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Conserved domains on  [gi|1002285531|ref|XP_015647062|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 198-385 2.51e-75

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


The actual alignment was detected with superfamily member cd18010:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 213  Bit Score: 247.89  E-value: 2.51e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEGPVLIVCPAVLRYTWAEELERWDPSFLPKDIHLVFGH 277
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  278 QDSLERLGacPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELAPNVSRIVLLSGTPSLSR 357
Cdd:cd18010     81 KDGLRDGD--AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKR----TKAALPLLKRAKRVILLSGTPALSR 154

                          170       180
                   ....*....|....*....|....*...
gi 1002285531  358 PFDIYHQINMLWPHLLGSNKfDFANKYC 385
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFH-DFGRRYC 181
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 190-627 6.94e-73

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 256.69  E-value: 6.94e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  190 LPQHLRDALLPFQLEGVKF--GLRRHG-RCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELERWD 263
Cdd:COG0553    234 LPAGLKATLRPYQLEGAAWllFLRRLGlGGLLADDMGLGKTIQALALLLELKERGlarPVLIVAPTSLVGNWQRELAKFA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  264 PSFlpkDIHLVFGHQDSLERLGACPKA--VVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLELap 341
Cdd:COG0553    314 PGL---RVLVLDGTRERAKGANPFEDAdlVITSYGLLRRDIELLAAVDWDLVILDEAQHI----KNPATKRAKAVRAL-- 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  342 NVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKFdFANKYCLLhtVQGCNGRTYQ----------IRRLKEHLLNEL 411
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKA-FRERFARP--IEKGDEEALErlrrllrpflLRRTKEDVLKDL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  412 PPKRRQIIWLKLNASDIK--TAIScikgvntsdeiptiaspdnsnDSEEVNMEEADGCKK----------------SPRn 473
Cdd:COG0553    462 PEKTEETLYVELTPEQRAlyEAVL---------------------EYLRRELEGAEGIRRrglilaaltrlrqicsHPA- 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  474 LTTQEIGIVKIPgfS---EWFLNhfIMKEPADNGsldsqsncQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRE 550
Cdd:COG0553    520 LLLEEGAELSGR--SaklEALLE--LLEELLAEG--------EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531  551 RKDAVDSFRLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYIFCARNTLDE 627
Cdd:COG0553    588 RDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1067-1102 7.80e-06

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


:

Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 44.59  E-value: 7.80e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002285531 1067 PNEGNAWHADHIVPVYKGGGEcTLENLRTLCVACHS 1102
Cdd:COG1403     28 PFSGDALEVDHIIPRSRGGTD-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 ...
 198-385 2.51e-75

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: 247.89  E-value: 2.51e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEGPVLIVCPAVLRYTWAEELERWDPSFLPKDIHLVFGH 277
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  278 QDSLERLGacPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELAPNVSRIVLLSGTPSLSR 357
Cdd:cd18010     81 KDGLRDGD--AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKR----TKAALPLLKRAKRVILLSGTPALSR 154

                          170       180
                   ....*....|....*....|....*...
gi 1002285531  358 PFDIYHQINMLWPHLLGSNKfDFANKYC 385
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFH-DFGRRYC 181
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 190-627 6.94e-73

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 256.69  E-value: 6.94e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  190 LPQHLRDALLPFQLEGVKF--GLRRHG-RCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELERWD 263
Cdd:COG0553    234 LPAGLKATLRPYQLEGAAWllFLRRLGlGGLLADDMGLGKTIQALALLLELKERGlarPVLIVAPTSLVGNWQRELAKFA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  264 PSFlpkDIHLVFGHQDSLERLGACPKA--VVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLELap 341
Cdd:COG0553    314 PGL---RVLVLDGTRERAKGANPFEDAdlVITSYGLLRRDIELLAAVDWDLVILDEAQHI----KNPATKRAKAVRAL-- 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  342 NVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKFdFANKYCLLhtVQGCNGRTYQ----------IRRLKEHLLNEL 411
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKA-FRERFARP--IEKGDEEALErlrrllrpflLRRTKEDVLKDL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  412 PPKRRQIIWLKLNASDIK--TAIScikgvntsdeiptiaspdnsnDSEEVNMEEADGCKK----------------SPRn 473
Cdd:COG0553    462 PEKTEETLYVELTPEQRAlyEAVL---------------------EYLRRELEGAEGIRRrglilaaltrlrqicsHPA- 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  474 LTTQEIGIVKIPgfS---EWFLNhfIMKEPADNGsldsqsncQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRE 550
Cdd:COG0553    520 LLLEEGAELSGR--SaklEALLE--LLEELLAEG--------EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531  551 RKDAVDSFRLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYIFCARNTLDE 627
Cdd:COG0553    588 RDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 513-620 4.72e-35

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: 130.29  E-value: 4.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  513 QKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRERKDAVDSFRLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELP 592
Cdd:cd18793     28 EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPW 107

                           90       100
                   ....*....|....*....|....*...
gi 1002285531  593 KSASELLQAEDRAHRRGQTNAVNIYIFC 620
Cdd:cd18793    108 WNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 202-425 4.38e-31

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: 124.33  E-value: 4.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  202 QLEGVKFGLRRH---GR-CLIADEMGLGKTLQAIA-IACCY----KDEGPVLIVCPAVLRYTWAEELERW-DPSFLPKDI 271
Cdd:pfam00176    2 QIEGVNWMLSLEnnlGRgGILADEMGLGKTLQTISlLLYLKhvdkNWGGPTLIVVPLSLLHNWMNEFERWvSPPALRVVV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HlvFGHQDSLERLGACPK------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELapNVSR 345
Cdd:pfam00176   82 L--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KTRN 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  346 IVLLSGTPSLSRPFDIYHQINMLWPHLLGS-----NKFDF-------ANKYCLLHTVQgcngRTYQIRRLKEHLLNELPP 413
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSlstfrNWFDRpiergggKKGVSRLHKLL----KPFLLRRTKKDVEKSLPP 229

                          250
                   ....*....|..
gi 1002285531  414 KRRQIIWLKLNA 425
Cdd:pfam00176  230 KVEYILFCRLSK 241
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 194-627 2.78e-26

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 116.82  E-value: 2.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  194 LRDallpFQLEGVKFGLR--RHG-RCLIADEMGLGKTLQAIAIACcYKDE-----GPVLIVCPAVLRYTWAEELERWDPS 265
Cdd:PLN03142   170 MRD----YQLAGLNWLIRlyENGiNGILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPV 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  266 FLPKDIHlvfGHQDSL----ERLGACPK--AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNETQAVLEL 339
Cdd:PLN03142   245 LRAVKFH---GNPEERahqrEELLVAGKfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI-----KNENSLLSKTMRL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  340 APNVSRIvLLSGTPSLSRPFDIYHQINMLWPHLLGS-NKFD--FANK--------YCLLHTVQgcngRTYQIRRLKEHLL 408
Cdd:PLN03142   317 FSTNYRL-LITGTPLQNNLHELWALLNFLLPEIFSSaETFDewFQISgendqqevVQQLHKVL----RPFLLRRLKSDVE 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  409 NELPPKRRQIiwLKLNASDIKTAI------SCIKGVNTSDEiptiaspdnsnDSEEVNME-EADGCKKSPRNLTTQEIGI 481
Cdd:PLN03142   392 KGLPPKKETI--LKVGMSQMQKQYykallqKDLDVVNAGGE-----------RKRLLNIAmQLRKCCNHPYLFQGAEPGP 458

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  482 VKIPGfsewflNHFImkepADNGS---LDS-----QSNCQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRERKD 553
Cdd:PLN03142   459 PYTTG------EHLV----ENSGKmvlLDKllpklKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDA 528

