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Conserved domains on  [gi|2771685888|ref|WP_367184336|]
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DEAD/DEAH box helicase [Acidiferrobacter sp.]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
131-807 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 554.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 131 RPQHLPLSQALAEFAGVRRRAQLLSLLEPVQRAAEGCPWLDEMVQSGEMYHPLRWQPQDAWRFLQDVPRLEAAGIVVRM- 209
Cdd:COG0553     7 LLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLr 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 210 -PPSWAGGRPARPKVSASVGCEPASRVGLEALLDFEAAITLDGEKLHREEIERLLSRTDGLQLLRGRWVEVDRKRLTKML 288
Cdd:COG0553    87 lLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 289 DRFAEIERRARAGGLSFAEAMRLTAGMEAGAEGGILERDWADVAAGPWLAETLRHLRSPEGLARVDPGP-ALHATLRPYQ 367
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPaGLKATLRPYQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 368 QAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVVHPSAm 447
Cdd:COG0553   247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 448 ppeeVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRL 526
Cdd:COG0553   326 ----ERAKGANPFEDADLVITSYGLLRRdIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 527 SDLWSIFDFTHPGLLGSEKAFAALSRRLGESG---HFAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAAWCALTPVQAV 603
Cdd:COG0553   402 EELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeALERLRRLLRPFLLRRTKED--VLKDLPEKTEETLYVELTPEQRA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 604 LYQRAVKELAQRLERAEGIDRRGLVLAFLMRFKQICNHPSQWLGDGLWRPADSGKFARLKELAEVIAIRQEKMLLFTQFR 683
Cdd:COG0553   480 LYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFT 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 684 ETAEPLRAFLGGIfGRQGLVLHGGTPVKQRRELVRRFQEDEQTPFFILSLKAGGAGLNLTAARHVIHFDRWWNPAVEDQA 763
Cdd:COG0553   560 DTLDLLEERLEER-GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 2771685888 764 TDRAFRIGQKYNVLAHKFLCRGTIEERIDALIRDKRELVRGVLE 807
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
131-807 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 554.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 131 RPQHLPLSQALAEFAGVRRRAQLLSLLEPVQRAAEGCPWLDEMVQSGEMYHPLRWQPQDAWRFLQDVPRLEAAGIVVRM- 209
Cdd:COG0553     7 LLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLr 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 210 -PPSWAGGRPARPKVSASVGCEPASRVGLEALLDFEAAITLDGEKLHREEIERLLSRTDGLQLLRGRWVEVDRKRLTKML 288
Cdd:COG0553    87 lLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 289 DRFAEIERRARAGGLSFAEAMRLTAGMEAGAEGGILERDWADVAAGPWLAETLRHLRSPEGLARVDPGP-ALHATLRPYQ 367
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPaGLKATLRPYQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 368 QAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVVHPSAm 447
Cdd:COG0553   247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 448 ppeeVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRL 526
Cdd:COG0553   326 ----ERAKGANPFEDADLVITSYGLLRRdIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 527 SDLWSIFDFTHPGLLGSEKAFAALSRRLGESG---HFAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAAWCALTPVQAV 603
Cdd:COG0553   402 EELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeALERLRRLLRPFLLRRTKED--VLKDLPEKTEETLYVELTPEQRA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 604 LYQRAVKELAQRLERAEGIDRRGLVLAFLMRFKQICNHPSQWLGDGLWRPADSGKFARLKELAEVIAIRQEKMLLFTQFR 683
Cdd:COG0553   480 LYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFT 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 684 ETAEPLRAFLGGIfGRQGLVLHGGTPVKQRRELVRRFQEDEQTPFFILSLKAGGAGLNLTAARHVIHFDRWWNPAVEDQA 763
Cdd:COG0553   560 DTLDLLEERLEER-GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 2771685888 764 TDRAFRIGQKYNVLAHKFLCRGTIEERIDALIRDKRELVRGVLE 807
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
359-576 3.38e-95

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: 296.78  E-value: 3.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 359 LHATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLR 438
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 439 VLVVHPSAMPPEEVrsvdgRDLAGADLVVTTYGMLLKQP-VLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIAL 517
Cdd:cd18012    81 VLVIHGTKRKREKL-----RALEDYDLVITSYGLLRRDIeLLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2771685888 518 TGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGH----FAPLKKLVQPYILRRLK 576
Cdd:cd18012   156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdeeaLEELKKLISPFILRRLK 218
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
366-642 1.14e-61

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: 209.85  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 366 YQQAGVRWLY-LLTRLGLGGCLADDMGLGKTIQLLALLLILQRESP--GHPSLLVAPASLLANWQAQAERFA--PTLRVL 440
Cdd:pfam00176   1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 441 VVHPSAMPPEEVRSvDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTG 519
Cdd:pfam00176  81 VLHGNKRPQERWKN-DPNFLADFDVVITTYETLRKhKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 520 TPVENRLSDLWSIFDFTHPGLLGS----EKAFAALSRRLGESGHFAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAAWC 595
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSlstfRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKD--VEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2771685888 596 ALTPVQAVLYQRavKELAQRLERAEG--IDRRGL--VLAFLMRFKQICNHP 642
Cdd:pfam00176 238 RLSKLQRKLYQT--FLLKKDLNAIKTgeGGREIKasLLNILMRLRKICNHP 286
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
362-827 1.51e-57

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 213.51  E-value: 1.51e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  362 TLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLL--ILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGylHEYRGITG-PHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  440 LVVHPSampPEEVRSVDGRDLA--GADLVVTTYGMLLKQP-VLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:PLN03142   248 VKFHGN---PEERAHQREELLVagKFDVCVTSFEMAIKEKtALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGH---FAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAA 593
Cdd:PLN03142   325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRRLKSD--VEKGLPPKKETIL 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  594 WCALTPVQAVLYQRAVKELAQRLERaeGIDRRGLvLAFLMRFKQICNHPSQWLGDGLWRP--------ADSGKFARLKEL 665
Cdd:PLN03142   403 KVGMSQMQKQYYKALLQKDLDVVNA--GGERKRL-LNIAMQLRKCCNHPYLFQGAEPGPPyttgehlvENSGKMVLLDKL 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  666 AEVIAIRQEKMLLFTQFRETAEPLRAFLggIF-GRQGLVLHGGTPVKQRRELVRRFQEDEQTPF-FILSLKAGGAGLNLT 743
Cdd:PLN03142   480 LPKLKERDSRVLIFSQMTRLLDILEDYL--MYrGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFvFLLSTRAGGLGINLA 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  744 AARHVIHFDRWWNPAVEDQATDRAFRIGQKYNVLAHKFLCRGTIEERIDALIRDKRELVRGVLEPGQEINLTELDDTALL 823
Cdd:PLN03142   558 TADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELL 637

