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Conserved domains on  [gi|1443618724|ref|XP_025907243|]
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DNA excision repair protein ERCC-6 [Nothoprocta perdicaria]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
336-994 1.74e-141

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 450.45  E-value: 1.74e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  336 DKRLKKHMSRLQKRALQFQSKAGIPKEKKYLEAKAKLTHEQRDDSGESEYVPDEELFDPEAAEEEEQQASSHAENDSDYE 415
Cdd:COG0553     59 ELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  416 LKPLSRKGKNLVKKDFKGDDDPDFYPSSEEEEEHAVGKRRIKRWRDDGDEDYYKQRLRRWQKERLKDKDHDTAEELSDES 495
Cdd:COG0553    139 LVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  496 DTEF------EEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSNyry 569
Cdd:COG0553    219 VDAFrlrrlrEALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL-----KERGLA--- 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  570 qglGPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETgsytNKKVKLIREIAScHGILITSYSYIRLMQDNIHSYDWHYV 649
Cdd:COG0553    291 ---RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT----RERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLV 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  650 ILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASpvq 729
Cdd:COG0553    363 ILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE--- 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  730 vktaykcacVLRDTINPYLLRRMKADVKmsLSLPDKNEQVLFCRLTDEQRRVYQNFIDskEVYQILNGE------MQIFS 803
Cdd:COG0553    440 ---------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAegirrrGLILA 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  804 GLVALRKICNHPDLFsggpstlkafpdteVEEADQFGYWkrSGKMIVVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVR 883
Cdd:COG0553    507 ALTRLRQICSHPALL--------------LEEGAELSGR--SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE 570
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  884 ERNYSYLRMDGTTTIASRQPLITRYNEDKSIFIFLLTTRVGGIGVNLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQ 963
Cdd:COG0553    571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1443618724  964 VTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 994
Cdd:COG0553    651 VQVYKLVAEGTIEEKILELLEEKRALAESVL 681
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
86-162 6.95e-33

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


:

Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 122.32  E-value: 6.95e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443618724   86 VSDSAQAAELRGLGVDVYDQDVLEQGVLQQVDHAINEASKAAKIADAEKEYQSVLEDVRSCTISLKQINKIIEQLSP 162
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1439-1511 3.04e-32

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


:

Pssm-ID: 439329  Cd Length: 72  Bit Score: 120.31  E-value: 3.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443618724 1439 STEYDELLVDVRNFIAFQArvDGEASTQEILQEFEGKLPTAQACVFRELLRNLCTFHRSPNGEGVWRLKPEFR 1511
Cdd:cd22254      2 STEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
85-391 3.66e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   85 SVSDSAQAAELRGlgvDVYDQDVLEQGVLQQVDHAINEASKA-AKIADAEKEyqsvLEDVRsctislKQINKIIEQLSPQ 163
Cdd:TIGR02169  669 SRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELsQELSDASRK----IGEIE------KEIEQLEQEEEKL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  164 AATSKDVNRKLDSVKRQKYNKEQQLKKIKAKQKRLRAILAGtgILDEINDGEIEDDEEPGPSSSPLhlgsmlMPAQETE- 242
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--LEEALNDLEARLSHSRIPEIQAE------LSKLEEEv 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  243 --WEELIRtgqmtpfgtKIPQKPQRK--PRQLMLNETSDFEKYLAD-QAKLSSERKKLSLLKGAKRKaqaktaqhatstp 317
Cdd:TIGR02169  808 srIEARLR---------EIEQKLNRLtlEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEE------------- 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  318 IQSPTKEKRSKARTLSKTDKRLKKHMSRL--QKRALQF---QSKAGIPKEK---KYLEAKAKLTHEQ----RDDSGESEY 385
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKKERDELeaQLRELERkieELEAQIEKKRkrlSELKAKLEALEEElseiEDPKGEDEE 945

                   ....*.
gi 1443618724  386 VPDEEL 391
Cdd:TIGR02169  946 IPEEEL 951
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
336-994 1.74e-141

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 450.45  E-value: 1.74e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  336 DKRLKKHMSRLQKRALQFQSKAGIPKEKKYLEAKAKLTHEQRDDSGESEYVPDEELFDPEAAEEEEQQASSHAENDSDYE 415
Cdd:COG0553     59 ELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  416 LKPLSRKGKNLVKKDFKGDDDPDFYPSSEEEEEHAVGKRRIKRWRDDGDEDYYKQRLRRWQKERLKDKDHDTAEELSDES 495
Cdd:COG0553    139 LVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  496 DTEF------EEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSNyry 569
Cdd:COG0553    219 VDAFrlrrlrEALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL-----KERGLA--- 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  570 qglGPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETgsytNKKVKLIREIAScHGILITSYSYIRLMQDNIHSYDWHYV 649
Cdd:COG0553    291 ---RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT----RERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLV 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  650 ILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASpvq 729
Cdd:COG0553    363 ILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE--- 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  730 vktaykcacVLRDTINPYLLRRMKADVKmsLSLPDKNEQVLFCRLTDEQRRVYQNFIDskEVYQILNGE------MQIFS 803
Cdd:COG0553    440 ---------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAegirrrGLILA 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  804 GLVALRKICNHPDLFsggpstlkafpdteVEEADQFGYWkrSGKMIVVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVR 883
Cdd:COG0553    507 ALTRLRQICSHPALL--------------LEEGAELSGR--SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE 570
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  884 ERNYSYLRMDGTTTIASRQPLITRYNEDKSIFIFLLTTRVGGIGVNLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQ 963
Cdd:COG0553    571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1443618724  964 VTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 994
Cdd:COG0553    651 VQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
513-700 1.81e-119

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: 372.04  E-value: 1.81e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyryQGLGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAVLHETGSYTNK---------KVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAA 663
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTGSeeklgsierKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1443618724  664 VTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
516-818 5.22e-115

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: 363.54  E-value: 5.22e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFHTW 594
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  595 W--PPFRVAVLHETGSYTNKkVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 752
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443618724  753 KADVkmSLSLPDKNEQVLFCRLTDEQRRVYQNFIDSKEVYQILNGE------MQIFSGLVALRKICNHPDLF 818
Cdd:pfam00176  220 KKDV--EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
469-982 4.96e-86

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 305.19  E-value: 4.96e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  469 KQRLRRWQKERLKDKDHDtAEELSDESDTEFEEG----FKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGK 544
Cdd:PLN03142   123 KAKGRGRHASKLTEEEED-EEYLKEEEDGLGGSGgtrlLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGK 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  545 TIQIIAFLAGLsyskirtrgsnYRYQGL-GPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETgsytNKKVKLIRE---I 620
Cdd:PLN03142   202 TLQTISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGN----PEERAHQREellV 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  621 ASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:PLN03142   267 AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  701 GKLGTLPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKADVKMSLslPDKNEQVLFCRLTDEQRR 780
Cdd:PLN03142   347 EIFSSAETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQ 412
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  781 VY----QNFIDS----KEVYQILNGEMQifsglvaLRKICNHPDLFSG---GPSTLKAfpDTEVEEadqfgywkrSGKMI 849
Cdd:PLN03142   413 YYkallQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG--EHLVEN---------SGKMV 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  850 VVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVRERNYSYLRMDGTTTIASRQPLITRYNEDKS-IFIFLLTTRVGGIGV 928
Cdd:PLN03142   475 LLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSeKFVFLLSTRAGGLGI 554
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1443618724  929 NLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHR 982
Cdd:PLN03142   555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
86-162 6.95e-33

