR 748
Cdd:cd18006  155 LLTGTPIQNSLQELYALLSFIEPNVF-PKDKLDDFIKAYSETDDESETV------EELHLLLQPFLLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
518-760 8.92e-65

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: 220.31  E-value: 8.92e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  518 GKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKV 597
Cdd:cd18064   14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  598 LPYWGNPHDRKVIRRfwsqKTLYTQDapFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRN 677
Cdd:cd18064   94 VCLIGDKDQRAAFVR----DVLLPGE--WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  678 RLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKdieshaeNKSAIDENQLSRLHMILKPFMLRRIKKDVENEL 757
Cdd:cd18064  168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT-------NNCLGDQKLVERLHMVLRPFLLRRIKADVEKSL 240

                 ...
gi 62234443  758 SDK 760
Cdd:cd18064  241 PPK 243
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
512-748 1.43e-63

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: 216.41  E-value: 1.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  512 QPTIFNGK---LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEF 588
Cdd:cd18054   10 QPSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  589 TRFVPKFKVLPYWGNPHDRKVIRRF-WSQKTlyTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRW 667
Cdd:cd18054   90 EIWAPEINVVVYIGDLMSRNTIREYeWIHSQ--TKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  668 KILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNewfskdiESHAENKsaidENQLSRLHMILKPFMLR 747
Cdd:cd18054  168 KTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFE-------EDHGKGR----ENGYQSLHKVLEPFLLR 236

                 .
gi 62234443  748 R 748
Cdd:cd18054  237 R 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1093-1228 8.32e-63

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: 210.03  E-value: 8.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1093 IPGKESlITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDI 1172
Cdd:cd18793    1 LPPKIE-EVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443 1173 FVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLI 1228
Cdd:cd18793   80 RVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
518-750 2.05e-62

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: 212.96  E-value: 2.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  518 GKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKV 597
Cdd:cd18065   14 GTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  598 LPYWGNPHDRKVIRRFwsqktlYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRN 677
Cdd:cd18065   94 VCLIGDKDARAAFIRD------VMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62234443  678 RLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKdieshaeNKSAIDENQLSRLHMILKPFMLRRIK 750
Cdd:cd18065  168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT-------KNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
520-705 7.87e-62

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: 209.55  E-value: 7.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAErENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFwsqktLYTQDAPFHVVITSYQLVV---QDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCR 676
Cdd:cd17998   80 YYGSQEERKHLRYD-----ILKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINAN 154
                        170       180
                 ....*....|....*....|....*....
gi 62234443  677 NRLLLTGTPIQNTMAELWALLHFIMPTLF 705
Cdd:cd17998  155 FRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
515-750 6.08e-58

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: 201.04  E-value: 6.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  515 IFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPK 594
Cdd:cd18062   19 LVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  595 FKVLPYWGNPHDRkviRRFWSQktlyTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKIL-LQF 673
Cdd:cd18062   99 VVKVSYKGSPAAR---RAFVPQ----LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  674 QCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQ---LSRLHMILKPFMLRRIK 750
Cdd:cd18062  172 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
515-750 1.82e-56

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: 196.44  E-value: 1.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  515 IFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPK 594
Cdd:cd18063   19 LINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  595 FKVLPYWGNPHDRKVIrrfwsqkTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKIL-LQF 673
Cdd:cd18063   99 VVKISYKGTPAMRRSL-------VPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  674 QCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQ---LSRLHMILKPFMLRRIK 750
Cdd:cd18063  172 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETiliIRRLHKVLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1097-1255 7.12e-55

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 209.66  E-value: 7.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  1097 ESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRN-DIFVF 1175
Cdd:PLN03142  464 EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGsEKFVF 543
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  1176 LLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRMVISGG 1255
Cdd:PLN03142  544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1091-1253 1.13e-54

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 204.30  E-value: 1.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1091 IRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRN 1170
Cdd:COG0553  520 LLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1171 DIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRM 1250
Cdd:COG0553  600 EAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAES 679

                 ...
gi 62234443 1251 VIS 1253
Cdd:COG0553  680 VLG 682
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
520-748 2.38e-51