                   ....
gi 2771685888  824 DLVR 827
Cdd:PLN03142   638 QMVR 641
DEXDc smart00487
DEAD-like helicases superfamily;
362-539 4.90e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 89.09  E-value: 4.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  362 TLRPYQQAGVRWLYLLTRlglGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAP-ASLLANWQAQAERFAP--TLR 438
Cdd:smart00487   8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPslGLK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  439 VLVVHPSAMPPEEVRSVDGRDlagADLVVTTYGML---LKQPVLAGQDWRILAIDEAQAIKNPGAK-QTRAVKGLTAQA- 513
Cdd:smart00487  85 VVGLYGGDSKREQLRKLESGK---TDILVTTPGRLldlLENDKLSLSNVDLVILDEAHRLLDGGFGdQLEKLLKLLPKNv 161
                          170       180       190
                   ....*....|....*....|....*....|
gi 2771685888  514 -RIALTGTP---VENRLSDLWSIFDFTHPG 539
Cdd:smart00487 162 qLLLLSATPpeeIENLLELFLNDPVFIDVG 191
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
131-807 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 554.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 131 RPQHLPLSQALAEFAGVRRRAQLLSLLEPVQRAAEGCPWLDEMVQSGEMYHPLRWQPQDAWRFLQDVPRLEAAGIVVRM- 209
Cdd:COG0553     7 LLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLr 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 210 -PPSWAGGRPARPKVSASVGCEPASRVGLEALLDFEAAITLDGEKLHREEIERLLSRTDGLQLLRGRWVEVDRKRLTKML 288
Cdd:COG0553    87 lLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 289 DRFAEIERRARAGGLSFAEAMRLTAGMEAGAEGGILERDWADVAAGPWLAETLRHLRSPEGLARVDPGP-ALHATLRPYQ 367
Cdd:COG0553   167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPaGLKATLRPYQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 368 QAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVVHPSAm 447
Cdd:COG0553   247 LEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 448 ppeeVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRL 526
Cdd:COG0553   326 ----ERAKGANPFEDADLVITSYGLLRRdIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 527 SDLWSIFDFTHPGLLGSEKAFAALSRRLGESG---HFAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAAWCALTPVQAV 603
Cdd:COG0553   402 EELWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeALERLRRLLRPFLLRRTKED--VLKDLPEKTEETLYVELTPEQRA 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 604 LYQRAVKELAQRLERAEGIDRRGLVLAFLMRFKQICNHPSQWLGDGLWRPADSGKFARLKELAEVIAIRQEKMLLFTQFR 683
Cdd:COG0553   480 LYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFT 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 684 ETAEPLRAFLGGIfGRQGLVLHGGTPVKQRRELVRRFQEDEQTPFFILSLKAGGAGLNLTAARHVIHFDRWWNPAVEDQA 763
Cdd:COG0553   560 DTLDLLEERLEER-GIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 2771685888 764 TDRAFRIGQKYNVLAHKFLCRGTIEERIDALIRDKRELVRGVLE 807
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
359-576 3.38e-95

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: 296.78  E-value: 3.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 359 LHATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLR 438
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 439 VLVVHPSAMPPEEVrsvdgRDLAGADLVVTTYGMLLKQP-VLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIAL 517
Cdd:cd18012    81 VLVIHGTKRKREKL-----RALEDYDLVITSYGLLRRDIeLLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLAL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2771685888 518 TGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGH----FAPLKKLVQPYILRRLK 576
Cdd:cd18012   156 TGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGdeeaLEELKKLISPFILRRLK 218
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
366-642 1.14e-61

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: 209.85  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 366 YQQAGVRWLY-LLTRLGLGGCLADDMGLGKTIQLLALLLILQRESP--GHPSLLVAPASLLANWQAQAERFA--PTLRVL 440
Cdd:pfam00176   1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 441 VVHPSAMPPEEVRSvDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTG 519
Cdd:pfam00176  81 VLHGNKRPQERWKN-DPNFLADFDVVITTYETLRKhKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 520 TPVENRLSDLWSIFDFTHPGLLGS----EKAFAALSRRLGESGHFAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAAWC 595
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSlstfRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKD--VEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2771685888 596 ALTPVQAVLYQRavKELAQRLERAEG--IDRRGL--VLAFLMRFKQICNHP 642
Cdd:pfam00176 238 RLSKLQRKLYQT--FLLKKDLNAIKTgeGGREIKasLLNILMRLRKICNHP 286
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
362-827 1.51e-57

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 213.51  E-value: 1.51e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  362 TLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLL--ILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGylHEYRGITG-PHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  440 LVVHPSampPEEVRSVDGRDLA--GADLVVTTYGMLLKQP-VLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:PLN03142   248 VKFHGN---PEERAHQREELLVagKFDVCVTSFEMAIKEKtALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGH---FAPLKKLVQPYILRRLKTDkaVIADLPDKTEMAA 593
Cdd:PLN03142   325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQqevVQQLHKVLRPFLLRRLKSD--VEKGLPPKKETIL 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  594 WCALTPVQAVLYQRAVKELAQRLERaeGIDRRGLvLAFLMRFKQICNHPSQWLGDGLWRP--------ADSGKFARLKEL 665
Cdd:PLN03142   403 KVGMSQMQKQYYKALLQKDLDVVNA--GGERKRL-LNIAMQLRKCCNHPYLFQGAEPGPPyttgehlvENSGKMVLLDKL 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  666 AEVIAIRQEKMLLFTQFRETAEPLRAFLggIF-GRQGLVLHGGTPVKQRRELVRRFQEDEQTPF-FILSLKAGGAGLNLT 743
Cdd:PLN03142   480 LPKLKERDSRVLIFSQMTRLLDILEDYL--MYrGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFvFLLSTRAGGLGINLA 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  744 AARHVIHFDRWWNPAVEDQATDRAFRIGQKYNVLAHKFLCRGTIEERIDALIRDKRELVRGVLEPGQEINLTELDDTALL 823
Cdd:PLN03142   558 TADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKDELL 637

