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Conserved domains on  [gi|1366038577|ref|XP_024170415|]
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DNA annealing helicase and endonuclease ZRANB3 isoform X2 [Rosa chinensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
206-430 1.29e-82

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: 269.07  E-value: 1.29e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPADIHLVFGh 285
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  286 eNNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARKVKRIVLLSGTPSLSR 365
Cdd:cd18010     80 -SKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYL----KNSKAKRTKAALPLLKRAKRVILLSGTPALSR 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577  366 PFDIFHQIDMLWPGLLGRDKFkFGETYCDAKyvrgvQGKVFQDFSKGTRLEELNMLLTRTVMIRR 430
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFHD-FGRRYCAAK-----QGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
182-646 2.42e-76

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 267.48  E-value: 2.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  182 RPEHLLDDKVDELIGKLPKRLLDSLLPFQLEGVRF--GLQR-GGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVC 255
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWllFLRRlGLGGLLADDMGLGKTIQALALLLELKERGLarpVLIVA 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  256 PAILRYSWAEELEHWLPfCLPADIHlvFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctk 333
Cdd:COG0553    298 PTSLVGNWQRELAKFAP-GLRVLVL--DGTRERAKGANPFEDadLVITSYGLLRRDIELLAAVDWDLVILDEAQHI---- 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  334 KKSEPREIKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGrDKFKFGETYCDAKYVRGVQgkvfqdfskgt 413
Cdd:COG0553    371 KNPATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLG-SLKAFRERFARPIEKGDEE----------- 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  414 RLEELNMLLtRTVMIRRLKEHVLSQLPPKRRQIIQVVLKKsdivsAKAAIRvgkshdEDVSSEHLDELNDSMGcciskqL 493
Cdd:COG0553    437 ALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYVELTP-----EQRALY------EAVLEYLRRELEGAEG------I 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  494 SHQELGIAKLAGFREwLSIHPVIAEADGV------AKL--------ESDSSSHKMLIFAHHHKVLDGVQEFIIHKEIDFV 559
Cdd:COG0553    499 RRRGLILAALTRLRQ-ICSHPALLLEEGAelsgrsAKLeallelleELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYA 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  560 RIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFS 639
Cdd:COG0553    578 YLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLV 657

                   ....*..
gi 1366038577  640 GKDTIDE 646
Cdd:COG0553    658 AEGTIEE 664
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1131-1163 5.59e-03

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


:

Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 36.50  E-value: 5.59e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1366038577 1131 GNAWHADHLVPVYLGGGEcRLENMRTLCVACHS 1163
Cdd:COG1403     31 GDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
206-430 1.29e-82

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: 269.07  E-value: 1.29e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPADIHLVFGh 285
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  286 eNNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARKVKRIVLLSGTPSLSR 365
Cdd:cd18010     80 -SKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYL----KNSKAKRTKAALPLLKRAKRVILLSGTPALSR 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577  366 PFDIFHQIDMLWPGLLGRDKFkFGETYCDAKyvrgvQGKVFQDFSKGTRLEELNMLLTRTVMIRR 430
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFHD-FGRRYCAAK-----QGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
182-646 2.42e-76

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 267.48  E-value: 2.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  182 RPEHLLDDKVDELIGKLPKRLLDSLLPFQLEGVRF--GLQR-GGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVC 255
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWllFLRRlGLGGLLADDMGLGKTIQALALLLELKERGLarpVLIVA 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  256 PAILRYSWAEELEHWLPfCLPADIHlvFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctk 333
Cdd:COG0553    298 PTSLVGNWQRELAKFAP-GLRVLVL--DGTRERAKGANPFEDadLVITSYGLLRRDIELLAAVDWDLVILDEAQHI---- 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  334 KKSEPREIKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGrDKFKFGETYCDAKYVRGVQgkvfqdfskgt 413
Cdd:COG0553    371 KNPATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLG-SLKAFRERFARPIEKGDEE----------- 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  414 RLEELNMLLtRTVMIRRLKEHVLSQLPPKRRQIIQVVLKKsdivsAKAAIRvgkshdEDVSSEHLDELNDSMGcciskqL 493
Cdd:COG0553    437 ALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYVELTP-----EQRALY------EAVLEYLRRELEGAEG------I 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  494 SHQELGIAKLAGFREwLSIHPVIAEADGV------AKL--------ESDSSSHKMLIFAHHHKVLDGVQEFIIHKEIDFV 559
Cdd:COG0553    499 RRRGLILAALTRLRQ-ICSHPALLLEEGAelsgrsAKLeallelleELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYA 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  560 RIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFS 639
Cdd:COG0553    578 YLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLV 657

                   ....*..
gi 1366038577  640 GKDTIDE 646
Cdd:COG0553    658 AEGTIEE 664
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
529-638 9.78e-36

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: 132.22  E-value: 9.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  529 SSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFL 608
Cdd:cd18793     25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILY 104
                           90       100       110
                   ....*....|....*....|....*....|
gi 1366038577  609 ELPQSPSLMLQAEDRAHRRGQTNAVNIYFF 638
Cdd:cd18793    105 DPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
210-449 5.25e-25

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: 106.61  E-value: 5.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  210 QLEGVRF------GLQRGgrCLIADEMGLGKTLQAIAI-----ACCFMSEGSILVVCPAILRYSWAEELEHWL-PFCLPA 277
Cdd:pfam00176    2 QIEGVNWmlslenNLGRG--GILADEMGLGKTLQTISLllylkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVsPPALRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  278 DIHlvFGHENNPANLKKWPR------VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLDVarKV 351
Cdd:pfam00176   80 VVL--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  352 KRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-----RDKF--KFGETYCDAKYVRgvqgkvfqdfskgtrleeLNMLLTR 424
Cdd:pfam00176  152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGslstfRNWFdrPIERGGGKKGVSR------------------LHKLLKP 213
                          250       260
                   ....*....|....*....|....*
gi 1366038577  425 TvMIRRLKEHVLSQLPPKRRQIIQV 449
Cdd:pfam00176  214 F-LLRRTKKDVEKSLPPKVEYILFC 237
DEXDc smart00487
DEAD-like helicases superfamily;
198-362 9.87e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.56  E-value: 9.87e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   198 LPKRLLDSLLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVCP-AILRYSWAEELEHWLPF 273
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggrVLVLVPtRELAEQWAEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   274 cLPADIHLVFGHENNPANLKKW----PRVVVISY-TMLHHLQKSMLD-REWALLIVDESHHvrcTKKKSEPREIKAVLDV 347
Cdd:smart00487   81 -LGLKVVGLYGGDSKREQLRKLesgkTDILVTTPgRLLDLLENDKLSlSNVDLVILDEAHR---LLDGGFGDQLEKLLKL 156
                           170
                    ....*....|....*
gi 1366038577   348 ARKVKRIVLLSGTPS 362
Cdd:smart00487  157 LPKNVQLLLLSATPP 171
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
225-646 9.66e-22

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 102.57  E-value: 9.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIACcFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANLKKWP--- 296
Cdd:PLN03142   192 ILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFH---GNPEERAHQREELlva 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  297 ---RVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKRIvLLSGTPSLSRPFDIFHQ 372
Cdd:PLN03142   268 gkfDVCVTSFEMAIK-EKTALKRfSWRYIIIDEAHRI-----KNENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWAL 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  373 IDMLWPGLLGrDKFKFGETYCDAKyvRGVQGKVFQDFSKgtrleelnmlLTRTVMIRRLKEHVLSQLPPKRRQIIQVVLK 452
Cdd:PLN03142   341 LNFLLPEIFS-SAETFDEWFQISG--ENDQQEVVQQLHK----------VLRPFLLRRLKSDVEKGLPPKKETILKVGMS 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  453 KSDIVSAKAAIRvgksHDEDV---SSEHLDELNDSM---GCCiskqlSHQELGIAKLAGFREWLSIHPViaEADG----- 521
Cdd:PLN03142   408 QMQKQYYKALLQ----KDLDVvnaGGERKRLLNIAMqlrKCC-----NHPYLFQGAEPGPPYTTGEHLV--ENSGkmvll 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  522 ---VAKLESDSSshKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKF-QLSSEVKIAIVGITAGGVGL 597
Cdd:PLN03142   477 dklLPKLKERDS--RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLLSTRAGGLGI 554
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1366038577  598 DFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFSGKDTIDE 646
Cdd:PLN03142   555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
522-628 1.09e-17