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: 181.01  E-value: 2.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLA----HLAERENIWG-PFLIISPASTLNNWHQEFTRFVPK 594
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhhKRANSFNSENlPSLVVCPPTLVGHWVAEIKKYFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  595 F--KVLPYWGNPHDRKVIRRFWSQKtlytqdapfHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQ 672
Cdd:cd17999   81 AflKPLAYVGPPQERRRLREQGEKH---------NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  673 FQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDE-----NQLSRLHMILKPFMLR 747
Cdd:cd17999  152 LKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEqeagaLALEALHKQVLPFLLR 231

                 .
gi 62234443  748 R 748
Cdd:cd17999  232 R 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
520-748 3.57e-51

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: 179.17  E-value: 3.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNphdrkvirrfwsqktlytqdapfHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRL 679
Cdd:cd17994   81 YVGD-----------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKL 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  680 LLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFMLRR 748
Cdd:cd17994  138 LLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFA-DISK---------EDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
512-748 6.61e-51

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: 180.25  E-value: 6.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  512 QPTIFNG----KLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQE 587
Cdd:cd18053    9 QPSYIGGheglELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  588 FTRFVPKFKVLPYWGNPHDRKVIRRF-WSQKTlyTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:cd18053   89 IQTWAPQMNAVVYLGDINSRNMIRTHeWMHPQ--TKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNewfskdiESHAENKsaidENQLSRLHMILKPFML 746
Cdd:cd18053  167 YKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFE-------EEHGKGR----EYGYASLHKELEPFLL 235

                 ..
gi 62234443  747 RR 748
Cdd:cd18053  236 RR 237
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
520-748 1.44e-47

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: 170.19  E-value: 1.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIR--RFWSQKTL---------YTQDAP--FHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:cd18055   81 YTGDKDSRAIIRenEFSFDDNAvkggkkafkMKREAQvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFML 746
Cdd:cd18055  161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-DISK---------EDQIKKLHDLLGPHML 230

                 ..
gi 62234443  747 RR 748
Cdd:cd18055  231 RR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
520-748 5.63e-46

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: 165.62  E-value: 5.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRR---------FWSQKTLYTQDA----PFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:cd18057   81 YTGDKESRSVIREnefsfednaIRSGKKVFRMKKeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFML 746
Cdd:cd18057  161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-DISK---------EDQIKKLHDLLGPHML 230

                 ..
gi 62234443  747 RR 748
Cdd:cd18057  231 RR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
520-748 3.50e-45

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: 163.61  E-value: 3.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLanlYEQGinGILADEMGLGKTVQSIAL-LAHLAERENI----------------WGPFLIISPASTLN 582
Cdd:cd18008    1 LLPYQKQGLAWM---LPRG--GILADEMGLGKTIQALALiLATRPQDPKIpeeleenssdpkklylSKTTLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  583 NWHQEFTRFV--PKFKVLPYWGNPHDRKVirrfwsqKTLYTQDapfhVVITSYQLVVQDVKYFQ---------------- 644
Cdd:cd18008   76 QWKDEIEKHTkpGSLKVYVYHGSKRIKSI-------EELSDYD----IVITTYGTLASEFPKNKkgggrdskekeasplh 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  645 RVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHae 724
Cdd:cd18008  145 RIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKN-- 222
                        250       260
                 ....*....|....*....|....
gi 62234443  725 nksaiDENQLSRLHMILKPFMLRR 748
Cdd:cd18008  223 -----DRKALERLQALLKPILLRR 241
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
520-748 7.72e-45

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: 162.13  E-value: 7.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAEReNIWGPFLIISPASTLNNWHQEFtRFVPKFKVLP 599
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLM-GIRGPFLIIAPLSTITNWEREF-RTWTEMNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFW-----SQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQ 674
Cdd:cd18058   79 YHGSQISRQMIQQYEmyyrdEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  675 CRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFMLRR 748
Cdd:cd18058  159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG-DLKT---------EEQVKKLQSILKPMMLRR 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
523-748 8.60e-45