                   ....
gi 2771685888  824 DLVR 827
Cdd:PLN03142   638 QMVR 641
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
363-538 4.45e-52

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: 179.68  E-value: 4.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPG-HPSLLVAPASLLANWQAQAERFAPTLRVLV 441
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKErGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAmpPEEVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGT 520
Cdd:cd17919    81 YHGSQ--RERAQIRAKEKLDKFDVVLTTYETLRRdKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGT 158
                         170
                  ....*....|....*...
gi 2771685888 521 PVENRLSDLWSIFDFTHP 538
Cdd:cd17919   159 PLQNNLEELWALLDFLDP 176
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
656-782 2.20e-49

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: 170.35  E-value: 2.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 656 SGKFARLKELAEVIAIRQEKMLLFTQFRETAEPLRAFLGGIfGRQGLVLHGGTPVKQRRELVRRFQEDEQTPFFILSLKA 735
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER-GIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2771685888 736 GGAGLNLTAARHVIHFDRWWNPAVEDQATDRAFRIGQKYNVLAHKFL 782
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
363-574 8.30e-49

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: 172.54  E-value: 8.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGH------PSLLVAPASLLANWQAQAERFAPT 436
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSfnsenlPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 437 LRVLVVHPSAMPPEEVRSVDgrDLAGADLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARI 515
Cdd:cd17999    81 AFLKPLAYVGPPQERRRLRE--QGEKHNVIVASYDVLRNDiEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 516 ALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAAL-------------SRRLGESGHFA--PLKKLVQPYILRR 574
Cdd:cd17999   159 ILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRflkpilasrdskaSAKEQEAGALAleALHKQVLPFLLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
363-574 5.12e-42

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: 153.30  E-value: 5.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVV 442
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 443 HPSamppeevrSVDGRD------LAGADLVVTTYGMLLK-----QPVLAGQ---DWRILaiDEAQAIKNPGAKQTRAVKG 508
Cdd:cd18001    81 HGT--------SKKERErnleriQRGGGVLLTTYGMVLSnteqlSADDHDEfkwDYVIL--DEGHKIKNSKTKSAKSLRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 509 LTAQARIALTGTPVENRLSDLWSIFDFTHPG-LLGSEKAFA--------------------ALSRRLGESghfapLKKLV 567
Cdd:cd18001   151 IPAKNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKmefenpitrgrdkdatqgekALGSEVAEN-----LRQII 225

                  ....*..
gi 2771685888 568 QPYILRR 574
Cdd:cd18001   226 KPYFLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
363-541 3.04e-39

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 144.00  E-value: 3.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGH-PSLLVAPASLLANWQAQAERFAPTLRVLV 441
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLgPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSA---MPPEEVRSVDGRDL------AGADLVVTTY-GMLLKQPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTA 511
Cdd:cd18000    81 LHSSGsgtGSEEKLGSIERKSQlirkvvGDGGILITTYeGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 2771685888 512 QARIALTGTPVENRLSDLWSIFDFTHPGLL 541
Cdd:cd18000   161 PHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
363-547 1.03e-38

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: 144.44  E-value: 1.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKT---------------------IQLLALLLILQRESPGHPSLLVAPAS 421
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTvqviaflaavlgktgtrrdreNNRPRFKKKPPASSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 422 LLANWQAQAERFApTLRVLVVHPSAmpPEEVRSVDgRDLAGADLVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGA 500
Cdd:cd18005    81 VLYNWKDELDTWG-HFEVGVYHGSR--KDDELEGR-LKAGRLEVVVTTYDTLrRCIDSLNSINWSAVIADEAHRIKNPKS 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2771685888 501 KQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAF 547
Cdd:cd18005   157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQF 203
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
363-574 4.98e-38

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: 142.04  E-value: 4.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLylLTRlglGGCLADDMGLGKT------------------IQLLALLLILQRESPGHPSLLVAPASLLA 424
Cdd:cd18008     1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTiqalalilatrpqdpkipEELEENSSDPKKLYLSKTTLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 425 NWQAQAERF--APTLRVLVVHPSAmppeevRSVDGRDLAGADLVVTTYGMLLK-----------------QPVLAGQDW- 484
Cdd:cd18008    76 QWKDEIEKHtkPGSLKVYVYHGSK------RIKSIEELSDYDIVITTYGTLASefpknkkgggrdskekeASPLHRIRWy 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 485 RILaIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGH---FA 561
Cdd:cd18008   150 RVI-LDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDrkaLE 228
                         250
                  ....*....|...
gi 2771685888 562 PLKKLVQPYILRR 574
Cdd:cd18008   229 RLQALLKPILLRR 241
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
362-576 1.92e-35

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: 134.44  E-value: 1.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 362 TLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQL-LALLLILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRVL 440
Cdd:cd18009     3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTiALLAHLRERGVWG-PFLVIAPLSTLPNWVNEFARFTPSVPVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 441 VVHPSAMPPEEVRSVDGRDLAGADL---VVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:cd18009    82 LYHGTKEERERLRKKIMKREGTLQDfpvVVTSYEIAMRdRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2771685888 517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAF------AALSRRLGESGHFAP---------LKKLVQPYILRRLK 576
Cdd:cd18009   162 LTGTPLQNNLSELWSLLNFLLPDVFDDLSSFeswfdfSSLSDNAADISNLSEereqnivhmLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
360-576 4.63e-35

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: 132.83  E-value: 4.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 360 HATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALL--LILQRESPGhPSLLVAPASLLANWQAQAERFAPTL 437
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLgyLKHYKNING-PHLIIVPKSTLDNWMREFKRWCPSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 438 RVLVVHPSamppEEVRSVDGRDL---AGADLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQA 513
Cdd:cd17997    80 RVVVLIGD----KEERADIIRDVllpGKFDVCITSYEMVIKEkTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2771685888 514 RIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAA---LSRRLGESGHFAP-LKKLVQPYILRRLK 576
Cdd:cd17997   156 RLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEwfnVNNCDDDNQEVVQrLHKVLRPFLLRRIK 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
363-588 3.73e-33