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 122.32  E-value: 6.95e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443618724   86 VSDSAQAAELRGLGVDVYDQDVLEQGVLQQVDHAINEASKAAKIADAEKEYQSVLEDVRSCTISLKQINKIIEQLSP 162
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1439-1511 3.04e-32

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 120.31  E-value: 3.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443618724 1439 STEYDELLVDVRNFIAFQArvDGEASTQEILQEFEGKLPTAQACVFRELLRNLCTFHRSPNGEGVWRLKPEFR 1511
Cdd:cd22254      2 STEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
DEXDc smart00487
DEAD-like helicases superfamily;
505-713 2.46e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.04  E-value: 2.46e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   505 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRYQGLGPTVIVCP-ATV 583
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPtREL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   584 MHQWVKEFHTWWPPFRVAVLHETGSYTnkKVKLIREIAS-CHGILITSYSYIR--LMQDNIHSYDWHYVILDEGHKIRNP 660
Cdd:smart00487   67 AEQWAEELKKLGPSLGLKVVGLYGGDS--KREQLRKLESgKTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDG 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443618724   661 NAAVTLACKQFRTP---HRIILSGSP---MQNNLKELWSLFDFVFPGKLGTLPVfmEQF 713
Cdd:smart00487  145 GFGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI--EQF 201
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-391 3.66e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   85 SVSDSAQAAELRGlgvDVYDQDVLEQGVLQQVDHAINEASKA-AKIADAEKEyqsvLEDVRsctislKQINKIIEQLSPQ 163
Cdd:TIGR02169  669 SRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELsQELSDASRK----IGEIE------KEIEQLEQEEEKL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  164 AATSKDVNRKLDSVKRQKYNKEQQLKKIKAKQKRLRAILAGtgILDEINDGEIEDDEEPGPSSSPLhlgsmlMPAQETE- 242
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--LEEALNDLEARLSHSRIPEIQAE------LSKLEEEv 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  243 --WEELIRtgqmtpfgtKIPQKPQRK--PRQLMLNETSDFEKYLAD-QAKLSSERKKLSLLKGAKRKaqaktaqhatstp 317
Cdd:TIGR02169  808 srIEARLR---------EIEQKLNRLtlEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEE------------- 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  318 IQSPTKEKRSKARTLSKTDKRLKKHMSRL--QKRALQF---QSKAGIPKEK---KYLEAKAKLTHEQ----RDDSGESEY 385
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKKERDELeaQLRELERkieELEAQIEKKRkrlSELKAKLEALEEElseiEDPKGEDEE 945

                   ....*.
gi 1443618724  386 VPDEEL 391
Cdd:TIGR02169  946 IPEEEL 951
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
113-350 5.07e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  113 LQQVDHAINEASKaaKIADAEKEYQSVLEDvrsctisLKQINKIIEQLspqAATSKDVNRKLDSVKRQKYNKEQQLKKIK 192
Cdd:COG4942     29 LEQLQQEIAELEK--ELAALKKEEKALLKQ-------LAALERRIAAL---ARRIRALEQELAALEAELAELEKEIAELR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  193 AKQKRLRAILAG-------TGILDEINdgEIEDDEEPGPSSSPLHLGSMLMPAQETEWEELIRTgqmtpfgtkipQKPQR 265
Cdd:COG4942     97 AELEAQKEELAEllralyrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-----------LAELA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  266 KPRQLMLNETSDFEKYLADQAKlssERKKLSLLKGAKRKAQAKtaqhatstpIQSPTKEKRSKARTLSKTDKRLKKHMSR 345
Cdd:COG4942    164 ALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLAR---------LEKELAELAAELAELQQEAEELEALIAR 231

                   ....*
gi 1443618724  346 LQKRA 350
Cdd:COG4942    232 LEAEA 236
PTZ00121 PTZ00121
MAEBL; Provisional
120-491 8.87e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  120 INEASKAAKIADAEKEYQSvlEDVRSCTISLK--QINKIIEQLSPQAATSKDVNRKLDSVKR-QKYNKEQQLKKIKAKQK 196
Cdd:PTZ00121  1130 AEEARKAEDARKAEEARKA--EDAKRVEIARKaeDARKAEEARKAEDAKKAEAARKAEEVRKaEELRKAEDARKAEAARK 1207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  197 --RLRAILAGTGILDEINDGEIEDDEEPGPSSSPLHLGSMLMPAQETEWEELIRTGQMTPFGTKIPQKPQRKPRQLMLNE 274
Cdd:PTZ00121  1208 aeEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  275 tsdfEKYLADQAKLSSERKKLSLLKG-----------------AKRKAQA--KTAQHATSTPiQSPTKEKRSKARTLSKT 335
Cdd:PTZ00121  1288 ----EKKKADEAKKAEEKKKADEAKKkaeeakkadeakkkaeeAKKKADAakKKAEEAKKAA-EAAKAEAEAAADEAEAA 1362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  336 DKRL---KKHMSRLQKRALQFQSKAGIPKEKKYLEAKAKLTHEQRDD--SGESEYVPDEELFDPEAAEEEEQQASSHAEN 410
Cdd:PTZ00121  1363 EEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  411 DSDY-ELKPLS---RKGKNLVKKDFKGDDDPDFYPSSEEEEEHAVGKRRIKRWRDDGDEDYYKQRLRRWQKERLKDKDHD 486
Cdd:PTZ00121  1443 AKKAdEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                   ....*
gi 1443618724  487 TAEEL 491
Cdd:PTZ00121  1523 KADEA 1527
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
336-994 1.74e-141

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 450.45  E-value: 1.74e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  336 DKRLKKHMSRLQKRALQFQSKAGIPKEKKYLEAKAKLTHEQRDDSGESEYVPDEELFDPEAAEEEEQQASSHAENDSDYE 415
Cdd:COG0553     59 ELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  416 LKPLSRKGKNLVKKDFKGDDDPDFYPSSEEEEEHAVGKRRIKRWRDDGDEDYYKQRLRRWQKERLKDKDHDTAEELSDES 495
Cdd:COG0553    139 LVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  496 DTEF------EEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSNyry 569
Cdd:COG0553    219 VDAFrlrrlrEALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLEL-----KERGLA--- 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  570 qglGPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETgsytNKKVKLIREIAScHGILITSYSYIRLMQDNIHSYDWHYV 649
Cdd:COG0553    291 ---RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGT----RERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLV 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  650 ILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASpvq 729
Cdd:COG0553    363 ILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALE--- 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  730 vktaykcacVLRDTINPYLLRRMKADVKmsLSLPDKNEQVLFCRLTDEQRRVYQNFIDskEVYQILNGE------MQIFS 803
Cdd:COG0553    440 ---------RLRRLLRPFLLRRTKEDVL--KDLPEKTEETLYVELTPEQRALYEAVLE--YLRRELEGAegirrrGLILA 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  804 GLVALRKICNHPDLFsggpstlkafpdteVEEADQFGYWkrSGKMIVVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVR 883
Cdd:COG0553    507 ALTRLRQICSHPALL--------------LEEGAELSGR--SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE 570
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  884 ERNYSYLRMDGTTTIASRQPLITRYNEDKSIFIFLLTTRVGGIGVNLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQ 963
Cdd:COG0553    571 ERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1443618724  964 VTVYRLLTAGTIEEKIYHRQIFKQFLTNRVL 994
Cdd:COG0553    651 VQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
513-700 1.81e-119