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 79.95  E-value: 1.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  522 VAKLESDSSSHKMLIFAHHHKVLDgVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSS 601
Cdd:pfam00271    6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPD 82
                           90       100
                   ....*....|....*....|....*..
gi 1366038577  602 ATHVVFLELPQSPSLMLQAEDRAHRRG 628
Cdd:pfam00271   83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
547-628 2.41e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.16  E-value: 2.41e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   547 VQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHR 626
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 1366038577   627 RG 628
Cdd:smart00490   81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
205-627 5.55e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 76.60  E-value: 5.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQLEGV----RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAI-LRYSWAEELEHWLPfclpaDI 279
Cdd:COG1061     80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRReLLEQWAEELRRFLG-----DP 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  280 HLVFGHENNPAnlkkwpRVVVISY-TMLHHLQKSMLDREWALLIVDESHHVRctkkksePREIKAVLDvARKVKRIVLLS 358
Cdd:COG1061    155 LAGGGKKDSDA------PITVATYqSLARRAHLDELGDRFGLVIIDEAHHAG-------APSYRRILE-AFPAAYRLGLT 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  359 GTP--SLSRPFDIFHQIdmlwpgllgrdkfkfgetycdakyvrgvqGKVFqdfskGTRLEELnmlltrtvmirrLKEHVL 436
Cdd:COG1061    221 ATPfrSDGREILLFLFD-----------------------------GIVY-----EYSLKEA------------IEDGYL 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  437 SqlpPKRRQIIQVVLKKsdivsakaairvgKSHDEDVSSEHLDelndsmgccisKQLSHQElgIAKLAGFREWLSIHPvi 516
Cdd:COG1061    255 A---PPEYYGIRVDLTD-------------ERAEYDALSERLR-----------EALAADA--ERKDKILRELLREHP-- 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  517 aeadgvaklesdsSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVG 596
Cdd:COG1061    304 -------------DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR-DGELRI-LVTVDVLNEG 368
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1366038577  597 LDFSSATHVVFLELPQSPSLMLQAEDRAHRR 627
Cdd:COG1061    369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRP 399
DpdE NF041062
protein DpdE;
223-366 2.42e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 61.91  E-value: 2.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  223 RCLIADEMGLGKTLQA-IAIACCFM--SEGSILVVCPAILRYSWAEELE---HWLPFcLPADIHLVfGHEnNPANLKKWP 296
Cdd:NF041062   172 RYLLADEVGLGKTIEAgLVIRQHLLdnPDARVLVLVPDALVRQWRRELRdkfFLDDF-PGARVRVL-SHE-EPERWEPLL 248
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577  297 RVVvisytmlhhlqksmldrewALLIVDESHHVRCTKKKSEPREI---KAVLDVARKVKRIVLLSGTPSLSRP 366
Cdd:NF041062   249 DAP-------------------DLLVVDEAHQLARLAWSGDPPERaryRELAALAHAAPRLLLLSATPVLGNE 302
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
205-361 1.38e-06

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 52.92  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQL----E-GVRFGlqrgGRCLIADEMGLGKTLQAiaiaccfmseGSI-------------LVVCPAILRYSWAEE 266
Cdd:PRK04914   152 SLIPHQLyiahEvGRRHA----PRVLLADEVGLGKTIEA----------GMIihqqlltgraervLILVPETLQHQWLVE 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  267 L--EHWLPFCL-----PADIhlvFGHENNP---ANLkkwprvVVISYTML---HHLQKSMLDREWALLIVDESHHVRCTK 333
Cdd:PRK04914   218 MlrRFNLRFSLfdeerYAEA---QHDADNPfetEQL------VICSLDFLrrnKQRLEQALAAEWDLLVVDEAHHLVWSE 288
                          170       180
                   ....*....|....*....|....*...
gi 1366038577  334 KKSEpREIKAVLDVARKVKRIVLLSGTP 361
Cdd:PRK04914   289 EAPS-REYQVVEQLAEVIPGVLLLTATP 315
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1131-1163 5.59e-03

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 36.50  E-value: 5.59e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1366038577 1131 GNAWHADHLVPVYLGGGEcRLENMRTLCVACHS 1163
Cdd:COG1403     31 GDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
206-329 6.54e-03

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 40.94  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmsEGSILVVC-PAILRYSWAEELEHWlpfCLPADIHL- 281
Cdd:TIGR00603  256 IRPYQEKSLSkmFGNGRARSGIIVLPCGAGKSLVGVTAACTV--KKSCLVLCtSAVSVEQWKQQFKMW---STIDDSQIc 330
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577  282 VFGHENnpanlKKWPR----VVVISYTMLHHLQKS----------MLDREWALLIVDESHHV 329
Cdd:TIGR00603  331 RFTSDA-----KERFHgeagVVVSTYSMVAHTGKRsyesekvmewLTNREWGLILLDEVHVV 387
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1126-1166 7.24e-03

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 35.91  E-value: 7.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1366038577 1126 KDPTEGNAWHADHLVPVYlGGGECRLENMRTLCVACHSDVT 1166
Cdd:cd00085     18 GKPGGTEGLEVDHIIPLS-DGGNNDLDNLVLLCRKCHRKKH 57
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
206-430 1.29e-82

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: 269.07  E-value: 1.29e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPADIHLVFGh 285
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVK- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  286 eNNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARKVKRIVLLSGTPSLSR 365
Cdd:cd18010     80 -SKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYL----KNSKAKRTKAALPLLKRAKRVILLSGTPALSR 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577  366 PFDIFHQIDMLWPGLLGRDKFkFGETYCDAKyvrgvQGKVFQDFSKGTRLEELNMLLTRTVMIRR 430
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFHD-FGRRYCAAK-----QGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
182-646 2.42e-76

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 267.48  E-value: 2.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  182 RPEHLLDDKVDELIGKLPKRLLDSLLPFQLEGVRF--GLQR-GGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVC 255
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWllFLRRlGLGGLLADDMGLGKTIQALALLLELKERGLarpVLIVA 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  256 PAILRYSWAEELEHWLPfCLPADIHlvFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctk 333
Cdd:COG0553    298 PTSLVGNWQRELAKFAP-GLRVLVL--DGTRERAKGANPFEDadLVITSYGLLRRDIELLAAVDWDLVILDEAQHI---- 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  334 KKSEPREIKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGrDKFKFGETYCDAKYVRGVQgkvfqdfskgt 413
Cdd:COG0553    371 KNPATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLG-SLKAFRERFARPIEKGDEE----------- 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  414 RLEELNMLLtRTVMIRRLKEHVLSQLPPKRRQIIQVVLKKsdivsAKAAIRvgkshdEDVSSEHLDELNDSMGcciskqL 493
Cdd:COG0553    437 ALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYVELTP-----EQRALY------EAVLEYLRRELEGAEG------I 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  494 SHQELGIAKLAGFREwLSIHPVIAEADGV------AKL--------ESDSSSHKMLIFAHHHKVLDGVQEFIIHKEIDFV 559
Cdd:COG0553    499 RRRGLILAALTRLRQ-ICSHPALLLEEGAelsgrsAKLeallelleELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYA 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  560 RIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFS 639
Cdd:COG0553    578 YLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLV 657

                   ....*..
gi 1366038577  640 GKDTIDE 646
Cdd:COG0553    658 AEGTIEE 664
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
529-638 9.78e-36