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: 128.24  E-value: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALL--LILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRVL 440
Cdd:cd18064    16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgyMKHYRNIPG-PHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 441 VVhpsaMPPEEVRSVDGRD--LAGA-DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:cd18064    95 CL----IGDKDQRAAFVRDvlLPGEwDVCVTSYEMLIKEkSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLL 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2771685888 517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAA---LSRRLGESGHFAPLKKLVQPYILRRLKTDkaVIADLPDK 588
Cdd:cd18064   171 LTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdTNNCLGDQKLVERLHMVLRPFLLRRIKAD--VEKSLPPK 243
DUF3670 pfam12419
SNF2 Helicase protein; This domain family is found in bacteria, archaea and eukaryotes, and is ...
178-313 8.07e-33

SNF2 Helicase protein; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00271, pfam00176. Most of the proteins in this family are annotated as SNF2 helicases but there is little accompanying literature to confirm this.


Pssm-ID: 463572  Cd Length: 136  Bit Score: 123.41  E-value: 8.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 178 EMYHPLRWQPQDAWRFLQD-VPRLEAAGIVVRMPPSWAGGRPARPKVSASV---GCEPASRVGLEALLDFEAAITLDGEK 253
Cdd:pfam12419   1 AVPTGLALTTEEAYEFLKEaAPRLEAAGFGVLLPAWWTKRRRPRLGLKLSAkgpAAAGGSFLGLDALLDFDWELALGDEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 254 LHREEIERLLSRTDGLQLLRGRWVEVDRKRLTKMLDRFaeieRRARAGGLSFAEAMRLTA 313
Cdd:pfam12419  81 LTEEEFERLAEAKRPLVRLRGQWVELDPEDLRAALEFL----ERRGKGGLTLADALRLAL 136
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
363-574 1.15e-31

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: 122.93  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKT-IQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLv 441
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTcQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 vhpSAMPPEEVRSVDGRDLAGA---DLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIAL 517
Cdd:cd18006    80 ---TYMGDKEKRLDLQQDIKSTnrfHVLLTTYEICLKdASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 518 TGTPVENRLSDLWSIFDFTHPGLLGSEKA---FAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18006   157 TGTPIQNSLQELYALLSFIEPNVFPKDKLddfIKAYSETDDESETVEELHLLLQPFLLRR 216
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
363-574 2.10e-31

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: 122.46  E-value: 2.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQ--LLALLLILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRVL 440
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQtiALLAHLACEKGNWG-PHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 441 VVHPSAMPPEEVRSVDGRDLAgADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTG 519
Cdd:cd18003    80 TYYGSAKERKLKRQGWMKPNS-FHVCITSYQLVVQdHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2771685888 520 TPVENRLSDLWSIFDFTHPGLLGSEKAFAA-LSRRL-----GESGHFAP----LKKLVQPYILRR 574
Cdd:cd18003   159 TPLQNSLMELWSLMHFLMPHIFQSHQEFKEwFSNPLtamseGSQEENEElvrrLHKVLRPFLLRR 223
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
362-576 1.31e-30

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: 120.55  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 362 TLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLL--ILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd17996     3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITylMEKKKNNG-PYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVVHPsamPPEEVRSVDGRDLAGA-DLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKG-LTAQARIA 516
Cdd:cd17996    82 IVYKG---TPDVRKKLQSQIRAGKfNVLLTTYEYIIKdKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2771685888 517 LTGTPVENRLSDLWSIFDFTHPGLLGS----EKAFAALSRRLGESGHFA-----------PLKKLVQPYILRRLK 576
Cdd:cd17996   159 LTGTPLQNNLPELWALLNFLLPKIFKScktfEQWFNTPFANTGEQVKIElneeetlliirRLHKVLRPFLLRRLK 233
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
363-574 2.57e-30

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: 119.28  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLA-LLLILQRESPGHPSLLVAPASLLANWQAQAERFApTLRVLV 441
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAfLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEVRSVD-------GRDLAGA---DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLT 510
Cdd:cd17995    80 YHGSGESRQIIQQYEmyfkdaqGRKKKGVykfDVLITTYEMVIADaEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 511 AQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
353-576 4.60e-30

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: 118.97  E-value: 4.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 353 VDPGPALHATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALL--LILQRESPGhPSLLVAPASLLANWQAQA 430
Cdd:cd18065     6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLgyLKHYRNIPG-PHMVLVPKSTLHNWMNEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 431 ERFAPTLRVLVVhpsaMPPEEVRSVDGRD--LAGA-DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAV 506
Cdd:cd18065    85 KRWVPSLRAVCL----IGDKDARAAFIRDvmMPGEwDVCVTSYEMVIKEkSVFKKFNWRYLVIDEAHRIKNEKSKLSEIV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2771685888 507 KGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAA---LSRRLGESGHFAPLKKLVQPYILRRLK 576
Cdd:cd18065   161 REFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
363-538 2.46e-29

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: 115.18  E-value: 2.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVV 442
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 443 HPSAMPPEEVRSVDGRDLAGADLVVTTYGMLLKQP----VLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALT 518
Cdd:cd17998    81 YGSQEERKHLRYDILKGLEDFDVIVTTYNLATSNPddrsFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160
                         170       180
                  ....*....|....*....|
gi 2771685888 519 GTPVENRLSDLWSIFDFTHP 538
Cdd:cd17998   161 GTPLQNNLLELMSLLNFIMP 180
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
362-574 2.78e-29

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: 116.30  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 362 TLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLA--LLLILQRESPGhPSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISflSYLFHSQQQYG-PFLVVVPLSTMPAWQREFAKWAPDMNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVVHPSAMPPEEVR----SVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQAR 514
Cdd:cd17993    80 IVYLGDIKSRDTIReyefYFSQTKKLKFNVLLTTYEIILKdKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 515 IALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGhFAPLKKLVQPYILRR 574
Cdd:cd17993   160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
365-574 2.35e-28