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: 162.16  E-value: 8.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  523 YQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIwGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWG 602
Cdd:cd18001    4 HQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLI-KSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  603 -NPHDRKVIRRFWSQKtlytqdapFHVVITSYQLVVQDVKYFQ-----RVKWQYMVLDEAQALKSSSSVRWKILLQFQCR 676
Cdd:cd18001   83 tSKKERERNLERIQRG--------GGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSLREIPAK 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62234443  677 NRLLLTGTPIQNTMAELWALLHFIMP-TLFDSHEEFNEWFSKDIESHAENKSAIDENQLSR-----LHMILKPFMLRR 748
Cdd:cd18001  155 NRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSevaenLRQIIKPYFLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
520-748 2.61e-44

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: 160.60  E-value: 2.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAErENIWGPFLIISPASTLNNWHQEFTRFVpKFKVLP 599
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFwsqkTLYTQDAPFHVV---------ITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKIL 670
Cdd:cd18060   79 YHGSLASRQMIQQY----EMYCKDSRGRLIpgaykfdalITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSL 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62234443  671 LQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFMLRR 748
Cdd:cd18060  155 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-DLKT---------EEQVQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
520-748 7.61e-44

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: 159.46  E-value: 7.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLP 599
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIR-----------RFWSQKTLYTQDAP--FHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVR 666
Cdd:cd18056   81 YVGDKDSRAIIRenefsfednaiRGGKKASRMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  667 WKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFML 746
Cdd:cd18056  161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA-DIAK---------EDQIKKLHDMLGPHML 230

                 ..
gi 62234443  747 RR 748
Cdd:cd18056  231 RR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
523-702 1.14e-43

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: 157.49  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  523 YQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLPYW- 601
Cdd:cd18000    4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVLHs 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  602 ---GNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNR 678
Cdd:cd18000   84 sgsGTGSEEKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHR 163
                        170       180
                 ....*....|....*....|....
gi 62234443  679 LLLTGTPIQNTMAELWALLHFIMP 702
Cdd:cd18000  164 LILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
520-748 6.51e-43

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: 157.54  E-value: 6.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHL-------AERENI-------------WGPFLIISPAS 579
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrRDRENNrprfkkkppassaKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  580 TLNNWHQEFTRFvPKFKVLPYWGNPHDRKVIRRFWSQKtlytqdapFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQAL 659
Cdd:cd18005   81 VLYNWKDELDTW-GHFEVGVYHGSRKDDELEGRLKAGR--------LEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  660 KSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIE---SHAENKS--AIDENQL 734
Cdd:cd18005  152 KNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKrgqRHTATARelRLGRKRK 231
                        250
                 ....*....|....
gi 62234443  735 SRLHMILKPFMLRR 748
Cdd:cd18005  232 QELAVKLSKFFLRR 245
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
520-748 1.51e-41

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: 152.49  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAEReNIWGPFLIISPASTLNNWHQEFtRFVPKFKVLP 599
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLK-GIHGPFLVIAPLSTIPNWEREF-RTWTELNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFW-----SQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQ 674
Cdd:cd18059   79 YHGSQASRRTIQLYEmyfkdPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  675 CRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFMLRR 748
Cdd:cd18059  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-DLKT---------EEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
520-748 3.89e-39

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: 145.53  E-value: 3.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAeRENIWGPFLIISPASTLNNWHQEFtRFVPKFKVLP 599
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEIL-LTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  600 YWGNPHDRKVIRRFW-----SQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQ 674
Cdd:cd18061   79 YHGSLISRQMIQQYEmyfrdSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62234443  675 CRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSkDIEShaenksaidENQLSRLHMILKPFMLRR 748
Cdd:cd18061  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG-DLKT---------EEQVQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
538-748 1.99e-36

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: 138.57  E-value: 1.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  538 GING-ILADEMGLGKTVQSIALLAHLAERENIWGP----FLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRr 612
Cdd:cd18004   23 GGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDKWLGLRRIKVVTADGNAKDVKA- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  613 fwsQKTLYTQDAPFHVVITSYQLVVQDV-KYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMA 691
Cdd:cd18004  102 ---SLDFFSSASTYPVLIISYETLRRHAeKLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLD 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62234443  692 ELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHM-----ILKPFMLRR 748
Cdd:cd18004  179 EFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSqelseLTSRFILRR 240
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
520-748 4.27e-32