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002285531  554 AVDSF-RLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYIFCARNTLDE 627
Cdd:PLN03142   529 SIDAFnKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
DEXDc smart00487
DEAD-like helicases superfamily;
190-368 4.03e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 98.33  E-value: 4.03e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531   190 LPQHLRDALLPFQLEGVKFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCP-AVLRYTWAEELERWDPS 265
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGkggRVLVLVPtRELAEQWAEELKKLGPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531   266 FLPKDIHLVFGHQDSLER---LGACPKAVVISYQMLSRL--RKSMMNRRWALMIIDESHNIrctKKKHEKNETQAVLELA 340
Cdd:smart00487   81 LGLKVVGLYGGDSKREQLrklESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRL---LDGGFGDQLEKLLKLL 157

                           170       180
                    ....*....|....*....|....*...
gi 1002285531   341 PNVSRIVLLSGTPSLSRPFDIYHQINML 368
Cdd:smart00487  158 PKNVQLLLLSATPPEEIENLLELFLNDP 185
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 514-609 2.19e-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: 78.79  E-value: 2.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  514 KTIIFAHHLKVLDgVQVFVTEQRIKYVRIDGSTSPRERKDAVDSFRlNPEVMVaIIGITAGGVGLDFSSAQNVVFVELPK 593
Cdd:pfam00271   17 KVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPDVDLVINYDLPW 93

                           90
                   ....*....|....*.
gi 1002285531  594 SASELLQAEDRAHRRG 609
Cdd:pfam00271   94 NPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
533-609 1.63e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.55  E-value: 1.63e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531   533 TEQRIKYVRIDGSTSPRERKDAVDSFRlNPEVMVaIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRG 609
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DpdE NF041062
protein DpdE;
215-358 1.41e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 59.21  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  215 RCLIADEMGLGKTLQAIAIACCY---KDEGPVLIVCPAVLRYTWAEELErwdpsflpkdihlvfghqdslER--LGACPK 289
Cdd:NF041062   172 RYLLADEVGLGKTIEAGLVIRQHlldNPDARVLVLVPDALVRQWRRELR---------------------DKffLDDFPG 230

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002285531  290 A--VVISYQMLSRLRKsmMNRRWALMIIDESHNIrcTKKKHEKNETQAVL-----ELAPNVSRIVLLSGTPSLSRP 358
Cdd:NF041062   231 ArvRVLSHEEPERWEP--LLDAPDLLVVDEAHQL--ARLAWSGDPPERARyrelaALAHAAPRLLLLSATPVLGNE 302
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1067-1102 7.80e-06

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


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 44.59  E-value: 7.80e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002285531 1067 PNEGNAWHADHIVPVYKGGGEcTLENLRTLCVACHS 1102
Cdd:COG1403     28 PFSGDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 1066-1105 3.08e-05

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: 42.46  E-value: 3.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002285531 1066 EPNEGNAWHADHIVPVyKGGGECTLENLRTLCVACHSEVT 1105
Cdd:cd00085     19 KPGGTEGLEVDHIIPL-SDGGNNDLDNLVLLCRKCHRKKH 57
HNH pfam01844
HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic ...
 1071-1102 1.82e-04

HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic acid-binding proteins that are generally associated with endonuclease activity.


Pssm-ID: 396422 [Multi-domain]  Cd Length: 47  Bit Score: 40.03  E-value: 1.82e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1002285531 1071 NAWHADHIVPVYKGGGEcTLENLRTLCVACHS 1102
Cdd:pfam01844   12 DALTVDHIIPLSDGGAD-DIENLILLCPSCHN 42
HNHc smart00507
HNH nucleases;
1073-1102 1.65e-03

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 37.44  E-value: 1.65e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1002285531  1073 WHADHIVPvYKGGGECTLENLRTLCVACHS 1102
Cdd:smart00507   24 LEVDHIIP-LSDGGNDDLDNLVLLCPKCHI 52
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 198-385 2.51e-75

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: 247.89  E-value: 2.51e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEGPVLIVCPAVLRYTWAEELERWDPSFLPKDIHLVFGH 277
Cdd:cd18010      1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  278 QDSLERLGacPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELAPNVSRIVLLSGTPSLSR 357
Cdd:cd18010     81 KDGLRDGD--AKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKR----TKAALPLLKRAKRVILLSGTPALSR 154

                          170       180
                   ....*....|....*....|....*...
gi 1002285531  358 PFDIYHQINMLWPHLLGSNKfDFANKYC 385
Cdd:cd18010    155 PIELFTQLDALDPKLFGRFH-DFGRRYC 181
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 190-627 6.94e-73

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 256.69  E-value: 6.94e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  190 LPQHLRDALLPFQLEGVKF--GLRRHG-RCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELERWD 263
Cdd:COG0553    234 LPAGLKATLRPYQLEGAAWllFLRRLGlGGLLADDMGLGKTIQALALLLELKERGlarPVLIVAPTSLVGNWQRELAKFA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  264 PSFlpkDIHLVFGHQDSLERLGACPKA--VVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLELap 341
Cdd:COG0553    314 PGL---RVLVLDGTRERAKGANPFEDAdlVITSYGLLRRDIELLAAVDWDLVILDEAQHI----KNPATKRAKAVRAL-- 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  342 NVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKFdFANKYCLLhtVQGCNGRTYQ----------IRRLKEHLLNEL 411
Cdd:COG0553    385 KARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKA-FRERFARP--IEKGDEEALErlrrllrpflLRRTKEDVLKDL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  412 PPKRRQIIWLKLNASDIK--TAIScikgvntsdeiptiaspdnsnDSEEVNMEEADGCKK----------------SPRn 473
Cdd:COG0553    462 PEKTEETLYVELTPEQRAlyEAVL---------------------EYLRRELEGAEGIRRrglilaaltrlrqicsHPA- 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  474 LTTQEIGIVKIPgfS---EWFLNhfIMKEPADNGsldsqsncQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRE 550
Cdd:COG0553    520 LLLEEGAELSGR--SaklEALLE--LLEELLAEG--------EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531  551 RKDAVDSFRLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYIFCARNTLDE 627
Cdd:COG0553    588 RDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 198-373 3.08e-40

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: 146.94  E-value: 3.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRR---HGRCLIADEMGLGKTLQAIAIA----CCYKDEGPVLIVCPAVLRYTWAEELERWDPSFLPKD 270
Cdd:cd17919      1 LRPYQLEGLNFLLELyenGPGGILADEMGLGKTLQAIAFLayllKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  271 IHlvfGHQDSLERLGACPKA-----VVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLELAPNvsR 345
Cdd:cd17919     81 YH---GSQRERAQIRAKEKLdkfdvVLTTYETLRRDKASLRKFRWDLVVVDEAHRL----KNPKSQLSKALKALRAK--R 151

                          170       180
                   ....*....|....*....|....*...
gi 1002285531  346 IVLLSGTPSLSRPFDIYHQINMLWPHLL 373
Cdd:cd17919    152 RLLLTGTPLQNNLEELWALLDFLDPPFL 179
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 513-620 4.72e-35

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: 130.29  E-value: 4.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  513 QKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRERKDAVDSFRLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELP 592
Cdd:cd18793     28 EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILYDPW 107

                           90       100
                   ....*....|....*....|....*...
gi 1002285531  593 KSASELLQAEDRAHRRGQTNAVNIYIFC 620
Cdd:cd18793    108 WNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 198-372 5.84e-35

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: 132.80  E-value: 5.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLR-RHGRCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELerWDPSFLPKDIhL 273
Cdd:cd18011      1 PLPHQIDAVLRALRkPPVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWQDEL--QDKFGLPFLI-L 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  274 VFGHQDSLERLGACPKA----VVISYQMLSRLRKS---MMNRRWALMIIDESHNIRCTKKKHEKNETQAVLELAPNVSRI 346
Cdd:cd18011     78 DRETAAQLRRLIGNPFEefpiVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLGRLLAKRARHV 157