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: 372.04  E-value: 1.81e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgsnyryQGLGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSK----------LGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAVLHETGSYTNK---------KVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAA 663
Cdd:cd18000     71 RWWPPFRVVVLHSSGSGTGSeeklgsierKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAE 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1443618724  664 VTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:cd18000    151 ITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
516-818 5.22e-115

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: 363.54  E-value: 5.22e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQ-QAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFHTW 594
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGG---------PTLIVVPLSLLHNWMNEFERW 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  595 W--PPFRVAVLHETGSYTNKkVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:pfam00176   72 VspPALRVVVLHGNKRPQER-WKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktAYKCACVLRDTINPYLLRRM 752
Cdd:pfam00176  151 TRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRT 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443618724  753 KADVkmSLSLPDKNEQVLFCRLTDEQRRVYQNFIDSKEVYQILNGE------MQIFSGLVALRKICNHPDLF 818
Cdd:pfam00176  220 KKDV--EKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRLRKICNHPGLI 289
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
469-982 4.96e-86

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 305.19  E-value: 4.96e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  469 KQRLRRWQKERLKDKDHDtAEELSDESDTEFEEG----FKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGK 544
Cdd:PLN03142   123 KAKGRGRHASKLTEEEED-EEYLKEEEDGLGGSGgtrlLVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGK 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  545 TIQIIAFLAGLsyskirtrgsnYRYQGL-GPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETgsytNKKVKLIRE---I 620
Cdd:PLN03142   202 TLQTISLLGYL-----------HEYRGItGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGN----PEERAHQREellV 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  621 ASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:PLN03142   267 AGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  701 GKLGTLPVFMEQFSvpitMGGYSNASPVqVKTAYKcacVLRdtinPYLLRRMKADVKMSLslPDKNEQVLFCRLTDEQRR 780
Cdd:PLN03142   347 EIFSSAETFDEWFQ----ISGENDQQEV-VQQLHK---VLR----PFLLRRLKSDVEKGL--PPKKETILKVGMSQMQKQ 412
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  781 VY----QNFIDS----KEVYQILNGEMQifsglvaLRKICNHPDLFSG---GPSTLKAfpDTEVEEadqfgywkrSGKMI 849
Cdd:PLN03142   413 YYkallQKDLDVvnagGERKRLLNIAMQ-------LRKCCNHPYLFQGaepGPPYTTG--EHLVEN---------SGKMV 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  850 VVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVRERNYSYLRMDGTTTIASRQPLITRYNEDKS-IFIFLLTTRVGGIGV 928
Cdd:PLN03142   475 LLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSeKFVFLLSTRAGGLGI 554
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1443618724  929 NLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHR 982
Cdd:PLN03142   555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIER 608
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
513-700 3.84e-73

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: 241.70  E-value: 3.84e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqgLGPTVIVCPATVMHQWVKEFH 592
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKE----------RGPVLVVCPLSVLENWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAVLHetGSYTNKKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:cd17919     71 KWTPDLRVVVYH--GSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
513-751 1.13e-70

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: 236.50  E-value: 1.13e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRgsnyryqglgpTVIVCPATVMHQWVKEFH 592
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKS-----------VLVVMPTSLIPHWVKEFA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAVLHetGSYTNKKVKLIREIASCHGILITSYSYIRLMQDNIHSYD-----WHYVILDEGHKIRNPNAAVTLA 667
Cdd:cd18001     70 KWTPGLRVKVFH--GTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  668 CKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGK-LGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINP 746
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKP 227

                   ....*
gi 1443618724  747 YLLRR 751
Cdd:cd18001    228 YFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
516-753 2.95e-65

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: 220.51  E-value: 2.95e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRYQGLGPTVIVCPATVMHQWVKEFHTWW 595
Cdd:cd18012      8 YQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLL-----------SRKEEGRKGPSLVVAPTSLIYNWEEEAAKFA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  596 PPFRVAVLHETgsytNKKVKLIREIAScHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFRTPH 675
Cdd:cd18012     77 PELKVLVIHGT----KRKREKLRALED-YDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADH 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443618724  676 RIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPvqvktaykcacVLRDTINPYLLRRMK 753
Cdd:cd18012    152 RLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALE-----------ELKKLISPFILRRLK 218
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
513-751 7.17e-62

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: 211.44  E-value: 7.17e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAglsySKIRTRGSNYRYQGLgPTVIVCPATVMHQWVKEFH 592
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILA----SDHHKRANSFNSENL-PSLVVCPPTLVGHWVAEIK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAVLHETGSYTnKKVKLiREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:cd17999     76 KYFPNAFLKPLAYVGPPQ-ERRRL-REQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLK 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRR 751
Cdd:cd17999    154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
516-751 3.53e-60

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: 206.85  E-value: 3.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGSNYRYQGL-----------GPTVIVCPATVM 584
Cdd:cd18005      4 YQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAV-LGKTGTRRDRENNRPRfkkkppassakKPVLIVAPLSVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  585 HQWVKEFHTW-WppFRVAVLHetgSYTNKKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAA 663
Cdd:cd18005     83 YNWKDELDTWgH--FEVGVYH---GSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  664 VTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDT 743
Cdd:cd18005    158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVK 237

                   ....*...
gi 1443618724  744 INPYLLRR 751
Cdd:cd18005    238 LSKFFLRR 245
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
845-970 5.74e-60

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: 201.94  E-value: 5.74e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  845 SGKMIVVESLLKIWHKQGHRVLFFTQSRQMLQILEVFVRERNYSYLRMDGTTTIASRQPLITRYNEDKSIFIFLLTTRVG 924
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1443618724  925 GIGVNLTGADRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLL 970
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
517-735 2.22e-47

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: 169.78  E-value: 2.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  517 QQTGVRWLWE-----LHCQQAGG--ILGDEMGLGKTIQIIAFL-AGLSYSKIRTRgsnyryqglgpTVIVCPATVMHQWV 588
Cdd:cd18007      5 QVEGVRFLWSnlvgtDVGSDEGGgcILAHTMGLGKTLQVITFLhTYLAAAPRRSR-----------PLVLCPASTLYNWE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  589 KEFHTWWPPFRVAVLHETGSYTNKKVKL-IREIASCH---GILITSY-SYIRLMQDNIHSYDWHY-------------VI 650
Cdd:cd18007     74 DEFKKWLPPDLRPLLVLVSLSASKRADArLRKINKWHkegGVLLIGYeLFRNLASNATTDPRLKQefiaalldpgpdlLV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  651 LDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQV 730
Cdd:cd18007    154 LDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDV 233

                   ....*
gi 1443618724  731 KTAYK 735
Cdd:cd18007    234 RLMLK 238
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
516-753 4.48e-47

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: 169.10  E-value: 4.48e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskiRTRGSnyryqgLGPTVIVCPATVMHQWVKEFHTWW 595
Cdd:cd18009      7 YQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL-----RERGV------WGPFLVIAPLSTLPNWVNEFARFT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  596 PPFRVAVLHETGSYTNKKVKLIR---EIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:cd18009     76 PSVPVLLYHGTKEERERLRKKIMkreGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRM 752
Cdd:cd18009    156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRL 235

                   .
gi 1443618724  753 K 753
Cdd:cd18009    236 K 236
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
517-751 3.38e-46