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: 132.22  E-value: 9.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  529 SSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFL 608
Cdd:cd18793     25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILY 104
                           90       100       110
                   ....*....|....*....|....*....|
gi 1366038577  609 ELPQSPSLMLQAEDRAHRRGQTNAVNIYFF 638
Cdd:cd18793    105 DPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
206-378 2.90e-35

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: 132.69  E-value: 2.90e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQR---GGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPFCLPAD 278
Cdd:cd17919      1 LRPYQLEGLNFLLELyenGPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IHLVFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARkvKRIVL 356
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDKfdVVLTTYETLRRDKASLRKFRWDLVVVDEAHRL----KNPKSQLSKALKALRA--KRRLL 154
                          170       180
                   ....*....|....*....|..
gi 1366038577  357 LSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd17919    155 LTGTPLQNNLEELWALLDFLDP 176
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
206-385 8.45e-34

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: 129.33  E-value: 8.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRG-GRCLIADEMGLGKTLQAIAIACCFMSEG---SILVVCPAILRYSWAEELEH--WLPF--CLPA 277
Cdd:cd18011      1 PLPHQIDAVLRALRKPpVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWQDELQDkfGLPFliLDRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  278 DIHLVFGHENNPANLkkwPRVVVISYTMLH---HLQKSMLDREWALLIVDESHHVRCTKKKSEPREIKAVLDVARKVKRI 354
Cdd:cd18011     81 TAAQLRRLIGNPFEE---FPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLGRLLAKRARHV 157
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1366038577  355 VLLSGTPSLSRPFDIFHQIDMLWPGLLGRDK 385
Cdd:cd18011    158 LLLTATPHNGKEEDFRALLSLLDPGRFAVLG 188
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
210-449 5.25e-25

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: 106.61  E-value: 5.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  210 QLEGVRF------GLQRGgrCLIADEMGLGKTLQAIAI-----ACCFMSEGSILVVCPAILRYSWAEELEHWL-PFCLPA 277
Cdd:pfam00176    2 QIEGVNWmlslenNLGRG--GILADEMGLGKTLQTISLllylkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVsPPALRV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  278 DIHlvFGHENNPANLKKWPR------VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLDVarKV 351
Cdd:pfam00176   80 VVL--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  352 KRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-----RDKF--KFGETYCDAKYVRgvqgkvfqdfskgtrleeLNMLLTR 424
Cdd:pfam00176  152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGslstfRNWFdrPIERGGGKKGVSR------------------LHKLLKP 213
                          250       260
                   ....*....|....*....|....*
gi 1366038577  425 TvMIRRLKEHVLSQLPPKRRQIIQV 449
Cdd:pfam00176  214 F-LLRRTKKDVEKSLPPKVEYILFC 237
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
206-418 3.64e-24

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 102.75  E-value: 3.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF----------GLQRGGRCLIADEMGLGKTLQAI----AIACCFMSEGSILVVCPAILRYSWAEELEHWL 271
Cdd:cd18007      1 LKPHQVEGVRFlwsnlvgtdvGSDEGGGCILAHTMGLGKTLQVItflhTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  272 PFCLPAD---IHLVFGH--ENNPANLKKW---PRVVVISYTML-------------HHLQ-KSMLDREWALLIVDESHHV 329
Cdd:cd18007     81 PPDLRPLlvlVSLSASKraDARLRKINKWhkeGGVLLIGYELFrnlasnattdprlKQEFiAALLDPGPDLLVLDEGHRL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  330 RCTKKKsepreikaVLDVARKVK--RIVLLSGTPsLSRPFDIFHQ-IDMLWPGLLGR-DKFKfgetycdAKYVRGVQGKV 405
Cdd:cd18007    161 KNEKSQ--------LSKALSKVKtkRRILLTGTP-LQNNLKEYWTmVDFARPKYLGTlKEFK-------KKFVKPIEAGQ 224
                          250
                   ....*....|...
gi 1366038577  406 FQDFSKGTRLEEL 418
Cdd:cd18007    225 CVDSTEEDVRLML 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
206-432 5.65e-24

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: 101.49  E-value: 5.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFgLQR------GGrCLiADEMGLGKTLQAIAIACCFMSEGSI---LVVCPAILRYSWAEELEHWLPfclp 276
Cdd:cd18012      5 LRPYQKEGFNW-LSFlrhyglGG-IL-ADDMGLGKTLQTLALLLSRKEEGRKgpsLVVAPTSLIYNWEEEAAKFAP---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  277 aDIHLVFGHENNPANLKKWPR----VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarKVK 352
Cdd:cd18012     78 -ELKVLVIHGTKRKREKLRALedydLVITSYGLLRRDIELLKEVKFHYLVLDEAQNI----KNPQTKTAKAVKAL--KAD 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  353 RIVLLSGTP---SLSRPFDIFhqiDMLWPGLLG-RDKFKfgetycdAKYVRGVqgkvfQDFSKGTRLEELnMLLTRTVMI 428
Cdd:cd18012    151 HRLALTGTPienHLGELWSIF---DFLNPGLLGsYKRFK-------KRFAKPI-----EKDGDEEALEEL-KKLISPFIL 214

                   ....
gi 1366038577  429 RRLK 432
Cdd:cd18012    215 RRLK 218
DEXDc smart00487
DEAD-like helicases superfamily;
198-362 9.87e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.56  E-value: 9.87e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   198 LPKRLLDSLLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVCP-AILRYSWAEELEHWLPF 273
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggrVLVLVPtRELAEQWAEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   274 cLPADIHLVFGHENNPANLKKW----PRVVVISY-TMLHHLQKSMLD-REWALLIVDESHHvrcTKKKSEPREIKAVLDV 347
Cdd:smart00487   81 -LGLKVVGLYGGDSKREQLRKLesgkTDILVTTPgRLLDLLENDKLSlSNVDLVILDEAHR---LLDGGFGDQLEKLLKL 156
                           170
                    ....*....|....*
gi 1366038577   348 ARKVKRIVLLSGTPS 362
Cdd:smart00487  157 LPKNVQLLLLSATPP 171
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
225-646 9.66e-22

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 102.57  E-value: 9.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIACcFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANLKKWP--- 296
Cdd:PLN03142   192 ILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFH---GNPEERAHQREELlva 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  297 ---RVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKRIvLLSGTPSLSRPFDIFHQ 372
Cdd:PLN03142   268 gkfDVCVTSFEMAIK-EKTALKRfSWRYIIIDEAHRI-----KNENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWAL 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  373 IDMLWPGLLGrDKFKFGETYCDAKyvRGVQGKVFQDFSKgtrleelnmlLTRTVMIRRLKEHVLSQLPPKRRQIIQVVLK 452
Cdd:PLN03142   341 LNFLLPEIFS-SAETFDEWFQISG--ENDQQEVVQQLHK----------VLRPFLLRRLKSDVEKGLPPKKETILKVGMS 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  453 KSDIVSAKAAIRvgksHDEDV---SSEHLDELNDSM---GCCiskqlSHQELGIAKLAGFREWLSIHPViaEADG----- 521
Cdd:PLN03142   408 QMQKQYYKALLQ----KDLDVvnaGGERKRLLNIAMqlrKCC-----NHPYLFQGAEPGPPYTTGEHLV--ENSGkmvll 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  522 ---VAKLESDSSshKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKF-QLSSEVKIAIVGITAGGVGL 597
Cdd:PLN03142   477 dklLPKLKERDS--RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLLSTRAGGLGI 554
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1366038577  598 DFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFSGKDTIDE 646
Cdd:PLN03142   555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
206-392 1.08e-19

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: 89.33  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGV-------RFGLQRggrcLIADEMGLGKTLQAIAI--ACCFMSEGSI-------LVVCPAILRYSWAEELEH 269
Cdd:cd17999      1 LRPYQQEGInwlaflnKYNLHG----ILCDDMGLGKTLQTLCIlaSDHHKRANSFnsenlpsLVVCPPTLVGHWVAEIKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  270 WLPFCLPADIHLVfGHENNPANLKKWP---RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLD 346
Cdd:cd17999     77 YFPNAFLKPLAYV-GPPQERRRLREQGekhNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL----SKAVKQ 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1366038577  347 VARKvKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLGRDKfKFGETY 392
Cdd:cd17999    152 LKAN-HRLI-LSGTPIQNNVLELWSLFDFLMPGYLGTEK-QFQRRF 194
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
206-430 2.55e-19