                          170       180
                   ....*....|....*....|....*.
gi 1002285531  347 VLLSGTPSLSRPFDIYHQINMLWPHL 372
Cdd:cd18011    158 LLLTATPHNGKEEDFRALLSLLDPGR 183
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 202-425 4.38e-31

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: 124.33  E-value: 4.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  202 QLEGVKFGLRRH---GR-CLIADEMGLGKTLQAIA-IACCY----KDEGPVLIVCPAVLRYTWAEELERW-DPSFLPKDI 271
Cdd:pfam00176    2 QIEGVNWMLSLEnnlGRgGILADEMGLGKTLQTISlLLYLKhvdkNWGGPTLIVVPLSLLHNWMNEFERWvSPPALRVVV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HlvFGHQDSLERLGACPK------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELapNVSR 345
Cdd:pfam00176   82 L--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KTRN 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  346 IVLLSGTPSLSRPFDIYHQINMLWPHLLGS-----NKFDF-------ANKYCLLHTVQgcngRTYQIRRLKEHLLNELPP 413
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSlstfrNWFDRpiergggKKGVSRLHKLL----KPFLLRRTKKDVEKSLPP 229

                          250
                   ....*....|..
gi 1002285531  414 KRRQIIWLKLNA 425
Cdd:pfam00176  230 KVEYILFCRLSK 241
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 198-384 1.53e-29

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: 117.28  E-value: 1.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK---FgLRRH--GRCLiADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELERWDPSFLPK 269
Cdd:cd18012      5 LRPYQKEGFNwlsF-LRHYglGGIL-ADDMGLGKTLQTLALLLSRKEEGrkgPSLVVAPTSLIYNWEEEAAKFAPELKVL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  270 DIHLVFGHQDSLERLGacPKAVVI-SYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLEL-APNvsRIV 347
Cdd:cd18012     83 VIHGTKRKREKLRALE--DYDLVItSYGLLRRDIELLKEVKFHYLVLDEAQNI----KNPQTKTAKAVKALkADH--RLA 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002285531  348 lLSGTP---SLSrpfDIYHQINMLWPHLLGSNKfDFANKY 384
Cdd:cd18012    155 -LTGTPienHLG---ELWSIFDFLNPGLLGSYK-RFKKRF 189
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 194-627 2.78e-26

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 116.82  E-value: 2.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  194 LRDallpFQLEGVKFGLR--RHG-RCLIADEMGLGKTLQAIAIACcYKDE-----GPVLIVCPAVLRYTWAEELERWDPS 265
Cdd:PLN03142   170 MRD----YQLAGLNWLIRlyENGiNGILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPV 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  266 FLPKDIHlvfGHQDSL----ERLGACPK--AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNETQAVLEL 339
Cdd:PLN03142   245 LRAVKFH---GNPEERahqrEELLVAGKfdVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI-----KNENSLLSKTMRL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  340 APNVSRIvLLSGTPSLSRPFDIYHQINMLWPHLLGS-NKFD--FANK--------YCLLHTVQgcngRTYQIRRLKEHLL 408
Cdd:PLN03142   317 FSTNYRL-LITGTPLQNNLHELWALLNFLLPEIFSSaETFDewFQISgendqqevVQQLHKVL----RPFLLRRLKSDVE 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  409 NELPPKRRQIiwLKLNASDIKTAI------SCIKGVNTSDEiptiaspdnsnDSEEVNME-EADGCKKSPRNLTTQEIGI 481
Cdd:PLN03142   392 KGLPPKKETI--LKVGMSQMQKQYykallqKDLDVVNAGGE-----------RKRLLNIAmQLRKCCNHPYLFQGAEPGP 458

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  482 VKIPGfsewflNHFImkepADNGS---LDS-----QSNCQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRERKD 553
Cdd:PLN03142   459 PYTTG------EHLV----ENSGKmvlLDKllpklKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDA 528

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002285531  554 AVDSF-RLNPEVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYIFCARNTLDE 627
Cdd:PLN03142   529 SIDAFnKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
DEXDc smart00487
DEAD-like helicases superfamily;
190-368 4.03e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 98.33  E-value: 4.03e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531   190 LPQHLRDALLPFQLEGVKFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEG---PVLIVCP-AVLRYTWAEELERWDPS 265
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGkggRVLVLVPtRELAEQWAEELKKLGPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531   266 FLPKDIHLVFGHQDSLER---LGACPKAVVISYQMLSRL--RKSMMNRRWALMIIDESHNIrctKKKHEKNETQAVLELA 340
Cdd:smart00487   81 LGLKVVGLYGGDSKREQLrklESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRL---LDGGFGDQLEKLLKLL 157

                           170       180
                    ....*....|....*....|....*...
gi 1002285531   341 PNVSRIVLLSGTPSLSRPFDIYHQINML 368
Cdd:smart00487  158 PKNVQLLLLSATPPEEIENLLELFLNDP 185
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 198-377 7.37e-23

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: 98.58  E-value: 7.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGV-------KFGLrrHGrcLIADEMGLGKTLQAIAI--ACCYKDEG-------PVLIVCPAVLRYTWAEELER 261
Cdd:cd17999      1 LRPYQQEGInwlaflnKYNL--HG--ILCDDMGLGKTLQTLCIlaSDHHKRANsfnsenlPSLVVCPPTLVGHWVAEIKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  262 WDPSFLPKDIHLVFGHQD--SLERLGACPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHEKnetqAVLEL 339
Cdd:cd17999     77 YFPNAFLKPLAYVGPPQErrRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSK----AVKQL 152

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1002285531  340 APNvSRIVlLSGTPSLSRPFDIYHQINMLWPHLLGSNK 377
Cdd:cd17999    153 KAN-HRLI-LSGTPIQNNVLELWSLFDFLMPGYLGTEK 188
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 198-384 8.78e-23

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: 98.52  E-value: 8.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFgLRRH-----------GRCLIADEMGLGKTLQAI----AIACCYKDEGPVLIVCPAVLRYTWAEELERW 262
Cdd:cd18007      1 LKPHQVEGVRF-LWSNlvgtdvgsdegGGCILAHTMGLGKTLQVItflhTYLAAAPRRSRPLVLCPASTLYNWEDEFKKW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  263 DPSFLPKDihLVFGHQDSLERLGACPKAV----------VISYQMLSRL--------RKSMMNRRWALM------IIDES 318
Cdd:cd18007     80 LPPDLRPL--LVLVSLSASKRADARLRKInkwhkeggvlLIGYELFRNLasnattdpRLKQEFIAALLDpgpdllVLDEG 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002285531  319 HNIrctkkkheKNETQAVLELAPNV--SRIVLLSGTPsLSRPFDIYHQ-INMLWPHLLGSNKfDFANKY 384
Cdd:cd18007    158 HRL--------KNEKSQLSKALSKVktKRRILLTGTP-LQNNLKEYWTmVDFARPKYLGTLK-EFKKKF 216
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 198-353 2.77e-21

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: 93.99  E-value: 2.77e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFgLRR------HGrcLIADEMGLGKTLQAIAIACCYKDE---GPVLIVCPAVLRYTWAEELERWDPSfLP 268
Cdd:cd18009      4 MRPYQLEGMEW-LRMlwengiNG--ILADEMGLGKTIQTIALLAHLRERgvwGPFLVIAPLSTLPNWVNEFARFTPS-VP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  269 kdIHLVFGHQDSLERL-----------GACPkAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRctkkkheKNETQAVL 337
Cdd:cd18009     80 --VLLYHGTKEERERLrkkimkregtlQDFP-VVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLK-------NLNCRLIQ 149

                          170
                   ....*....|....*..
gi 1002285531  338 ELAP-NVSRIVLLSGTP 353
Cdd:cd18009    150 ELKTfNSDNRLLLTGTP 166
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 198-353 4.19e-21