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: 125.01  E-value: 4.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNW-LANlyeqgiNG--ILADEMGLGKTVQSIALLAHLaeRENiWgPFLIISPASTLNNWHQEFTRFVPKFK 596
Cdd:cd18010    1 LLPFQREGVCFaLRR------GGrvLIADEMGLGKTVQAIAIAAYY--REE-W-PLLIVCPSSLRLTWADEIERWLPSLP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  597 vlpywgnPHDRKVIRRfwSQKTLYTQDApfHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQF--Q 674
Cdd:cd18010   71 -------PDDIQVIVK--SKDGLRDGDA--KVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkR 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62234443  675 CRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEW--FSKDIESHAENKSAidENQLSRLHMILKPFMLRR 748
Cdd:cd18010  140 AKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycAAKQGGFGWDYSGS--SNLEELHLLLLATIMIRR 213
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
520-742 6.45e-28

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: 113.93  E-value: 6.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWL-ANLYEQGING------ILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFV 592
Cdd:cd18007    1 LKPHQVEGVRFLwSNLVGTDVGSdegggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  593 PK----FKVLPYWGNPHDRK----VIRRFWSQKTlytqdapfhVVITSYQLVV--------QDVKYFQRVKWQYM----- 651
Cdd:cd18007   81 PPdlrpLLVLVSLSASKRADarlrKINKWHKEGG---------VLLIGYELFRnlasnattDPRLKQEFIAALLDpgpdl 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  652 -VLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIeshaENKSAID 730
Cdd:cd18007  152 lVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPI----EAGQCVD 227
                        250
                 ....*....|..
gi 62234443  731 ENQLSRLHMILK 742
Cdd:cd18007  228 STEEDVRLMLKR 239
DEXDc smart00487
DEAD-like helicases superfamily;
516-702 1.59e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.43  E-value: 1.59e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443     516 FNGKLKGYQLKGMNWLANLYEqgiNGILADEMGLGKT-VQSIALLAHLaeRENIWGPFLIISPASTL-NNWHQEFTRFVP 593
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443     594 KF--KVLPYWGNPHDRKVIRRFWSQKTlytqdapfHVVITSYQLVVQDVK--YFQRVKWQYMVLDEAQALKSSS-SVRWK 668
Cdd:smart00487   80 SLglKVVGLYGGDSKREQLRKLESGKT--------DILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfGDQLE 151
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 62234443     669 ILLQF--QCRNRLLLTGTP---IQNTMAELWALLHFIMP 702
Cdd:smart00487  152 KLLKLlpKNVQLLLLSATPpeeIENLLELFLNDPVFIDV 190
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1104-1217 8.72e-27

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: 106.14  E-value: 8.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   1104 GKLYALDVLLTrlKSQGHRVLIYSQMTRMIDLlEEYMVYRKHTYMRLDGSSKISERRDMVADFqtRNDIFVFLLSTRAGG 1183
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 62234443   1184 LGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLG 1217
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
520-747 5.08e-25

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 105.89  E-value: 5.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLANLyeqgiNGILADEMGLGKTVQSIAL-LAH-----------LAERENIW-------------GPFLI 574
Cdd:cd18070    1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALiLLHprpdndldaadDDSDEMVCcpdclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  575 ISPASTLNNWHQEFTRFVPK-FKVLPYWGnphdrkVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKY----------- 642
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPSsLKVLTYQG------VKKDGALASPAPEILAEYDIVVTTYDVLRTELHYaeanrsnrrrr 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  643 -FQR----------VKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSheef 711
Cdd:cd18070  150 rQKRyeappsplvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD---- 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 62234443  712 NEWFSKDIESHAENKSAIDenqlsRLHMILKPFMLR 747
Cdd:cd18070  226 SDWWARVLIRPQGRNKARE-----PLAALLKELLWR 256
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
537-748 6.10e-25