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: 88.50  E-value: 2.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQR--------GGRCLIADEMGLGKTLQAIAIACCFMSEG--------SILVVCPAILRYSWAEELEH 269
Cdd:cd18004      1 LRPHQREGVQFLYDCltgrrgygGGGAILADEMGLGKTLQAIALVWTLLKQGpygkptakKALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  270 WLPFCLPADIHLVFGHENNPANLKK------WPrVVVISY-TMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIK 342
Cdd:cd18004     81 WLGLRRIKVVTADGNAKDVKASLDFfssastYP-VLIISYeTLRRHAEKLSKKISIDLLICDEGHRL----KNSESKTTK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  343 AVLdvARKVKRIVLLSGTPsLSRPFDIFHQ-IDMLWPGLLG-RDKFKfgeTYCDAKYVRGVQ-GKVFQDFSKGT-RLEEL 418
Cdd:cd18004    156 ALN--SLPCRRRLLLTGTP-IQNDLDEFFAlVDFVNPGILGsLASFR---KVFEEPILRSRDpDASEEDKELGAeRSQEL 229
                          250
                   ....*....|..
gi 1366038577  419 NmLLTRTVMIRR 430
Cdd:cd18004    230 S-ELTSRFILRR 240
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
522-628 1.09e-17

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 79.95  E-value: 1.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  522 VAKLESDSSSHKMLIFAHHHKVLDgVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSS 601
Cdd:pfam00271    6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPD 82
                           90       100
                   ....*....|....*....|....*..
gi 1366038577  602 ATHVVFLELPQSPSLMLQAEDRAHRRG 628
Cdd:pfam00271   83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
206-387 2.82e-17

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: 82.90  E-value: 2.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF------GLQRGGR--CLIADEMGLGKTLQAIAIACCFMSEGSI--------LVVCPAILRYSWAEELEH 269
Cdd:cd18067      1 LRPHQREGVKFlyrcvtGRRIRGShgCIMADEMGLGKTLQCITLMWTLLRQSPQckpeidkaIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  270 WLP---FCLPADihlvfG--HENNPANLKKWPR---------VVVISYTMLH----HLQKSmldrEWALLIVDESHHVrc 331
Cdd:cd18067     81 WLGgrlQPLAID-----GgsKKEIDRKLVQWASqqgrrvstpVLIISYETFRlhveVLQKG----EVGLVICDEGHRL-- 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  332 tkKKSEPREIKAVLDVarKVKRIVLLSGTP---SLSRPFDIFHQIDmlwPGLLG-RDKFK 387
Cdd:cd18067    150 --KNSDNQTYQALDSL--NTQRRVLLSGTPiqnDLSEYFSLVNFVN---PGILGtAAEFK 202
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
206-430 1.01e-16

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 81.27  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF---GLQRGGRCLIADEMGLGKTLQAIA-----------------IACCFMSEGS-------ILVVCPAI 258
Cdd:cd18005      1 LRDYQREGVEFmydLYKNGRGGILGDDMGLGKTVQVIAflaavlgktgtrrdrenNRPRFKKKPPassakkpVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  259 LRYSWAEELEHWLPFCLpADIHLVfGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKS 336
Cdd:cd18005     81 VLYNWKDELDTWGHFEV-GVYHGS-RKDDELEGRLKAGRleVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  337 EpreiKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-RDKFKfgETYCDAKYVRGVQGKVFQDFSKGTRL 415
Cdd:cd18005    159 T----QAMKEL--KCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGsRSQFK--KHFSEPIKRGQRHTATARELRLGRKR 230
                          250
                   ....*....|....*
gi 1366038577  416 EELNMLLTRTVMIRR 430
Cdd:cd18005    231 KQELAVKLSKFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
206-361 1.84e-16

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 78.90  E-value: 1.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGRC---LIADEMGLGKTLQAIA----IACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPAD 278
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflaaLHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IH-------------LVFGHENNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKksepreikavl 345
Cdd:cd18000     81 LHssgsgtgseeklgSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA----------- 149
                          170       180
                   ....*....|....*....|.
gi 1366038577  346 DVARKVKRI-----VLLSGTP 361
Cdd:cd18000    150 EITLACKQLrtphrLILSGTP 170
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
206-430 2.93e-16

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: 78.64  E-value: 2.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd17994      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghskGPFLVSAPLSTIINWEREFEMWAP-----D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IHLVFGHENNpanlkkwprVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKSEPREIKAVLDVARKvkriVLLS 358
Cdd:cd17994     76 FYVVTYVGDH---------VLLTSYELISIDQAILGSIDWAVLVVDEAH--RLKNNQSKFFRILNSYKIGYK----LLLT 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577  359 GTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSKGTRLEELNMLLTRTvMIRR 430
Cdd:cd17994    141 GTPLQNNLEELFHLLNFLTP-----ERFNNLQGFLEE----------FADISKEDQIKKLHDLLGPH-MLRR 196
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
206-430 5.88e-16

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: 78.87  E-value: 5.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGrcLIADEMGLGKTLQAIAIACCFMSEGSI---------------------LVVCPAILRYSWA 264
Cdd:cd18008      1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALALILATRPQDPKipeeleenssdpkklylskttLIVVPLSLLSQWK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  265 EELE-HWLPFCLPADIHLVFGHENNPANLKKwPRVVVISYTML----------------HHLQKSMLDREWALLIVDESH 327
Cdd:cd18008     79 DEIEkHTKPGSLKVYVYHGSKRIKSIEELSD-YDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYRVILDEAH 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  328 HVRCTK-KKSepreiKAVLDVarKVKRIVLLSGTPSLSRpfdifhqIDMLWPgllgrdKFKFG--ETYCDAKYVRGVQGK 404
Cdd:cd18008    158 NIKNRStKTS-----RAVCAL--KAERRWCLTGTPIQNS-------LDDLYS------LLRFLrvEPFGDYPWFNSDISK 217
                          250       260
                   ....*....|....*....|....*.
gi 1366038577  405 VFQDFSKGtRLEELNMLLtRTVMIRR 430
Cdd:cd18008    218 PFSKNDRK-ALERLQALL-KPILLRR 241
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
206-361 2.59e-15

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: 76.66  E-value: 2.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIACCfMSE----GSILVVCPAILRYSWAEELEHWLPfCLPAD 278
Cdd:cd18009      4 MRPYQLEGMEWLRmlwENGINGILADEMGLGKTIQTIALLAH-LRErgvwGPFLVIAPLSTLPNWVNEFARFTP-SVPVL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IH---------LVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVAR 349
Cdd:cd18009     82 LYhgtkeererLRKKIMKREGTLQDFP-VVVTSYEIAMRDRKALQHYAWKYLIVDEGHRL----KNLNCRLIQELKTFNS 156
                          170
                   ....*....|..
gi 1366038577  350 KVKriVLLSGTP 361
Cdd:cd18009    157 DNR--LLLTGTP 166
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
208-394 9.74e-15

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: 74.69  E-value: 9.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  208 PFQLEGVRFGLQRGGRCLIADeMGLGKTLQAI-AIACCFMSE--GSILVVCPA-ILRYSWAEELEHW-LPFCLPADIHLV 282
Cdd:cd18013      3 PYQKVAINFIIEHPYCGLFLD-MGLGKTVTTLtALSDLQLDDftRRVLVIAPLrVARSTWPDEVEKWnHLRNLTVSVAVG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  283 FGHENNPAnLKKWPRVVVISYTMLHHLQKSMLDR-EWALLIVDESHhvrcTKKKSEPREIKAVLDVARKVKRIVLLSGTP 361
Cdd:cd18013     82 TERQRSKA-ANTPADLYVINRENLKWLVNKSGDPwPFDMVVIDELS----SFKSPRSKRFKALRKVRPVIKRLIGLTGTP 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1366038577  362 SLSRPFDIFHQIDMLWPG-LLGRDKFKFGETYCD 394
Cdd:cd18013    157 SPNGLMDLWAQIALLDQGeRLGRSITAYRERWFD 190
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
206-396 1.98e-14