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: 92.39  E-value: 4.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGRC---LIADEMGLGKTLQAIA----IACCYKDEGPVLIVCPAVLRYTWAEELERWDP------ 264
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflaaLHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  265 ------SFLPKDIHLVFGHQDSL-ERLGACPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRctkkkhekNE----T 333
Cdd:cd18000     81 lhssgsGTGSEEKLGSIERKSQLiRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIR--------NPdaeiT 152

                          170       180
                   ....*....|....*....|
gi 1002285531  334 QAVLELaPNVSRIvLLSGTP 353
Cdd:cd18000    153 LACKQL-RTPHRL-ILSGTP 170
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 194-380 5.54e-21

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: 92.80  E-value: 5.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  194 LRDallpFQLEGVKFGLRRHGRCL---IADEMGLGKTLQAIAI----ACCYKDEGPVLIVCPAVLRYTWAEELERWDPSF 266
Cdd:cd18003      1 LRE----YQHIGLDWLATLYEKNLngiLADEMGLGKTIQTIALlahlACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  267 lpkDIHLVFGHQD--SLERLG-ACPKA--VVI-SYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHekneTQAVLELa 340
Cdd:cd18003     77 ---KILTYYGSAKerKLKRQGwMKPNSfhVCItSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQR----WQTLLNF- 148

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002285531  341 pNVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKfDF 380
Cdd:cd18003    149 -NTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQ-EF 186
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 198-375 3.30e-20

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: 91.29  E-value: 3.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF--GLRRHGR-CLIADEMGLGKTLQAIA-IACCYKDEG-----------------------PVLIVCPAV 250
Cdd:cd18005      1 LRDYQREGVEFmyDLYKNGRgGILGDDMGLGKTVQVIAfLAAVLGKTGtrrdrennrprfkkkppassakkPVLIVAPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  251 LRYTWAEELERWDpSFLPKDIHLVfGHQDSLE---RLGACpKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKK 327
Cdd:cd18005     81 VLYNWKDELDTWG-HFEVGVYHGS-RKDDELEgrlKAGRL-EVVVTTYDTLRRCIDSLNSINWSAVIADEAHRI----KN 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1002285531  328 HEKNETQAVLELAPNVsRIVlLSGTpSLSRPFDIYHQI-NMLWPHLLGS 375
Cdd:cd18005    154 PKSKLTQAMKELKCKV-RIG-LTGT-LLQNNMKELWCLlDWAVPGALGS 199
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 198-375 2.09e-18

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 85.98  E-value: 2.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF------GLRRHGR--CLIADEMGLGKTLQAIAIACCYKDEGP--------VLIVCPAVLRYTWAEELER 261
Cdd:cd18067      1 LRPHQREGVKFlyrcvtGRRIRGShgCIMADEMGLGKTLQCITLMWTLLRQSPqckpeidkAIVVSPSSLVKNWANELGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  262 W-DPSFLP-------KDIHLVFGHQDSLERLGACPKAV-VISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNE 332
Cdd:cd18067     81 WlGGRLQPlaidggsKKEIDRKLVQWASQQGRRVSTPVlIISYETFRLHVEVLQKGEVGLVICDEGHRL-----KNSDNQ 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1002285531  333 TQAVLElAPNVSRIVLLSGTP---SLSRPFDIYHQINmlwPHLLGS 375
Cdd:cd18067    156 TYQALD-SLNTQRRVLLSGTPiqnDLSEYFSLVNFVN---PGILGT 197
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 198-389 1.35e-17

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: 83.07  E-value: 1.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLR--RHGR-CLIADEMGLGKTLQAIA----IACCYKDEGPVLIVCPAVLRYTWAEELERWdpsflpKD 270
Cdd:cd17995      1 LRDYQLEGVNWLLFnwYNRRnCILADEMGLGKTIQSIAflehLYQVEGIRGPFLVIAPLSTIPNWQREFETW------TD 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  271 IHLVFGH--QDSLERL-----------GACPK------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheKN 331
Cdd:cd17995     75 MNVVVYHgsGESRQIIqqyemyfkdaqGRKKKgvykfdVLITTYEMVIADAEELRKIPWRVVVVDEAHRL--------KN 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002285531  332 ETQAVLE--LAPNVSRIVLLSGTPSlsrpfdiyhQINM--LWP--HLLGSNKF----DFANKYCLLHT 389
Cdd:cd17995    147 RNSKLLQglKKLTLEHKLLLTGTPL---------QNNTeeLWSllNFLEPEKFpsseEFLEEFGDLKT 205
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 514-609 2.19e-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: 78.79  E-value: 2.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  514 KTIIFAHHLKVLDgVQVFVTEQRIKYVRIDGSTSPRERKDAVDSFRlNPEVMVaIIGITAGGVGLDFSSAQNVVFVELPK 593
Cdd:pfam00271   17 KVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPDVDLVINYDLPW 93

                           90
                   ....*....|....*.
gi 1002285531  594 SASELLQAEDRAHRRG 609
Cdd:pfam00271   94 NPASYIQRIGRAGRAG 109
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 198-384 3.03e-17

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: 82.33  E-value: 3.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRR-HGR-------CLIADEMGLGKTLQAIAIACCYKDEGP--------VLIVCPAVLRYTWAEELER 261
Cdd:cd18004      1 LRPHQREGVQFLYDClTGRrgyggggAILADEMGLGKTLQAIALVWTLLKQGPygkptakkALIVCPSSLVGNWKAEFDK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  262 WDPSFLPKDIHL----VFGHQDSLERLGACPKAV-VISYQML----SRLRKSMmnrRWALMIIDESHNIrctkKKHEKNE 332
Cdd:cd18004     81 WLGLRRIKVVTAdgnaKDVKASLDFFSSASTYPVlIISYETLrrhaEKLSKKI---SIDLLICDEGHRL----KNSESKT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002285531  333 TQAVLELapNVSRIVLLSGTP---SLSRPFDIYHQINmlwPHLLGSNKfDFANKY 384
Cdd:cd18004    154 TKALNSL--PCRRRLLLTGTPiqnDLDEFFALVDFVN---PGILGSLA-SFRKVF 202
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 198-408 5.71e-17

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: 81.56  E-value: 5.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGrcLIADEMGLGKTLQAIAIACCYKDEGPV---------------------LIVCPAVLRYTWA 256
Cdd:cd18008      1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALALILATRPQDPKipeeleenssdpkklylskttLIVVPLSLLSQWK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  257 EELER-WDPSFLPKDIHLVFGHQDSLERLGACpKAVVISYQMLSRLRK----------------SMMNRRWALMIIDESH 319
Cdd:cd18008     79 DEIEKhTKPGSLKVYVYHGSKRIKSIEELSDY-DIVITTYGTLASEFPknkkgggrdskekeasPLHRIRWYRVILDEAH 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  320 NIRCTKKKheknETQAVLELaPNVSRIVlLSGTPSLSRPFDIYHQINMLWPHLLGSNKFDfaNKYCLLHTVQGCNGRTYQ 399
Cdd:cd18008    158 NIKNRSTK----TSRAVCAL-KAERRWC-LTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF--NSDISKPFSKNDRKALER 229


                   ....*....
gi 1002285531  400 IRRLKEHLL 408
Cdd:cd18008    230 LQALLKPIL 238
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 198-389 1.28e-16

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: 80.49  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF--GL--RRHGRCLiADEMGLGKTLQAIAIACCYKDEG---PVLIVCPAVLRYTWAEELERWDPSFLPKD 270
Cdd:cd18001      1 LYPHQREGVAWlwSLhdGGKGGIL-ADDMGLGKTVQICAFLSGMFDSGlikSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  271 IH--LVFGHQDSLERLGACPKAVVISYQMLSRLRKSMMNR-----RWALMIIDESHNIRCTKKKheknETQAVLELaPNV 343
Cdd:cd18001     80 FHgtSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADdhdefKWDYVILDEGHKIKNSKTK----SAKSLREI-PAK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1002285531  344 SRIvLLSGTPslsrpfdIYHQINMLWphllgsNKFDFANKYCLLHT 389
Cdd:cd18001    155 NRI-ILTGTP-------IQNNLKELW------ALFDFACNGSLLGT 186
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 198-384 1.32e-16