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: 166.69  E-value: 3.38e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  517 QQTGVRWLWE-LHCQQAGG----ILGDEMGLGKTIQIIAflagLSYSKIRTRgsnyryQGLGPT----VIVCPATVMHQW 587
Cdd:cd18004      5 QREGVQFLYDcLTGRRGYGgggaILADEMGLGKTLQAIA----LVWTLLKQG------PYGKPTakkaLIVCPSSLVGNW 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  588 VKEFHTWWPPFRVAVLHETGS--YTNKKVKLIREIASCHgILITSYSYIRLMQDNI-HSYDWHYVILDEGHKIRNPNAAV 664
Cdd:cd18004     75 KAEFDKWLGLRRIKVVTADGNakDVKASLDFFSSASTYP-VLIISYETLRRHAEKLsKKISIDLLICDEGHRLKNSESKT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  665 TLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTI 744
Cdd:cd18004    154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELT 233

                   ....*..
gi 1443618724  745 NPYLLRR 751
Cdd:cd18004    234 SRFILRR 240
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
513-751 4.91e-45

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: 162.52  E-value: 4.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKirtrgSNYryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEK-----GNW-----GPHLIVVPTSVMLNWEMEFK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRvaVLHETGSytNKKVKLIR----EIASCHgILITSYSYIrlMQDnIHSY---DWHYVILDEGHKIRNPNAAVT 665
Cdd:cd18003     71 RWCPGFK--ILTYYGS--AKERKLKRqgwmKPNSFH-VCITSYQLV--VQD-HQVFkrkKWKYLILDEAHNIKNFKSQRW 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  666 LACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITmggysnaSPVQVKTAYKCACV--LRDT 743
Cdd:cd18003    143 QTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT-------AMSEGSQEENEELVrrLHKV 215

                   ....*...
gi 1443618724  744 INPYLLRR 751
Cdd:cd18003    216 LRPFLLRR 223
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
512-753 3.09e-44

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: 160.61  E-value: 3.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  512 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsyskIRTRGSNyryqglGPTVIVCPATVMHQWVKEF 591
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYL----MEKKKNN------GPYLVIVPLSTLSNWVSEF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPpfRVAVLHETGSYTNKKVKLIREIASCHGILITSYSYIrlMQDN--IHSYDWHYVILDEGHKIRNPNAAVTLACK 669
Cdd:cd17996     73 EKWAP--SVSKIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYI--IKDKplLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  670 Q-FRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPV----QVKTAYKCACVLRdti 744
Cdd:cd17996    149 TyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELneeeTLLIIRRLHKVLR--- 225

                   ....*....
gi 1443618724  745 nPYLLRRMK 753
Cdd:cd17996    226 -PFLLRRLK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
513-751 1.11e-43

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: 159.38  E-value: 1.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLweLHCqqaGGILGDEMGLGKTIQIIAF-LAGLSYSKIRTRGSNYRYQGL------GPTVIVCPATVMH 585
Cdd:cd18008      1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALALiLATRPQDPKIPEELEENSSDPkklylsKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  586 QWVKEF--HTWWPPFRVAVLHetGSytnKKVKLIREIASCHgILITSYSyiRLMQDN------------------IHSYD 645
Cdd:cd18008     76 QWKDEIekHTKPGSLKVYVYH--GS---KRIKSIEELSDYD-IVITTYG--TLASEFpknkkgggrdskekeaspLHRIR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  646 WHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNA 725
Cdd:cd18008    148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKAL 227
                          250       260
                   ....*....|....*....|....*.
gi 1443618724  726 SPVQVktaykcacvlrdTINPYLLRR 751
Cdd:cd18008    228 ERLQA------------LLKPILLRR 241
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
512-753 3.20e-43

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: 157.48  E-value: 3.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  512 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyrYQGL-GPTVIVCPATVMHQWVKE 590
Cdd:cd17997      3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKH-----------YKNInGPHLIIVPKSTLDNWMRE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  591 FHTWWPPFRVAVLHETgsyTNKKVKLIREIaSCHG---ILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLA 667
Cdd:cd17997     72 FKRWCPSLRVVVLIGD---KEERADIIRDV-LLPGkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  668 CKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNAspvqVKTAYKcacVLRdtinPY 747
Cdd:cd17997    148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEV----VQRLHK---VLR----PF 216

                   ....*.
gi 1443618724  748 LLRRMK 753
Cdd:cd17997    217 LLRRIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
516-751 5.90e-43

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: 156.64  E-value: 5.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLaglsySKIRTRGsNYRyqglGPTVIVCPATVMHQWVKEFHTWw 595
Cdd:cd17995      4 YQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFL-----EHLYQVE-GIR----GPFLVIAPLSTIPNWQREFETW- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  596 PPFRVAVLHETGS-----------YTNKKVKLIREIASCHgILITSYSYIrlMQD-----NIHsydWHYVILDEGHKIRN 659
Cdd:cd17995     73 TDMNVVVYHGSGEsrqiiqqyemyFKDAQGRKKKGVYKFD-VLITTYEMV--IADaeelrKIP---WRVVVVDEAHRLKN 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  660 PNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacV 739
Cdd:cd17995    147 RNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF------GDLKTAEQVE---------K 211
                          250
                   ....*....|..
gi 1443618724  740 LRDTINPYLLRR 751
Cdd:cd17995    212 LQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
512-751 8.45e-41

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: 150.20  E-value: 8.45e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  512 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSkirtrgsnyrYQGLGPTVIVCPATVMHQWVKEF 591
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHS----------QQQYGPFLVVVPLSTMPAWQREF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPPFRVAVL------------HETGSYTNKKVKLireiaschGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRN 659
Cdd:cd17993     71 AKWAPDMNVIVYlgdiksrdtireYEFYFSQTKKLKF--------NVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKN 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  660 PNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQfsvpitmggYSNASPVQVKTaykcacv 739
Cdd:cd17993    143 DESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE---------HDEEQEKGIAD------- 206
                          250
                   ....*....|..
gi 1443618724  740 LRDTINPYLLRR 751
Cdd:cd17993    207 LHKELEPFILRR 218
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
516-731 3.06e-38

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: 143.42  E-value: 3.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQA---------GGILGDEMGLGKTIQIIAFLAGLsyskirtrgsnYRYQGLGPTVIVCPATVMHQ 586
Cdd:cd18069      4 HQIGGIRFLYDNIIESLerykgssgfGCILAHSMGLGKTLQVISFLDVL-----------LRHTGAKTVLAIVPVNTLQN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  587 WVKEFHTWWPP-----------FRVAVLHETGSYTNKKVKLIREIASCHGILITSYSYIRLMQDNihsydwHYVILDEGH 655
Cdd:cd18069     73 WLSEFNKWLPPpealpnvrprpFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGP------DVVICDEGH 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443618724  656 KIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVK 731
Cdd:cd18069    147 RIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQDVK 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
513-751 1.56e-37

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: 140.65  E-value: 1.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWE-LHCQQaGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRYQGLGPTVIVCPATVMHQWVKEF 591
Cdd:cd18006      1 LRPYQLEGVNWLLQcRAEQH-GCILGDEMGLGKTCQTISLLWYLAG----------RLKLLGPFLVLCPLSVLDNWKEEL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPpfRVAVLHETGSyTNKKVKLIREIASCH--GILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACK 669
Cdd:cd18006     70 NRFAP--DLSVITYMGD-KEKRLDLQQDIKSTNrfHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  670 QFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLG--TLPVFMEQFSvpitmggysnaspvQVKTAYKCACVLRDTINPY 747
Cdd:cd18006    147 EFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPkdKLDDFIKAYS--------------ETDDESETVEELHLLLQPF 212