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: 105.31  E-value: 6.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  537 QGINGILADEMGLGKTVQSIALLAHLaERENIWGP------FLIISPASTLNNWHQEFTRFV--PKFKVLPYwgnPHDRK 608
Cdd:cd18066   23 ERFGAILADEMGLGKTLQCISLIWTL-LRQGPYGGkpvikrALIVTPGSLVKNWKKEFQKWLgsERIKVFTV---DQDHK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  609 ViRRFWSQKTlytqdapFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQN 688
Cdd:cd18066   99 V-EEFIASPL-------YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQN 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62234443  689 TMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQL-----SRLHMILKPFMLRR 748
Cdd:cd18066  171 DLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLgearaAELTRLTGLFILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
536-748 1.05e-24

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: 104.47  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  536 EQGINGILADEMGLGKTVQSIALLAHlaereniwGPFLIISPASTLNNWHQEFTRFVPK--FKVLPYWGNPHDRKVirrf 613
Cdd:cd18071   46 ELVRGGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGGERNRDP---- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  614 wsqKTLYTQDapfhVVITSYQLVVQDVKY-----FQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQN 688
Cdd:cd18071  114 ---KLLSKYD----IVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQN 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  689 TMAELWALLHFIMPTLFDSheefNEWFSKDIESHAenkSAIDENQLSRLHMILKPFMLRR 748
Cdd:cd18071  187 SPKDLGSLLSFLHLKPFSN----PEYWRRLIQRPL---TMGDPTGLKRLQVLMKQITLRR 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
542-711 1.15e-24

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: 103.52  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  542 ILADEMGLGKTVQsIALLAHLAERENIWGPFLIISPASTLNNWHQE-FTRFVPKFKVLpywgnphDRKVIRRFWSQKtlY 620
Cdd:cd18011   21 LLADEVGLGKTIE-AGLIIKELLLRGDAKRVLILCPASLVEQWQDElQDKFGLPFLIL-------DRETAAQLRRLI--G 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  621 TQDAPFHVVITSYQLVVQDVKY---FQRVKWQYMVLDEAQALKSSSSVRWKILLQF------QCRNRLLLTGTPIQNTMA 691
Cdd:cd18011   91 NPFEEFPIVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrllakRARHVLLLTATPHNGKEE 170
                        170       180
                 ....*....|....*....|
gi 62234443  692 ELWALLHFIMPTLFDSHEEF 711
Cdd:cd18011  171 DFRALLSLLDPGRFAVLGRF 190
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
525-748 1.17e-24

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: 104.48  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  525 LKGMNWLANLYEQGinGILADEMGLGKTVQSIALLAHLAEREN-----------IW-----------GPFLIISPASTLN 582
Cdd:cd18072    9 LAWLLWRERQKPRG--GILADDMGLGKTLTMIALILAQKNTQNrkeeekekaltEWeskkdstlvpsAGTLVVCPASLVH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  583 NWHQEFTRFVP--KFKVLPYWGNPHDRKVirrfwsqKTLYTQDapfhVVITSYQLVVQDVKYFQ---------RVKWQYM 651
Cdd:cd18072   87 QWKNEVESRVAsnKLRVCLYHGPNRERIG-------EVLRDYD----IVITTYSLVAKEIPTYKeesrssplfRIAWARI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  652 VLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDsheEFNEWfskdiESHAENKSAIDE 731
Cdd:cd18072  156 ILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFD---DLKVW-----KKQVDNKSRKGG 227
                        250
                 ....*....|....*..
gi 62234443  732 NqlsRLHMILKPFMLRR 748
Cdd:cd18072  228 E---RLNILTKSLLLRR 241
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
520-748 4.01e-24

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: 102.93  E-value: 4.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWL----ANLYEQGING-ILADEMGLGKTVQSIALLAHLAERENIWGPFL----IISPASTLNNWHQEFTR 590
Cdd:cd18067    1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  591 FV-PKFKVLPYWGNPHDRKVIR--RFWSQKTLytqDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRW 667
Cdd:cd18067   81 WLgGRLQPLAIDGGSKKEIDRKlvQWASQQGR---RVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  668 KILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDI-----ESHAENKSAIDENQLSRLHMILK 742
Cdd:cd18067  158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlkgrdADASEKERQLGEEKLQELISIVN 237