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: 79.79  E-value: 1.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRR----HGrCLIADEMGLGKTLQAIAI----ACCYKDEGPVLIVCPAVLRYTWAEELERWDPsflpk 269
Cdd:cd18006      1 LRPYQLEGVNWLLQCraeqHG-CILGDEMGLGKTCQTISLlwylAGRLKLLGPFLVLCPLSVLDNWKEELNRFAP----- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  270 DIHLVFGHQDSLERLGACPK--------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheKNET----QAVL 337
Cdd:cd18006     75 DLSVITYMGDKEKRLDLQQDikstnrfhVLLTTYEICLKDASFLKSFPWASLVVDEAHRL--------KNQNsllhKTLS 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1002285531  338 ELApnVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKFD-FANKY 384
Cdd:cd18006    147 EFS--VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDdFIKAY 192
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 198-375 2.13e-16

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: 79.89  E-value: 2.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF------GLRRHGR--CLIADEMGLGKTLQAIAIACCYKDEGP---------VLIVCPAVLRYTWAEELE 260
Cdd:cd18066      1 LRPHQREGIEFlyecvmGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  261 RWDPSflpKDIHLVFGHQD-SLERLGACP--KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKheknETQAVL 337
Cdd:cd18066     81 KWLGS---ERIKVFTVDQDhKVEEFIASPlySVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIK----TTTALT 153

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1002285531  338 ELApnVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGS 375
Cdd:cd18066    154 SLS--CERRIILTGTPIQNDLQEFFALIDFVNPGILGS 189
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 217-415 4.43e-16

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: 79.32  E-value: 4.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCYKD----EGPVLIVCPAVLRYTWAEELERWDPSFlpKDIHLVFGHQD--SLERLGACP-- 288
Cdd:cd18064     38 ILADEMGLGKTLQTISLLGYMKHyrniPGPHMVLVPKSTLHNWMAEFKRWVPTL--RAVCLIGDKDQraAFVRDVLLPge 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  289 -KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNETQAVLELAPNVSRIvLLSGTPSLSRPFDIYHQINM 367
Cdd:cd18064    116 wDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRI-----KNEKSKLSEIVREFKTTNRL-LLTGTPLQNNLHELWALLNF 189

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002285531  368 LWPHLLGS-NKFD--FANKYCL--------LHTVQgcngRTYQIRRLKEHLLNELPPKR 415
Cdd:cd18064    190 LLPDVFNSaEDFDswFDTNNCLgdqklverLHMVL----RPFLLRRIKADVEKSLPPKK 244
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 200-368 1.11e-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: 77.39  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  200 PFQLEGVKFGLRRHGRCLIADeMGLGKT---LQAIAIACCYKDEGPVLIVCPA-VLRYTWAEELERWDpsfLPKDIH--L 273
Cdd:cd18013      3 PYQKVAINFIIEHPYCGLFLD-MGLGKTvttLTALSDLQLDDFTRRVLVIAPLrVARSTWPDEVEKWN---HLRNLTvsV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  274 VFGHQDSLERLGACPKAV-VISYQMLSRLRKsMMNRRW--ALMIIDESHNIrctkKKHEKNETQAVLELAPNVSRIVLLS 350
Cdd:cd18013     79 AVGTERQRSKAANTPADLyVINRENLKWLVN-KSGDPWpfDMVVIDELSSF----KSPRSKRFKALRKVRPVIKRLIGLT 153

                          170
                   ....*....|....*...
gi 1002285531  351 GTPSLSRPFDIYHQINML 368
Cdd:cd18013    154 GTPSPNGLMDLWAQIALL 171
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 217-404 1.46e-15

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: 76.98  E-value: 1.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCYKD----EGPVLIVCPAVLRYTWAEELERWDPSFLPKDIHlvfGHQD---SLERLGACPK 289
Cdd:cd17997     26 ILADEMGLGKTLQTISLLGYLKHykniNGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLI---GDKEeraDIIRDVLLPG 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  290 ---AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNETQAVLELAPNVSRIvLLSGTPSLSRPFDIYHQIN 366
Cdd:cd17997    103 kfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRI-----KNEKSKLSQIVRLFNSRNRL-LLTGTPLQNNLHELWALLN 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1002285531  367 MLWPHLLGSNK-FD--FANKYCL---------LHTVQgcngRTYQIRRLK 404
Cdd:cd17997    177 FLLPDVFTSSEdFDewFNVNNCDddnqevvqrLHKVL----RPFLLRRIK 222
HELICc smart00490
helicase superfamily c-terminal domain;
533-609 1.63e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.55  E-value: 1.63e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531   533 TEQRIKYVRIDGSTSPRERKDAVDSFRlNPEVMVaIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRG 609
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 217-353 3.68e-14

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: 73.31  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCYKDE----GPVLIVCPAVLRYTWAEELERWDPSF--LP-------KDIHLVFGHQDSLER 283
Cdd:cd18002     23 ILADEMGLGKTVQSIAVLAHLAEEhniwGPFLVIAPASTLHNWQQEISRFVPQFkvLPywgnpkdRKVLRKFWDRKNLYT 102

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  284 LGACPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHEKNetqavlELAPNVSRIVLLSGTP 353
Cdd:cd18002    103 RDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT------LLSFHCRNRLLLTGTP 166
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 198-370 5.39e-14

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: 71.70  E-value: 5.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGV---KFGLRRHGRCLIADEMGLGKTLQAIA-IACCYKD---EGPVLIVCPAVLRYTWAEELERWDPsflpkD 270
Cdd:cd17994      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVfLYSLYKEghsKGPFLVSAPLSTIINWEREFEMWAP-----D 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  271 IHLVFGHQDSLerlgacpkaVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHEKNETQAvlelapNVSRIVLLS 350
Cdd:cd17994     76 FYVVTYVGDHV---------LLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSY------KIGYKLLLT 140

                          170       180
                   ....*....|....*....|
gi 1002285531  351 GTPSLSRPFDIYHQINMLWP 370
Cdd:cd17994    141 GTPLQNNLEELFHLLNFLTP 160
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
198-623 8.60e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 75.83  E-value: 8.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGV----KFGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEGPVLIVCP-AVLRYTWAEELERWDPsflpkDIH 272
Cdd:COG1061     81 LRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPrRELLEQWAEELRRFLG-----DPL 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  273 LVFGHQDSLERLgacpkaVVISYQMLS-RLRKSMMNRRWALMIIDESHNIRctkkkheKNETQAVLELAPNVsRIVLLSG 351
Cdd:COG1061    156 AGGGKKDSDAPI------TVATYQSLArRAHLDELGDRFGLVIIDEAHHAG-------APSYRRILEAFPAA-YRLGLTA 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  352 TPSLSRPFDIYHQInmlwphllgsnkfdfankycllhtvqgCNGRTYQIrRLKEhLLNE--LPPKRRQIIWlklnasdik 429
Cdd:COG1061    222 TPFRSDGREILLFL---------------------------FDGIVYEY-SLKE-AIEDgyLAPPEYYGIR--------- 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  430 taiscikgVNTSDEIPTIASPDNSNDseevnmeeadgckkspRNLTTQEIGIVKIpgfsewfLNHFIMKEPADngsldsq 509
Cdd:COG1061    264 --------VDLTDERAEYDALSERLR----------------EALAADAERKDKI-------LRELLREHPDD------- 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  510 sncQKTIIFAHHLKVLDGVQVFVTEQRIKYVRIDGSTSPRERKDAVDSFRLNP-EVMVAiigITAGGVGLDFSSAQNVVF 588
Cdd:COG1061    306 ---RKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGElRILVT---VDVLNEGVDVPRLDVAIL 379