                   ....
gi 1443618724  748 LLRR 751
Cdd:cd18006    213 LLRR 216
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
497-760 7.30e-37

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 139.80  E-value: 7.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  497 TEFEEGfkvPGFL-FKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyrYQGL-GP 574
Cdd:cd18064      2 TRFEDS---PSYVkWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKH-----------YRNIpGP 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  575 TVIVCPATVMHQWVKEFHTWWPPFRVAVL---HETGSYTNKKVKLIREIASChgilITSYSYIRLMQDNIHSYDWHYVIL 651
Cdd:cd18064     68 HMVLVPKSTLHNWMAEFKRWVPTLRAVCLigdKDQRAAFVRDVLLPGEWDVC----VTSYEMLIKEKSVFKKFNWRYLVI 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  652 DEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGgysnaspvQVK 731
Cdd:cd18064    144 DEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG--------DQK 215
                          250       260
                   ....*....|....*....|....*....
gi 1443618724  732 TAYKCACVLRdtinPYLLRRMKADVKMSL 760
Cdd:cd18064    216 LVERLHMVLR----PFLLRRIKADVEKSL 240
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
516-700 1.43e-35

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: 134.05  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEFHTWW 595
Cdd:cd17998      4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIP-----------GPHLVVVPSSTLDNWLREFKRWC 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  596 PPFRVAVLHetGSYTNKKVklIREIASC----HGILITSY------SYIRLMQDNIhSYDwhYVILDEGHKIRNPNAAVT 665
Cdd:cd17998     73 PSLKVEPYY--GSQEERKH--LRYDILKgledFDVIVTTYnlatsnPDDRSFFKRL-KLN--YVVYDEGHMLKNMTSERY 145
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1443618724  666 LACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFP 700
Cdd:cd17998    146 RHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
516-751 9.92e-35

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: 133.43  E-value: 9.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWEL-----HCQQAGGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYryqGLGP----TVIVCPATVMHQ 586
Cdd:cd18066      4 HQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTL------LRQGPY---GGKPvikrALIVTPGSLVKN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  587 WVKEFHTWWPPFRVAVlhetgsYTNKKVKLIREIASC--HGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAV 664
Cdd:cd18066     75 WKKEFQKWLGSERIKV------FTVDQDHKVEEFIASplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  665 TLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTI 744
Cdd:cd18066    149 TTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLT 228

                   ....*..
gi 1443618724  745 NPYLLRR 751
Cdd:cd18066    229 GLFILRR 235
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
512-751 1.11e-34

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: 133.21  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  512 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRYQGLGPTVIVCPATVMHQWVKEF 591
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFH----------QHQLYGPFLLVVPLSTLTSWQREF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPPFRVAVLheTGSYTNKKVklIREIASCH--------GILITSYSYirLMQDN--IHSYDWHYVILDEGHKIRNPN 661
Cdd:cd18054     90 EIWAPEINVVVY--IGDLMSRNT--IREYEWIHsqtkrlkfNALITTYEI--LLKDKtvLGSINWAFLGVDEAHRLKNDD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  662 AAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSvpitmGGYSNaspvqvktAYKCacvLR 741
Cdd:cd18054    164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHG-----KGREN--------GYQS---LH 227
                          250
                   ....*....|
gi 1443618724  742 DTINPYLLRR 751
Cdd:cd18054    228 KVLEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
513-751 1.43e-34

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: 132.63  E-value: 1.43e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRYQGLGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAE----------EHNIWGPFLVIAPASTLHNWQQEIS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVavLHETGSYTNKKV--------KLIREIASCHgILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAV 664
Cdd:cd18002     71 RFVPQFKV--LPYWGNPKDRKVlrkfwdrkNLYTRDAPFH-VVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  665 TLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPIT--MGGYSNASPVQVKTaykcacvLRD 742
Cdd:cd18002    148 WKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshAENKTGLNEHQLKR-------LHM 220

                   ....*....
gi 1443618724  743 TINPYLLRR 751
Cdd:cd18002    221 ILKPFMLRR 229
cc_ERCC-6_N cd21397
coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 ...
86-162 6.95e-33

coiled-coil domain located near the N-terminus of human Excision Repair Cross Complementing 6 (ERCC-6) and related proteins; This model represents a coiled-coil domain located near the N-terminus of ERCC-6 and related proteins. ERCC-6 (also known as Cockayne syndrome group B, CSB) is a DNA-binding protein important in eukaryotic transcription-coupled repair (TCR). TCR is a well-conserved sub-pathway of nucleotide excision repair (NER) that preferentially removes DNA lesions from the template strand blocking translocation of RNA polymerase II (Pol II). In a model for TCR, the processing Pol II encounters the lesion on the transcribed DNA strand and stalls; it is then displaced by the TCR-initiation complex which includes ERCC-6, ERCC-8, UVSSA and USP7; TCR-specific factors then access the lesion for the DNA damage incision process. The N-terminal region, the ATPase domain and the C-terminal region of ERCC-6 all directly contribute to DNA association and catalytic activity. The ATPase domain functions in concert with either the N- or C-terminal region to mediate UV-induced chromatin association. The N-terminal region prevents ERCC-6 from stably associating with chromatin under normal growth conditions, and the C-terminal region of ERCC-6 promotes stable chromatin association in the presence of lesion-stalled transcription. In addition to this coiled-coil domain, the N-terminal region of ERCC-6 includes two lysine residues subject to SUMOylation, a nucleolar localization signal NoLS1, and a nuclear localization signal NLS1. ERCC-6 also includes a SWI/SNF-like ATPase domain, a nucleotide-binding domain and a ubiquitin-binding domain. This coiled-coil domain binds magnesium. This domain family does not include Saccharomyces cerevisiae RAD26, and Schizosaccharomyces pombe Rhp26.


Pssm-ID: 411064 [Multi-domain]  Cd Length: 77  Bit Score: 122.32  E-value: 6.95e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443618724   86 VSDSAQAAELRGLGVDVYDQDVLEQGVLQQVDHAINEASKAAKIADAEKEYQSVLEDVRSCTISLKQINKIIEQLSP 162
Cdd:cd21397      1 VPESDQASELQGLGVDVYDQDEFEQGVLQQVDQAIAEEEEERRKKDAEKELKSVLDDIRSVKQDLEHIEKVLEQLEP 77
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
513-753 1.06e-32

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: 128.24  E-value: 1.06e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGL-SYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEF 591
Cdd:cd18062     24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLmEHKRIN-----------GPFLIIVPLSTLSNWVYEF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPpfRVAVLHETGSYTNKKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACK-Q 670
Cdd:cd18062     93 DKWAP--SVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  671 FRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYL 748
Cdd:cd18062    171 YVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----EKVDLNEEETILIIrrLHKVLRPFL 246

                   ....*
gi 1443618724  749 LRRMK 753
Cdd:cd18062    247 LRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
513-753 1.48e-32

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: 127.06  E-value: 1.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyrYQGL-GPTVIVCPATVMHQWVKEF 591
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKH-----------YRNIpGPHMVLVPKSTLHNWMNEF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPPFRVAVLheTGSyTNKKVKLIRE--IASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACK 669
Cdd:cd18065     85 KRWVPSLRAVCL--IGD-KDARAAFIRDvmMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  670 QFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGysnaspvqvktaYKCACVLRDTINPYLL 749
Cdd:cd18065    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGD------------QKLVERLHAVLKPFLL 229