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: 73.82  E-value: 1.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGL-----QRGgrCLIADEMGLGKTLQAIAIACCFMSEGSI----LVVCPAILRYSWAEELEHWlpfclp 276
Cdd:cd17995      1 LRDYQLEGVNWLLfnwynRRN--CILADEMGLGKTIQSIAFLEHLYQVEGIrgpfLVIAPLSTIPNWQREFETW------ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  277 ADIHLVFGHEN-------------NPANLKKWPR------VVVISYTMLhhlqksMLDRE------WALLIVDESHHVRC 331
Cdd:cd17995     73 TDMNVVVYHGSgesrqiiqqyemyFKDAQGRKKKgvykfdVLITTYEMV------IADAEelrkipWRVVVVDEAHRLKN 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577  332 TKKKsepreikaVLDVARKVK--RIVLLSGTPslsrpfdIFHQIDMLWPGL--LGRDKF----KFGETYCDAK 396
Cdd:cd17995    147 RNSK--------LLQGLKKLTleHKLLLTGTP-------LQNNTEELWSLLnfLEPEKFpsseEFLEEFGDLK 204
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
206-382 2.38e-14

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: 74.11  E-value: 2.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF------GLQRGGR--CLIADEMGLGKTLQAIAIACCFMSEG---------SILVVCPAILRYSWAEELE 268
Cdd:cd18066      1 LRPHQREGIEFlyecvmGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGpyggkpvikRALIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  269 HWLP------FCLPADiHLVFGHENNPANlkkwpRVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreiK 342
Cdd:cd18066     81 KWLGserikvFTVDQD-HKVEEFIASPLY-----SVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT-----T 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1366038577  343 AVLDVARKVKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLG 382
Cdd:cd18066    150 TALTSLSCERRII-LTGTPIQNDLQEFFALIDFVNPGILG 188
HELICc smart00490
helicase superfamily c-terminal domain;
547-628 2.41e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.16  E-value: 2.41e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577   547 VQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHR 626
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                    ..
gi 1366038577   627 RG 628
Cdd:smart00490   81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
205-627 5.55e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 76.60  E-value: 5.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQLEGV----RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAI-LRYSWAEELEHWLPfclpaDI 279
Cdd:COG1061     80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRReLLEQWAEELRRFLG-----DP 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  280 HLVFGHENNPAnlkkwpRVVVISY-TMLHHLQKSMLDREWALLIVDESHHVRctkkksePREIKAVLDvARKVKRIVLLS 358
Cdd:COG1061    155 LAGGGKKDSDA------PITVATYqSLARRAHLDELGDRFGLVIIDEAHHAG-------APSYRRILE-AFPAAYRLGLT 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  359 GTP--SLSRPFDIFHQIdmlwpgllgrdkfkfgetycdakyvrgvqGKVFqdfskGTRLEELnmlltrtvmirrLKEHVL 436
Cdd:COG1061    221 ATPfrSDGREILLFLFD-----------------------------GIVY-----EYSLKEA------------IEDGYL 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  437 SqlpPKRRQIIQVVLKKsdivsakaairvgKSHDEDVSSEHLDelndsmgccisKQLSHQElgIAKLAGFREWLSIHPvi 516
Cdd:COG1061    255 A---PPEYYGIRVDLTD-------------ERAEYDALSERLR-----------EALAADA--ERKDKILRELLREHP-- 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  517 aeadgvaklesdsSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVG 596
Cdd:COG1061    304 -------------DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR-DGELRI-LVTVDVLNEG 368
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1366038577  597 LDFSSATHVVFLELPQSPSLMLQAEDRAHRR 627
Cdd:COG1061    369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRP 399
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
206-430 7.33e-14

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: 72.40  E-value: 7.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd18057      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEghskGPYLVSAPLSTIINWEREFEMWAP-----D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IHLV----------------FGHENNPA-------NLKKWPR----VVVISYTMLHHLQKSMLDREWALLIVDESHHVRC 331
Cdd:cd18057     76 FYVVtytgdkesrsvireneFSFEDNAIrsgkkvfRMKKEAQikfhVLLTSYELITIDQAILGSIEWACLVVDEAHRLKN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  332 TKKKsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSK 411
Cdd:cd18057    156 NQSK-----FFRVLN-SYKIDYKLLLTGTPLQNNLEELFHLLNFLTP-----ERFNNLEGFLEE----------FADISK 214
                          250
                   ....*....|....*....
gi 1366038577  412 GTRLEELNMLLTRTvMIRR 430
Cdd:cd18057    215 EDQIKKLHDLLGPH-MLRR 232
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
206-443 3.18e-13

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: 70.85  E-value: 3.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIaCCFMSE-----GSILVVCPAILRYSWAEELEHWLP----F 273
Cdd:cd18064     16 LRDYQVRGLNWLIslyENGINGILADEMGLGKTLQTISL-LGYMKHyrnipGPHMVLVPKSTLHNWMAEFKRWVPtlraV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  274 CLPADIHLVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKR 353
Cdd:cd18064     95 CLIGDKDQRAAFVRDVLLPGEWD-VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRI-----KNEKSKLSEIVREFKTTNR 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  354 IvLLSGTPSLSRPFDIFHQIDMLWPGLLGR-DKFkfgETYCDAKYVRGVQGKVfqdfskgtrlEELNMLLtRTVMIRRLK 432
Cdd:cd18064    169 L-LLTGTPLQNNLHELWALLNFLLPDVFNSaEDF---DSWFDTNNCLGDQKLV----------ERLHMVL-RPFLLRRIK 233
                          250
                   ....*....|.
gi 1366038577  433 EHVLSQLPPKR 443
Cdd:cd18064    234 ADVEKSLPPKK 244
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
225-361 2.02e-12

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: 68.15  E-value: 2.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAI----ACCFMSEGSILVVCPAILRYSWAEELEHWLPfCLpaDIHLVFGhenNPANLKK----WP 296
Cdd:cd18003     23 ILADEMGLGKTIQTIALlahlACEKGNWGPHLIVVPTSVMLNWEMEFKRWCP-GF--KILTYYG---SAKERKLkrqgWM 96
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  297 R-----VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarKVKRIVLLSGTP 361
Cdd:cd18003     97 KpnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNI----KNFKSQRWQTLLNF--NTQRRLLLTGTP 160
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
206-430 2.67e-12

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: 67.46  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQR---GGRCLIADEMGLGKTLQAIAI----ACCFMSEGSILVVCPAILRYSWAEELEHWLP------ 272
Cdd:cd18006      1 LRPYQLEGVNWLLQCraeQHGCILGDEMGLGKTCQTISLlwylAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPdlsvit 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  273 --------FCLPADIhlvfgHENNPANlkkwprVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkkKSEPREIKAV 344
Cdd:cd18006     81 ymgdkekrLDLQQDI-----KSTNRFH------VLLTTYEICLKDASFLKSFPWASLVVDEAHRL-----KNQNSLLHKT 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  345 LDvARKVKRIVLLSGTP---SLSRPFDIFHQIDmlwPGLLGRDKFKfgetycdaKYVrgvqgKVFQDFSKGTRL-EELNM 420
Cdd:cd18006    145 LS-EFSVDFRLLLTGTPiqnSLQELYALLSFIE---PNVFPKDKLD--------DFI-----KAYSETDDESETvEELHL 207
                          250
                   ....*....|
gi 1366038577  421 LLtRTVMIRR 430
Cdd:cd18006    208 LL-QPFLLRR 216
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
206-387 2.89e-12