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1002285531  589 VELPKSASELLQAEDRAHR--RGQTNAVnIYIFCARN 623
Cdd:COG1061    380 LRPTGSPREFIQRLGRGLRpaPGKEDAL-VYDFVGND 415
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 198-353 2.10e-13

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: 70.86  E-value: 2.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGRCL---IADEMGLGKTLQAIAIaCCY-----KDEGPVLIVCPAVLRYTWAEELERWDPSFL-- 267
Cdd:cd17996      4 LKEYQLKGLQWMVSLYNNNLngiLADEMGLGKTIQTISL-ITYlmekkKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSki 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  268 ----PKDIHLVFGHQdslERLGACpKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQaVLELAPNV 343
Cdd:cd17996     83 vykgTPDVRKKLQSQ---IRAGKF-NVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRM----KNAQSKLTQ-TLNTYYHA 153

                          170
                   ....*....|
gi 1002285531  344 SRIVLLSGTP 353
Cdd:cd17996    154 RYRLLLTGTP 163
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 193-407 2.27e-13

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: 70.46  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  193 HLRDallpFQLEGVKFGLR---RHGRCLIADEMGLGKTLQAIA-IACCYKDE---GPVLIVCPAVLRYTWAEELERWDPs 265
Cdd:cd17993      1 ELRD----YQLTGLNWLAHswcKGNNGILADEMGLGKTVQTISfLSYLFHSQqqyGPFLVVVPLSTMPAWQREFAKWAP- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  266 flpkDIHLV--FGHQDSLE-----RLGACPK------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNE 332
Cdd:cd17993     76 ----DMNVIvyLGDIKSRDtireyEFYFSQTkklkfnVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRL----KNDESLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531  333 TQAVLELapNVSRIVLLSGTPslsrpfdIYHQINMLWP--HLLGSNKFDFANKYCLLHTvqgcNGRTYQIRRLKEHL 407
Cdd:cd17993    148 YEALKEF--KTNNRLLITGTP-------LQNSLKELWAllHFLMPGKFDIWEEFEEEHD----EEQEKGIADLHKEL 211
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 217-404 2.35e-13

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: 70.82  E-value: 2.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCYKD----EGPVLIVCPAVLRYTWAEELERWDPSFL------PKDIHLVFGHQdslERLGA 286
Cdd:cd18065     38 ILADEMGLGKTLQTIALLGYLKHyrniPGPHMVLVPKSTLHNWMNEFKRWVPSLRavcligDKDARAAFIRD---VMMPG 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  287 CPKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkKHEKNETQAVLELAPNVSRIvLLSGTPSLSRPFDIYHQIN 366
Cdd:cd18065    115 EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRI-----KNEKSKLSEIVREFKTTNRL-LLTGTPLQNNLHELWALLN 188

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1002285531  367 MLWPHLLGS-NKFD--FANKYCL--------LHTVQgcngRTYQIRRLK 404
Cdd:cd18065    189 FLLPDVFNSaDDFDswFDTKNCLgdqklverLHAVL----KPFLLRRIK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 201-375 1.01e-12

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: 69.32  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  201 FQLEGVKFGLRRHGRCL---IADEMGLGKTLQAIAIACCYKDE----GPVLIVCPAVLRYTWAEELERWDPSFLPKDIHL 273
Cdd:cd18063     27 YQLQGLEWMVSLYNNNLngiLADEMGLGKTIQTIALITYLMEHkrlnGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKG 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  274 VFGHQDSLE---RLGACpKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQaVLELAPNVSRIVLLS 350
Cdd:cd18063    107 TPAMRRSLVpqlRSGKF-NVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRM----KNHHCKLTQ-VLNTHYVAPRRILLT 180

                          170       180
                   ....*....|....*....|....*
gi 1002285531  351 GTPSLSRPFDIYHQINMLWPHLLGS 375
Cdd:cd18063    181 GTPLQNKLPELWALLNFLLPTIFKS 205
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 217-375 3.89e-12

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: 67.76  E-value: 3.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCYKD----EGPVLIVCPAVLRYTWAEELERWDPSFLPkdihlVFGHQDSLERLGACPK--- 289
Cdd:cd18062     46 ILADEMGLGKTIQTIALITYLMEhkriNGPFLIIVPLSTLSNWVYEFDKWAPSVVK-----VSYKGSPAARRAFVPQlrs 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  290 ----AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQaVLELAPNVSRIVLLSGTPSLSRPFDIYHQI 365
Cdd:cd18062    121 gkfnVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRM----KNHHCKLTQ-VLNTHYVAPRRLLLTGTPLQNKLPELWALL 195

                          170
                   ....*....|
gi 1002285531  366 NMLWPHLLGS 375
Cdd:cd18062    196 NFLLPTIFKS 205
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 198-370 5.86e-12

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: 66.63  E-value: 5.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGV---KFGLRRHGRCLIADEMGLGKTLQAIA-IACCYKD---EGPVLIVCPAVLRYTWAEELERWDPSFL--- 267
Cdd:cd18057      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVfLYSLYKEghsKGPYLVSAPLSTIINWEREFEMWAPDFYvvt 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  268 ---PKDIHLV-----FGHQDSLERLGACP-----------KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKH 328
Cdd:cd18057     81 ytgDKESRSVireneFSFEDNAIRSGKKVfrmkkeaqikfHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1002285531  329 EKnetqaVLElAPNVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18057    161 FR-----VLN-SYKIDYKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 201-371 7.90e-12

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: 66.57  E-value: 7.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  201 FQLEGV---KFGLRRHGRCLIADEMGLGKTLQAIA-IACCYKD---EGPVLIVCPAVLRYTWAEELERWDPSFL------ 267
Cdd:cd18055      4 YQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVfLYSLYKEghtKGPFLVSAPLSTIINWEREFQMWAPDFYvvtytg 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  268 PKDIHLV-----FGHQDSLERLGACP-----------KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKHEK- 330
Cdd:cd18055     84 DKDSRAIireneFSFDDNAVKGGKKAfkmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRv 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1002285531  331 -NETQavlelapnVSRIVLLSGTPSLSRPFDIYHQINMLWPH 371
Cdd:cd18055    164 lNGYK--------IDHKLLLTGTPLQNNLEELFHLLNFLTPE 197
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 198-353 1.43e-11

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: 64.71  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF--GLRRHG-RCLIADEMGLGKTLQAIAIACCYK---DEGPVLIVCPAVLRYTWAEELERWDPSFLpkdI 271
Cdd:cd17998      1 LKDYQLIGLNWlnLLYQKKlSGILADEMGLGKTIQVIAFLAYLKeigIPGPHLVVVPSSTLDNWLREFKRWCPSLK---V 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HLVFGHQDSLERLGACPK-------AVVISYQML---SRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAVLELap 341
Cdd:cd17998     78 EPYYGSQEERKHLRYDILkgledfdVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHML----KNMTSERYRHLMTI-- 151

                          170
                   ....*....|..
gi 1002285531  342 NVSRIVLLSGTP 353
Cdd:cd17998    152 NANFRLLLTGTP 163
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 194-380 3.50e-11