                   ....
gi 1443618724  750 RRMK 753
Cdd:cd18065    230 RRIK 233
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
1439-1511 3.04e-32

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 120.31  E-value: 3.04e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443618724 1439 STEYDELLVDVRNFIAFQArvDGEASTQEILQEFEGKLPTAQACVFRELLRNLCTFHRSPNGEGVWRLKPEFR 1511
Cdd:cd22254      2 STEAEELLADIRDFLAFQA--GGQATTDEIVDHFKDRLPPEQSALFKALLKQICTFERDPGGRGVWVLKPEFR 72
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
513-753 4.53e-32

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: 126.33  E-value: 4.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTrgsnyryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLN----------GPYLIIVPLSTLSNWTYEFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPpfRVAVLHETGSYTNKKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACK-QF 671
Cdd:cd18063     94 KWAP--SVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  672 RTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGysnaSPVQVKTAYKCACV--LRDTINPYLL 749
Cdd:cd18063    172 VAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG----ERVDLNEEETILIIrrLHKVLRPFLL 247

                   ....
gi 1443618724  750 RRMK 753
Cdd:cd18063    248 RRLK 251
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
516-751 2.57e-31

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: 123.73  E-value: 2.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWElhCQQA-------GGILGDEMGLGKTIQIIAFLAGLsyskirTRGSNYRYQGLGPTVIVCPATVMHQWV 588
Cdd:cd18067      4 HQREGVKFLYR--CVTGrrirgshGCIMADEMGLGKTLQCITLMWTL------LRQSPQCKPEIDKAIVVSPSSLVKNWA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  589 KEFHTWWPPFRVAVLHETGSYTNKKVKLIReIASCHG------ILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNA 662
Cdd:cd18067     76 NELGKWLGGRLQPLAIDGGSKKEIDRKLVQ-WASQQGrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  663 AVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRD 742
Cdd:cd18067    155 QTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELIS 234

                   ....*....
gi 1443618724  743 TINPYLLRR 751
Cdd:cd18067    235 IVNRCIIRR 243
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
513-751 2.79e-31

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: 122.16  E-value: 2.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFH 592
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAvlhetgSYTNKKVklireiaschgiLITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACKQFR 672
Cdd:cd17994     71 MWAPDFYVV------TYVGDHV------------LLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443618724  673 TPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPitmggysnASPVQVKTaykcacvLRDTINPYLLRR 751
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADI--------SKEDQIKK-------LHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
513-751 1.95e-29

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: 118.19  E-value: 1.95e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFH 592
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSL-YKEGHTKG---------PFLVSAPLSTIINWEREFQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRV----------AVLHETG-SYTN-------KKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEG 654
Cdd:cd18055     71 MWAPDFYVvtytgdkdsrAIIRENEfSFDDnavkggkKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  655 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 734
Cdd:cd18055    151 HRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1443618724  735 kcacvLRDTINPYLLRR 751
Cdd:cd18055    221 -----LHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
512-751 7.08e-29

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 116.69  E-value: 7.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  512 KLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYskirtrgsnyRYQGLGPTVIVCPATVMHQWVKEF 591
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFH----------EHQLYGPFLLVVPLSTLTSWQREI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPPFRVAVL------------HETGSYTNKKVKLireiaschGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRN 659
Cdd:cd18053     90 QTWAPQMNAVVYlgdinsrnmirtHEWMHPQTKRLKF--------NILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  660 PNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSnaspvqvktaykcacv 739
Cdd:cd18053    162 DDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYAS---------------- 225
                          250
                   ....*....|..
gi 1443618724  740 LRDTINPYLLRR 751
Cdd:cd18053    226 LHKELEPFLLRR 237
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
516-731 7.76e-29

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: 116.91  E-value: 7.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  516 YQQTGVRWLWELHCQQ---------AGGILGDEMGLGKTIQIIAFLaglsyskiRTRGSNYRYQGLGPTVIVCPATVMHQ 586
Cdd:cd18068      4 HQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFL--------HTVLLCEKLENFSRVLVVCPLNTVLN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  587 WVKEFHTWWPPFRVAVLHETGSYTNKKVKLIREIASCH-----GILITSYSYIRLM--QDNIHSYDW------------- 646
Cdd:cd18068     76 WLNEFEKWQEGLKDEEKIEVNELATYKRPQERSYKLQRwqeegGVMIIGYDMYRILaqERNVKSREKlkeifnkalvdpg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  647 -HYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNA 725
Cdd:cd18068    156 pDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADS 235

                   ....*.
gi 1443618724  726 SPVQVK 731
Cdd:cd18068    236 TLVDVR 241
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
533-730 1.55e-27

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: 112.56  E-value: 1.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  533 GGILGDEMGLGKTIQIIAFLAGlsyskirtrgsnyryqglGPTVIVCPATVMHQWVKEFHTWWPPFRVAVLHETGSYTNK 612
Cdd:cd18071     50 GGILADDMGLGKTLTTISLILA------------------NFTLIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  613 KVKLIREiascHGILITSYSYIRLMQDN-----IHSYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNN 687
Cdd:cd18071    112 DPKLLSK----YDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1443618724  688 LKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGYSNASPVQV 730
Cdd:cd18071    188 PKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLKRLQV 230
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
513-751 2.10e-27

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: 112.08  E-value: 2.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFH 592
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSL-YKEGHSKG---------PYLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRVAV-----------------LHETGSYTNKKV-KLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEG 654
Cdd:cd18057     71 MWAPDFYVVTytgdkesrsvirenefsFEDNAIRSGKKVfRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  655 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 734
Cdd:cd18057    151 HRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA--------DISKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1443618724  735 kcacvLRDTINPYLLRR 751
Cdd:cd18057    221 -----LHDLLGPHMLRR 232
DEXDc smart00487
DEAD-like helicases superfamily;
505-713 2.46e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 111.04  E-value: 2.46e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   505 VPGFLFKKLFKYQQTGVRWLWELHCqqaGGILGDEMGLGKTIQIIAFLAglsyskirtrgSNYRYQGLGPTVIVCP-ATV 583
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPAL-----------EALKRGKGGRVLVLVPtREL 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   584 MHQWVKEFHTWWPPFRVAVLHETGSYTnkKVKLIREIAS-CHGILITSYSYIR--LMQDNIHSYDWHYVILDEGHKIRNP 660
Cdd:smart00487   67 AEQWAEELKKLGPSLGLKVVGLYGGDS--KREQLRKLESgKTDILVTTPGRLLdlLENDKLSLSNVDLVILDEAHRLLDG 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443618724   661 NAAVTLACKQFRTP---HRIILSGSP---MQNNLKELWSLFDFVFPGKLGTLPVfmEQF 713
Cdd:smart00487  145 GFGDQLEKLLKLLPknvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI--EQF 201
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
513-741 1.60e-26

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: 108.83  E-value: 1.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRW-LwelhcqQAGG--ILGDEMGLGKTIQIIAFLAglsyskirtrgsnyRYQGLGPTVIVCPATVMHQWVK 589
Cdd:cd18010      1 LLPFQREGVCFaL------RRGGrvLIADEMGLGKTVQAIAIAA--------------YYREEWPLLIVCPSSLRLTWAD 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  590 EFHTWwppFRVAVLHETGSYTNKKVKLIREIASchgILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLACK 669
Cdd:cd18010     61 EIERW---LPSLPPDDIQVIVKSKDGLRDGDAK---VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAAL 134
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443618724  670 QF--RTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSVPITMGGY----SNASPVQVKTAYKCACVLR 741
Cdd:cd18010    135 PLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGwdysGSSNLEELHLLLLATIMIR 212
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
513-751 2.26e-26