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: 114.10  E-value: 2.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 365 PYQQAGVRWLYLLTR--------LGLGGCLADDMGLGKTIQLLALLLIlqrespgHPSLLVAPASLLANWQAQ-AERFAP 435
Cdd:cd18071    24 FWEEAVGLFLNTITNfsqkkrpeLVRGGILADDMGLGKTLTTISLILA-------NFTLIVCPLSVLSNWETQfEEHVKP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 436 -TLRVLVVHPSAmppeevRSVDGRDLAGADLVVTTYGMLLKQ------PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKG 508
Cdd:cd18071    97 gQLKVYTYHGGE------RNRDPKLLSKYDIVLTTYNTLASDfgakgdSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLN 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2771685888 509 LTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRR---LGESGHFAPLKKLVQPYILRR 574
Cdd:cd18071   171 LSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRpltMGDPTGLKRLQVLMKQITLRR 239
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
363-574 3.33e-27

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: 110.84  E-value: 3.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLY--LLTRLGLG--GC-LADDMGLGKTIQLLALLLILQRESPG-----HPSLLVAPASLLANWQAQAER 432
Cdd:cd18004     1 LRPHQREGVQFLYdcLTGRRGYGggGAiLADEMGLGKTLQAIALVWTLLKQGPYgkptaKKALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 433 FAPTLRVLVVHPSAMPPEEVRSVDGRDLAGA-DLVVTTYGMLLKQPVLAGQDWRI--LAIDEAQAIKNPGAKQTRAVKGL 509
Cdd:cd18004    81 WLGLRRIKVVTADGNAKDVKASLDFFSSASTyPVLIISYETLRRHAEKLSKKISIdlLICDEGHRLKNSESKTTKALNSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 510 TAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAAL----------------SRRLGESGHfAPLKKLVQPYILR 573
Cdd:cd18004   161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVfeepilrsrdpdaseeDKELGAERS-QELSELTSRFILR 239

                  .
gi 2771685888 574 R 574
Cdd:cd18004   240 R 240
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
363-574 2.77e-26

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: 107.98  E-value: 2.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLL-ILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLV 441
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAhLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEVRSV-DGRDLAGAD----LVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARI 515
Cdd:cd18002    81 YWGNPKDRKVLRKFwDRKNLYTRDapfhVVITSYQLVvQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2771685888 516 ALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGES----------GHFAPLKKLVQPYILRR 574
Cdd:cd18002   161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEShaenktglneHQLKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
363-574 1.08e-25

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: 106.63  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGH-PSLLVAPASLLANWQAQAERFAPTLRVLV 441
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYgPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEVRSVDGRDLAGADL----VVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:cd18054   101 YIGDLMSRNTIREYEWIHSQTKRLkfnaLITTYEILLKdKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2771685888 517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGhFAPLKKLVQPYILRR 574
Cdd:cd18054   181 ITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-YQSLHKVLEPFLLRR 237
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
363-574 5.69e-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: 100.90  E-value: 5.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLyLLTRLGLGGC-LADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFApTLRVLV 441
Cdd:cd18060     1 LREYQLEGVNWL-LFNWYNRQNCiLADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEVRSVD-------GRDLAGA---DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLT 510
Cdd:cd18060    79 YHGSLASRQMIQQYEmyckdsrGRLIPGAykfDALITTFEMILSDcPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 511 AQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
363-574 7.30e-24

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: 101.08  E-value: 7.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLY-----LLTRLGLGGCLADDMGLGKTIQLLALLLILQRESP--GHP----SLLVAPASLLANWQAQAE 431
Cdd:cd18066     1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPygGKPvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 432 RFAPTLRVLVVHPSAMPPEEvrsvdgrDLAGADL---VVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVK 507
Cdd:cd18066    81 KWLGSERIKVFTVDQDHKVE-------EFIASPLysvLIISYEMLLRSlDQISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 508 GLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAAL----------------SRRLGESgHFAPLKKLVQPYI 571
Cdd:cd18066   154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVyeepivrsreptatpeEKKLGEA-RAAELTRLTGLFI 232

                  ...
gi 2771685888 572 LRR 574
Cdd:cd18066   233 LRR 235
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
363-574 1.13e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 100.08  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLyLLTRLGLGGC-LADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAeRFAPTLRVLV 441
Cdd:cd18061     1 LREYQLEGLNWL-LFNWYNRRNCiLADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEV-------RSVDGRDLAGA---DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLT 510
Cdd:cd18061    79 YHGSLISRQMIqqyemyfRDSQGRIIRGAyrfQAIITTFEMILGGcPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 511 AQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
363-574 1.13e-23

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: 100.11  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLyLLTRLGLGGC-LADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAeRFAPTLRVLV 441
Cdd:cd18059     1 LREYQLEGVNWL-LFNWYNTRNCiLADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREF-RTWTELNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEV-------RSVDGRDLAGA---DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLT 510
Cdd:cd18059    79 YHGSQASRRTIqlyemyfKDPQGRVIKGSykfHAIITTFEMILTDcPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 511 AQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
363-574 1.54e-23

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: 99.73  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLyLLTRLGLGGC-LADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAeRFAPTLRVLV 441
Cdd:cd18058     1 LREYQLEGMNWL-LFNWYNRKNCiLADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREF-RTWTEMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEV-------RSVDGRDLAGA---DLVVTTYGMLLKQ-PVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLT 510
Cdd:cd18058    79 YHGSQISRQMIqqyemyyRDEQGNPLSGIfkfQVVITTFEMILADcPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 511 AQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
352-576 1.97e-23

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: 100.52  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 352 RVDPGPAL--HATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLL-ILQRESPGHPSLLVAPASLLANWQA 428
Cdd:cd18063    11 RVEKQSSLliNGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 429 QAERFAPTlrVLVVHPSAMPPEEVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVK 507
Cdd:cd18063    91 EFDKWAPS--VVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKdKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 508 G-LTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGS----EKAFAALSRRLGESGHFAP---------LKKLVQPYILR 573
Cdd:cd18063   169 ThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGERVDLNEeetiliirrLHKVLRPFLLR 248

                  ...
gi 2771685888 574 RLK 576
Cdd:cd18063   249 RLK 251
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
657-771 2.16e-23