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: 67.78  E-value: 2.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF--GL---QRGGrcLIADEMGLGKTLQAIA-IACCFMSE--GSILVVCPAILRYSWAEELEHWLPfclpa 277
Cdd:cd18001      1 LYPHQREGVAWlwSLhdgGKGG--ILADDMGLGKTVQICAfLSGMFDSGliKSVLVVMPTSLIPHWVKEFAKWTP----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  278 DIHLVFGHENNPANLKKWPR-------VVVISYTML--HHLQKSMLDRE---WALLIVDESHHVRCTKKKSEpreiKAVL 345
Cdd:cd18001     74 GLRVKVFHGTSKKERERNLEriqrgggVLLTTYGMVlsNTEQLSADDHDefkWDYVILDEGHKIKNSKTKSA----KSLR 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1366038577  346 DVARKVKriVLLSGTP---SLSRPFDIFhqiDMLWPG-LLG-RDKFK 387
Cdd:cd18001    150 EIPAKNR--IILTGTPiqnNLKELWALF---DFACNGsLLGtRKTFK 191
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
209-430 3.73e-11

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: 64.65  E-value: 3.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  209 FQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaDIHL 281
Cdd:cd18055      4 YQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghtkGPFLVSAPLSTIINWEREFQMWAP-----DFYV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  282 V----------------FGHENNPANLKKWP-----------RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKK 334
Cdd:cd18055     79 VtytgdkdsraiireneFSFDDNAVKGGKKAfkmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  335 KsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSKGTR 414
Cdd:cd18055    159 K-----FFRVLN-GYKIDHKLLLTGTPLQNNLEELFHLLNFLTP-----ERFNNLEGFLEE----------FADISKEDQ 217
                          250
                   ....*....|....*.
gi 1366038577  415 LEELNMLLTRTvMIRR 430
Cdd:cd18055    218 IKKLHDLLGPH-MLRR 232
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
220-370 4.50e-11

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: 64.41  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  220 RGGrcLIADEMGLGKTLQAIA-IACCFMsegsiLVVCPAILRYSWAEEL-EHWLPFCLpaDIHLVFGHENN--PANLKKW 295
Cdd:cd18071     49 RGG--ILADDMGLGKTLTTISlILANFT-----LIVCPLSVLSNWETQFeEHVKPGQL--KVYTYHGGERNrdPKLLSKY 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  296 PrVVVISYTMLHHLQKSMLDR-----EWALLIVDESHHVRCTKKKseprEIKAVLDVarKVKRIVLLSGTPSLSRPFDIF 370
Cdd:cd18071    120 D-IVLTTYNTLASDFGAKGDSplhtiNWLRVVLDEGHQIRNPNAQ----QTKAVLNL--SSERRWVLTGTPIQNSPKDLG 192
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
206-378 6.67e-11

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: 63.93  E-value: 6.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQ-AIAIACCFM---SEGSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd18056      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQtAVFLYSLYKeghSKGPFLVSAPLSTIINWEREFEMWAP-----D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  279 IHLV----------------FGHENN-------PANLKKWP----RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRC 331
Cdd:cd18056     76 MYVVtyvgdkdsraiireneFSFEDNairggkkASRMKKEAsvkfHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKN 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1366038577  332 TKKKsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18056    156 NQSK-----FFRVLN-GYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
225-361 7.84e-11

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: 63.49  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIaCCFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANL------- 292
Cdd:cd17997     26 ILADEMGLGKTLQTISL-LGYLKHykninGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLI---GDKEERADIirdvllp 101
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  293 KKWPrVVVISYTMLHHlQKSMLDR-EWALLIVDESHhvRCTKKKSEPREIKAVLDVARKvkriVLLSGTP 361
Cdd:cd17997    102 GKFD-VCITSYEMVIK-EKTVLKKfNWRYIIIDEAH--RIKNEKSKLSQIVRLFNSRNR----LLLTGTP 163
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
225-361 1.10e-10

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


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 63.16  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIACCFM----SEGSILVVCPAILRYSWAEELEHWLP------FCLPADIHLVFGHENNPANLKk 294
Cdd:cd17996     26 ILADEMGLGKTIQTISLITYLMekkkNNGPYLVIVPLSTLSNWVSEFEKWAPsvskivYKGTPDVRKKLQSQIRAGKFN- 104
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1366038577  295 wprVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVRCTKKKsepreIKAVLDVARKVKRIVLLSGTP 361
Cdd:cd17996    105 ---VLLTTYEYIIK-DKPLLSKiKWKYMIIDEGHRMKNAQSK-----LTQTLNTYYHARYRLLLTGTP 163
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
206-361 3.21e-10

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: 62.36  E-value: 3.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQRGGrcLIADEMGLGKTLQAIA------------------------IACCFMSE-----GSILVVCP 256
Cdd:cd18070      1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLAlillhprpdndldaadddsdemvcCPDCLVAEtpvssKATLIVCP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  257 AILRYSWAEELEHWLPFCLPADIHlvFGHENNPANLKKWPR------VVVISYTML----HH------------LQKSML 314
Cdd:cd18070     79 SAILAQWLDEINRHVPSSLKVLTY--QGVKKDGALASPAPEilaeydIVVTTYDVLrtelHYaeanrsnrrrrrQKRYEA 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577  315 DR------EWALLIVDESHHVRCTKKKSEpreikavlDVARKVKRIV--LLSGTP 361
Cdd:cd18070    157 PPsplvlvEWWRVCLDEAQMVESSTSKAA--------EMARRLPRVNrwCVSGTP 203
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
209-361 3.48e-10

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: 61.22  E-value: 3.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  209 FQLEGVRFGLQ---RGGRCLIADEMGLGKTLQAIaiacCFMS--------EGSILVVCPAILRYSWAEELEHWLPfclpa 277
Cdd:cd17993      5 YQLTGLNWLAHswcKGNNGILADEMGLGKTVQTI----SFLSylfhsqqqYGPFLVVVPLSTMPAWQREFAKWAP----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  278 DIHLV--FGHENNPANLKKWP-----------RVVVISYTMLhhLQ-KSMLDR-EWALLIVDESHHVrctkKKSEPREIK 342
Cdd:cd17993     76 DMNVIvyLGDIKSRDTIREYEfyfsqtkklkfNVLLTTYEII--LKdKAFLGSiKWQYLAVDEAHRL----KNDESLLYE 149
                          170
                   ....*....|....*....
gi 1366038577  343 AVLDVarKVKRIVLLSGTP 361
Cdd:cd17993    150 ALKEF--KTNNRLLITGTP 166
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
225-361 7.24e-10

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: 60.60  E-value: 7.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLP--FCLPadihlVFGHENNPANLKK-WPR 297
Cdd:cd18002     23 ILADEMGLGKTVQSIAVLAHLAEEhniwGPFLVIAPASTLHNWQQEISRFVPqfKVLP-----YWGNPKDRKVLRKfWDR 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577  298 -----------VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLdvARKVKRIVLLSGTP 361
Cdd:cd18002     98 knlytrdapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAI----KSSSSSRWKTLL--SFHCRNRLLLTGTP 166
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
206-386 2.00e-09

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: 59.44  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF-------GLQR-----GGRCLIADEMGLGKTLQAIAIACCFM---SEGSILVVCPAILRYSWAEELEHW 270
Cdd:cd18069      1 LKPHQIGGIRFlydniieSLERykgssGFGCILAHSMGLGKTLQVISFLDVLLrhtGAKTVLAIVPVNTLQNWLSEFNKW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  271 LP--------FCLPADIHLVF-GHENNPANLK---KWPR---VVVISYTMLHhlqksmLDREWALLIVDESHHVRCTKKk 335
Cdd:cd18069     81 LPppealpnvRPRPFKVFILNdEHKTTAARAKvieDWVKdggVLLMGYEMFR------LRPGPDVVICDEGHRIKNCHA- 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1366038577  336 seprEIKAVLDVARKVKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLG-RDKF 386
Cdd:cd18069    154 ----STSQALKNIRSRRRIV-LTGYPLQNNLIEYWCMVDFVRPDFLGtRQEF 200
DpdE NF041062
protein DpdE;
223-366 2.42e-09