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 109.38  E-value: 2.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLsYSKIRTRGsnyryqglgPTVIVCPATVMHQWVKEFH 592
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSL-YKEGHSKG---------PFLVSAPLSTIINWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWWPPFRV----------AVLHETG-SYTN-------KKVKLIREIASCHGILITSYSYIRLMQDNIHSYDWHYVILDEG 654
Cdd:cd18056     71 MWAPDMYVvtyvgdkdsrAIIRENEfSFEDnairggkKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  655 HKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTay 734
Cdd:cd18056    151 HRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA--------DIAKEDQIKK-- 220
                          250
                   ....*....|....*..
gi 1443618724  735 kcacvLRDTINPYLLRR 751
Cdd:cd18056    221 -----LHDMLGPHMLRR 232
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
846-959 4.99e-26

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: 103.83  E-value: 4.99e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  846 GKMIVVESLLKiwHKQGHRVLFFTQSRQMLQIlEVFVRERNYSYLRMDGTTTIASRQPLITRYNEDKsiFIFLLTTRVGG 925
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGK--IDVLVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1443618724  926 IGVNLTGADRVIIYDPDWNPSTDTQARERAWRIG 959
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
513-751 5.97e-26

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: 107.82  E-value: 5.97e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIR-----------GPFLIIAPLSTITNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWwPPFRVAVLHetGS-------------YTNKKVKLIREIASCHGIlITSYSYIRLMQDNIHSYDWHYVILDEGHKIRN 659
Cdd:cd18058     70 TW-TEMNAIVYH--GSqisrqmiqqyemyYRDEQGNPLSGIFKFQVV-ITTFEMILADCPELKKINWSCVIIDEAHRLKN 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  660 PNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFSvpitmggySNASPVQVKTaykcacv 739
Cdd:cd18058    146 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG--------DLKTEEQVKK------- 210
                          250
                   ....*....|..
gi 1443618724  740 LRDTINPYLLRR 751
Cdd:cd18058    211 LQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
513-713 1.35e-25

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: 106.65  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIH-----------GPFLVIAPLSTIPNWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWwPPFRVAVLHETGS-----------YTNKKVKLIREIASCHGIlITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNPN 661
Cdd:cd18059     70 TW-TELNVVVYHGSQAsrrtiqlyemyFKDPQGRVIKGSYKFHAI-ITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1443618724  662 AAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQF 713
Cdd:cd18059    148 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
513-698 3.09e-25

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: 106.03  E-value: 3.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWL-WELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRG-------------SNYRYQGLGpTVIV 578
Cdd:cd18072      1 LLLHQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIALILAQKNTQNRKEEekekalteweskkDSTLVPSAG-TLVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  579 CPATVMHQWVKEF--HTWWPPFRVAVLHetGSYTNKKVKLIREiascHGILITSYSYI-----RLMQDNIHS----YDWH 647
Cdd:cd18072     80 CPASLVHQWKNEVesRVASNKLRVCLYH--GPNRERIGEVLRD----YDIVITTYSLVakeipTYKEESRSSplfrIAWA 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1443618724  648 YVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFV 698
Cdd:cd18072    154 RIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
513-713 6.48e-25

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: 104.70  E-value: 6.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIR-----------GPFLIIAPLSTIANWEREFR 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWwPPFRVAVLHetGSYTNKKV-------------KLIREIASCHGIlITSYSYIRLMQDNIHSYDWHYVILDEGHKIRN 659
Cdd:cd18061     70 TW-TDLNVVVYH--GSLISRQMiqqyemyfrdsqgRIIRGAYRFQAI-ITTFEMILGGCPELNAIDWRCVIIDEAHRLKN 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1443618724  660 PNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQF 713
Cdd:cd18061    146 KNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
513-751 9.99e-24

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: 101.28  E-value: 9.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRtrgsnyryqglGPTVIVCPATVMHQWVKEFH 592
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIH-----------GPFLVIAPLSTITNWEREFN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  593 TWwPPFRVAVLHetGSYTNKKVKLIREI------------ASCHGILITSYSYIRLMQDNIHSYDWHYVILDEGHKIRNP 660
Cdd:cd18060     70 TW-TEMNTIVYH--GSLASRQMIQQYEMyckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  661 NAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDFVFPGKLGTLPVFMEQFsvpitmGGYSNASPVQvktaykcacVL 740
Cdd:cd18060    147 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF------GDLKTEEQVQ---------KL 211
                          250
                   ....*....|.
gi 1443618724  741 RDTINPYLLRR 751
Cdd:cd18060    212 QAILKPMMLRR 222
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
513-697 3.89e-21

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: 94.72  E-value: 3.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWElhcqqAGGILGDEMGLGKTIQIIAFLA-------GLSYSKIRTRGSNYRYQGL--------GPTVI 577
Cdd:cd18070      1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALILlhprpdnDLDAADDDSDEMVCCPDCLvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  578 VCPATVMHQWVKEFHTWWPPfRVAVLHETGSYTNKKVKL--IREIAScHGILITSYS--------------------YIR 635
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPS-SLKVLTYQGVKKDGALASpaPEILAE-YDIVVTTYDvlrtelhyaeanrsnrrrrrQKR 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443618724  636 LMQDN--IHSYDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLKELWSLFDF 697
Cdd:cd18070    154 YEAPPspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSF 217
HELICc smart00490
helicase superfamily c-terminal domain;
876-959 4.83e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 85.73  E-value: 4.83e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   876 QILEVFVRERNYSYLRMDGTTTIASRQPLITRYNEDKSIFifLLTTRVGGIGVNLTGADRVIIYDPDWNPSTDTQARERA 955
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1443618724   956 WRIG 959
Cdd:smart00490   79 GRAG 82
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
513-694 4.57e-17

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: 81.57  E-value: 4.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWELhcQQAGGILGDEMGLGKTIQiiaflAGL--SYSKIRTRGsnyryqglGPTVIVCPATVMHQWVKE 590
Cdd:cd18011      1 PLPHQIDAVLRALRK--PPVRLLLADEVGLGKTIE-----AGLiiKELLLRGDA--------KRVLILCPASLVEQWQDE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  591 -FHTWWPPFRVAvlheTGSYTNKKVKLIREIASCHGILITSYSYIRLM---QDNIHSYDWHYVILDEGHKIRN-PNAAVT 665
Cdd:cd18011     66 lQDKFGLPFLIL----DRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNsGGGKET 141
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1443618724  666 L---ACKQF--RTPHRIILSGSPMQNNLKELWSL 694
Cdd:cd18011    142 KrykLGRLLakRARHVLLLTATPHNGKEEDFRAL 175
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
458-683 3.57e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.11  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  458 RWRDDGDEDYYKQRLRRWQKERLKDKDHDTAEELSDESDTEFEEGFKVPGFLFKkLFKYQQTGVRWLWELHCQQAG-GIL 536
Cdd:COG1061     27 ELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE-LRPYQQEALEALLAALERGGGrGLV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  537 gdEM--GLGKTIqIIAFLAglsyskirtrgsnYRYQGLGPTVIVCP-ATVMHQWVKEFHTWWPPFRVAVlhetgsytnkk 613
Cdd:COG1061    106 --VAptGTGKTV-LALALA-------------AELLRGKRVLVLVPrRELLEQWAEELRRFLGDPLAGG----------- 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443618724  614 vkliREIASCHGILITSY-SYIRLMQDNIHSYDWHYVILDEGHKIRNPNAAVTLacKQFRTPHRIILSGSP 683
Cdd:COG1061    159 ----GKKDSDAPITVATYqSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRIL--EAFPAAYRLGLTATP 223
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
912-962 1.24e-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: 47.70  E-value: 1.24e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1443618724  912 KSIFIFLLTTRVGGIGVNLTGADRVIIYDPDWNPSTDTQARERAWRIGQKK 962
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
513-723 3.41e-06