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 95.36  E-value: 2.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 657 GKFARLKELaeVIAIRQEKMLLFTQFRETAEplRAFLGGIFGRQGLVLHGGTPVKQRRELVRRFQEDEQtpFFILSLKAG 736
Cdd:pfam00271   1 EKLEALLEL--LKKERGGKVLIFSQTKKTLE--AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKI--DVLVATDVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2771685888 737 GAGLNLTAARHVIHFDRWWNPAVEDQATDRAFRIG 771
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
363-535 2.87e-23

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: 99.48  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTR-LGLGGCLADDMGLGKT-------------------IQLLALLLILQRES----PGHPSLLVA 418
Cdd:cd18072     1 LLLHQKQALAWLLWRERqKPRGGILADDMGLGKTltmialilaqkntqnrkeeEKEKALTEWESKKDstlvPSAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 419 PASLLANWQAQAERFAPT--LRVLVVH-PSamppeevRSVDGRDLAGADLVVTTYGMLLKQ----------PVLAGQDWR 485
Cdd:cd18072    81 PASLVHQWKNEVESRVASnkLRVCLYHgPN-------RERIGEVLRDYDIVITTYSLVAKEiptykeesrsSPLFRIAWA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2771685888 486 ILAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDF 535
Cdd:cd18072   154 RIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKF 203
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
363-549 4.28e-23

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: 98.05  E-value: 4.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWlylltrlGL---GGCL-ADDMGLGKTIQLLALLLILQREspgHPSLLVAPASLLANWQAQAERFAPTLr 438
Cdd:cd18010     1 LLPFQREGVCF-------ALrrgGRVLiADEMGLGKTVQAIAIAAYYREE---WPLLIVCPSSLRLTWADEIERWLPSL- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 439 vlvvhpsamPPEEVRSV----DGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQA 513
Cdd:cd18010    70 ---------PPDDIQVIvkskDGLRDGDAKVVIVSYDLLRRlEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRA 140
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2771685888 514 RIA--LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAA 549
Cdd:cd18010   141 KRVilLSGTPALSRPIELFTQLDALDPKLFGRFHDFGR 178
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
363-574 6.50e-23

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: 97.12  E-value: 6.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQREspGH---PSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKE--GHskgPFLVSAPLSTIINWEREFEMWAPDFYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVVHpsamppeevrsvdgrdlaGADLVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIALT 518
Cdd:cd17994    79 VTYV------------------GDHVLLTSYELIsIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLT 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2771685888 519 GTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd17994   141 GTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
352-576 3.40e-22

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: 96.65  E-value: 3.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 352 RVDPGPAL--HATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQR-ESPGHPSLLVAPASLLANWQA 428
Cdd:cd18062    11 KVEKQSSLlvNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRINGPFLIIVPLSTLSNWVY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 429 QAERFAPTlrVLVVHPSAMPPEEVRSVDGRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVK 507
Cdd:cd18062    91 EFDKWAPS--VVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKdKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 508 G-LTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGS----EKAFAALSRRLGESGHFAP---------LKKLVQPYILR 573
Cdd:cd18062   169 ThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKVDLNEeetiliirrLHKVLRPFLLR 248

                  ...
gi 2771685888 574 RLK 576
Cdd:cd18062   249 RLK 251
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
363-574 7.99e-22

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: 95.12  E-value: 7.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGH-PSLLVAPASLLANWQAQAERFAPTLRVLV 441
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYgPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMPPEEVRSVD----GRDLAGADLVVTTYGMLLK-QPVLAGQDWRILAIDEAQAIKNPGAKQTRAVKGLTAQARIA 516
Cdd:cd18053   101 YLGDINSRNMIRTHEwmhpQTKRLKFNILLTTYEILLKdKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2771685888 517 LTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGhFAPLKKLVQPYILRR 574
Cdd:cd18053   181 ITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG-YASLHKELEPFLLRR 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
363-573 2.01e-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: 2.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLylltrLGLGGCLADDMGLGKT----------------IQLLALLLILQRESPGH----------PSLL 416
Cdd:cd18070     1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTvevlalillhprpdndLDAADDDSDEMVCCPDClvaetpvsskATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 417 VAPASLLANWQAQAERFAPT-LRVLV---VHPSAMPPEEVRSvdgrDLAGADLVVTTY---------------------- 470
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSsLKVLTyqgVKKDGALASPAPE----ILAEYDIVVTTYdvlrtelhyaeanrsnrrrrrq 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 471 --GMLLKQPVLAGQDWRILaIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDF--THPGLLGSEKA 546
Cdd:cd18070   152 krYEAPPSPLVLVEWWRVC-LDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFlgVEPFCDSDWWA 230
                         250       260
                  ....*....|....*....|....*..
gi 2771685888 547 FaALSRRLGESGHFAPLKKLVQPYILR 573
Cdd:cd18070   231 R-VLIRPQGRNKAREPLAALLKELLWR 256
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
363-574 2.14e-21

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: 93.98  E-value: 2.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQREspGH---PSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKE--GHskgPFLVSAPLSTIINWEREFEMWAPDMYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVV----HPSAMPPEEVRSVDGRDLAGAD--------------LVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGA 500
Cdd:cd18056    79 VTYvgdkDSRAIIRENEFSFEDNAIRGGKkasrmkkeasvkfhVLLTSYELItIDMAILGSIDWACLIVDEAHRLKNNQS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 501 KQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18056   159 KFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
363-547 2.30e-20

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: 90.64  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLY-----LLTRL----GLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERF 433
Cdd:cd18069     1 LKPHQIGGIRFLYdniieSLERYkgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 434 APTlrvlvvhPSAMPPEEVRSVDGRDL--------AGADLV---VTTYGMLLK-------QPvlaGQDwrILAIDEAQAI 495
Cdd:cd18069    81 LPP-------PEALPNVRPRPFKVFILndehkttaARAKVIedwVKDGGVLLMgyemfrlRP---GPD--VVICDEGHRI 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2771685888 496 KNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAF 547
Cdd:cd18069   149 KNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEF 200
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
363-574 2.51e-20