                 ....*.
gi 62234443  743 PFMLRR 748
Cdd:cd18067  238 RCIIRR 243
HELICc smart00490
helicase superfamily c-terminal domain;
1134-1217 9.50e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 9.50e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    1134 DLLEEYMVYRKHTYMRLDGSSKISERRDMVADFqtRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRA 1213
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 62234443    1214 HRLG 1217
Cdd:smart00490   79 GRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
520-736 6.96e-19

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 87.18  E-value: 6.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWL-ANLYE--------QGINGILADEMGLGKTVQSIALLaHLAERENIWGPFLIISPASTLNNWHQEFTR 590
Cdd:cd18069    1 LKPHQIGGIRFLyDNIIEslerykgsSGFGCILAHSMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNWLSEFNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  591 FVPKFKVLPYwGNPHDRKVIRRFWSQKTL---------YTQDApfHVVITSYQLvvqdvkYFQRVKWQYMVLDEAQALKS 661
Cdd:cd18069   80 WLPPPEALPN-VRPRPFKVFILNDEHKTTaarakviedWVKDG--GVLLMGYEM------FRLRPGPDVVICDEGHRIKN 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62234443  662 SSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSR 736
Cdd:cd18069  151 CHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMR 225
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
538-720 3.21e-18

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 86.10  E-value: 3.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  538 GINGILADEMGLGKTVQSIALLAHLAERENIWG--PFLIISPASTLNNWHQEFTRFVPKFK--------VLPYWGNPHDR 607
Cdd:cd18068   28 GSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEFEKWQEGLKdeekievnELATYKRPQER 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  608 KVIRRFWSQKTlytqdapfHVVITSYQL-----VVQDVKYFQRVKWQYM-----------VLDEAQALKSSSSVRWKILL 671
Cdd:cd18068  108 SYKLQRWQEEG--------GVMIIGYDMyrilaQERNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMN 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 62234443  672 QFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIE 720
Cdd:cd18068  180 SIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ 228
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
520-700 5.36e-13

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 70.07  E-value: 5.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGMNWLAnlyEQGINGILADeMGLGKTVQSIALLAHLAErENIWGPFLIISPASTL-NNWHQEFTRF--VPKFK 596
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVArSTWPDEVEKWnhLRNLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  597 VLPYWGNPHDRKvirrfwsqKTLytqDAPFHVVITSYQLVVQDVKYFQRvKWQY--MVLDEAQALKSSSSVRWKIL--LQ 672
Cdd:cd18013   76 VSVAVGTERQRS--------KAA---NTPADLYVINRENLKWLVNKSGD-PWPFdmVVIDELSSFKSPRSKRFKALrkVR 143
                        170       180
                 ....*....|....*....|....*...
gi 62234443  673 FQCRNRLLLTGTPIQNTMAELWALLHFI 700
Cdd:cd18013  144 PVIKRLIGLTGTPSPNGLMDLWAQIALL 171
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
451-685 1.66e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 62.35  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  451 AQALKNAENAYHIHQARTRSFDEDAKESRAAALRAADKSGSGFGESYSLANPS-IRAGEDIPQPTIFNGKLKGYQLKGMN 529
Cdd:COG1061   11 ADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAeAEALEAGDEASGTSFELRPYQQEALE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  530 -WLANLYEQGINGILADEMGLGKTVqsiaLLAHLAERENIWGPFLIISPASTLNN-WHQEFTRFVPKFkvlpywGNPHDR 607
Cdd:COG1061   91 aLLAALERGGGRGLVVAPTGTGKTV----LALALAAELLRGKRVLVLVPRRELLEqWAEELRRFLGDP------LAGGGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  608 KvirrfwsqktlytqDAPFHVVITSYQLVVQD--VKYFQRvKWQYMVLDEAQALkSSSSVRwKILLQFQCRNRLLLTGTP 685
Cdd:COG1061  161 K--------------DSDAPITVATYQSLARRahLDELGD-RFGLVIIDEAHHA-GAPSYR-RILEAFPAAYRLGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
520-685 2.93e-09