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: 49.66  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  513 LFKYQQTGVRWLWElhcQQAGGILGDeMGLGKTIqiiAFLAGLSYSKIRTRgsnyryqgLGPTVIVCPATVM-HQWVKEF 591
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTV---TTLTALSDLQLDDF--------TRRVLVIAPLRVArSTWPDEV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  592 HTWWPPF--RVAVLHETGSytnkkvKLIREIASCHGILITSYSYIRLMqDNIHSYDWHY--VILDEGHKIRNPNAAVTLA 667
Cdd:cd18013     66 EKWNHLRnlTVSVAVGTER------QRSKAANTPADLYVINRENLKWL-VNKSGDPWPFdmVVIDELSSFKSPRSKRFKA 138
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  668 CKQFR-TPHRII-LSGSPMQNNLKELWSLFDFVFPGK-LG-TLPVFMEQFSVPITMGGYS 723
Cdd:cd18013    139 LRKVRpVIKRLIgLTGTPSPNGLMDLWAQIALLDQGErLGrSITAYRERWFDPDKRNGQQ 198
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-391 3.66e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 3.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724   85 SVSDSAQAAELRGlgvDVYDQDVLEQGVLQQVDHAINEASKA-AKIADAEKEyqsvLEDVRsctislKQINKIIEQLSPQ 163
Cdd:TIGR02169  669 SRSEPAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELsQELSDASRK----IGEIE------KEIEQLEQEEEKL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  164 AATSKDVNRKLDSVKRQKYNKEQQLKKIKAKQKRLRAILAGtgILDEINDGEIEDDEEPGPSSSPLhlgsmlMPAQETE- 242
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--LEEALNDLEARLSHSRIPEIQAE------LSKLEEEv 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  243 --WEELIRtgqmtpfgtKIPQKPQRK--PRQLMLNETSDFEKYLAD-QAKLSSERKKLSLLKGAKRKaqaktaqhatstp 317
Cdd:TIGR02169  808 srIEARLR---------EIEQKLNRLtlEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEE------------- 865
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  318 IQSPTKEKRSKARTLSKTDKRLKKHMSRL--QKRALQF---QSKAGIPKEK---KYLEAKAKLTHEQ----RDDSGESEY 385
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKKERDELeaQLRELERkieELEAQIEKKRkrlSELKAKLEALEEElseiEDPKGEDEE 945

                   ....*.
gi 1443618724  386 VPDEEL 391
Cdd:TIGR02169  946 IPEEEL 951
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
533-680 3.25e-05

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 45.47  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  533 GGILGDEMGLGKTIqiIAFLAGLSYskIRTRGsnyryqglGPTVIVCP-ATVMHQWVKEFHTWW-PPFRVAVLHetgSYT 610
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLAALLL--LLKKG--------KKVLVLVPtKALALQTAERLRELFgPGIRVAVLV---GGS 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443618724  611 NKKVKLIREIASCHgILITSYSYIR---LMQDNIHSYDWHYVILDEGHKI----RNPNAAVTLACKQFRTPHRIILS 680
Cdd:cd00046     68 SAEEREKNKLGDAD-IIIATPDMLLnllLREDRLFLKDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILL 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
113-350 5.07e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  113 LQQVDHAINEASKaaKIADAEKEYQSVLEDvrsctisLKQINKIIEQLspqAATSKDVNRKLDSVKRQKYNKEQQLKKIK 192
Cdd:COG4942     29 LEQLQQEIAELEK--ELAALKKEEKALLKQ-------LAALERRIAAL---ARRIRALEQELAALEAELAELEKEIAELR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  193 AKQKRLRAILAG-------TGILDEINdgEIEDDEEPGPSSSPLHLGSMLMPAQETEWEELIRTgqmtpfgtkipQKPQR 265
Cdd:COG4942     97 AELEAQKEELAEllralyrLGRQPPLA--LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD-----------LAELA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  266 KPRQLMLNETSDFEKYLADQAKlssERKKLSLLKGAKRKAQAKtaqhatstpIQSPTKEKRSKARTLSKTDKRLKKHMSR 345
Cdd:COG4942    164 ALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLAR---------LEKELAELAAELAELQQEAEELEALIAR 231

                   ....*
gi 1443618724  346 LQKRA 350
Cdd:COG4942    232 LEAEA 236
PTZ00121 PTZ00121
MAEBL; Provisional
120-491 8.87e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  120 INEASKAAKIADAEKEYQSvlEDVRSCTISLK--QINKIIEQLSPQAATSKDVNRKLDSVKR-QKYNKEQQLKKIKAKQK 196
Cdd:PTZ00121  1130 AEEARKAEDARKAEEARKA--EDAKRVEIARKaeDARKAEEARKAEDAKKAEAARKAEEVRKaEELRKAEDARKAEAARK 1207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  197 --RLRAILAGTGILDEINDGEIEDDEEPGPSSSPLHLGSMLMPAQETEWEELIRTGQMTPFGTKIPQKPQRKPRQLMLNE 274
Cdd:PTZ00121  1208 aeEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  275 tsdfEKYLADQAKLSSERKKLSLLKG-----------------AKRKAQA--KTAQHATSTPiQSPTKEKRSKARTLSKT 335
Cdd:PTZ00121  1288 ----EKKKADEAKKAEEKKKADEAKKkaeeakkadeakkkaeeAKKKADAakKKAEEAKKAA-EAAKAEAEAAADEAEAA 1362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  336 DKRL---KKHMSRLQKRALQFQSKAGIPKEKKYLEAKAKLTHEQRDD--SGESEYVPDEELFDPEAAEEEEQQASSHAEN 410
Cdd:PTZ00121  1363 EEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  411 DSDY-ELKPLS---RKGKNLVKKDFKGDDDPDFYPSSEEEEEHAVGKRRIKRWRDDGDEDYYKQRLRRWQKERLKDKDHD 486
Cdd:PTZ00121  1443 AKKAdEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                   ....*
gi 1443618724  487 TAEEL 491
Cdd:PTZ00121  1523 KADEA 1527
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
541-655 2.58e-03

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


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 40.36  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443618724  541 GLGKTIQIIAflaglSYSKIRTRgsnyryqglgpTVIVCPATV-MHQWVKEFHTW--WPPFRVAVlhetgsYTNKKvkli 617
Cdd:cd18029     36 GAGKTLVGIT-----AACTIKKS-----------TLVLCTSAVsVEQWRRQFLDWttIDDEQIGR------FTSDK---- 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1443618724  618 REIASCHGILITSYSYIR----------LMQDNIHSYDWHYVILDEGH 655
Cdd:cd18029     90 KEIFPEAGVTVSTYSMLAntrkrspeseKFMEFITEREWGLIILDEVH 137
 
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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