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: 90.89  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQREspGH---PSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKE--GHskgPYLVSAPLSTIINWEREFEMWAPDFYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVV-----HPSAMPPEEVRSVDGRDLAGAD-------------LVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGA 500
Cdd:cd18057    79 VTYtgdkeSRSVIRENEFSFEDNAIRSGKKvfrmkkeaqikfhVLLTSYELItIDQAILGSIEWACLVVDEAHRLKNNQS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 501 KQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18057   159 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXDc smart00487
DEAD-like helicases superfamily;
362-539 4.90e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 89.09  E-value: 4.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  362 TLRPYQQAGVRWLYLLTRlglGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAP-ASLLANWQAQAERFAP--TLR 438
Cdd:smart00487   8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPslGLK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  439 VLVVHPSAMPPEEVRSVDGRDlagADLVVTTYGML---LKQPVLAGQDWRILAIDEAQAIKNPGAK-QTRAVKGLTAQA- 513
Cdd:smart00487  85 VVGLYGGDSKREQLRKLESGK---TDILVTTPGRLldlLENDKLSLSNVDLVILDEAHRLLDGGFGdQLEKLLKLLPKNv 161
                          170       180       190
                   ....*....|....*....|....*....|
gi 2771685888  514 -RIALTGTP---VENRLSDLWSIFDFTHPG 539
Cdd:smart00487 162 qLLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
363-574 1.35e-18

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: 85.83  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQREspGH---PSLLVAPASLLANWQAQAERFAPTLRV 439
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKE--GHtkgPFLVSAPLSTIINWEREFQMWAPDFYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 440 LVV----HPSAMPPEEVRSVDGRDLAGAD--------------LVVTTYGML-LKQPVLAGQDWRILAIDEAQAIKNPGA 500
Cdd:cd18055    79 VTYtgdkDSRAIIRENEFSFDDNAVKGGKkafkmkreaqvkfhVLLTSYELVtIDQAALGSIRWACLVVDEAHRLKNNQS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2771685888 501 KQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRR 574
Cdd:cd18055   159 KFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
363-574 9.49e-18

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: 83.67  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLT----RLGLGGC-LADDMGLGKTIQLLALLLILQRESP-GHP----SLLVAPASLLANWQAQAER 432
Cdd:cd18067     1 LRPHQREGVKFLYRCVtgrrIRGSHGCiMADEMGLGKTLQCITLMWTLLRQSPqCKPeidkAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 433 F-APTLRVLVVHPSAMPPEEVR-----SVDGRDLAGADLVVTTYGMLLKQPVLAGQDWRILAIDEAQAIKNPGAKQTRAV 506
Cdd:cd18067    81 WlGGRLQPLAIDGGSKKEIDRKlvqwaSQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 507 KGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAF-------------AALS---RRLGESgHFAPLKKLVQPY 570
Cdd:cd18067   161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFkknfelpilkgrdADASekeRQLGEE-KLQELISIVNRC 239

                  ....
gi 2771685888 571 ILRR 574
Cdd:cd18067   240 IIRR 243
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
363-547 3.34e-17

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: 81.95  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLY------LLTRLGLGGC-LADDMGLGKTIQLLALLLILQRESPG--HPsLLVAPASLLANWQAQAERF 433
Cdd:cd18007     1 LKPHQVEGVRFLWsnlvgtDVGSDEGGGCiLAHTMGLGKTLQVITFLHTYLAAAPRrsRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 434 AP--TLRVLVVHPSAMPPEEVRSVD---------GRDLAGADLVVTTYGMLLKQPVLAGQDWR--------ILAIDEAQA 494
Cdd:cd18007    80 LPpdLRPLLVLVSLSASKRADARLRkinkwhkegGVLLIGYELFRNLASNATTDPRLKQEFIAalldpgpdLLVLDEGHR 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2771685888 495 IKNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAF 547
Cdd:cd18007   160 LKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
HELICc smart00490
helicase superfamily c-terminal domain;
702-771 3.69e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 76.87  E-value: 3.69e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  702 LVLHGGTPVKQRRELVRRFQEDEQTpfFILSLKAGGAGLNLTAARHVIHFDRWWNPAVEDQATDRAFRIG 771
Cdd:smart00490  15 ARLHGGLSQEEREEILDKFNNGKIK--VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
363-531 3.17e-13

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 69.69  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLylLTRLGlgGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLAN-WQAQAERFAptlrvlv 441
Cdd:cd18013     1 PHPYQKVAINFI--IEHPY--CGLFLDMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWN------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 vHPSAMppeEVRSVDGRDL-------AGADLVVTTYGMLLKQPVLAGQDW--RILAIDEAQAIKNPGAKQTRAVKGLTAQ 512
Cdd:cd18013    70 -HLRNL---TVSVAVGTERqrskaanTPADLYVINRENLKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALRKVRPV 145
                         170       180
                  ....*....|....*....|.
gi 2771685888 513 AR--IALTGTPVENRLSDLWS 531
Cdd:cd18013   146 IKrlIGLTGTPSPNGLMDLWA 166
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
363-574 9.81e-12

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: 65.00  E-value: 9.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLYLLTRLGLggCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQ-AERFAptLRVLV 441
Cdd:cd18011     1 PLPHQIDAVLRALRKPPVRL--LLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDElQDKFG--LPFLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 442 VHPSAMppEEVRSVDGRDLAGADLVVTTYGML----LKQPVLAGQDWRILAIDEAQAIKN-PGAKQT---RAVKGLTAQA 513
Cdd:cd18011    77 LDRETA--AQLRRLIGNPFEEFPIVIVSLDLLkrseERRGLLLSEEWDLVVVDEAHKLRNsGGGKETkryKLGRLLAKRA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2771685888 514 R--IALTGTPVENRLSDLWSIFDFTHPGllgsekAFAALSRRLGESGHFAPLKKLVqpyiLRR 574
Cdd:cd18011   155 RhvLLLTATPHNGKEEDFRALLSLLDPG------RFAVLGRFLRLDGLREVLAKVL----LRR 207
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
363-548 4.24e-09