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: 64.64  E-value: 3.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  194 LRDallpFQLEGVKFGLRRHGRC---LIADEMGLGKTLQAIAIAC----CYKDEGPVLIVCPAVLRYTWAEELERWDPsf 266
Cdd:cd18054     21 LRD----YQLEGLNWLAHSWCKNnsvILADEMGLGKTIQTISFLSylfhQHQLYGPFLLVVPLSTLTSWQREFEIWAP-- 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  267 lpkDIHLV----------------FGHQDSlERLGAcpKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEK 330
Cdd:cd18054     95 ---EINVVvyigdlmsrntireyeWIHSQT-KRLKF--NALITTYEILLKDKTVLGSINWAFLGVDEAHRL----KNDDS 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1002285531  331 NETQAVLELAPNVSriVLLSGTPslsrpfdIYHQINMLWP--HLLGSNKFDF 380
Cdd:cd18054    165 LLYKTLIDFKSNHR--LLITGTP-------LQNSLKELWSllHFIMPEKFEF 207
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 198-370 5.01e-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: 5.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGV---KFGLRRHGRCLIADEMGLGKTLQ-AIAIACCYKD---EGPVLIVCPAVLRYTWAEELERWDPSFL--- 267
Cdd:cd18056      1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQtAVFLYSLYKEghsKGPFLVSAPLSTIINWEREFEMWAPDMYvvt 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  268 ---PKDIHLV-----FGHQDSLERLGACPK-----------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIRCTKKKH 328
Cdd:cd18056     81 yvgDKDSRAIireneFSFEDNAIRGGKKASrmkkeasvkfhVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1002285531  329 EKnetqaVLElAPNVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18056    161 FR-----VLN-GYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 223-321 9.39e-11

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: 61.17  E-value: 9.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  223 GLGKTLQAIAIACCYKdEGPVLIVCP-AVLRYTWAEELERWdpsFLPKDIHLVFGhqDSLERLGACPkAVVISYQMLSRL 301
Cdd:cd17926     28 GSGKTLTALALIAYLK-ELRTLIVVPtDALLDQWKERFEDF---LGDSSIGLIGG--GKKKDFDDAN-VVVATYQSLSNL 100

                           90       100
                   ....*....|....*....|..
gi 1002285531  302 RK--SMMNRRWALMIIDESHNI 321
Cdd:cd17926    101 AEeeKDLFDQFGLLIVDEAHHL 122
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 213-352 2.66e-10

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: 59.72  E-value: 2.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  213 HGRCLIADEMGLGKTLQAIAIACCY--KDEGPVLIVCP-AVLRYTWAEELERWdpSFLPKDIHLVFGHQDSLERLGAC-P 288
Cdd:cd00046      1 GENVLITAPTGSGKTLAALLAALLLllKKGKKVLVLVPtKALALQTAERLREL--FGPGIRVAVLVGGSSAEEREKNKlG 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  289 KAVVI--SYQMLSRLRKSMMN---RRWALMIIDESHniRCTKKKHEKN-ETQAVLELAPNVSRIVLLSGT 352
Cdd:cd00046     79 DADIIiaTPDMLLNLLLREDRlflKDLKLIIVDEAH--ALLIDSRGALiLDLAVRKAGLKNAQVILLSAT 146
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 217-362 3.75e-10

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: 61.72  E-value: 3.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIAIACCykdeGPVLIVCPAVLRYTWAEELERW-DPSFLpkDIHLVFGHQDSLERLGACPKAVVI-S 294
Cdd:cd18071     52 ILADDMGLGKTLTTISLILA----NFTLIVCPLSVLSNWETQFEEHvKPGQL--KVYTYHGGERNRDPKLLSKYDIVLtT 125

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002285531  295 YQMLS-----RLRKSMMNRRWALMIIDESHNIRCTKkkheKNETQAVLELAPnvSRIVLLSGTPSLSRPFDIY 362
Cdd:cd18071    126 YNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPN----AQQTKAVLNLSS--ERRWVLTGTPIQNSPKDLG 192
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 198-384 9.16e-10

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: 60.67  E-value: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF-----------GLRRHGR-CLIADEMGLGKTLQAIA----IACCYKDEG--PVLIVCPAVLRYTWAEEL 259
Cdd:cd18068      1 LKPHQVDGVQFmwdccceslkkTKKSPGSgCILAHCMGLGKTLQVVTflhtVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  260 ERW------DPSFLPKDIHLVFGHQD---SLERLGACPKAVVISYQMLSRL----------------RKSMMNRRWALMI 314
Cdd:cd18068     81 EKWqeglkdEEKIEVNELATYKRPQErsyKLQRWQEEGGVMIIGYDMYRILaqernvksreklkeifNKALVDPGPDFVV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002285531  315 IDESHNIrctkkkheKNETQAVLELAPNV--SRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKfDFANKY 384
Cdd:cd18068    161 CDEGHIL--------KNEASAVSKAMNSIrtKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIK-EFRNRF 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 198-370 4.58e-09

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 58.13  E-value: 4.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK---FGLRRHGRCLIADEMGLGKTLQAIAIAC---CYKDEGPVLIVCPAVLRYTWAEELERWdpsflpKDI 271
Cdd:cd18058      1 LREYQLEGMNwllFNWYNRKNCILADEMGLGKTIQSITFLSeifLMGIRGPFLIIAPLSTITNWEREFRTW------TEM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HLVFGHQDSLER-----------------LGACPK--AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheKNE 332
Cdd:cd18058     75 NAIVYHGSQISRqmiqqyemyyrdeqgnpLSGIFKfqVVITTFEMILADCPELKKINWSCVIIDEAHRL--------KNR 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002285531  333 TQAVLELAP--NVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18058    147 NCKLLEGLKlmALEHKVLLTGTPLQNSVEELFSLLNFLEP 186
DpdE NF041062
protein DpdE;
215-358 1.41e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 59.21  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  215 RCLIADEMGLGKTLQAIAIACCY---KDEGPVLIVCPAVLRYTWAEELErwdpsflpkdihlvfghqdslER--LGACPK 289
Cdd:NF041062   172 RYLLADEVGLGKTIEAGLVIRQHlldNPDARVLVLVPDALVRQWRRELR---------------------DKffLDDFPG 230

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002285531  290 A--VVISYQMLSRLRKsmMNRRWALMIIDESHNIrcTKKKHEKNETQAVL-----ELAPNVSRIVLLSGTPSLSRP 358
Cdd:NF041062   231 ArvRVLSHEEPERWEP--LLDAPDLLVVDEAHQL--ARLAWSGDPPERARyrelaALAHAAPRLLLLSATPVLGNE 302
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 198-408 2.19e-08

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: 56.58  E-value: 2.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKFGLRRHGrcLIADEMGLGKTLQAIA------------------------IACCYKDEGPV-----LIVCP 248
Cdd:cd18070      1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLAlillhprpdndldaadddsdemvcCPDCLVAETPVsskatLIVCP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  249 AVLRYTWAEELERWDPSFLPKDIH-----LVFGHQDSLERLgACPKAVVISYQML-------------SRLRKS------ 304
Cdd:cd18070     79 SAILAQWLDEINRHVPSSLKVLTYqgvkkDGALASPAPEIL-AEYDIVVTTYDVLrtelhyaeanrsnRRRRRQkryeap 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  305 ---MMNRRWALMIIDESHNIRCTkkkhekneTQAVLELAPNVSRIV--LLSGTPsLSRPFDiyhQINMLwPHLLGSNKFD 379
Cdd:cd18070    158 pspLVLVEWWRVCLDEAQMVESS--------TSKAAEMARRLPRVNrwCVSGTP-IQRGLD---DLFGL-LSFLGVEPFC 224

                          250       260       270
                   ....*....|....*....|....*....|
gi 1002285531  380 FANKYC-LLHTVQGCNGRTYQIRRLKEHLL 408
Cdd:cd18070    225 DSDWWArVLIRPQGRNKAREPLAALLKELL 254
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 198-370 4.72e-08

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: 55.06  E-value: 4.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK---FGLRRHGRCLIADEMGLGKTLQAIAIACCYKD---EGPVLIVCPAVLRYTWAEELERWdpsflpKDI 271
Cdd:cd18060      1 LREYQLEGVNwllFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNvgiHGPFLVIAPLSTITNWEREFNTW------TEM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HLVFGH----------------QDSLERL--GACP-KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheKNE 332
Cdd:cd18060     75 NTIVYHgslasrqmiqqyemycKDSRGRLipGAYKfDALITTFEMILSDCPELREIEWRCVIIDEAHRL--------KNR 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002285531  333 TQAVLELAP--NVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18060    147 NCKLLDSLKhmDLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 198-384 1.53e-07