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 57.32  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  520 LKGYQLKGM-NWLANLYEQGinGILADEMGLGKTVQSIALLAHLAEReniwgPFLIISP-ASTLNNWHQEFTRFVPKfkv 597
Cdd:cd17926    1 LRPYQEEALeAWLAHKNNRR--GILVLPTGSGKTLTALALIAYLKEL-----RTLIVVPtDALLDQWKERFEDFLGD--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  598 lpywgnphdrKVIRRFWSQKTLYTQDAPfhVVITSYQLVVQDVK----YFQRvkWQYMVLDEAQALKSSSsvrWK-ILLQ 672
Cdd:cd17926   71 ----------SSIGLIGGGKKKDFDDAN--VVVATYQSLSNLAEeekdLFDQ--FGLLIVDEAHHLPAKT---FSeILKE 133
                        170
                 ....*....|...
gi 62234443  673 FQCRNRLLLTGTP 685
Cdd:cd17926  134 LNAKYRLGLTATP 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1171-1220 8.67e-06

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.00  E-value: 8.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 62234443 1171 DIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTK 1220
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
540-684 1.48e-05

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 46.63  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443  540 NGILADEMGLGKTVQ-SIALLAHLAEREniwGPFLIISPASTL-NNWHQEF-TRFVPKFKVLPYWG--NPHDRKVIRRfw 614
Cdd:cd00046    3 NVLITAPTGSGKTLAaLLAALLLLLKKG---KKVLVLVPTKALaLQTAERLrELFGPGIRVAVLVGgsSAEEREKNKL-- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62234443  615 sqktlytQDAPfhVVITSYQ----LVVQDVKYFQRvKWQYMVLDEAQALKSSSSVRWKILLQFQCRNR-----LLLTGT 684
Cdd:cd00046   78 -------GDAD--IIIATPDmllnLLLREDRLFLK-DLKLIIVDEAHALLIDSRGALILDLAVRKAGLknaqvILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1101-1324 3.72e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 45.02  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1101 TDSGKLYALDVLLTRLKsQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFqtRNDIFVFLLSTR 1180
Cdd:COG1061  287 DAERKDKILRELLREHP-DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF--RDGELRILVTVD 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443 1181 AGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQ-VTVYRLICKGTIEERILQRAKEKSEIQRMVISGGNFKP 1259
Cdd:COG1061  364 VLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESE 443
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62234443 1260 DTLKPKEVVSLLLDDEELEKKLRLRQEEKRQQEESNRVKERKRKREKYAEKKKKEDELDGKRRKE 1324
Cdd:COG1061  444 ELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEE 508
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1097-1262 1.52e-03

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 42.31  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   1097 ESLITDSGKL----YALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDI 1172
Cdd:pfam11496   83 EKLAYTSGKFlvlnDLVNLLIERDRKEPINVAIVARSGKTLDLVEALLLGKGLSYKRYSGEMLYGENKKVSDSGNKKIHS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443   1173 FVFLL------STRAGGLGINlTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAK--EK 1244
Cdd:pfam11496  163 TTCHLlsstgqLTNDDSLLEN-YKFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIEHVELCFPKppDS 241
                          170       180
                   ....*....|....*....|....*.
gi 62234443   1245 SEIQRMVISG--------GNFKPDTL 1262
Cdd:pfam11496  242 PDYLYKVIAAivvlrdvvGDLPDDLL 267
eNOPS_SF cd12931
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ...
349-385 1.71e-03

NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore.


Pssm-ID: 240579 [Multi-domain]  Cd Length: 90  Bit Score: 39.15  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 62234443  349 WKKYEKVEKEHRKRAEKEALEQR-KLDEEMREAKRQQR 385
Cdd:cd12931   53 WKALYELEKQQREQLEKELKEAReKLEAEMEAARYEHQ 90
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
267-386 2.66e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 41.78  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62234443    267 KKHLSIEQLNARRRkVWLSIVkkeLPKANKQKSSARNLF---------LTNSRKLAHQCMKEVRRAALQAQKNCKETLPR 337
Cdd:pfam07946  204 EKPETLKETTPRKR-LILSLR---LPSSKSDYEALLPLLqlvlylidkLAKRAKLRPEALKKAKKTREEEIEKIKKAAEE 279
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 62234443    338 ARRltkEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEemREAKRQQRK 386
Cdd:pfam07946  280 ERA---EEAQEKKEEAKKKEREEKLAKLSPEEQRKYEE--KERKKEQRK 323
 
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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