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 61.91  E-value: 2.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  223 RCLIADEMGLGKTLQA-IAIACCFM--SEGSILVVCPAILRYSWAEELE---HWLPFcLPADIHLVfGHEnNPANLKKWP 296
Cdd:NF041062   172 RYLLADEVGLGKTIEAgLVIRQHLLdnPDARVLVLVPDALVRQWRRELRdkfFLDDF-PGARVRVL-SHE-EPERWEPLL 248
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577  297 RVVvisytmlhhlqksmldrewALLIVDESHHVRCTKKKSEPREI---KAVLDVARKVKRIVLLSGTPSLSRP 366
Cdd:NF041062   249 DAP-------------------DLLVVDEAHQLARLAWSGDPPERaryRELAALAHAAPRLLLLSATPVLGNE 302
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
182-394 6.56e-09

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: 58.09  E-value: 6.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  182 RPEHLLDDKVDELIGKLPKRLLDsllpFQLEGVRFGLQRGGRC---LIADEMGLGKTLQAIAIACCFMSE----GSILVV 254
Cdd:cd18054      1 RPRFVALKKQPSYIGGENLELRD----YQLEGLNWLAHSWCKNnsvILADEMGLGKTIQTISFLSYLFHQhqlyGPFLLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  255 CPAILRYSWAEELEHWLPfclpaDIHLV--FGHENNPANLKKWP-----------RVVVISYTMLHHLQKSMLDREWALL 321
Cdd:cd18054     77 VPLSTLTSWQREFEIWAP-----EINVVvyIGDLMSRNTIREYEwihsqtkrlkfNALITTYEILLKDKTVLGSINWAFL 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1366038577  322 IVDESHHVrctkKKSEPREIKAVLDVarKVKRIVLLSGTP---SLSRPFDIFHqidMLWPgllgrDKFKFGETYCD 394
Cdd:cd18054    152 GVDEAHRL----KNDDSLLYKTLIDF--KSNHRLLITGTPlqnSLKELWSLLH---FIMP-----EKFEFWEDFEE 213
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
205-432 8.69e-09

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 57.33  E-value: 8.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIACCFMS----EGSILVVCPAILRYSWAEELEHWLP----F 273
Cdd:cd18065     15 TLRDYQVRGLNWMIslyENGVNGILADEMGLGKTLQTIALLGYLKHyrniPGPHMVLVPKSTLHNWMNEFKRWVPslraV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  274 CLPADIHLVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKsepreikaVLDVARKVKR 353
Cdd:cd18065     95 CLIGDKDARAAFIRDVMMPGEWD-VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSK--------LSEIVREFKT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  354 I--VLLSGTPSLSRPFDIFHQIDMLWPGLLGR-DKFkfgETYCDAKYVRGVQGKVfqdfskgtrlEELNMLLtRTVMIRR 430
Cdd:cd18065    166 TnrLLLTGTPLQNNLHELWALLNFLLPDVFNSaDDF---DSWFDTKNCLGDQKLV----------ERLHAVL-KPFLLRR 231

                   ..
gi 1366038577  431 LK 432
Cdd:cd18065    232 IK 233
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
225-381 9.83e-09

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 57.75  E-value: 9.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  225 LIADEMGLGKTLQAIAIACCFMS----EGSILVVCPAILRYSWAEELEHWLPFCLPADihlvfgHENNPANLKKWP---- 296
Cdd:cd18062     46 ILADEMGLGKTIQTIALITYLMEhkriNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS------YKGSPAARRAFVpqlr 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  297 ----RVVVISYTMLHHLQKSMLDREWALLIVDESHhvrctKKKSEPREIKAVLDVARKVKRIVLLSGTPSLSRPFDIFHQ 372
Cdd:cd18062    120 sgkfNVLLTTYEYIIKDKQILAKIRWKYMIVDEGH-----RMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWAL 194

                   ....*....
gi 1366038577  373 IDMLWPGLL 381
Cdd:cd18062    195 LNFLLPTIF 203
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
206-373 1.78e-08

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: 56.60  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGLQ---RGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLP----FC 274
Cdd:cd18053     21 LRDYQLNGLNWLAHswcKGNSCILADEMGLGKTIQTISFLNYLFHEhqlyGPFLLVVPLSTLTSWQREIQTWAPqmnaVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  275 LPADI---HLVFGHE-NNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarK 350
Cdd:cd18053    101 YLGDInsrNMIRTHEwMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRL----KNDDSLLYKTLIDF--K 174
                          170       180
                   ....*....|....*....|....*.
gi 1366038577  351 VKRIVLLSGTP---SLSRPFDIFHQI 373
Cdd:cd18053    175 SNHRLLITGTPlqnSLKELWSLLHFI 200
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
221-360 5.12e-08

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 53.18  E-value: 5.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  221 GGRCLIADEMGLGKTLQA-IAIACCFMSEGS-ILVVCPAI-LRYSWAEELEHWLPfcLPADIHLVFGHENNPANLKKW-- 295
Cdd:cd00046      1 GENVLITAPTGSGKTLAAlLAALLLLLKKGKkVLVLVPTKaLALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNKlg 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1366038577  296 -PRVVVISYTMLHHLQKSML---DREWALLIVDESHHVRcTKKKSEPREIKAVLDVARKVKRIVLLSGT 360
Cdd:cd00046     79 dADIIIATPDMLLNLLLREDrlfLKDLKLIIVDEAHALL-IDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
206-385 5.74e-08

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: 55.28  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRF-------GLQR-----GGRCLIADEMGLGKTLQAIA----IACCFMSEG--SILVVCPAILRYSWAEEL 267
Cdd:cd18068      1 LKPHQVDGVQFmwdccceSLKKtkkspGSGCILAHCMGLGKTLQVVTflhtVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  268 EHWLPFCLP------ADIHLVFGHENNPANLKKW---PRVVVISYTMLHHL----------------QKSMLDREWALLI 322
Cdd:cd18068     81 EKWQEGLKDeekievNELATYKRPQERSYKLQRWqeeGGVMIIGYDMYRILaqernvksreklkeifNKALVDPGPDFVV 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1366038577  323 VDESHhvrctKKKSEPREI-KAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGRDK 385
Cdd:cd18068    161 CDEGH-----ILKNEASAVsKAMNSI--RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIK 217
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
206-361 7.10e-08

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 53.08  E-value: 7.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmSEGSILVVCPAI-LRYSWAEELEHWLPfclPADIHLV 282
Cdd:cd17926      1 LRPYQEEALEawLAHKNNRRGILVLPTGSGKTLTALALIAYL-KELRTLIVVPTDaLLDQWKERFEDFLG---DSSIGLI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  283 FGHENNPANLKKwprVVVISYTMLHHLQK--SMLDREWALLIVDESHHVrCTKKksepreIKAVLDVARKvKRIVLLSGT 360
Cdd:cd17926     77 GGGKKKDFDDAN---VVVATYQSLSNLAEeeKDLFDQFGLLIVDEAHHL-PAKT------FSEILKELNA-KYRLGLTAT 145

                   .
gi 1366038577  361 P 361
Cdd:cd17926    146 P 146
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
191-381 7.27e-08

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


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 55.07  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  191 VDELIGKLPKRLLDSLLP-FQLEGVRFGLQRGGRCL---IADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYS 262
Cdd:cd18063      8 ITERVEKQSSLLINGTLKhYQLQGLEWMVSLYNNNLngiLADEMGLGKTIQTIALITYLMEHkrlnGPYLIIVPLSTLSN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  263 WAEELEHWLPFCLPadihlvFGHENNPANLKKW-PR-------VVVISYTMLHHLQKSMLDREWALLIVDESHhvrctKK 334
Cdd:cd18063     88 WTYEFDKWAPSVVK------ISYKGTPAMRRSLvPQlrsgkfnVLLTTYEYIIKDKHILAKIRWKYMIVDEGH-----RM 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1366038577  335 KSEPREIKAVLDVARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLL 381
Cdd:cd18063    157 KNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIF 203
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
208-329 1.69e-07