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: 53.67  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVKF-------GLRRHGR-----CLIADEMGLGKTLQAIA---IACCYKDEGPVLIVCPAVLRYTWAEELERW 262
Cdd:cd18069      1 LKPHQIGGIRFlydniieSLERYKGssgfgCILAHSMGLGKTLQVISfldVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  263 DPSF------LPK--DIHLVF-GHQDSLERLGACPK------AVVISYQMLsRLRKSMmnrrwALMIIDESHNIRCTKkk 327
Cdd:cd18069     81 LPPPealpnvRPRpfKVFILNdEHKTTAARAKVIEDwvkdggVLLMGYEMF-RLRPGP-----DVVICDEGHRIKNCH-- 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002285531  328 heKNETQAVLELapNVSRIVLLSGTPSLSRPFDIYHQINMLWPHLLGSNKfDFANKY 384
Cdd:cd18069    153 --ASTSQALKNI--RSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQ-EFSNMF 204
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 198-370 1.62e-07

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: 53.47  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK---FGLRRHGRCLIADEMGLGKTLQAIA-IACCYKD--EGPVLIVCPAVLRYTWAEELERWdpsflpKDI 271
Cdd:cd18061      1 LREYQLEGLNwllFNWYNRRNCILADEMGLGKTIQSITfLYEILLTgiRGPFLIIAPLSTIANWEREFRTW------TDL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  272 HLVFGH----------------QDSLERL--GACP-KAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheKNE 332
Cdd:cd18061     75 NVVVYHgslisrqmiqqyemyfRDSQGRIirGAYRfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRL--------KNK 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002285531  333 TQAVLE--LAPNVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18061    147 NCKLLEglKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 198-370 1.65e-07

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: 53.50  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK---FGLRRHGRCLIADEMGLGKTLQAIAIacCYK-----DEGPVLIVCPAVLRYTWAEELERWdpsflpK 269
Cdd:cd18059      1 LREYQLEGVNwllFNWYNTRNCILADEMGLGKTIQSITF--LYEiylkgIHGPFLVIAPLSTIPNWEREFRTW------T 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  270 DIHLVFGHQDSLER-------------LGACPK------AVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkkkheK 330
Cdd:cd18059     73 ELNVVVYHGSQASRrtiqlyemyfkdpQGRVIKgsykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRL--------K 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1002285531  331 NETQAVLE--LAPNVSRIVLLSGTPSLSRPFDIYHQINMLWP 370
Cdd:cd18059    145 NRNCKLLEglKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 186
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 217-368 3.54e-07

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 52.48  E-value: 3.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  217 LIADEMGLGKTLQAIA--IAC-------------------CYKDEGPV-----LIVCPAVLRYTWAEELERWDPSflpKD 270
Cdd:cd18072     24 ILADDMGLGKTLTMIAliLAQkntqnrkeeekekalteweSKKDSTLVpsagtLVVCPASLVHQWKNEVESRVAS---NK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  271 IHLVFGHQDSLERLGACPKA---VVISYQMLSRLRKSMMNR---------RWALMIIDESHNIrctkKKHEKNETQAVLE 338
Cdd:cd18072    101 LRVCLYHGPNRERIGEVLRDydiVITTYSLVAKEIPTYKEEsrssplfriAWARIILDEAHNI----KNPKVQASIAVCK 176

                          170       180       190
                   ....*....|....*....|....*....|
gi 1002285531  339 LApNVSRIVlLSGTPSLSRPFDIYHQINML 368
Cdd:cd18072    177 LR-AHARWA-LTGTPIQNNLLDMYSLLKFL 204
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
 200-319 5.16e-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: 50.76  E-value: 5.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  200 PFQLEGVK--FGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEgpVLIVCP-AVLRYTWAEELERWdpSFLPKDIHLVFG 276
Cdd:cd18029     11 PYQEKALSkmFGNGRARSGVIVLPCGAGKTLVGITAACTIKKS--TLVLCTsAVSVEQWRRQFLDW--TTIDDEQIGRFT 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002285531  277 hQDSLERLGACPkaVVIS-YQMLSRLRK------SMMN----RRWALMIIDESH 319
Cdd:cd18029     87 -SDKKEIFPEAG--VTVStYSMLANTRKrspeseKFMEfiteREWGLIILDEVH 137
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 194-365 1.10e-06

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


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 51.20  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  194 LRDallpFQLEGVKFGLR---RHGRCLIADEMGLGKTLQAIAIACCYKDE----GPVLIVCPAVLRYTWAEELERWDPSF 266
Cdd:cd18053     21 LRD----YQLNGLNWLAHswcKGNSCILADEMGLGKTIQTISFLNYLFHEhqlyGPFLLVVPLSTLTSWQREIQTWAPQM 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  267 ----LPKDI---HLVFGHQ---DSLERLGAcpKAVVISYQMLSRLRKSMMNRRWALMIIDESHNIrctkKKHEKNETQAV 336
Cdd:cd18053     97 navvYLGDInsrNMIRTHEwmhPQTKRLKF--NILLTTYEILLKDKSFLGGLNWAFIGVDEAHRL----KNDDSLLYKTL 170

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1002285531  337 LELAPNvsRIVLLSGTP---SLSRPFDIYHQI 365
Cdd:cd18053    171 IDFKSN--HRLLITGTPlqnSLKELWSLLHFI 200
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
1067-1102 7.80e-06

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


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 44.59  E-value: 7.80e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002285531 1067 PNEGNAWHADHIVPVYKGGGEcTLENLRTLCVACHS 1102
Cdd:COG1403     28 PFSGDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 1066-1105 3.08e-05

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: 42.46  E-value: 3.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002285531 1066 EPNEGNAWHADHIVPVyKGGGECTLENLRTLCVACHSEVT 1105
Cdd:cd00085     19 KPGGTEGLEVDHIIPL-SDGGNNDLDNLVLLCRKCHRKKH 57
HNH pfam01844
HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic ...
 1071-1102 1.82e-04

HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic acid-binding proteins that are generally associated with endonuclease activity.


Pssm-ID: 396422 [Multi-domain]  Cd Length: 47  Bit Score: 40.03  E-value: 1.82e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1002285531 1071 NAWHADHIVPVYKGGGEcTLENLRTLCVACHS 1102
Cdd:pfam01844   12 DALTVDHIIPLSDGGAD-DIENLILLCPSCHN 42
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 563-618 2.67e-04

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: 40.77  E-value: 2.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002285531  563 EVMVAIIGITAGGVGLDFSSAQNVVFVELPKSASELLQAEDRAHRRGQTNAVNIYI 618
Cdd:cd18785     21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
ResIII pfam04851
Type III restriction enzyme, res subunit;
198-353 5.25e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  198 LLPFQLEGVK----FGLRRHGRCLIADEMGLGKTLQAIAIACCYKDEGP---VLIVCPAV-LRYTWAEELERWdpsFLPK 269
Cdd:pfam04851    4 LRPYQIEAIEnlleSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPikkVLFLVPRKdLLEQALEEFKKF---LPNY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285531  270 DIHLVFGHQDSLERLGACPKAVVISYQMLSRLRKSMMNR----RWALMIIDESHniRCTKKKHEKnetqaVLELAPNvSR 345
Cdd:pfam04851   81 VEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLEllpdFFDVIIIDEAH--RSGASSYRN-----ILEYFKP-AF 152


                   ....*...
gi 1002285531  346 IVLLSGTP 353
Cdd:pfam04851  153 LLGLTATP 160
HNHc smart00507
HNH nucleases;
1073-1102 1.65e-03

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 37.44  E-value: 1.65e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1002285531  1073 WHADHIVPvYKGGGECTLENLRTLCVACHS 1102
Cdd:smart00507   24 LEVDHIIP-LSDGGNDDLDNLVLLCPKCHI 52
 
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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