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: 57.98  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 363 LRPYQQAGVRWLY---------LLTRLGLGGCLADDMGLGKTIQLLALLLIL---QRESPGHPSLLVAPASLLANWQAQA 430
Cdd:cd18068     1 LKPHQVDGVQFMWdccceslkkTKKSPGSGCILAHCMGLGKTLQVVTFLHTVllcEKLENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 431 ERF------APTLRVLVVHPSAMPPEEVRSV-----DG----------RDLAGADLVVTTYGM---LLKQPVLAGQDwrI 486
Cdd:cd18068    81 EKWqeglkdEEKIEVNELATYKRPQERSYKLqrwqeEGgvmiigydmyRILAQERNVKSREKLkeiFNKALVDPGPD--F 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2771685888 487 LAIDEAQAIKNPGAKQTRAVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFA 548
Cdd:cd18068   159 VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFR 220
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
336-749 5.31e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.65  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 336 WLAETLRHLRSPEGLARVDPGPALHATLRPYQQAGV-RWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRespGHPS 414
Cdd:COG1061    54 PEEDTERELAEAEALEAGDEASGTSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLR---GKRV 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 415 LLVAP-ASLLANWQAQAERFAPtlrvlvvhpsamppeEVRSVDGRDLAGADLVVTTYGMLLKQPVLA--GQDWRILAIDE 491
Cdd:COG1061   131 LVLVPrRELLEQWAEELRRFLG---------------DPLAGGGKKDSDAPITVATYQSLARRAHLDelGDRFGLVIIDE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 492 AQAIknpGAKQTRAV-KGLTAQARIALTGTPVenRLSDLWsIFDFTHPGLlgsekAFAALSRRLGESGHFAPLKklvqpY 570
Cdd:COG1061   196 AHHA---GAPSYRRIlEAFPAAYRLGLTATPF--RSDGRE-ILLFLFDGI-----VYEYSLKEAIEDGYLAPPE-----Y 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 571 IlrrlktdkAVIADLPDKtemaawcaltpvqavlyQRAVKELAQRLERAegidrrglvLAflmrfkqicnhpsqwlgdgl 650
Cdd:COG1061   260 Y--------GIRVDLTDE-----------------RAEYDALSERLREA---------LA-------------------- 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 651 wrPADSGKFARLKELAEVIAiRQEKMLLFTQFRETAEplraFLGGIFGRQGL---VLHGGTPVKQRRELVRRFQEDEQTp 727
Cdd:COG1061   286 --ADAERKDKILRELLREHP-DDRKTLVFCSSVDHAE----ALAELLNEAGIraaVVTGDTPKKEREEILEAFRDGELR- 357
                         410       420
                  ....*....|....*....|..
gi 2771685888 728 fFILSLKAGGAGLNLTAARHVI 749
Cdd:COG1061   358 -ILVTVDVLNEGVDVPRLDVAI 378
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
729-774 5.73e-05

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: 41.92  E-value: 5.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2771685888 729 FILSLKAGGAGLNLTAARHVIHFDRWWNPAVEDQATDRAFRIGQKY 774
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
COG3903 COG3903
Predicted ATPase [General function prediction only];
48-463 1.90e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.01  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  48 DAPPFAGAENLSVERLEALWNEIHAALRAALAKGETLAGFLAARHSAWHVVGRVHFNLAENRKDPAAPFAFLATYVSGLS 127
Cdd:COG3903   506 AAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAA 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 128 AYGRPQHLPLSQALAEFAGVRRRAQLLSLLEPVQRAAEGCPWLDEMVQSGEMYHPLRWQPQDAWRFLQDVPRLEAAGIVV 207
Cdd:COG3903   586 AALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 208 RMPPSWAGGRPARPKVSASVGCEPASRVGLEALLDFEAAITLDGEKLHREEIERLLSRTDGLQLLRGRWVEVDRKRLTKM 287
Cdd:COG3903   666 LAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAAL 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 288 LDRFAEIERRARAGGLSFAEAMRLTAGMEAGAEGGILERDWADVAAGPWLAETLRHLRSPEGLARVDPGPALHATLRPYQ 367
Cdd:COG3903   746 ALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAA 825
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 368 QAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPASLLANWQAQAERFAPTLRVLVVHPSAM 447
Cdd:COG3903   826 AAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAAL 905
                         410
                  ....*....|....*.
gi 2771685888 448 PPEEVRSVDGRDLAGA 463
Cdd:COG3903   906 AAAAAAAAAAALAAAA 921
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
185-704 4.71e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  185 WQPQDAWRFLQDVPRLEAAGIVVRMPPSWAGGRPARPKVSASVGCEPASRVGLEALLDFEAAITLDGEKLHREEIERLLS 264
Cdd:COG3321    868 FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAA 947
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  265 RTDGLQLLRGRWVEVDRKRLTKMLDRFAEIERRARAGGLSFAEAMRLTAGMEAGAEGGILERDWADVAAGPWLAETLRHL 344
Cdd:COG3321    948 AAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAAL 1027
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  345 RSPEGLARVDPGPALHATLRPYQQAGVRWLYLLTRLGLGGCLADDMGLGKTIQLLALLLILQRESPGHPSLLVAPAsLLA 424
Cdd:COG3321   1028 LAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA-AAL 1106
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  425 NWQAQAERFAPTLRVLVVHPSAMPPEEVRSVDGRDLAGADLVVTTYGMLLKQPVLAGQDWRILAIDEAQAIKNPGAKQTR 504
Cdd:COG3321   1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  505 AVKGLTAQARIALTGTPVENRLSDLWSIFDFTHPGLLGSEKAFAALSRRLGESGHFAPLKKLVQPYILRRLKTDKAVIAD 584
Cdd:COG3321   1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLA 1266
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888  585 LPDKTEMAAWCALTPVQAVLYQRAVKELAQRLERAEGIDRRglvLAFLMRFKQICNHPSQWLGDGLWRPADSGKFARLKE 664
Cdd:COG3321   1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAA---AAAAAAAAAAAAALAAALLAAALAALAAAVAAALAL 1343
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2771685888  665 LAEVIAIRQEKMLLFTQFRETAEPLRAFLGGIFGRQGLVL 704
Cdd:COG3321   1344 AAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
658-752 2.87e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 41.25  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2771685888 658 KFARLKE-LAEVIAIRQ-EKMLLFTQFRETAEPLRAFLG------GIF-------GRQGLVlhggtpVKQRRELVRRFQE 722
Cdd:COG1111   336 KLSKLREiLKEQLGTNPdSRIIVFTQYRDTAEMIVEFLSepgikaGRFvgqaskeGDKGLT------QKEQIEILERFRA 409
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2771685888 723 DEqtpFFIL-SLKAGGAGLNLTAARHVIHFD 752
Cdd:COG1111   410 GE---FNVLvATSVAEEGLDIPEVDLVIFYE 437
 
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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