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


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 52.30  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  208 PFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFMSegSILVVCPAILR-YSWAEELEHWlpfCLPADIHL-VF 283
Cdd:cd18029     11 PYQEKALSkmFGNGRARSGVIVLPCGAGKTLVGITAACTIKK--STLVLCTSAVSvEQWRRQFLDW---TTIDDEQIgRF 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1366038577  284 GHENNPanlKKWPRVVVIS-YTML-------HHLQKSM---LDREWALLIVDESHHV 329
Cdd:cd18029     86 TSDKKE---IFPEAGVTVStYSMLantrkrsPESEKFMefiTEREWGLIILDEVHVV 139
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
206-430 1.79e-07

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: 53.52  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWLP--- 272
Cdd:cd18060      1 LREYQLEGVNwllFNWYNRQNCILADEMGLGKTIQSIA----FLQEvynvgihGPFLVIAPLSTITNWEREFNTWTEmnt 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  273 ------------------FCLPADIHLVFGHENNPAnlkkwprvVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKK 334
Cdd:cd18060     77 ivyhgslasrqmiqqyemYCKDSRGRLIPGAYKFDA--------LITTFEMILSDCPELREIEWRCVIIDEAH--RLKNR 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  335 KSEPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWPgllgrdkfkfGETYCDAKYVRGvqgkvFQDFSKGTR 414
Cdd:cd18060    147 NCKLLDSLKHMDLEHK----VLLTGTPLQNTVEELFSLLHFLEP----------SQFPSESEFLKD-----FGDLKTEEQ 207
                          250
                   ....*....|....*.
gi 1366038577  415 LEELNMLLtRTVMIRR 430
Cdd:cd18060    208 VQKLQAIL-KPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
206-378 4.28e-07

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: 52.35  E-value: 4.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWlpfcl 275
Cdd:cd18058      1 LREYQLEGMNwllFNWYNRKNCILADEMGLGKTIQSIT----FLSEiflmgirGPFLIIAPLSTITNWEREFRTW----- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  276 pADIHLVFGH-------------------ENNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKS 336
Cdd:cd18058     72 -TEMNAIVYHgsqisrqmiqqyemyyrdeQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAH--RLKNRNC 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1366038577  337 EPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18058    149 KLLEGLKLMALEHK----VLLTGTPLQNSVEELFSLLNFLEP 186
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
206-361 1.26e-06

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: 50.08  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAiaccFMS-------EGSILVVCPAILRYSWAEELEHWLPFCL 275
Cdd:cd17998      1 LKDYQLIGLNWLNllyQKKLSGILADEMGLGKTIQVIA----FLAylkeigiPGPHLVVVPSSTLDNWLREFKRWCPSLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  276 padIHLVFGHENNPANLK--------KWpRVVVISYTML--HHLQKSMLDR-EWALLIVDESHHVrctkKKSEPREIKAV 344
Cdd:cd17998     77 ---VEPYYGSQEERKHLRydilkgleDF-DVIVTTYNLAtsNPDDRSFFKRlKLNYVVYDEGHML----KNMTSERYRHL 148
                          170
                   ....*....|....*..
gi 1366038577  345 LDVaRKVKRIvLLSGTP 361
Cdd:cd17998    149 MTI-NANFRL-LLTGTP 163
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
206-402 1.37e-06

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: 50.80  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWLPFcl 275
Cdd:cd18059      1 LREYQLEGVNwllFNWYNTRNCILADEMGLGKTIQSIT----FLYEiylkgihGPFLVIAPLSTIPNWEREFRTWTEL-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  276 paDIHLVFGHENNPANLKKWP-----------------RVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKSEP 338
Cdd:cd18059     75 --NVVVYHGSQASRRTIQLYEmyfkdpqgrvikgsykfHAIITTFEMILTDCPELRNIPWRCVVIDEAH--RLKNRNCKL 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1366038577  339 REIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWPGLLGRDKfKFGETYCDAKYVRGVQ 402
Cdd:cd18059    151 LEGLKMMDLEHK----VLLTGTPLQNTVEELFSLLHFLEPSRFPSET-TFMQEFGDLKTEEQVQ 209
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
205-361 1.38e-06

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 52.92  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQL----E-GVRFGlqrgGRCLIADEMGLGKTLQAiaiaccfmseGSI-------------LVVCPAILRYSWAEE 266
Cdd:PRK04914   152 SLIPHQLyiahEvGRRHA----PRVLLADEVGLGKTIEA----------GMIihqqlltgraervLILVPETLQHQWLVE 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  267 L--EHWLPFCL-----PADIhlvFGHENNP---ANLkkwprvVVISYTML---HHLQKSMLDREWALLIVDESHHVRCTK 333
Cdd:PRK04914   218 MlrRFNLRFSLfdeerYAEA---QHDADNPfetEQL------VICSLDFLrrnKQRLEQALAAEWDLLVVDEAHHLVWSE 288
                          170       180
                   ....*....|....*....|....*...
gi 1366038577  334 KKSEpREIKAVLDVARKVKRIVLLSGTP 361
Cdd:PRK04914   289 EAPS-REYQVVEQLAEVIPGVLLLTATP 315
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
206-378 1.00e-04

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: 45.00  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWlpfcl 275
Cdd:cd18061      1 LREYQLEGLNwllFNWYNRRNCILADEMGLGKTIQSIT----FLYEilltgirGPFLIIAPLSTIANWEREFRTW----- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  276 pADIHLVFGHEN--NPANLKKWP-----------------RVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKS 336
Cdd:cd18061     72 -TDLNVVVYHGSliSRQMIQQYEmyfrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAH--RLKNKNC 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1366038577  337 EPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18061    149 KLLEGLKLMNLEHK----VLLTGTPLQNTVEELFSLLHFLEP 186
ResIII pfam04851
Type III restriction enzyme, res subunit;
205-328 6.40e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  205 SLLPFQLEGVR----FGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSI---LVVCPAI-LRYSWAEELEHWLPFCLP 276
Cdd:pfam04851    3 ELRPYQIEAIEnlleSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIkkvLFLVPRKdLLEQALEEFKKFLPNYVE 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1366038577  277 ADIhlVFGHENNPANLKKWpRVVVISYTMLH---HLQKSMLDRE-WALLIVDESHH 328
Cdd:pfam04851   83 IGE--IISGDKKDESVDDN-KIVVTTIQSLYkalELASLELLPDfFDVIIIDEAHR 135
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
578-637 1.34e-03

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: 38.84  E-value: 1.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  578 QLSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYF 637
Cdd:cd18785     18 EIASSLEI-LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1131-1163 5.59e-03

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 36.50  E-value: 5.59e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1366038577 1131 GNAWHADHLVPVYLGGGEcRLENMRTLCVACHS 1163
Cdd:COG1403     31 GDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
206-329 6.54e-03

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 40.94  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577  206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmsEGSILVVC-PAILRYSWAEELEHWlpfCLPADIHL- 281
Cdd:TIGR00603  256 IRPYQEKSLSkmFGNGRARSGIIVLPCGAGKSLVGVTAACTV--KKSCLVLCtSAVSVEQWKQQFKMW---STIDDSQIc 330
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577  282 VFGHENnpanlKKWPR----VVVISYTMLHHLQKS----------MLDREWALLIVDESHHV 329
Cdd:TIGR00603  331 RFTSDA-----KERFHgeagVVVSTYSMVAHTGKRsyesekvmewLTNREWGLILLDEVHVV 387
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1126-1166 7.24e-03

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 35.91  E-value: 7.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1366038577 1126 KDPTEGNAWHADHLVPVYlGGGECRLENMRTLCVACHSDVT 1166
Cdd:cd00085     18 GKPGGTEGLEVDHIIPLS-DGGNNDLDNLVLLCRKCHRKKH 57
 
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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